diff --git "a/psimod/psimod.owl" "b/psimod/psimod.owl" new file mode 100755--- /dev/null +++ "b/psimod/psimod.owl" @@ -0,0 +1,110181 @@ + + + + + 13:06:2021 12:12 + PSI-MOD + 1.2 + Joshua Klein + Annotation note 01 - "[PSI-MOD:ref]" has been replaced by PubMed:18688235. + Annotation note 02 - When an entry in the RESID Database is annotated with different sources because the same modification can arise from different encoded amino acids, then the PSI-MOD definition for each different source instance carries the RESID cross-reference followed by a hash symbol "#" and a 3 or 4 character label. When an entry in the RESID Database is annotated as a general modification with the same enzymatic activity producing different chemical structures depending on natural variation in the nonproteinaceous substrate, on secondary modifications that do not change the nature of the primary modification, or on a combination of a primary and one or more secondary modifications on the same residue, then the PSI-MOD definition for each different instance carries the RESID cross-reference followed by the special tag "#var". + Annotation note 03 - When an entry in the Unimod database is annotated as a general modification, and one or more instance sites are listed, then the PSI-MOD definition for each different site instance carries the Unimod cross-reference followed by a hash symbol and an amino acid code, "N-term" or "C-term". + Annotation note 04 - The elemental formulas are in strict alphabetical order, not in CAS ("C" and "H" first) order. Isotope numbers are in parentheses before the element symbol, and an element should not occur in a formula both with and without an isotope number. In difference formulas, counts can be zero or negative. + Annotation note 05 - In entries with an isotope indicator in the formula, average masses are meaningless and are assigned the value equal to the monoisotopic mass, but rounded to a lower precision; monoisotopic masses are calculated by using the masses for the indicated isotopes and the most common isotopes for other elements without isotope indicators in the formulas. + Annotation note 06 - For cross-link modifications, the number following "Cross-link" in the comment record indicates the number of amino acid residues that appear in the origin record, used to check the difference formula and masses. This usage differs from RESID, where the cross-link number indicates the maximum number of peptide chains that can be cross-linked. + Annotation note 07 - The synonym cross-reference "MOD:old name" has been replaced by "MOD:alternate name". + Annotation note 08 - The DeltaMass listings for free amino acids have been removed. Most Unimod entries that have not been "approved" have by general agreement not been incorporated unless there has been a request for a specific term by a PRIDE submitter. + Annotation note 09 - The Open Mass Spectrometry Search Algorithm, OMSSA, enumerated list of modifications are being incorporated. The string values are synonyms with the synonymtypedef "OMSSA-label", and their integer values (which are supposed to be stable) are definition cross-references. + Annotation note 10 - GNOme is the Glycan Naming and Subsumption Ontology (https://gnome.glyomics.org/), an ontology for the support of glycomics. PSI-MOD does not have all possible glycans in its entries, just the ones that are noted to be on proteins and have been requested for addition. GNOme uses GlyTouCan (http://glytoucan.org/) to provide stable accessions for glycans described at varyious degrees of characterization, including compositions (no linkage) and topologies (no carbon bond positions or anomeric configurations). + ISO-8601 date: 2022-06-13 12:12Z + PSI-MOD version: 1.031.6 + RESID release: 75.00 + + + + + + + + + + + + + definition + + + + + + + + term replaced by + + + + + + + + + Label from MS DeltaMass + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + Short label from OMSSA + + + + + + + + + + + + + + + + Alternate name curated by PSI-MOD + + + + + + + + + + Short label curated by PSI-MOD + + + + + + + + + subset of protein modifications + + + + + + + + + + Agreed label from MS community + + + + + + + + + + Alternate name from RESID + + + + + + + + + + Misnomer tagged alternate name from RESID + + + + + + + + + + Name from RESID + + + + + + + + + + Systematic name from RESID + + + + + + + + + + + + + + + + + + + + + + Protein feature description from UniProtKB + + + + + + + + + + Alternate name from Unimod + + + + + + + + + + Description (full_name) from Unimod + + + + + + + + + + Interim label from Unimod + + + + + + + + + subset_property + + + + + + + + synonym_type_property + + + + + + + + + + + + + + + + + + + + database_cross_reference + + + + + + + + has_exact_synonym + + + + + + + + has_obo_format_version + + + + + + + + has_obo_namespace + + + + + + + + has_related_synonym + + + + + + + + has_scope + + + + + + + + has_synonym_type + + + + + + + + + + + + + + in_subset + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + 'Entity A' contains 'Entity B' implies that 'Entity B' is a part of the structure of 'Entity A'. + PSI-MOD + contains + The inverse relationship to "part of". + contains + + + + + 'Entity A' contains 'Entity B' implies that 'Entity B' is a part of the structure of 'Entity A'. + PubMed:18688235 + + + + + + + + + 'Entity A' derives_from 'Entity B' implies that 'Entity A' is chemically derived from 'Entity B'. + PSI-MOD + derives_from + derives from + + + + + 'Entity A' derives_from 'Entity B' implies that 'Entity A' is chemically derived from 'Entity B'. + PubMed:18688235 + + + + + + + + + 'Entity A' has_functional_parent 'Entity B' implies that 'Entity B' has at least one chacteristic group from which 'Entity A' can be derived by functional modification. + PSI-MOD + has_functional_parent + This relationship indicates that the formula and mass of the child are not inherited from the mass of the parent. + has functional parent + + + + + 'Entity A' has_functional_parent 'Entity B' implies that 'Entity B' has at least one chacteristic group from which 'Entity A' can be derived by functional modification. + PubMed:18688235 + + + + + + + + + 'Entity A' part_of 'Entity B' implies that 'Entity A' is a part of the structure of 'Entity B'. + PSI-MOD + part_of + part of + + + + + 'Entity A' part_of 'Entity B' implies that 'Entity A' is a part of the structure of 'Entity B'. + PubMed:18688235 + + + + + + + + + + + + + Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue. + ModRes + PSI-MOD + MOD:00000 + + protein modification + + + + + Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue. + PubMed:18688235 + + + + + ModRes + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an alkyl group. + AlkylRes + PSI-MOD + MOD:00001 + + alkylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an alkyl group. + PubMed:18688235 + + + + + AlkylRes + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O3-glycosylserine. + S + natural + OGlycoSer + PSI-MOD + MOD:00002 + + O-glycosyl-L-serine + + + + + OGlycoSer + + + + + + A protein modification that effectively converts an L-serine residue to O3-glycosylserine. + PubMed:18688235 + + + + + + + + + Entry from Unimod. + PSI-MOD + MOD:00003 + This term is for organizational use only and should not be assigned. [JSG] + Unimod + + + + + Entry from Unimod. + PubMed:18688235 + + + + + + + + Artifact entry from Unimod - OBSOLETE because organizational use is no longer required. + PSI-MOD + MOD:00004 + artifact + true + + + + + Artifact entry from Unimod - OBSOLETE because organizational use is no longer required. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O3-glycosylthreonine. + T + natural + OGlycoThr + PSI-MOD + MOD:00005 + + O-glycosyl-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O3-glycosylthreonine. + PubMed:18688235 + + + + + OGlycoThr + + + + + + + + + + A protein modification that effectively replaces a residue hydrogen atom on a nitrogen with a carbohydrate-like group through a glycosidic bond. + NGlycoRes + PSI-MOD + MOD:00006 + + N-glycosylated residue + + + + + A protein modification that effectively replaces a residue hydrogen atom on a nitrogen with a carbohydrate-like group through a glycosidic bond. + PubMed:18688235 + + + + + NGlycoRes + + + + + + + + + + A protein modification that effectively substitutes a selenium atom for a sulfur atom. + 46.91 + C 0 H 0 N 0 O 0 S -1 Se 1 + 47.94445 + X + natural + Unimod:162 + Se(S)Res + PSI-MOD + Delta:S(-1)Se(1) + Selenium replaces sulphur + MOD:00007 + selenium substitution for sulfur + + + + + A protein modification that effectively substitutes a selenium atom for a sulfur atom. + PubMed:12148805 + Unimod:162 + + + + + Se(S)Res + + + + + + Delta:S(-1)Se(1) + + + + + + Selenium replaces sulphur + + + + + + + + + Entry from Unimod representing one or more entries in RESID. OBSOLETE because organizational use is no longer required. + PSI-MOD + MOD:00008 + common + true + + + + + Entry from Unimod representing one or more entries in RESID. OBSOLETE because organizational use is no longer required. + PubMed:18688235 + + + + + + + + + A protein modification that removes a residue, or inserts or replaces a residue with a natural, standard or nonstandard, encoded residue. + X + natural + Res + alpha-amino acid + PSI-MOD + MOD:00009 + + natural residue + + + + + A protein modification that removes a residue, or inserts or replaces a residue with a natural, standard or nonstandard, encoded residue. + PubMed:6692818 + RESID:AA0000 + + + + + Res + + + + + + alpha-amino acid + + + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to an L-alanine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 3 H 5 N 1 O 1 + 71.08 + 71.03712 + A + natural + (2S)-2-aminopropanoic acid + 2-aminopropionic acid + 2-azanylpropanoic acid + Ala + L-alanine + alpha-alanine + alpha-aminopropionic acid + PSI-MOD + MOD:00010 + + L-alanine residue + + + + + A protein modification that effectively converts a source amino acid residue to an L-alanine. + ChEBI:29948 + DeltaMass:0 + PubMed:6692818 + RESID:AA0001 + + + + + (2S)-2-aminopropanoic acid + + + + + + 2-aminopropionic acid + + + + + + 2-azanylpropanoic acid + + + + + + Ala + + + + + + L-alanine + + + + + + alpha-alanine + + + + + + alpha-aminopropionic acid + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to an L-arginine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 6 H 12 N 4 O 1 + 156.19 + 156.1011 + R + natural + (2S)-2-amino-5-[(diaminomethylidene)amino]pentanoic acid + 2-amino-5-(carbamimidamido)pentanoic acid [tautomer] + 2-amino-5-[(aminoiminomethyl)amino]pentanoic acid [tautomer] + 2-amino-5-guanidinopentanoic acid + 2-amino-5-guanidinovaleric acid + 2-azanyl-5-[bis(azanyl)methylideneazanyl]pentanoic acid + Arg + L-arginine + alpha-amino-delta-guanidinovaleric acid + PSI-MOD + MOD:00011 + + L-arginine residue + + + + + A protein modification that effectively converts a source amino acid residue to an L-arginine. + ChEBI:29952 + DeltaMass:0 + PubMed:518876 + PubMed:6692818 + RESID:AA0002 + + + + + (2S)-2-amino-5-[(diaminomethylidene)amino]pentanoic acid + + + + + + 2-amino-5-(carbamimidamido)pentanoic acid [tautomer] + + + + + + 2-amino-5-[(aminoiminomethyl)amino]pentanoic acid [tautomer] + + + + + + 2-amino-5-guanidinopentanoic acid + + + + + + 2-amino-5-guanidinovaleric acid + + + + + + 2-azanyl-5-[bis(azanyl)methylideneazanyl]pentanoic acid + + + + + + Arg + + + + + + L-arginine + + + + + + alpha-amino-delta-guanidinovaleric acid + + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to an L-asparagine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 4 H 6 N 2 O 2 + 114.1 + 114.04293 + N + natural + (2S)-2-amino-4-butanediamic acid + 2,4-bis(azanyl)-4-oxobutanoic acid + 2,4-diamino-4-oxobutanoic acid + 2-amino-3-carbamoylpropanoic acid + 2-amino-4-butanediamic acid + 2-aminosuccinamic acid + 2-aminosuccinic acid 4-amide + Asn + L-asparagine + alpha-amino-beta-carbamylpropionic acid + alpha-aminosuccinamic acid + aspartic acid 4-amide + aspartic acid beta-amide + beta-asparagine + PSI-MOD + MOD:00012 + + L-asparagine residue + + + + + A protein modification that effectively converts a source amino acid residue to an L-asparagine. + ChEBI:29956 + DeltaMass:0 + PubMed:15736973 + PubMed:5681232 + PubMed:6692818 + PubMed:9789001 + RESID:AA0003 + + + + + (2S)-2-amino-4-butanediamic acid + + + + + + 2,4-bis(azanyl)-4-oxobutanoic acid + + + + + + 2,4-diamino-4-oxobutanoic acid + + + + + + 2-amino-3-carbamoylpropanoic acid + + + + + + 2-amino-4-butanediamic acid + + + + + + 2-aminosuccinamic acid + + + + + + 2-aminosuccinic acid 4-amide + + + + + + Asn + + + + + + L-asparagine + + + + + + alpha-amino-beta-carbamylpropionic acid + + + + + + alpha-aminosuccinamic acid + + + + + + aspartic acid 4-amide + + + + + + aspartic acid beta-amide + + + + + + beta-asparagine + + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to an L-aspartic acid. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 4 H 5 N 1 O 3 + 115.09 + 115.02694 + D + natural + (2S)-2-aminobutanedioic acid + 2-azanylbutanedioic acid + Asp + L-aspartic acid + aminosuccinic acid + PSI-MOD + MOD:00013 + + L-aspartic acid residue + + + + + A protein modification that effectively converts a source amino acid residue to an L-aspartic acid. + ChEBI:29958 + DeltaMass:0 + PubMed:1097438 + PubMed:339692 + PubMed:4399050 + PubMed:5764436 + PubMed:6692818 + PubMed:8089117 + PubMed:9521123 + PubMed:9582379 + RESID:AA0004 + + + + + (2S)-2-aminobutanedioic acid + + + + + + 2-azanylbutanedioic acid + + + + + + Asp + + + + + + L-aspartic acid + + + + + + aminosuccinic acid + + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to an L-cysteine. + 0.0 + C 0 H 0 N 0 O 0 S 0 + 0.0 + C 3 H 5 N 1 O 1 S 1 + 103.14 + 103.009186 + C + natural + (2R)-2-amino-3-sulfanylpropanoic acid + (R)-cysteine + 2-amino-3-mercaptopropanoic acid + 2-amino-3-mercaptopropionic acid + 2-azanyl-3-sulfanylpropanoic acid + 3-mercapto-L-alanine + Cys + Cysteine (C, Cys) + L-(+)-cysteine + L-cysteine + alpha-amino-beta-mercaptopropanoic acid + alpha-amino-beta-mercaptopropionic acid + alpha-amino-beta-thiolpropionic acid + beta-mercaptoalanine + half-cystine + thioserine + PSI-MOD + MOD:00014 + + From DeltaMass: Average Mass: 121. + L-cysteine residue + + + + + A protein modification that effectively converts a source amino acid residue to an L-cysteine. + ChEBI:29950 + DeltaMass:0 + PubMed:1310545 + PubMed:15790858 + PubMed:3447159 + PubMed:6692818 + PubMed:7338899 + RESID:AA0005 + + + + + (2R)-2-amino-3-sulfanylpropanoic acid + + + + + + (R)-cysteine + + + + + + 2-amino-3-mercaptopropanoic acid + + + + + + 2-amino-3-mercaptopropionic acid + + + + + + 2-azanyl-3-sulfanylpropanoic acid + + + + + + 3-mercapto-L-alanine + + + + + + Cys + + + + + + Cysteine (C, Cys) + + + + + + L-(+)-cysteine + + + + + + L-cysteine + + + + + + alpha-amino-beta-mercaptopropanoic acid + + + + + + alpha-amino-beta-mercaptopropionic acid + + + + + + alpha-amino-beta-thiolpropionic acid + + + + + + beta-mercaptoalanine + + + + + + half-cystine + + + + + + thioserine + + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to an L-glutamic acid. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 5 H 7 N 1 O 3 + 129.12 + 129.04259 + E + natural + (2S)-2-aminopentanedioic acid + 1-aminopropane-1,3-dicarboxylic acid + 2-aminoglutaric acid + 2-azanylpentanedioic acid + Glu + L-glutamic acid + alpha-aminoglutaric acid + glutaminic acid + PSI-MOD + MOD:00015 + + L-glutamic acid residue + + + + + A protein modification that effectively converts a source amino acid residue to an L-glutamic acid. + ChEBI:29972 + DeltaMass:0 + PubMed:1881881 + PubMed:4565668 + PubMed:4922541 + PubMed:6692818 + PubMed:9326660 + PubMed:957425 + RESID:AA0006 + + + + + (2S)-2-aminopentanedioic acid + + + + + + 1-aminopropane-1,3-dicarboxylic acid + + + + + + 2-aminoglutaric acid + + + + + + 2-azanylpentanedioic acid + + + + + + Glu + + + + + + L-glutamic acid + + + + + + alpha-aminoglutaric acid + + + + + + glutaminic acid + + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to an L-glutamine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 5 H 8 N 2 O 2 + 128.13 + 128.05858 + Q + natural + (2S)-2-amino-5-pentanediamic acid + 2,5-bis(azanyl)-5-oxopentanoic acid + 2,5-diamino-5-oxopentanoic acid + 2-amino-4-carbamoylbutanoic acid + 2-aminoglutaramic acid + Gln + L-glutamine + alpha-amino-gamma-carbamylbutyric acid + glutamic acid 5-amide + glutamic acid gamma-amide + glutamide + PSI-MOD + MOD:00016 + + L-glutamine residue + + + + + glutamic acid gamma-amide + + + + + + glutamide + + + + + + A protein modification that effectively converts a source amino acid residue to an L-glutamine. + ChEBI:30011 + DeltaMass:0 + PubMed:3340166 + PubMed:6692818 + PubMed:9342308 + RESID:AA0007 + + + + + (2S)-2-amino-5-pentanediamic acid + + + + + + 2,5-bis(azanyl)-5-oxopentanoic acid + + + + + + 2,5-diamino-5-oxopentanoic acid + + + + + + 2-amino-4-carbamoylbutanoic acid + + + + + + 2-aminoglutaramic acid + + + + + + Gln + + + + + + L-glutamine + + + + + + alpha-amino-gamma-carbamylbutyric acid + + + + + + glutamic acid 5-amide + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to a glycine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 2 H 3 N 1 O 1 + 57.05 + 57.021465 + G + natural + Gly + aminoacetic acid + aminoethanoic acid + azanylethanoic acid + glycine + glycocoll + PSI-MOD + MOD:00017 + + glycine residue + + + + + A protein modification that effectively converts a source amino acid residue to a glycine. + ChEBI:29947 + DeltaMass:0 + PubMed:1310545 + PubMed:6692818 + RESID:AA0008 + + + + + Gly + + + + + + aminoacetic acid + + + + + + aminoethanoic acid + + + + + + azanylethanoic acid + + + + + + glycine + + + + + + glycocoll + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to an L-histidine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 6 H 7 N 3 O 1 + 137.14 + 137.05891 + H + natural + (2S)-2-amino-3-(1H-imidazol-4-yl)propanoic acid + (2S)-2-amino-3-(1H-imidazol-5-yl)propanoic acid [tautomer] + 2-azanyl-3-(1H-imidazol-4-yl)propanoic acid + 2-azanyl-3-(1H-imidazol-5-yl)propanoic acid [tautomer] + 4-(2-amino-2-carboxyethyl)imidazole + His + L-histidine + alpha-amino-beta-(4-imidazole)propionic acid + glyoxaline-5-alanine + PSI-MOD + MOD:00018 + + L-histidine residue + + + + + A protein modification that effectively converts a source amino acid residue to an L-histidine. + ChEBI:29979 + DeltaMass:0 + PubMed:14342316 + PubMed:2722967 + PubMed:512 + PubMed:5460889 + PubMed:6129252 + PubMed:6692818 + PubMed:6876174 + RESID:AA0009 + + + + + (2S)-2-amino-3-(1H-imidazol-4-yl)propanoic acid + + + + + + (2S)-2-amino-3-(1H-imidazol-5-yl)propanoic acid [tautomer] + + + + + + 2-azanyl-3-(1H-imidazol-4-yl)propanoic acid + + + + + + 2-azanyl-3-(1H-imidazol-5-yl)propanoic acid [tautomer] + + + + + + 4-(2-amino-2-carboxyethyl)imidazole + + + + + + His + + + + + + L-histidine + + + + + + alpha-amino-beta-(4-imidazole)propionic acid + + + + + + glyoxaline-5-alanine + + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to an L-isoleucine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 6 H 11 N 1 O 1 + 113.16 + 113.08406 + I + natural + (2S,3S)-2-amino-3-methylpentanoic acid + 2-azanyl-3-methylpentanoic acid + 3-methyl-norvaline + Ile + Isoleucyl + L-erythro-isoleucine + L-isoleucine + alpha-amino-beta-methylvaleric acid + PSI-MOD + MOD:00019 + + L-isoleucine residue + + + + + A protein modification that effectively converts a source amino acid residue to an L-isoleucine. + ChEBI:30009 + DeltaMass:0 + PubMed:6692818 + RESID:AA0010 + + + + + (2S,3S)-2-amino-3-methylpentanoic acid + + + + + + 2-azanyl-3-methylpentanoic acid + + + + + + 3-methyl-norvaline + + + + + + Ile + + + + + + Isoleucyl + + + + + + L-erythro-isoleucine + + + + + + L-isoleucine + + + + + + alpha-amino-beta-methylvaleric acid + + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to an L-leucine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 6 H 11 N 1 O 1 + 113.16 + 113.08406 + L + natural + (2S)-2-amino-4-methylpentanoic acid + 2-azanyl-4-methylpentanoic acid + 4-methyl-norvaline + L-leucine + Leu + alpha-amino-gamma-methylvaleric acid + alpha-aminoisocaproic acid + PSI-MOD + MOD:00020 + + L-leucine residue + + + + + A protein modification that effectively converts a source amino acid residue to an L-leucine. + ChEBI:30006 + DeltaMass:0 + PubMed:11478885 + PubMed:6692818 + RESID:AA0011 + + + + + (2S)-2-amino-4-methylpentanoic acid + + + + + + 2-azanyl-4-methylpentanoic acid + + + + + + 4-methyl-norvaline + + + + + + L-leucine + + + + + + Leu + + + + + + alpha-amino-gamma-methylvaleric acid + + + + + + alpha-aminoisocaproic acid + + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to L-lysine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 6 H 12 N 2 O 1 + 128.18 + 128.09496 + K + natural + (2S)-2,6-diaminohexanoic acid + 2,6-bis(azanyl)hexanoic acid + 6-amino-L-norleucine + ACT_SITE Schiff-base intermediate with substrate + L-lysine + Lys + alpha,epsilon-diaminocaproic acid + PSI-MOD + MOD:00021 + + L-lysine residue + + + + + A protein modification that effectively converts a source amino acid residue to L-lysine. + ChEBI:29967 + DeltaMass:0 + PubMed:3106962 + PubMed:6120171 + PubMed:6692818 + RESID:AA0012 + + + + + (2S)-2,6-diaminohexanoic acid + + + + + + 2,6-bis(azanyl)hexanoic acid + + + + + + 6-amino-L-norleucine + + + + + + ACT_SITE Schiff-base intermediate with substrate + + + + + + L-lysine + + + + + + Lys + + + + + + alpha,epsilon-diaminocaproic acid + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to L-methionine. + 0.0 + C 0 H 0 N 0 O 0 S 0 + 0.0 + C 5 H 9 N 1 O 1 S 1 + 131.19 + 131.04048 + M + natural + (2S)-2-amino-4-(methylsulfanyl)butanoic acid + 2-amino-4-(methylthio)butanoic acid + 2-amino-4-(methylthio)butyric acid + 2-azanyl-4-(methylsulfanyl)butanoic acid + L-(-)-methionine + L-methionine + Met + S-methyl-L-homocysteine + alpha-amino-gamma-methylmercaptobutyric acid + alpha-amino-gamma-methylthiobutyric acid + gamma-methylthio-alpha-aminobutyric acid + PSI-MOD + MOD:00022 + + From DeltaMass: Average Mass: 149 + L-methionine residue + + + + + A protein modification that effectively converts a source amino acid residue to L-methionine. + ChEBI:29983 + DeltaMass:0 + PubMed:6411710 + PubMed:6692818 + RESID:AA0013 + + + + + (2S)-2-amino-4-(methylsulfanyl)butanoic acid + + + + + + 2-amino-4-(methylthio)butanoic acid + + + + + + 2-amino-4-(methylthio)butyric acid + + + + + + 2-azanyl-4-(methylsulfanyl)butanoic acid + + + + + + L-(-)-methionine + + + + + + L-methionine + + + + + + Met + + + + + + S-methyl-L-homocysteine + + + + + + alpha-amino-gamma-methylmercaptobutyric acid + + + + + + alpha-amino-gamma-methylthiobutyric acid + + + + + + gamma-methylthio-alpha-aminobutyric acid + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to L-phenylalanine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 9 H 9 N 1 O 1 + 147.18 + 147.06842 + F + natural + (2S)-2-amino-3-phenylpropanoic acid + 2-azanyl-3-phenylpropanoic acid + L-phenylalanine + Phe + alpha-amino-beta-phenylpropionic acid + PSI-MOD + MOD:00023 + + L-phenylalanine residue + + + + + A protein modification that effectively converts a source amino acid residue to L-phenylalanine. + ChEBI:29997 + DeltaMass:0 + PubMed:6692818 + RESID:AA0014 + + + + + (2S)-2-amino-3-phenylpropanoic acid + + + + + + 2-azanyl-3-phenylpropanoic acid + + + + + + L-phenylalanine + + + + + + Phe + + + + + + alpha-amino-beta-phenylpropionic acid + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to L-proline. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 5 H 7 N 1 O 1 + 97.12 + 97.052765 + P + natural + (2S)-2-pyrrolidinecarboxylic acid + L-proline + Pro + pyrrolidine-2-carboxylic acid + PSI-MOD + MOD:00024 + + L-proline residue + + + + + A protein modification that effectively converts a source amino acid residue to L-proline. + ChEBI:30017 + DeltaMass:0 + PubMed:6692818 + PubMed:8547259 + RESID:AA0015 + + + + + (2S)-2-pyrrolidinecarboxylic acid + + + + + + L-proline + + + + + + Pro + + + + + + pyrrolidine-2-carboxylic acid + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to L-serine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 3 H 5 N 1 O 2 + 87.08 + 87.03203 + S + natural + (2S)-2-amino-3-hydroxypropanoic acid + 2-azanyl-3-hydroxypropanoic acid + 3-hydroxy-L-alanine + L-serine + Ser + alpha-amino-beta-hydroxypropionic acid + beta-hydroxyalanine + PSI-MOD + MOD:00025 + + L-serine residue + + + + + A protein modification that effectively converts a source amino acid residue to L-serine. + ChEBI:29999 + DeltaMass:0 + PubMed:4399050 + PubMed:6692818 + RESID:AA0016 + + + + + (2S)-2-amino-3-hydroxypropanoic acid + + + + + + 2-azanyl-3-hydroxypropanoic acid + + + + + + 3-hydroxy-L-alanine + + + + + + L-serine + + + + + + Ser + + + + + + alpha-amino-beta-hydroxypropionic acid + + + + + + beta-hydroxyalanine + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to L-threonine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 4 H 7 N 1 O 2 + 101.1 + 101.047676 + T + natural + (2S,3R)-2-amino-3-hydroxybutanoic acid + 2-azanyl-3-hydroxybutanoic acid + L-threo-threonine + L-threonine + Thr + alpha-amino-beta-hydroxybutyric acid + beta-methylserine + PSI-MOD + MOD:00026 + + L-threonine residue + + + + + A protein modification that effectively converts a source amino acid residue to L-threonine. + ChEBI:30013 + DeltaMass:0 + PubMed:2989287 + PubMed:6692818 + RESID:AA0017 + + + + + (2S,3R)-2-amino-3-hydroxybutanoic acid + + + + + + 2-azanyl-3-hydroxybutanoic acid + + + + + + L-threo-threonine + + + + + + L-threonine + + + + + + Thr + + + + + + alpha-amino-beta-hydroxybutyric acid + + + + + + beta-methylserine + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to L-tryptophan. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 11 H 10 N 2 O 1 + 186.21 + 186.07932 + W + natural + (2S)-2-amino-3-(1H-indol-3-yl)propanoic acid + 2-azanyl-3-(1H-indol-3-yl)propanoic acid + L-tryptophan + Trp + alpha-amino-beta-(3-indolyl)propionoic acid + beta(3-indolyl)alanine + PSI-MOD + MOD:00027 + + L-tryptophan residue + + + + + A protein modification that effectively converts a source amino acid residue to L-tryptophan. + ChEBI:29954 + DeltaMass:0 + PubMed:2059637 + PubMed:6692818 + PubMed:9324768 + RESID:AA0018 + + + + + (2S)-2-amino-3-(1H-indol-3-yl)propanoic acid + + + + + + 2-azanyl-3-(1H-indol-3-yl)propanoic acid + + + + + + L-tryptophan + + + + + + Trp + + + + + + alpha-amino-beta-(3-indolyl)propionoic acid + + + + + + beta(3-indolyl)alanine + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to L-tyrosine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 9 H 9 N 1 O 2 + 163.18 + 163.06332 + Y + natural + (2S)-2-amino-3-(4-hydoxyphenyl)propanoic acid + 2-azanyl-3-(4-hydoxyphenyl)propanoic acid + L-tyrosine + Tyr + alpha-amino-beta-(para-hydroxyphenyl)propionic acid + p-tyrosine + para-hydroxyphenylalanine + PSI-MOD + MOD:00028 + + L-tyrosine residue + + + + + A protein modification that effectively converts a source amino acid residue to L-tyrosine. + ChEBI:29975 + DeltaMass:0 + PubMed:2190093 + PubMed:2542938 + PubMed:5550972 + PubMed:6061414 + PubMed:6120171 + PubMed:6692818 + RESID:AA0019 + + + + + (2S)-2-amino-3-(4-hydoxyphenyl)propanoic acid + + + + + + 2-azanyl-3-(4-hydoxyphenyl)propanoic acid + + + + + + L-tyrosine + + + + + + Tyr + + + + + + alpha-amino-beta-(para-hydroxyphenyl)propionic acid + + + + + + p-tyrosine + + + + + + para-hydroxyphenylalanine + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to an L-valine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 5 H 9 N 1 O 1 + 99.13 + 99.06841 + V + natural + (2S)-2-amino-3-methylbutanoic acid + 2-azanyl-3-methylbutanoic acid + L-valine + Val + alpha-amino-beta-methylbutyric acid + alpha-aminoisovaleric acid + PSI-MOD + MOD:00029 + + L-valine residue + + + + + A protein modification that effectively converts a source amino acid residue to an L-valine. + ChEBI:30015 + DeltaMass:0 + PubMed:6692818 + RESID:AA0020 + + + + + (2S)-2-amino-3-methylbutanoic acid + + + + + + 2-azanyl-3-methylbutanoic acid + + + + + + L-valine + + + + + + Val + + + + + + alpha-amino-beta-methylbutyric acid + + + + + + alpha-aminoisovaleric acid + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to an N-formyl-L-methionine, a natural pretranslational modification. + 0.0 + C 0 H 0 N 0 O 0 S 0 + 0.0 + C 6 H 10 N 1 O 2 S 1 + 160.21 + 160.04323 + M + natural + N-term + (2S)-2-formylamino-4-(methylsulfanyl)butanoic acid + 2-formamido-4-(methylsulfanyl)butanoic acid + 2-formylamino-4-(methylthio)butanoic acid + 2-formylazanyl-4-(methylsulfanyl)butanoic acid + MOD_RES N-formylmethionine + N-formyl-L-methionine + N-formylated L-methionine + fMet + nformylmet + PSI-MOD + FormylMet + MOD:00030 + + N-formyl-L-methionine residue + + + + + A protein modification that effectively converts a source amino acid residue to an N-formyl-L-methionine, a natural pretranslational modification. + ChEBI:33718 + OMSSA:22 + PubMed:10825024 + PubMed:11152118 + PubMed:2165784 + PubMed:3042771 + PubMed:8758896 + RESID:AA0021#FMET + + + + + (2S)-2-formylamino-4-(methylsulfanyl)butanoic acid + + + + + + 2-formamido-4-(methylsulfanyl)butanoic acid + + + + + + 2-formylamino-4-(methylthio)butanoic acid + + + + + + 2-formylazanyl-4-(methylsulfanyl)butanoic acid + + + + + + MOD_RES N-formylmethionine + + + + + + N-formyl-L-methionine + + + + + + N-formylated L-methionine + + + + + + fMet + + + + + + nformylmet + + + + + + FormylMet + + + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to an L-selenocysteine, a natural pretranslational modification. + 0.0 + C 0 H 0 N 0 O 0 Se 0 + 0.0 + C 3 H 5 N 1 O 1 Se 1 + 150.05 + 150.95363 + U + natural + (2R)-2-amino-3-selanylpropanoic acid + 2-azanyl-3-selanylpropanoic acid + 3-selenylalanine + L-selenocysteine + NON_STD Selenocysteine + SeCys + Sec + selenium cysteine + PSI-MOD + MOD:00031 + + L-selenocysteine residue + + + + + A protein modification that effectively converts a source amino acid residue to an L-selenocysteine, a natural pretranslational modification. + ChEBI:30000 + PubMed:10523135 + PubMed:1066676 + PubMed:2037562 + PubMed:2963330 + PubMed:4734725 + PubMed:6076213 + PubMed:6217842 + PubMed:6714945 + RESID:AA0022 + + + + + (2R)-2-amino-3-selanylpropanoic acid + + + + + + 2-azanyl-3-selanylpropanoic acid + + + + + + 3-selenylalanine + + + + + + L-selenocysteine + + + + + + NON_STD Selenocysteine + + + + + + SeCys + + + + + + Sec + + + + + + selenium cysteine + + + + + + + + + + A protein modification that is not chemically categorized. + PSI-MOD + MOD:00032 + This term is for organizational use only and should not be assigned. [JSG] + uncategorized protein modification + + + + + A protein modification that is not chemically categorized. + PubMed:18688235 + + + + + + + + + A protein modification that crosslinks two or more amino acid residues with covalent bonds. + XLNK-Res-Res + PSI-MOD + MOD:00033 + + The covalent bond is formed directly between sidechain atoms. If non-aminoacid atoms are involved in connecting two or more peptide chain residues peptide chain, the connection is classified as a multivalent binding site. + crosslinked residues + + + + + A protein modification that crosslinks two or more amino acid residues with covalent bonds. + PubMed:18688235 + + + + + XLNK-Res-Res + + + + + + + + + + A protein modification that effectively cross-links two L-cysteine residues to form L-cystine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 6 H 8 N 2 O 2 S 2 + 204.26 + 204.00272 + C, C + natural + (2R,2'R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid) + 3,3'-disulfane-1,2-diylbis(2-azanylpropanoic acid) + 3,3'-dithiobis(2-aminopropanoic acid) + 3,3'-dithiobisalanine + 3,3'-dithiodialanine + Cys2 + Cystine ((Cys)2) + DISULFID + DISULFID Interchain + L-cystine + XLNK-SCys-SCys + beta,beta'-diamino-beta,beta'-dicarboxydiethyldisulfide + beta,beta'-dithiodialanine + bis(alpha-aminopropionic acid)-beta-disulfide + bis(beta-amino-beta-carboxyethyl)disulfide + dicysteine + PSI-MOD + 2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid + MOD:00034 + + Cross-link 2; for formation of a disulfide bond between a peptide cysteine and a free cysteine, see MOD:00765. + L-cystine (cross-link) + + + + + A protein modification that effectively cross-links two L-cysteine residues to form L-cystine. + ChEBI:16283 + DeltaMass:0 + PubMed:1988019 + PubMed:2001356 + PubMed:2076469 + PubMed:3083866 + PubMed:366603 + PubMed:7918467 + PubMed:8344916 + RESID:AA0025#CYS2 + + + + + (2R,2'R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid) + + + + + + 3,3'-disulfane-1,2-diylbis(2-azanylpropanoic acid) + + + + + + 3,3'-dithiobis(2-aminopropanoic acid) + + + + + + 3,3'-dithiobisalanine + + + + + + 3,3'-dithiodialanine + + + + + + Cys2 + + + + + + Cystine ((Cys)2) + + + + + + DISULFID + + + + + + DISULFID Interchain + + + + + + L-cystine + + + + + + XLNK-SCys-SCys + + + + + + beta,beta'-diamino-beta,beta'-dicarboxydiethyldisulfide + + + + + + beta,beta'-dithiodialanine + + + + + + bis(alpha-aminopropionic acid)-beta-disulfide + + + + + + bis(beta-amino-beta-carboxyethyl)disulfide + + + + + + dicysteine + + + + + + 2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to (2S,3R)-3-hydroxyasparagine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 4 H 6 N 2 O 3 + 130.1 + 130.03784 + N + natural + uniprot.ptm:PTM-0369 + (2S,3R)-2,4-diamino-3-hydroxy-4-oxobutanoic acid + (2S,3R)-2-amino-3-hydroxy-4-butanediamic acid + (2S,3R)-3-hydroxyasparagine + (3R)3HyAsn + 2-azanyl-3-hydroxy-4-butanediamic acid + L-erythro-beta-hydroxyasparagine + MOD_RES (3R)-3-hydroxyasparagine + erythro-beta-hydroxylated L-asparagine + PSI-MOD + MOD:00035 + + (2S,3R)-3-hydroxyasparagine + + + + + A protein modification that effectively converts an L-asparagine residue to (2S,3R)-3-hydroxyasparagine. + ChEBI:141853 + PubMed:11823643 + PubMed:2820791 + RESID:AA0026 + + + + + (2S,3R)-2,4-diamino-3-hydroxy-4-oxobutanoic acid + + + + + + (2S,3R)-2-amino-3-hydroxy-4-butanediamic acid + + + + + + (2S,3R)-3-hydroxyasparagine + + + + + + (3R)3HyAsn + + + + + + 2-azanyl-3-hydroxy-4-butanediamic acid + + + + + + L-erythro-beta-hydroxyasparagine + + + + + + MOD_RES (3R)-3-hydroxyasparagine + + + + + + erythro-beta-hydroxylated L-asparagine + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to (2S,3R)-3-hydroxyaspartic acid. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 4 H 5 N 1 O 4 + 131.09 + 131.02185 + D + natural + Unimod:35 + uniprot.ptm:PTM-0371 + (2S,3R)-2-amino-3-hydroxybutanedioic acid + (2S,3R)-3-hydroxyaspartic acid + (3R)3HyAsp + 2-amino-3-hydroxysuccinic acid + 2-azanyl-3-hydroxybutanedioic acid + 3-hydroxyaspartic acid + L-erythro-beta-hydroxyaspartic acid + MOD_RES (3R)-3-hydroxyaspartate + erythro-beta-hydroxylated L-aspartic acid + hydroxylationd + PSI-MOD + Oxidation + MOD:00036 + + (2S,3R)-3-hydroxyaspartic acid + + + + + A protein modification that effectively converts an L-aspartic acid residue to (2S,3R)-3-hydroxyaspartic acid. + ChEBI:141848 + OMSSA:59 + PubMed:6572939 + PubMed:6871167 + PubMed:8355279 + RESID:AA0027 + Unimod:35#D + + + + + (2S,3R)-2-amino-3-hydroxybutanedioic acid + + + + + + (2S,3R)-3-hydroxyaspartic acid + + + + + + (3R)3HyAsp + + + + + + 2-amino-3-hydroxysuccinic acid + + + + + + 2-azanyl-3-hydroxybutanedioic acid + + + + + + 3-hydroxyaspartic acid + + + + + + L-erythro-beta-hydroxyaspartic acid + + + + + + MOD_RES (3R)-3-hydroxyaspartate + + + + + + erythro-beta-hydroxylated L-aspartic acid + + + + + + hydroxylationd + + + + + + Oxidation + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to one of the diastereomeric 5-hydroxy-L-lysine residues. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 6 H 12 N 2 O 2 + 144.17 + 144.08987 + K + natural + uniprot.ptm:PTM-0044 + 5-hydroxylated L-lysine + 5HyLys + PSI-MOD + MOD:00037 + + 5-hydroxy-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to one of the diastereomeric 5-hydroxy-L-lysine residues. + ChEBI:60175 + PubMed:18688235 + + + + + 5-hydroxylated L-lysine + + + + + + 5HyLys + + + + + + + + + + A protein modification that effectively converts an L-proline residue to 3-hydroxy-L-proline. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 5 H 7 N 1 O 2 + 113.12 + 113.047676 + P + natural + uniprot.ptm:PTM-0030 + (2S,3S)-3-hydroxypyrrolidine-2-carboxylic acid + 3-hydroxy-L-proline + 3-hydroxylated L-proline + 3-trans-hydroxy-L-proline + 3HyPro + L-threo-3-hydroxyproline + MOD_RES 3-hydroxyproline + beta-hydroxypyrrolidine-alpha-carboxylic acid + PSI-MOD + MOD:00038 + + 3-hydroxy-L-proline + + + + + A protein modification that effectively converts an L-proline residue to 3-hydroxy-L-proline. + ChEBI:16889 + PubMed:2400108 + PubMed:3734192 + PubMed:4343807 + RESID:AA0029 + + + + + (2S,3S)-3-hydroxypyrrolidine-2-carboxylic acid + + + + + + 3-hydroxy-L-proline + + + + + + 3-hydroxylated L-proline + + + + + + 3-trans-hydroxy-L-proline + + + + + + 3HyPro + + + + + + L-threo-3-hydroxyproline + + + + + + MOD_RES 3-hydroxyproline + + + + + + beta-hydroxypyrrolidine-alpha-carboxylic acid + + + + + + + + + + A protein modification that effectively converts an L-proline residue to 4-hydroxy-L-proline + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 5 H 7 N 1 O 2 + 113.12 + 113.047676 + P + natural + uniprot.ptm:PTM-0043 + (2S,4R)-4-hydroxypyrrolidine-2-carboxylic acid + 4-hydroxy-L-proline + 4-hydroxylated L-proline + 4-hydroxyproline + 4-trans-hydroxy-L-proline + 4HyPro + L-threo-4-hydroxyproline + MOD_RES 4-hydroxyproline + gamma-hydroxypyrrolidine-alpha-carboxylic acid + PSI-MOD + MOD:00039 + + 4-hydroxy-L-proline + + + + + A protein modification that effectively converts an L-proline residue to 4-hydroxy-L-proline + ChEBI:18095 + PubMed:11292863 + PubMed:2400108 + PubMed:3734192 + RESID:AA0030 + + + + + (2S,4R)-4-hydroxypyrrolidine-2-carboxylic acid + + + + + + 4-hydroxy-L-proline + + + + + + 4-hydroxylated L-proline + + + + + + 4-hydroxyproline + + + + + + 4-trans-hydroxy-L-proline + + + + + + 4HyPro + + + + + + L-threo-4-hydroxyproline + + + + + + MOD_RES 4-hydroxyproline + + + + + + gamma-hydroxypyrrolidine-alpha-carboxylic acid + + + + + + + + + + + + A protein modification that effectively converts an L-glutamine residue to 2-pyrrolidone-5-carboxylic acid. + -17.03 + C 0 H -3 N -1 O 0 + -17.026548 + C 5 H 6 N 1 O 2 + 112.11 + 112.039856 + Q + natural + N-term + Unimod:28 + uniprot.ptm:PTM-0261 + (2S)-5-oxo-2-pyrrolidinecarboxylic acid + 2-oxopyrrolidine-5-carboxylic acid + 2-pyrrolidone-5-carboxylic acid + 5-oxoproline + 5-oxopyrrolidine-2-carboxylic acid + 5-pyrrolidone-2-carboxylic acid + MOD_RES Pyrrolidone carboxylic acid + N-pyrrolidone carboxyl (N terminus) + PCA + PyrGlu(Gln) + Pyroglutamic Acid formed from Gln + Pyroglutamyl + ntermpeppyroq + pyroglutamic acid + PSI-MOD + Gln->pyro-Glu + Pyro-glu from Q + MOD:00040 + + DeltaMass gives a formula C 5 H 5 N 1 O 2 with mass 111.1 + 2-pyrrolidone-5-carboxylic acid (Gln) + + + + + A protein modification that effectively converts an L-glutamine residue to 2-pyrrolidone-5-carboxylic acid. + ChEBI:30652 + DeltaMass:123 + OMSSA:110 + PubMed:10214721 + PubMed:1836357 + PubMed:26343 + PubMed:3473473 + RESID:AA0031#GLN + Unimod:28#Q + + + + + (2S)-5-oxo-2-pyrrolidinecarboxylic acid + + + + + + 2-oxopyrrolidine-5-carboxylic acid + + + + + + 2-pyrrolidone-5-carboxylic acid + + + + + + 5-oxoproline + + + + + + 5-oxopyrrolidine-2-carboxylic acid + + + + + + 5-pyrrolidone-2-carboxylic acid + + + + + + MOD_RES Pyrrolidone carboxylic acid + + + + + + N-pyrrolidone carboxyl (N terminus) + + + + + + PCA + + + + + + PyrGlu(Gln) + + + + + + Pyroglutamic Acid formed from Gln + + + + + + Pyroglutamyl + + + + + + ntermpeppyroq + + + + + + pyroglutamic acid + + + + + + Gln->pyro-Glu + + + + + + Pyro-glu from Q + + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-gamma-carboxyglutamic acid. + 44.01 + C 1 H 0 N 0 O 2 + 43.98983 + C 6 H 7 N 1 O 5 + 173.12 + 173.03242 + E + natural + Unimod:299 + uniprot.ptm:PTM-0039 + (3S)-3-aminopropane-1,1,3-tricarboxylic acid + (3S)-3-azanylpropane-1,1,3-tricarboxylic acid + 3-amino-1,1,3-propanetricarboxylic acid + 3-azanylpropane-1,1,3-tricarboxylic acid + 4-carboxyglutamic acid + 4CbxGlu + Carboxy Glutamyl + L-gamma-carboxyglutamic acid + MOD_RES 4-carboxyglutamate + gamma-carboxylated L-glutamic acid + gammacarboxyle + PSI-MOD + 1-carboxyglutamic acid + Carboxy + Carboxylation + MOD:00041 + + DeltaMass has an incorrect formula C 6 H 7 N 5 O 1 (N and O reversed) with mass 173. + L-gamma-carboxyglutamic acid + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-gamma-carboxyglutamic acid. + DeltaMass:217 + OMSSA:48 + PubMed:10517147 + PubMed:1807167 + PubMed:3263814 + PubMed:4528109 + PubMed:7457858 + PubMed:8135347 + PubMed:8868490 + PubMed:9188685 + RESID:AA0032 + Unimod:299#E + + + + + (3S)-3-aminopropane-1,1,3-tricarboxylic acid + + + + + + (3S)-3-azanylpropane-1,1,3-tricarboxylic acid + + + + + + 3-amino-1,1,3-propanetricarboxylic acid + + + + + + 3-azanylpropane-1,1,3-tricarboxylic acid + + + + + + 4-carboxyglutamic acid + + + + + + 4CbxGlu + + + + + + Carboxy Glutamyl + + + + + + L-gamma-carboxyglutamic acid + + + + + + MOD_RES 4-carboxyglutamate + + + + + + gamma-carboxylated L-glutamic acid + + + + + + gammacarboxyle + + + + + + 1-carboxyglutamic acid + + + + + + Carboxy + + + + + + Carboxy + + + + + + Carboxylation + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-aspartic 4-phosphoric anhydride. + 79.98 + C 0 H 1 N 0 O 3 P 1 + 79.96633 + C 4 H 6 N 1 O 6 P 1 + 195.07 + 194.99327 + D + natural + Unimod:21 + uniprot.ptm:PTM-0038 + (2S)-2-amino-4-oxo-4-(phosphonooxy)butanoic acid + 2-aminobutanedioic 4-phosphoric anhydride + 2-azanyl-4-oxo-4-(phosphonooxy)butanoic acid + 4-oxo-O-phosphono-L-homoserine + 4-phosphoaspartic acid + 4-phosphorylated L-aspartatic acid + ACT_SITE 4-aspartylphosphate intermediate + L-aspartic 4-phosphoric anhydride + MOD_RES 4-aspartylphosphate + PAsp + beta-aspartyl phosphate + PSI-MOD + Phospho + Phosphorylation + MOD:00042 + L-aspartic 4-phosphoric anhydride + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-aspartic 4-phosphoric anhydride. + ChEBI:15836 + PubMed:4357737 + RESID:AA0033 + Unimod:21#D + + + + + (2S)-2-amino-4-oxo-4-(phosphonooxy)butanoic acid + + + + + + 2-aminobutanedioic 4-phosphoric anhydride + + + + + + 2-azanyl-4-oxo-4-(phosphonooxy)butanoic acid + + + + + + 4-oxo-O-phosphono-L-homoserine + + + + + + 4-phosphoaspartic acid + + + + + + 4-phosphorylated L-aspartatic acid + + + + + + ACT_SITE 4-aspartylphosphate intermediate + + + + + + L-aspartic 4-phosphoric anhydride + + + + + + MOD_RES 4-aspartylphosphate + + + + + + PAsp + + + + + + beta-aspartyl phosphate + + + + + + Phospho + + + + + + Phosphorylation + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-phospho-L-cysteine. + 79.98 + C 0 H 1 N 0 O 3 P 1 S 0 + 79.96633 + C 3 H 6 N 1 O 4 P 1 S 1 + 183.12 + 182.97551 + C + natural + Unimod:21 + uniprot.ptm:PTM-0251 + (2R)-2-amino-3-(phosphonosulfanyl)propanoic acid + 2-azanyl-3-(phosphonosulfanyl)propanoic acid + ACT_SITE Phosphocysteine intermediate + MOD_RES Phosphocysteine + PCys + S-phospho-L-cysteine + S-phosphonocysteine + S-phosphorylated L-cysteine + S3-phosphocysteine + cysteine phosphate thioester + PSI-MOD + Phospho + Phosphorylation + MOD:00043 + S-phospho-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-phospho-L-cysteine. + PubMed:3142516 + PubMed:7961745 + PubMed:8128219 + RESID:AA0034 + Unimod:21#C + + + + + (2R)-2-amino-3-(phosphonosulfanyl)propanoic acid + + + + + + 2-azanyl-3-(phosphonosulfanyl)propanoic acid + + + + + + ACT_SITE Phosphocysteine intermediate + + + + + + MOD_RES Phosphocysteine + + + + + + PCys + + + + + + S-phospho-L-cysteine + + + + + + S-phosphonocysteine + + + + + + S-phosphorylated L-cysteine + + + + + + S3-phosphocysteine + + + + + + cysteine phosphate thioester + + + + + + Phospho + + + + + + Phosphorylation + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to tele-phospho-L-histidine (N-tau-phospho-L-histidine, 1'-phospho-L-histidine). + 79.98 + C 0 H 1 N 0 O 3 P 1 + 79.96633 + C 6 H 8 N 3 O 4 P 1 + 217.12 + 217.02524 + H + natural + uniprot.ptm:PTM-0325 + (2S)-2-amino-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid + 1'-phospho-L-histidine + 2-azanyl-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid + ACT_SITE Tele-phosphohistidine intermediate + MOD_RES Tele-phosphohistidine + N(tau)-phosphohistidine + N1-phosphonohistidine + NE2-phosphonohistidine + NtPHis + Ntau-phosphorylated L-histidine + histidine-N(epsilon)-phosphate + histidine-N1'-phosphate + tele-phosphohistidine + PSI-MOD + Phospho + Phosphorylation + histidine-3-phosphate + MOD:00044 + + 1'-phospho-L-histidine + + + + + A protein modification that effectively converts an L-histidine residue to tele-phospho-L-histidine (N-tau-phospho-L-histidine, 1'-phospho-L-histidine). + PubMed:11038361 + PubMed:5642389 + PubMed:6692818 + RESID:AA0035 + + + + + (2S)-2-amino-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid + + + + + + 1'-phospho-L-histidine + + + + + + 2-azanyl-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid + + + + + + ACT_SITE Tele-phosphohistidine intermediate + + + + + + MOD_RES Tele-phosphohistidine + + + + + + N(tau)-phosphohistidine + + + + + + N1-phosphonohistidine + + + + + + NE2-phosphonohistidine + + + + + + NtPHis + + + + + + Ntau-phosphorylated L-histidine + + + + + + histidine-N(epsilon)-phosphate + + + + + + histidine-N1'-phosphate + + + + + + tele-phosphohistidine + + + + + + Phospho + + + + + + Phosphorylation + + + + + + histidine-3-phosphate + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to pros-phospho-L-histidine (N-pi-phospho-L-histidine, 3'-phospho-L-histidine). + 79.98 + C 0 H 1 N 0 O 3 P 1 + 79.96633 + C 6 H 8 N 3 O 4 P 1 + 217.12 + 217.02524 + H + natural + uniprot.ptm:PTM-0260 + (2S)-2-amino-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid + 2-azanyl-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid + 3'-phospho-L-histidine + ACT_SITE Pros-phosphohistidine intermediate + MOD_RES Pros-phosphohistidine + N(pi)-phosphohistidine + N3-phosphonohistidine + ND1-phosphonohistidine + NpPHis + Npi-phosphorylated L-histidine + histidine-N(delta)-phosphate + histidine-N3'-phosphate + pros-phosphohistidine + PSI-MOD + Phospho + Phosphorylation + histidine-1-phosphate + MOD:00045 + + 3'-phospho-L-histidine + + + + + A protein modification that effectively converts an L-histidine residue to pros-phospho-L-histidine (N-pi-phospho-L-histidine, 3'-phospho-L-histidine). + PubMed:1549615 + PubMed:5642389 + PubMed:6692818 + PubMed:7669763 + PubMed:7803390 + RESID:AA0036 + + + + + (2S)-2-amino-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid + + + + + + 2-azanyl-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid + + + + + + 3'-phospho-L-histidine + + + + + + ACT_SITE Pros-phosphohistidine intermediate + + + + + + MOD_RES Pros-phosphohistidine + + + + + + N(pi)-phosphohistidine + + + + + + N3-phosphonohistidine + + + + + + ND1-phosphonohistidine + + + + + + NpPHis + + + + + + Npi-phosphorylated L-histidine + + + + + + histidine-N(delta)-phosphate + + + + + + histidine-N3'-phosphate + + + + + + pros-phosphohistidine + + + + + + Phospho + + + + + + Phosphorylation + + + + + + histidine-1-phosphate + + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-phospho-L-serine. + 79.98 + C 0 H 1 N 0 O 3 P 1 + 79.96633 + C 3 H 6 N 1 O 5 P 1 + 167.06 + 166.99835 + S + natural + Unimod:21 + uniprot.ptm:PTM-0253 + (2S)-2-amino-3-(phosphonooxy)propanoic acid + 2-amino-3-hydroxypropanoic acid 3-phosphate + 2-azanyl-3-(phosphonooxy)propanoic acid + ACT_SITE Phosphoserine intermediate + MOD_RES Phosphoserine + O-phospho-L-serine + O-phosphonoserine + O-phosphorylated L-serine + O3-phosphoserine + OPSer + Phospho Seryl + phosphorylations + serine phosphate ester + PSI-MOD + Phospho + Phosphorylation + MOD:00046 + + O-phospho-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-phospho-L-serine. + ChEBI:15811 + DeltaMass:0 + OMSSA:6 + PubMed:12923550 + PubMed:4065410 + PubMed:8061611 + RESID:AA0037 + Unimod:21#S + + + + + (2S)-2-amino-3-(phosphonooxy)propanoic acid + + + + + + 2-amino-3-hydroxypropanoic acid 3-phosphate + + + + + + 2-azanyl-3-(phosphonooxy)propanoic acid + + + + + + ACT_SITE Phosphoserine intermediate + + + + + + MOD_RES Phosphoserine + + + + + + O-phospho-L-serine + + + + + + O-phosphonoserine + + + + + + O-phosphorylated L-serine + + + + + + O3-phosphoserine + + + + + + OPSer + + + + + + Phospho Seryl + + + + + + phosphorylations + + + + + + serine phosphate ester + + + + + + Phospho + + + + + + Phosphorylation + + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-phospho-L-threonine. + 79.98 + C 0 H 1 N 0 O 3 P 1 + 79.96633 + C 4 H 8 N 1 O 5 P 1 + 181.08 + 181.014 + T + natural + Unimod:21 + uniprot.ptm:PTM-0254 + (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid + 2-amino-3-hydroxybutanoic acid 3-phosphate + 2-azanyl-3-(phosphonooxy)butanoic acid + MOD_RES Phosphothreonine + O-phospho-L-threonine + O-phosphorylated L-threonine + O3-phosphothreonine + OPThr + Phospho Threonyl + phosphorylationt + threonine phosphate ester + PSI-MOD + Phospho + Phosphorylation + MOD:00047 + + O-phospho-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-phospho-L-threonine. + ChEBI:21967 + DeltaMass:0 + OMSSA:7 + PubMed:12923550 + PubMed:7678926 + RESID:AA0038 + Unimod:21#T + + + + + (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid + + + + + + 2-amino-3-hydroxybutanoic acid 3-phosphate + + + + + + 2-azanyl-3-(phosphonooxy)butanoic acid + + + + + + MOD_RES Phosphothreonine + + + + + + O-phospho-L-threonine + + + + + + O-phosphorylated L-threonine + + + + + + O3-phosphothreonine + + + + + + OPThr + + + + + + Phospho Threonyl + + + + + + phosphorylationt + + + + + + threonine phosphate ester + + + + + + Phospho + + + + + + Phosphorylation + + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to O4'-phospho-L-tyrosine. + 79.98 + C 0 H 1 N 0 O 3 P 1 + 79.96633 + C 9 H 10 N 1 O 5 P 1 + 243.15 + 243.02966 + Y + natural + Unimod:21 + uniprot.ptm:PTM-0255 + (2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid + 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate + 2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid + MOD_RES Phosphotyrosine + O4'-phospho-L-tyrosine + O4'-phosphorylated L-tyrosine + O4-phosphotyrosine + OPTyr + Phospho Tyrosinyl + phosphorylationy + tyrosine phosphate + PSI-MOD + Phospho + Phosphorylation + MOD:00048 + + O4'-phospho-L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to O4'-phospho-L-tyrosine. + DeltaMass:0 + OMSSA:8 + PubMed:10226369 + PubMed:1725475 + RESID:AA0039 + Unimod:21#Y + + + + + (2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid + + + + + + 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate + + + + + + 2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid + + + + + + MOD_RES Phosphotyrosine + + + + + + O4'-phospho-L-tyrosine + + + + + + O4'-phosphorylated L-tyrosine + + + + + + O4-phosphotyrosine + + + + + + OPTyr + + + + + + Phospho Tyrosinyl + + + + + + phosphorylationy + + + + + + tyrosine phosphate + + + + + + Phospho + + + + + + Phosphorylation + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to diphthamide. + 143.21 + C 7 H 15 N 2 O 1 + 143.11789 + 1+ + C 13 H 22 N 5 O 2 + 280.35 + 280.1768 + H + natural + Unimod:375 + uniprot.ptm:PTM-0118 + (2R)-1-amino-4-(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-2-yl)-N,N,N-trimethyl-1-oxobutan-2-aminium + (3-[4-(2-amino-2-carboxy-ethyl)-1H-imidazol-2-yl]-1-carbamoyl-propyl)-trimethylammonium + 1-azanyl-4-(4-[2-azanyl-2-carboxyethyl]-1H-imidazol-2-yl)-N,N,N-trimethyl-1-oxobutan-2-azanium + 2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine + 2-[(R)-3-carboxamido-3-(trimethylammonio)propyl]-4-((S)-2-amino-2-carboxyethyl)-1H-imidazole + 2-[3-carboxamido-3-(trimethylammonio)propyl]histidine + 2-amino-3-[[2-(3-amino-3-carbamoyl-prop-1-enyl)-1,1,3-trimethyl-2,3-dihydroimidazol-5-yl]]propanoic acid + 2-amino-4-[[5-(2-amino-2-carboxylato-ethyl)-1,1,3-trimethyl-2,3-dihydroimidazol-2-yl]]but-3-enamide + Diphth + MOD_RES Diphthamide + alpha-(aminocarbonyl)-4-(2-amino-2-carboxyethyl)-N,N,N-trimethyl-1H-imidazole-2-propanaminium + diphthamide + diphthamide (from histidine) + PSI-MOD + Diphthamide + MOD:00049 + 2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine + + + + + A protein modification that effectively converts an L-histidine residue to diphthamide. + ChEBI:16692 + DeltaMass:122 + PubMed:15316019 + PubMed:7430147 + RESID:AA0040 + Unimod:375#H + + + + + (2R)-1-amino-4-(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-2-yl)-N,N,N-trimethyl-1-oxobutan-2-aminium + + + + + + (3-[4-(2-amino-2-carboxy-ethyl)-1H-imidazol-2-yl]-1-carbamoyl-propyl)-trimethylammonium + + + + + + 1-azanyl-4-(4-[2-azanyl-2-carboxyethyl]-1H-imidazol-2-yl)-N,N,N-trimethyl-1-oxobutan-2-azanium + + + + + + 2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine + + + + + + 2-[(R)-3-carboxamido-3-(trimethylammonio)propyl]-4-((S)-2-amino-2-carboxyethyl)-1H-imidazole + + + + + + 2-[3-carboxamido-3-(trimethylammonio)propyl]histidine + + + + + + 2-amino-3-[[2-(3-amino-3-carbamoyl-prop-1-enyl)-1,1,3-trimethyl-2,3-dihydroimidazol-5-yl]]propanoic acid + + + + + + 2-amino-4-[[5-(2-amino-2-carboxylato-ethyl)-1,1,3-trimethyl-2,3-dihydroimidazol-2-yl]]but-3-enamide + + + + + + Diphth + + + + + + MOD_RES Diphthamide + + + + + + alpha-(aminocarbonyl)-4-(2-amino-2-carboxyethyl)-N,N,N-trimethyl-1H-imidazole-2-propanaminium + + + + + + diphthamide + + + + + + diphthamide (from histidine) + + + + + + Diphthamide + + + + + + Diphthamide + + + + + + + + + + + A protein modification that effectively converts an L-alanine residue to N-acetyl-L-alanine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 5 H 8 N 1 O 2 + 114.12 + 114.055504 + A + natural + N-term + uniprot.ptm:PTM-0199 + (2S)-2-(acetamido)propanoic acid + 2-(acetylamino)propanoic acid + 2-(acetylazanyl)propanoic acid + AcAla + MOD_RES N-acetylalanine + N-acetyl-L-alanine + N-acetylated L-alanine + acetylalanine + PSI-MOD + MOD:00050 + + N-acetyl-L-alanine + + + + + A protein modification that effectively converts an L-alanine residue to N-acetyl-L-alanine. + PubMed:363452 + PubMed:4700463 + RESID:AA0041 + + + + + (2S)-2-(acetamido)propanoic acid + + + + + + 2-(acetylamino)propanoic acid + + + + + + 2-(acetylazanyl)propanoic acid + + + + + + AcAla + + + + + + MOD_RES N-acetylalanine + + + + + + N-acetyl-L-alanine + + + + + + N-acetylated L-alanine + + + + + + acetylalanine + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to N-acetyl-L-aspartic acid. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 6 H 8 N 1 O 4 + 158.13 + 158.04533 + D + natural + N-term + uniprot.ptm:PTM-0200 + (2S)-2-(acetamido)butanedioic acid + 2-(acetylamino)butanedioic acid + 2-(acetylazanyl)butanedioic acid + AcAsp + MOD_RES N-acetylaspartate + N-acetyl-L-aspartic acid + N-acetylated L-aspartic acid + acetylaspartic acid + PSI-MOD + MOD:00051 + + N-acetyl-L-aspartic acid + + + + + A protein modification that effectively converts an L-aspartic acid residue to N-acetyl-L-aspartic acid. + ChEBI:21547 + PubMed:1560020 + PubMed:2395459 + RESID:AA0042 + + + + + (2S)-2-(acetamido)butanedioic acid + + + + + + 2-(acetylamino)butanedioic acid + + + + + + 2-(acetylazanyl)butanedioic acid + + + + + + AcAsp + + + + + + MOD_RES N-acetylaspartate + + + + + + N-acetyl-L-aspartic acid + + + + + + N-acetylated L-aspartic acid + + + + + + acetylaspartic acid + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to N-acetyl-L-cysteine. + 42.04 + C 2 H 2 N 0 O 1 S 0 + 42.010567 + C 5 H 8 N 1 O 2 S 1 + 146.18 + 146.02757 + C + natural + N-term + uniprot.ptm:PTM-0201 + (2R)-2-acetamido-3-sulfanylpropanoic acid + 2-acetylamino-3-mercaptopropanoic acid + 2-acetylamino-3-sulfanylpropanoic acid + 2-acetylazanyl-3-sulfanylpropanoic acid + MOD_RES N-acetylcysteine + N-acetyl-L-cysteine + N-acetylated cysteine + N-acetylcysteine + NAcCys + PSI-MOD + Acetyl + MOD:00052 + + incidental to RESID:AA0223 + N-acetyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to N-acetyl-L-cysteine. + ChEBI:28939 + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + PubMed:14730666 + PubMed:1500421 + PubMed:15350136 + PubMed:6725286 + RESID:AA0043 + + + + + (2R)-2-acetamido-3-sulfanylpropanoic acid + + + + + + 2-acetylamino-3-mercaptopropanoic acid + + + + + + 2-acetylamino-3-sulfanylpropanoic acid + + + + + + 2-acetylazanyl-3-sulfanylpropanoic acid + + + + + + MOD_RES N-acetylcysteine + + + + + + N-acetyl-L-cysteine + + + + + + N-acetylated cysteine + + + + + + N-acetylcysteine + + + + + + NAcCys + + + + + + Acetyl + + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to N-acetyl-L-glutamic acid. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 7 H 10 N 1 O 4 + 172.16 + 172.06099 + E + natural + N-term + uniprot.ptm:PTM-0202 + (2S)-2-(acetamido)pentanedioic acid + 2-(acetylamino)pentanedioic acid + 2-(acetylazanyl)pentanedioic acid + AcGlu + MOD_RES N-acetylglutamate + N-acetyl-L-glutamic acid + N-acetylated L-glutamic acid + acetylglutamic acid + PSI-MOD + MOD:00053 + + N-acetyl-L-glutamic acid + + + + + A protein modification that effectively converts an L-glutamic acid residue to N-acetyl-L-glutamic acid. + ChEBI:17533 + PubMed:6725286 + RESID:AA0044 + + + + + (2S)-2-(acetamido)pentanedioic acid + + + + + + 2-(acetylamino)pentanedioic acid + + + + + + 2-(acetylazanyl)pentanedioic acid + + + + + + AcGlu + + + + + + MOD_RES N-acetylglutamate + + + + + + N-acetyl-L-glutamic acid + + + + + + N-acetylated L-glutamic acid + + + + + + acetylglutamic acid + + + + + + + + + + + A protein modification that effectively converts an L-glutamine residue to N-acetyl-L-glutamine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 7 H 11 N 2 O 3 + 171.18 + 171.07697 + Q + artifact + N-term + (2S)-2-acetamido-5-pentanediamic acid + 2-acetylamino-5-amino-5-oxopentanoic acid + 2-acetylamino-5-pentanediamic acid + 2-acetylazanyl-5-azanyl-5-oxopentanoic acid + AcGln + N-acetyl-L-glutamine + N-acetylated L-glutamine + acetylglutamine + PSI-MOD + MOD:00054 + This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. + N-acetyl-L-glutamine + + + + + A protein modification that effectively converts an L-glutamine residue to N-acetyl-L-glutamine. + RESID:AA0045 + + + + + (2S)-2-acetamido-5-pentanediamic acid + + + + + + 2-acetylamino-5-amino-5-oxopentanoic acid + + + + + + 2-acetylamino-5-pentanediamic acid + + + + + + 2-acetylazanyl-5-azanyl-5-oxopentanoic acid + + + + + + AcGln + + + + + + N-acetyl-L-glutamine + + + + + + N-acetylated L-glutamine + + + + + + acetylglutamine + + + + + + + + + + + A protein modification that effectively converts a glycine residue to N-acetylglycine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 4 H 6 N 1 O 2 + 100.1 + 100.039856 + G + natural + N-term + uniprot.ptm:PTM-0203 + (acetylamino)acetic acid + (acetylazanyl)ethanoic acid + 2-(acetamido)ethanoic acid + 2-(acetylamino)ethanoic acid + AcGly + MOD_RES N-acetylglycine + N-acetylated glycine + N-acetylglycine + aceturic acid + PSI-MOD + MOD:00055 + + N-acetylglycine + + + + + A protein modification that effectively converts a glycine residue to N-acetylglycine. + PubMed:272676 + PubMed:5545094 + PubMed:6754709 + RESID:AA0046 + + + + + (acetylamino)acetic acid + + + + + + (acetylazanyl)ethanoic acid + + + + + + 2-(acetamido)ethanoic acid + + + + + + 2-(acetylamino)ethanoic acid + + + + + + AcGly + + + + + + MOD_RES N-acetylglycine + + + + + + N-acetylated glycine + + + + + + N-acetylglycine + + + + + + aceturic acid + + + + + + + + + + + A protein modification that effectively converts an L-isoleucine residue to N-acetyl-L-isoleucine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 8 H 14 N 1 O 2 + 156.2 + 156.10245 + I + artifact + N-term + uniprot.ptm:PTM-0204 + (2S,3S)-2-acetamido-3-methylpentanoic acid + 2-acetylamino-3-methylpentanoic acid + 2-acetylazanyl-3-methylpentanoic acid + AcIle + N-acetyl-L-isoleucine + N-acetylated L-isoleucine + acetylisoleucine + PSI-MOD + MOD:00056 + This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. + N-acetyl-L-isoleucine + + + + + A protein modification that effectively converts an L-isoleucine residue to N-acetyl-L-isoleucine. + PubMed:8034631 + RESID:AA0047 + + + + + (2S,3S)-2-acetamido-3-methylpentanoic acid + + + + + + 2-acetylamino-3-methylpentanoic acid + + + + + + 2-acetylazanyl-3-methylpentanoic acid + + + + + + AcIle + + + + + + N-acetyl-L-isoleucine + + + + + + N-acetylated L-isoleucine + + + + + + acetylisoleucine + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N2-acetyl-L-lysine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 8 H 15 N 2 O 2 + 171.22 + 171.11336 + K + artifact + N-term + (2S)-2-acetamido-6-aminohexanoic acid + 2-acetylamino-6-aminohexanoic acid + 2-acetylazanyl-6-azanylhexanoic acid + N2-acetyl-L-lysine + N2-acetylated L-lysine + N2-acetyllysine + N2AcLys + PSI-MOD + Acetyl + MOD:00057 + This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. + N2-acetyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N2-acetyl-L-lysine. + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + PubMed:14730666 + PubMed:15350136 + RESID:AA0048 + + + + + (2S)-2-acetamido-6-aminohexanoic acid + + + + + + 2-acetylamino-6-aminohexanoic acid + + + + + + 2-acetylazanyl-6-azanylhexanoic acid + + + + + + N2-acetyl-L-lysine + + + + + + N2-acetylated L-lysine + + + + + + N2-acetyllysine + + + + + + N2AcLys + + + + + + Acetyl + + + + + + + + + + + A protein modification that effectively converts an L-methionine to N-acetyl-L-methionine. + 42.04 + C 2 H 2 N 0 O 1 S 0 + 42.010567 + C 7 H 12 N 1 O 2 S 1 + 174.24 + 174.05887 + M + natural + N-term + uniprot.ptm:PTM-0205 + (2S)-2-acetamido-4-(methylsulfanyl)butanoic acid + 2-acetylamino-4-(methylsulfanyl)butanoic acid + 2-acetylamino-4-(methylthio)butanoic acid + 2-acetylazanyl-4-(methylsulfanyl)butanoic acid + AcMet + MOD_RES N-acetylmethionine + N-acetyl-L-methionine + N-acetylated L-methionine + acetylmethionine + methionamine + PSI-MOD + MOD:00058 + + N-acetyl-L-methionine + + + + + A protein modification that effectively converts an L-methionine to N-acetyl-L-methionine. + PubMed:7944406 + RESID:AA0049 + + + + + (2S)-2-acetamido-4-(methylsulfanyl)butanoic acid + + + + + + 2-acetylamino-4-(methylsulfanyl)butanoic acid + + + + + + 2-acetylamino-4-(methylthio)butanoic acid + + + + + + 2-acetylazanyl-4-(methylsulfanyl)butanoic acid + + + + + + AcMet + + + + + + MOD_RES N-acetylmethionine + + + + + + N-acetyl-L-methionine + + + + + + N-acetylated L-methionine + + + + + + acetylmethionine + + + + + + methionamine + + + + + + + + + + + A protein modification that effectively converts an L-proline residue to N-acetyl-L-proline. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 7 H 10 N 1 O 2 + 140.16 + 140.07115 + P + natural + N-term + uniprot.ptm:PTM-0206 + (2S)-1-acetyl-2-pyrrolidinecarboxylic acid + 1-acetylproline + MOD_RES N-acetylproline + N-acetyl-L-proline + N-acetylated L-proline + N-acetylproline + NAcPro + acetylproline + PSI-MOD + MOD:00059 + + N-acetyl-L-proline + + + + + A protein modification that effectively converts an L-proline residue to N-acetyl-L-proline. + PubMed:2928307 + RESID:AA0050 + + + + + (2S)-1-acetyl-2-pyrrolidinecarboxylic acid + + + + + + 1-acetylproline + + + + + + MOD_RES N-acetylproline + + + + + + N-acetyl-L-proline + + + + + + N-acetylated L-proline + + + + + + N-acetylproline + + + + + + NAcPro + + + + + + acetylproline + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to N-acetyl-L-serine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 5 H 8 N 1 O 3 + 130.12 + 130.05042 + S + natural + N-term + uniprot.ptm:PTM-0207 + (2S)-2-acetamido-3-hydroxypropanoic acid + 2-acetylamino-3-hydroxypropanoic acid + 2-acetylazanyl-3-hydroxypropanoic acid + MOD_RES N-acetylserine + N-acetyl-L-serine + N-acetylated L-serine + N-acetylserine + NAcSer + PSI-MOD + Acetyl + MOD:00060 + + N-acetyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to N-acetyl-L-serine. + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + PubMed:14730666 + PubMed:15350136 + PubMed:1880797 + PubMed:2106685 + PubMed:6997045 + RESID:AA0051 + + + + + (2S)-2-acetamido-3-hydroxypropanoic acid + + + + + + 2-acetylamino-3-hydroxypropanoic acid + + + + + + 2-acetylazanyl-3-hydroxypropanoic acid + + + + + + MOD_RES N-acetylserine + + + + + + N-acetyl-L-serine + + + + + + N-acetylated L-serine + + + + + + N-acetylserine + + + + + + NAcSer + + + + + + Acetyl + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to N-acetyl-L-threonine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 6 H 10 N 1 O 3 + 144.15 + 144.06607 + T + natural + N-term + uniprot.ptm:PTM-0208 + (2S,3R)-2-acetamido-3-hydroxybutanoic acid + 2-acetylamino-3-hydroxybutanoic acid + 2-acetylazanyl-3-hydroxybutanoic acid + MOD_RES N-acetylthreonine + N-acetyl-L-threonine + N-acetylated L-threonine + N-acetylthreonine + N-methylcarbonylthreonine + NAcThr + PSI-MOD + Acetyl + Acetylation + MOD:00061 + + N-acetyl-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to N-acetyl-L-threonine. + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + PubMed:14730666 + PubMed:15350136 + PubMed:2106685 + PubMed:6997045 + RESID:AA0052 + + + + + (2S,3R)-2-acetamido-3-hydroxybutanoic acid + + + + + + 2-acetylamino-3-hydroxybutanoic acid + + + + + + 2-acetylazanyl-3-hydroxybutanoic acid + + + + + + MOD_RES N-acetylthreonine + + + + + + N-acetyl-L-threonine + + + + + + N-acetylated L-threonine + + + + + + N-acetylthreonine + + + + + + N-methylcarbonylthreonine + + + + + + NAcThr + + + + + + Acetyl + + + + + + Acetylation + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to N-acetyl-L-tyrosine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 11 H 12 N 1 O 3 + 206.22 + 206.08171 + Y + natural + N-term + uniprot.ptm:PTM-0209 + (2S)-2-acetamido-3-(4-hydoxyphenyl)propanoic acid + 2-acetylamino-3-(4-hydoxyphenyl)propanoic acid + 2-acetylazanyl-3-(4-hydoxyphenyl)propanoic acid + AcTyr + MOD_RES N-acetyltyrosine + N-acetyl-L-tyrosine + N-acetylated L-tyrosine + N-acetyltyrosine + PSI-MOD + Acetyl + MOD:00062 + N-acetyl-L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to N-acetyl-L-tyrosine. + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + PubMed:14730666 + PubMed:15350136 + PubMed:2506074 + PubMed:475783 + RESID:AA0053 + + + + + (2S)-2-acetamido-3-(4-hydoxyphenyl)propanoic acid + + + + + + 2-acetylamino-3-(4-hydoxyphenyl)propanoic acid + + + + + + 2-acetylazanyl-3-(4-hydoxyphenyl)propanoic acid + + + + + + AcTyr + + + + + + MOD_RES N-acetyltyrosine + + + + + + N-acetyl-L-tyrosine + + + + + + N-acetylated L-tyrosine + + + + + + N-acetyltyrosine + + + + + + Acetyl + + + + + + + + + + + A protein modification that effectively converts an L-valine residue to N-acetyl-L-valine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 7 H 12 N 1 O 2 + 142.18 + 142.0868 + V + natural + N-term + uniprot.ptm:PTM-0210 + (2S)-2-acetamido-3-methylbutanoic acid + 2-acetylamino-3-methylbutanoic acid + 2-acetylazanyl-3-methylbutanoic acid + AcVal + MOD_RES N-acetylvaline + N-acetyl-L-valine + N-acetylated L-valine + N-acetylvaline + PSI-MOD + MOD:00063 + + N-acetyl-L-valine + + + + + A protein modification that effectively converts an L-valine residue to N-acetyl-L-valine. + PubMed:1735421 + RESID:AA0054 + + + + + (2S)-2-acetamido-3-methylbutanoic acid + + + + + + 2-acetylamino-3-methylbutanoic acid + + + + + + 2-acetylazanyl-3-methylbutanoic acid + + + + + + AcVal + + + + + + MOD_RES N-acetylvaline + + + + + + N-acetyl-L-valine + + + + + + N-acetylated L-valine + + + + + + N-acetylvaline + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-acetyl-L-lysine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 8 H 14 N 2 O 2 + 170.21 + 170.10553 + K + natural + Unimod:1 + uniprot.ptm:PTM-0190 + (2S)-6-acetamido-2-aminohexanoic acid + 6-acetylamino-2-aminohexanoic acid + 6-acetylazanyl-2-aminohexanoic acid + MOD_RES N6-acetyllysine + N(zeta)-acetyllysine + N6-acetyl-L-lysine + N6-acetylated L-lysine + N6AcLys + acetylk + epsilon-acetyllysine + PSI-MOD + Acetyl + Acetylation + MOD:00064 + + N6-acetyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-acetyl-L-lysine. + ChEBI:17752 + DeltaMass:214 + OMSSA:24 + PubMed:11369851 + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + PubMed:14730666 + PubMed:15350136 + PubMed:1680872 + PubMed:670159 + RESID:AA0055 + Unimod:1#K + + + + + (2S)-6-acetamido-2-aminohexanoic acid + + + + + + 6-acetylamino-2-aminohexanoic acid + + + + + + 6-acetylazanyl-2-aminohexanoic acid + + + + + + MOD_RES N6-acetyllysine + + + + + + N(zeta)-acetyllysine + + + + + + N6-acetyl-L-lysine + + + + + + N6-acetylated L-lysine + + + + + + N6AcLys + + + + + + acetylk + + + + + + epsilon-acetyllysine + + + + + + Acetyl + + + + + + Acetylation + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-acetyl-L-cysteine. + 42.04 + C 2 H 2 N 0 O 1 S 0 + 42.010567 + C 5 H 7 N 1 O 2 S 1 + 145.18 + 145.01974 + C + natural + Unimod:1 + (2R)-3-acetylsulfanyl-2-aminopropanoic acid + 2-amino-3-(acetylthio)propanoic acid + 2-azanyl-3-(acetylsulfanyl)propanoic acid + ACT_SITE S-acetylcysteine intermediate + S-acetyl-L-cysteine + S-acetylcysteine + SAcCys + cysteine acetate thioester + PSI-MOD + Acetyl + Acetylation + MOD:00065 + + S-acetyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-acetyl-L-cysteine. + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + PubMed:1310545 + PubMed:14730666 + PubMed:15350136 + RESID:AA0056 + Unimod:1#C + + + + + (2R)-3-acetylsulfanyl-2-aminopropanoic acid + + + + + + 2-amino-3-(acetylthio)propanoic acid + + + + + + 2-azanyl-3-(acetylsulfanyl)propanoic acid + + + + + + ACT_SITE S-acetylcysteine intermediate + + + + + + S-acetyl-L-cysteine + + + + + + S-acetylcysteine + + + + + + SAcCys + + + + + + cysteine acetate thioester + + + + + + Acetyl + + + + + + Acetylation + + + + + + + + + + + + A protein modification that effectively converts a glycine residue to N-formylglycine. + 28.01 + C 1 H 0 N 0 O 1 + 27.994915 + C 3 H 4 N 1 O 2 + 86.07 + 86.0242 + G + natural + N-term + uniprot.ptm:PTM-0211 + (formylamino)acetic acid + (formylamino)ethanoic acid + (formylazanyl)ethanoic acid + 2-formamidoacetic acid + 2-formamidoethanoic acid + MOD_RES N-formylglycine + N(alpha)-formylglycine + N-formylated glycine + N-formylglycine + NFoGly + PSI-MOD + MOD:00066 + N-formylglycine + + + + + A protein modification that effectively converts a glycine residue to N-formylglycine. + PubMed:5139483 + RESID:AA0057 + + + + + (formylamino)acetic acid + + + + + + (formylamino)ethanoic acid + + + + + + (formylazanyl)ethanoic acid + + + + + + 2-formamidoacetic acid + + + + + + 2-formamidoethanoic acid + + + + + + MOD_RES N-formylglycine + + + + + + N(alpha)-formylglycine + + + + + + N-formylated glycine + + + + + + N-formylglycine + + + + + + NFoGly + + + + + + + + + + + A protein modification that effectively converts a glycine residue to N-D-glucuronoylglycine. + 176.12 + C 6 H 8 N 0 O 6 + 176.03209 + C 8 H 12 N 1 O 7 + 234.18 + 234.06137 + G + natural + N-term + uniprot.ptm:PTM-0331 + 2-(glucuronoylamino)ethanoic acid + MOD_RES N-D-glucuronoyl glycine + N-D-glucuronoyl-glycine + N-D-glucuronyl-glycine + NGlcAGly + ntermpepglucuronylg + PSI-MOD + Glucuronyl + MOD:00067 + N-D-glucuronoylglycine + + + + + A protein modification that effectively converts a glycine residue to N-D-glucuronoylglycine. + OMSSA:50 + PubMed:10858503 + PubMed:12716131 + PubMed:6493057 + PubMed:7398618 + RESID:AA0058 + + + + + 2-(glucuronoylamino)ethanoic acid + + + + + + MOD_RES N-D-glucuronoyl glycine + + + + + + N-D-glucuronoyl-glycine + + + + + + N-D-glucuronyl-glycine + + + + + + NGlcAGly + + + + + + ntermpepglucuronylg + + + + + + Glucuronyl + + + + + + + + + + + + A protein modification that effectively converts a glycine residue to N-myristoylglycine. + 210.36 + C 14 H 26 N 0 O 1 + 210.19836 + C 16 H 30 N 1 O 2 + 268.42 + 268.22766 + G + natural + N-term + Unimod:45 + uniprot.ptm:PTM-0221 + (tetradecanoylamino)ethanoic acid + LIPID N-myristoyl glycine + N-(1-oxotetradecyl)glycine + N-(C14:0 aliphatic acyl)glycine + N-myristoyl-glycine + N-myristoylated glycine + N-myristylglycine + N-tetradecanoylglycine + NMyrGly + ntermpepmyristoylationg + PSI-MOD + Myristoyl + Myristoylation + MOD:00068 + + N-myristoylglycine + + + + + A protein modification that effectively converts a glycine residue to N-myristoylglycine. + OMSSA:80 + PubMed:11955007 + PubMed:11955008 + PubMed:1326520 + PubMed:1386601 + PubMed:6436247 + PubMed:7543369 + RESID:AA0059 + Unimod:45#G + + + + + (tetradecanoylamino)ethanoic acid + + + + + + LIPID N-myristoyl glycine + + + + + + N-(1-oxotetradecyl)glycine + + + + + + N-(C14:0 aliphatic acyl)glycine + + + + + + N-myristoyl-glycine + + + + + + N-myristoylated glycine + + + + + + N-myristylglycine + + + + + + N-tetradecanoylglycine + + + + + + NMyrGly + + + + + + ntermpepmyristoylationg + + + + + + Myristoyl + + + + + + Myristoylation + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-L-cysteine. + 238.41 + C 16 H 30 N 0 O 1 S 0 + 238.22966 + C 19 H 36 N 1 O 2 S 1 + 342.56 + 342.24667 + C + natural + N-term + uniprot.ptm:PTM-0222 + (2R)-2-hexadecanoylamino-3-sulfanylpropanoic acid + 2-hexadecanamido-3-sulfanylpropanoic acid + 2-hexadecanoylamino-3-mercaptopropanoic acid + LIPID N-palmitoyl cysteine + N-(1-oxahexadecyl)-L-cysteine + N-hexadecanoylated L-cysteine + N-palmitoyl-L-cysteine + N-palmitoylated L-cysteine + NPamCys + PSI-MOD + Palmitoyl + Palmitoylation + MOD:00069 + + incidental to RESID:AA0107 incidental to RESID:AA0309 + N-palmitoyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-L-cysteine. + PubMed:10896212 + PubMed:4575979 + PubMed:9056182 + PubMed:9593755 + RESID:AA0060 + + + + + (2R)-2-hexadecanoylamino-3-sulfanylpropanoic acid + + + + + + 2-hexadecanamido-3-sulfanylpropanoic acid + + + + + + 2-hexadecanoylamino-3-mercaptopropanoic acid + + + + + + LIPID N-palmitoyl cysteine + + + + + + N-(1-oxahexadecyl)-L-cysteine + + + + + + N-hexadecanoylated L-cysteine + + + + + + N-palmitoyl-L-cysteine + + + + + + N-palmitoylated L-cysteine + + + + + + NPamCys + + + + + + Palmitoyl + + + + + + Palmitoylation + + + + + + + + + + + A protein modification that effectively converts an L-alanine residue to N-methyl-L-alanine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 4 H 7 N 1 O 1 + 85.11 + 85.052765 + A + natural + N-term + uniprot.ptm:PTM-0214 + (2S)-2-methylaminopropanoic acid + 2-methylazanylpropanoic acid + MOD_RES N-methylalanine + N-methyl-L-alanine + N-methylalanine + N-methylated L-alanine + NMe1Ala + PSI-MOD + Methyl + Methylation + MOD:00070 + + Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG]. + N-methyl-L-alanine + + + + + A protein modification that effectively converts an L-alanine residue to N-methyl-L-alanine. + ChEBI:17519 + PubMed:323502 + PubMed:337304 + PubMed:7007074 + RESID:AA0061 + + + + + (2S)-2-methylaminopropanoic acid + + + + + + 2-methylazanylpropanoic acid + + + + + + MOD_RES N-methylalanine + + + + + + N-methyl-L-alanine + + + + + + N-methylalanine + + + + + + N-methylated L-alanine + + + + + + NMe1Ala + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + A protein modification that effectively converts an L-alanine residue to N,N,N-trimethyl-L-alanine. + 43.09 + C 3 H 7 N 0 O 0 + 43.054226 + 1+ + C 6 H 13 N 1 O 1 + 115.18 + 115.09917 + A + natural + N-term + uniprot.ptm:PTM-0177 + (1S)-1-carboxy-N,N,N-trimethylethanaminium + (1S)-1-carboxy-N,N,N-trimethylethanazanium + (2S)-2-(trimethylammonio)propanoic acid + MOD_RES N,N,N-trimethylalanine + N,N,N-trimethyl-L-alanine + N,N,N-trimethylalanine cation + N,N,N-trimethylalaninium + N,N,N-trimethylated L-alanine + N2Me3+Ala + NMe3Ala + PSI-MOD + Trimethyl + tri-Methylation + MOD:00071 + + N,N,N-trimethyl-L-alanine + + + + + A protein modification that effectively converts an L-alanine residue to N,N,N-trimethyl-L-alanine. + PubMed:12590383 + PubMed:332162 + PubMed:3979397 + PubMed:6778808 + PubMed:7715456 + RESID:AA0062 + + + + + (1S)-1-carboxy-N,N,N-trimethylethanaminium + + + + + + (1S)-1-carboxy-N,N,N-trimethylethanazanium + + + + + + (2S)-2-(trimethylammonio)propanoic acid + + + + + + MOD_RES N,N,N-trimethylalanine + + + + + + N,N,N-trimethyl-L-alanine + + + + + + N,N,N-trimethylalanine cation + + + + + + N,N,N-trimethylalaninium + + + + + + N,N,N-trimethylated L-alanine + + + + + + N2Me3+Ala + + + + + + NMe3Ala + + + + + + Trimethyl + + + + + + tri-Methylation + + + + + + + + + + + + A protein modification that effectively converts a glycine residue to N-methylglycine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 3 H 5 N 1 O 1 + 71.08 + 71.03712 + G + natural + N-term + uniprot.ptm:PTM-0483 + L-sarcosine + MOD_RES N-methylglycine + N-methylated glycine + N-methylglycine + NMe1Gly + Sar + Sarcosine + Sarcosyl + methylaminoacetic acid + methylaminoethanoic acid + PSI-MOD + Methyl + Methylation + MOD:00072 + DeltaMass also has an entry for the free amino acid. Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG]. + N-methylglycine + + + + + A protein modification that effectively converts a glycine residue to N-methylglycine. + ChEBI:15611 + DeltaMass:0 + PubMed:1593629 + RESID:AA0063 + + + + + L-sarcosine + + + + + + MOD_RES N-methylglycine + + + + + + N-methylated glycine + + + + + + N-methylglycine + + + + + + NMe1Gly + + + + + + Sar + + + + + + Sarcosine + + + + + + Sarcosyl + + + + + + methylaminoacetic acid + + + + + + methylaminoethanoic acid + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to N-methyl-L-methionine. + 14.03 + C 1 H 2 N 0 O 0 S 0 + 14.01565 + C 6 H 11 N 1 O 1 S 1 + 145.22 + 145.05614 + M + natural + N-term + uniprot.ptm:PTM-0217 + (2S)-2-methylamino-4-(methylsulfanyl)butanoic acid + 2-methylamino-4-(methylthio)butanoic acid + MOD_RES N-methylmethionine + Methyl Methionyl + N-methyl-L-methionine + N-methylated L-methionine + N-methylmethionine + NMe1Met + PSI-MOD + Methyl + Methylation + MOD:00073 + + Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG]. + N-methyl-L-methionine + + + + + A protein modification that effectively converts an L-methionine residue to N-methyl-L-methionine. + DeltaMass:169 + PubMed:323502 + PubMed:3298225 + RESID:AA0064 + + + + + (2S)-2-methylamino-4-(methylsulfanyl)butanoic acid + + + + + + 2-methylamino-4-(methylthio)butanoic acid + + + + + + MOD_RES N-methylmethionine + + + + + + Methyl Methionyl + + + + + + N-methyl-L-methionine + + + + + + N-methylated L-methionine + + + + + + N-methylmethionine + + + + + + NMe1Met + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to N-methyl-L-phenylalanine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 10 H 11 N 1 O 1 + 161.2 + 161.08406 + F + natural + N-term + uniprot.ptm:PTM-0218 + (2S)-2-methylamino-3-phenylpropanoic acid + MOD_RES N-methylphenylalanine + N-methyl-L-phenylalanine + N-methylated L-phenylalanine + N-methylphenylalanine + NMe1Phe + PSI-MOD + Methyl + Methylation + MOD:00074 + + Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG]. + N-methyl-L-phenylalanine + + + + + A protein modification that effectively converts an L-phenylalanine residue to N-methyl-L-phenylalanine. + PubMed:2577730 + PubMed:413571 + RESID:AA0065 + + + + + (2S)-2-methylamino-3-phenylpropanoic acid + + + + + + MOD_RES N-methylphenylalanine + + + + + + N-methyl-L-phenylalanine + + + + + + N-methylated L-phenylalanine + + + + + + N-methylphenylalanine + + + + + + NMe1Phe + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + A protein modification that effectively converts an L-proline residue to N,N-dimethyl-L-proline. + 29.06 + C 2 H 5 N 0 O 0 + 29.038576 + 1+ + C 7 H 13 N 1 O 1 + 127.19 + 127.09917 + P + natural + N-term + Unimod:529 + uniprot.ptm:PTM-0179 + (2S)-2-carboxy-1,1-dimethylpyrrolidinium + 1,1-dimethyl-L-prolinium + MOD_RES N,N-dimethylproline + N,N-dimethyl-L-proline + N,N-dimethyl-L-prolinium + N,N-dimethylated L-proline + NMe2Pro + stachydrin + PSI-MOD + Delta:H(5)C(2) + Dimethyl + Dimethylation of proline residue + MOD:00075 + + Unimod terminal specification corrected [JSG]. + N,N-dimethyl-L-proline + + + + + A protein modification that effectively converts an L-proline residue to N,N-dimethyl-L-proline. + ChEBI:21451 + PubMed:12964758 + PubMed:14570711 + PubMed:193025 + PubMed:3882426 + PubMed:6254758 + RESID:AA0066 + Unimod:529 + + + + + (2S)-2-carboxy-1,1-dimethylpyrrolidinium + + + + + + 1,1-dimethyl-L-prolinium + + + + + + MOD_RES N,N-dimethylproline + + + + + + N,N-dimethyl-L-proline + + + + + + N,N-dimethyl-L-prolinium + + + + + + N,N-dimethylated L-proline + + + + + + NMe2Pro + + + + + + stachydrin + + + + + + Delta:H(5)C(2) + + + + + + Dimethyl + + + + + + Dimethylation of proline residue + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to symmetric dimethylarginine, N(omega),N'(omega)-dimethyl-L-arginine. + 28.05 + C 2 H 4 N 0 O 0 + 28.0313 + C 8 H 16 N 4 O 1 + 184.24 + 184.13242 + R + natural + Unimod:36 + uniprot.ptm:PTM-0287 + (2S)-2-amino-5-[((methylamino)(methylimino)methyl)amino]pentanoic acid + MOD_RES Omega-N-methylated arginine + MOD_RES Symmetric dimethylarginine + N3,N4-dimethylarginine + N5-[(methylamino)(methylimino)methyl]ornithine + NG,N'G-dimethylarginine + NoNo'Me2Arg + omega-N,omega-N'-dimethyl-L-arginine + omega-N,omega-N'-dimethylated L-arginine + symmetric dimethylarginine + PSI-MOD + Dimethyl + di-Methylation + MOD:00076 + + symmetric dimethyl-L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to symmetric dimethylarginine, N(omega),N'(omega)-dimethyl-L-arginine. + PubMed:12964758 + PubMed:14570711 + PubMed:15835918 + PubMed:2426402 + PubMed:5128665 + RESID:AA0067 + Unimod:36#R + + + + + (2S)-2-amino-5-[((methylamino)(methylimino)methyl)amino]pentanoic acid + + + + + + MOD_RES Omega-N-methylated arginine + + + + + + MOD_RES Symmetric dimethylarginine + + + + + + N3,N4-dimethylarginine + + + + + + N5-[(methylamino)(methylimino)methyl]ornithine + + + + + + NG,N'G-dimethylarginine + + + + + + NoNo'Me2Arg + + + + + + omega-N,omega-N'-dimethyl-L-arginine + + + + + + omega-N,omega-N'-dimethylated L-arginine + + + + + + symmetric dimethylarginine + + + + + + Dimethyl + + + + + + di-Methylation + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to asymmetric dimethylarginine, N(omega),N(omega)-dimethyl-L-arginine. + 28.05 + C 2 H 4 N 0 O 0 + 28.0313 + C 8 H 16 N 4 O 1 + 184.24 + 184.13242 + R + natural + Unimod:36 + uniprot.ptm:PTM-0066 + (2S)-2-amino-5-([(dimethylamino)(imino)methyl]amino)pentanoic acid + MOD_RES Asymmetric dimethylarginine + MOD_RES Omega-N-methylated arginine + N5-[(dimethylamino)(imino)methyl]ornithine + NG,NG-dimethylarginine + NoNoMe2Arg + asymmetric dimethylarginine + omega-N,omega-N-dimethlyated L-arginine + omega-N,omega-N-dimethyl-L-arginine + PSI-MOD + Dimethyl + di-Methylation + MOD:00077 + + asymmetric dimethyl-L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to asymmetric dimethylarginine, N(omega),N(omega)-dimethyl-L-arginine. + ChEBI:17929 + PubMed:11152131 + PubMed:12964758 + PubMed:14570711 + PubMed:15835918 + PubMed:3032834 + RESID:AA0068 + Unimod:36#R + + + + + (2S)-2-amino-5-([(dimethylamino)(imino)methyl]amino)pentanoic acid + + + + + + MOD_RES Asymmetric dimethylarginine + + + + + + MOD_RES Omega-N-methylated arginine + + + + + + N5-[(dimethylamino)(imino)methyl]ornithine + + + + + + NG,NG-dimethylarginine + + + + + + NoNoMe2Arg + + + + + + asymmetric dimethylarginine + + + + + + omega-N,omega-N-dimethlyated L-arginine + + + + + + omega-N,omega-N-dimethyl-L-arginine + + + + + + Dimethyl + + + + + + di-Methylation + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to N(omega)-methyl-L-arginine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 7 H 14 N 4 O 1 + 170.22 + 170.11676 + R + natural + uniprot.ptm:PTM-0237 + (2S)-2-amino-5-[(imino(methylamino)methyl)amino]pentanoic acid + MOD_RES Omega-N-methylarginine + MOD_RES Omega-N-methylated arginine + NG-methylarginine + NoMeArg + omega-N-methyl-L-arginine + omega-N-methylated L-arginine + PSI-MOD + Methyl + Methylation + MOD:00078 + + omega-N-methyl-L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to N(omega)-methyl-L-arginine. + PubMed:11875433 + PubMed:15835918 + PubMed:2426402 + PubMed:5128665 + RESID:AA0069 + + + + + (2S)-2-amino-5-[(imino(methylamino)methyl)amino]pentanoic acid + + + + + + MOD_RES Omega-N-methylarginine + + + + + + MOD_RES Omega-N-methylated arginine + + + + + + NG-methylarginine + + + + + + NoMeArg + + + + + + omega-N-methyl-L-arginine + + + + + + omega-N-methylated L-arginine + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to N4-methyl-L-asparagine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 5 H 8 N 2 O 2 + 128.13 + 128.05858 + N + natural + Unimod:34 + uniprot.ptm:PTM-0183 + (2S)-2-amino-N4-methylbutanediamic acid + MOD_RES N4-methylasparagine + N(gamma)-methylasparagine + N-methylasparagine + N4-methyl-L-asparagine + N4-methylated L-asparagine + N4Me1Asn + beta-aspartyl methylamide + methyln + PSI-MOD + Methyl + Methylation + beta-methylasparagine + MOD:00079 + + N4-methyl-L-asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to N4-methyl-L-asparagine. + OMSSA:75 + PubMed:11875433 + PubMed:2356973 + PubMed:3782095 + RESID:AA0070 + Unimod:34#N + + + + + (2S)-2-amino-N4-methylbutanediamic acid + + + + + + MOD_RES N4-methylasparagine + + + + + + N(gamma)-methylasparagine + + + + + + N-methylasparagine + + + + + + N4-methyl-L-asparagine + + + + + + N4-methylated L-asparagine + + + + + + N4Me1Asn + + + + + + beta-aspartyl methylamide + + + + + + methyln + + + + + + Methyl + + + + + + Methylation + + + + + + beta-methylasparagine + + + + + + + + + + + A protein modification that effectively converts an L-glutamine residue to N5-methyl-L-glutamine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 6 H 10 N 2 O 2 + 142.16 + 142.07423 + Q + natural + uniprot.ptm:PTM-0185 + (2S)-2-amino-5-methylamino-5-oxopentanoic acid + 2-amino-N5-methylpentanediamic acid + MOD_RES N5-methylglutamine + N(delta)-methylglutamine + N-methylglutamine + N5-methyl-L-glutamine + N5-methylated L-glutamine + N5Me1Gln + gamma-methylglutamine + PSI-MOD + Methyl + Methylation + MOD:00080 + + N5-methyl-L-glutamine + + + + + A protein modification that effectively converts an L-glutamine residue to N5-methyl-L-glutamine. + ChEBI:17592 + DeltaMass:166 + PubMed:11118225 + PubMed:11875433 + PubMed:365579 + RESID:AA0071 + + + + + (2S)-2-amino-5-methylamino-5-oxopentanoic acid + + + + + + 2-amino-N5-methylpentanediamic acid + + + + + + MOD_RES N5-methylglutamine + + + + + + N(delta)-methylglutamine + + + + + + N-methylglutamine + + + + + + N5-methyl-L-glutamine + + + + + + N5-methylated L-glutamine + + + + + + N5Me1Gln + + + + + + gamma-methylglutamine + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-methyl ester. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 6 H 9 N 1 O 3 + 143.14 + 143.05824 + E + natural + Unimod:34 + uniprot.ptm:PTM-0128 + (2S)-2-amino-5-methoxy-5-oxopentanoic acid + (5)-methyl L-hydrogen glutamate + 2-aminopentanedioic acid 5-methyl ester + 5-methyl L-2-aminoglutarate + 5-methyl L-glutamate + 5-methyl esterified L-glutamic acid + L-glutamic acid 5-methyl ester + MOD_RES Glutamate methyl ester (Glu) + O-methyl Glutamyl + O5MeGlu + glutamic acid 5-methyl ester + glutamic acid gamma-methyl ester + meestere + methyle + PSI-MOD + Methyl + Methylation + methyl ester + MOD:00081 + + DeltaMass gives the formula "C 6 H 9 O 1 N 3" with mass 143 (formula incorrect, N and O reversed) [JSG]. + L-glutamic acid 5-methyl ester (Glu) + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-methyl ester. + DeltaMass:167 + OMSSA:17 + OMSSA:70 + PubMed:16888 + PubMed:6300110 + RESID:AA0072#GLU + Unimod:34#E + + + + + (2S)-2-amino-5-methoxy-5-oxopentanoic acid + + + + + + (5)-methyl L-hydrogen glutamate + + + + + + 2-aminopentanedioic acid 5-methyl ester + + + + + + 5-methyl L-2-aminoglutarate + + + + + + 5-methyl L-glutamate + + + + + + 5-methyl esterified L-glutamic acid + + + + + + L-glutamic acid 5-methyl ester + + + + + + MOD_RES Glutamate methyl ester (Glu) + + + + + + O-methyl Glutamyl + + + + + + O5MeGlu + + + + + + glutamic acid 5-methyl ester + + + + + + glutamic acid gamma-methyl ester + + + + + + meestere + + + + + + methyle + + + + + + Methyl + + + + + + Methylation + + + + + + methyl ester + + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to pros-methyl-L-histidine (N-pi-methyl-L-histidine, 3'-methyl-L-histidine). + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 7 H 9 N 3 O 1 + 151.17 + 151.07455 + H + natural + uniprot.ptm:PTM-0259 + (2S)-2-amino-3-(3-methyl-3H-imidazol-4-yl)propanoic acid + 3'-methyl-L-histidine + MOD_RES Pros-methylhistidine + N(delta)-methylhistidine + N(pi)-methylhistidine + NpMeHis + pros-methylated L-histidine + pros-methylhistidine + PSI-MOD + 1-methylhistidine + Methyl + Methylation + MOD:00082 + + 3'-methyl-L-histidine + + + + + A protein modification that effectively converts an L-histidine residue to pros-methyl-L-histidine (N-pi-methyl-L-histidine, 3'-methyl-L-histidine). + PubMed:10660523 + PubMed:11875433 + PubMed:3467365 + PubMed:6692818 + PubMed:8076 + PubMed:8645219 + RESID:AA0073 + + + + + (2S)-2-amino-3-(3-methyl-3H-imidazol-4-yl)propanoic acid + + + + + + 3'-methyl-L-histidine + + + + + + MOD_RES Pros-methylhistidine + + + + + + N(delta)-methylhistidine + + + + + + N(pi)-methylhistidine + + + + + + NpMeHis + + + + + + pros-methylated L-histidine + + + + + + pros-methylhistidine + + + + + + 1-methylhistidine + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6,N6,N6-trimethyl-L-lysine. + 43.09 + C 3 H 7 N 0 O 0 + 43.054226 + 1+ + C 9 H 19 N 2 O 1 + 171.26 + 171.14919 + K + natural + uniprot.ptm:PTM-0187 + (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium + 2-amino-6-(trimethylammonio)hexanoic acid + 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium + MOD_RES N6,N6,N6-trimethyllysine + N(zeta)-trimethyllysine + N-trimethylation (of lysine) + N6,N6,N6-trimethyl-L-lysine + N6,N6,N6-trimethylated L-lysine + N6,N6,N6-trimethyllysin-N6-ium + N6,N6,N6-trimethyllysine cation + N6Me3+Lys + epsilon-trimethyllysine + PSI-MOD + Trimethyl + tri-Methylation + MOD:00083 + + DeltaMass calculates the mass difference from protonated lysine rather than neutral lysine; for trimethylated lysine starting from protonated lysine see MOD:00855 + N6,N6,N6-trimethyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6,N6,N6-trimethyl-L-lysine. + ChEBI:17311 + PubMed:12590383 + PubMed:3145979 + PubMed:4304194 + PubMed:6778808 + PubMed:7093227 + PubMed:8453381 + RESID:AA0074 + + + + + (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium + + + + + + 2-amino-6-(trimethylammonio)hexanoic acid + + + + + + 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium + + + + + + MOD_RES N6,N6,N6-trimethyllysine + + + + + + N(zeta)-trimethyllysine + + + + + + N-trimethylation (of lysine) + + + + + + N6,N6,N6-trimethyl-L-lysine + + + + + + N6,N6,N6-trimethylated L-lysine + + + + + + N6,N6,N6-trimethyllysin-N6-ium + + + + + + N6,N6,N6-trimethyllysine cation + + + + + + N6Me3+Lys + + + + + + epsilon-trimethyllysine + + + + + + Trimethyl + + + + + + tri-Methylation + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6,N6-dimethyl-L-lysine. + 28.05 + C 2 H 4 N 0 O 0 + 28.0313 + C 8 H 16 N 2 O 1 + 156.23 + 156.12627 + K + natural + Unimod:36 + uniprot.ptm:PTM-0188 + (2S)-2-amino-6-(dimethylamino)hexanoic acid + MOD_RES N6,N6-dimethyllysine + N(zeta)-dimethyllysine + N6,N6-dimethyl-L-lysine + N6,N6-dimethylated L-lysine + N6Me2Lys + dimethylk + epsilon-dimethyllysine + lysine derivative Lys(y) + PSI-MOD + Dimethyl + di-Methylation + MOD:00084 + + N6,N6-dimethyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6,N6-dimethyl-L-lysine. + OMSSA:36 + PubMed:10550045 + PubMed:12964758 + PubMed:14570711 + PubMed:3100523 + PubMed:8453381 + RESID:AA0075 + Unimod:36#K + + + + + (2S)-2-amino-6-(dimethylamino)hexanoic acid + + + + + + MOD_RES N6,N6-dimethyllysine + + + + + + N(zeta)-dimethyllysine + + + + + + N6,N6-dimethyl-L-lysine + + + + + + N6,N6-dimethylated L-lysine + + + + + + N6Me2Lys + + + + + + dimethylk + + + + + + epsilon-dimethyllysine + + + + + + lysine derivative Lys(y) + + + + + + Dimethyl + + + + + + di-Methylation + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 7 H 14 N 2 O 1 + 142.2 + 142.11061 + K + natural + Unimod:34 + uniprot.ptm:PTM-0194 + (2S)-2-amino-6-methylaminohexanoic acid + MOD_RES N6-methyllysine + N(zeta)-methyllysine + N-methyl Lysyl + N6-methyl-L-lysine + N6-methylated L-lysine + N6Me1Lys + epsilon-methyllysine + PSI-MOD + Methyl + Methylation + MOD:00085 + + N6-methyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine. + ChEBI:17604 + DeltaMass:165 + PubMed:11875433 + PubMed:3926756 + RESID:AA0076 + Unimod:34#K + + + + + (2S)-2-amino-6-methylaminohexanoic acid + + + + + + MOD_RES N6-methyllysine + + + + + + N(zeta)-methyllysine + + + + + + N-methyl Lysyl + + + + + + N6-methyl-L-lysine + + + + + + N6-methylated L-lysine + + + + + + N6Me1Lys + + + + + + epsilon-methyllysine + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-palmitoyl-L-lysine. + 238.41 + C 16 H 30 N 0 O 1 + 238.22966 + C 22 H 42 N 2 O 2 + 366.59 + 366.32462 + K + natural + Unimod:47 + uniprot.ptm:PTM-0197 + (2S)-2-amino-6-(hexadecanoylamino)hexanoic acid + 2-amino-6-(hexadecanamido)hexanoic acid + LIPID N6-palmitoyl lysine + N(zeta)-palmitoyllysine + N6-(1-oxohexadecyl)-L-lysine + N6-hexadecanoylated L-lysine + N6-palmitoyl-L-lysine + N6-palmitoylated L-lysine + N6PamLys + epsilon-palmitoyllysine + palmitoylationk + PSI-MOD + Palmitoyl + Palmitoylation + MOD:00086 + + N6-palmitoyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-palmitoyl-L-lysine. + OMSSA:93 + PubMed:2498336 + PubMed:7801126 + PubMed:7939682 + RESID:AA0077 + Unimod:47#K + + + + + (2S)-2-amino-6-(hexadecanoylamino)hexanoic acid + + + + + + 2-amino-6-(hexadecanamido)hexanoic acid + + + + + + LIPID N6-palmitoyl lysine + + + + + + N(zeta)-palmitoyllysine + + + + + + N6-(1-oxohexadecyl)-L-lysine + + + + + + N6-hexadecanoylated L-lysine + + + + + + N6-palmitoyl-L-lysine + + + + + + N6-palmitoylated L-lysine + + + + + + N6PamLys + + + + + + epsilon-palmitoyllysine + + + + + + palmitoylationk + + + + + + Palmitoyl + + + + + + Palmitoylation + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-myristoyl-L-lysine. + 210.36 + C 14 H 26 N 0 O 1 + 210.19836 + C 20 H 38 N 2 O 2 + 338.54 + 338.29333 + K + natural + Unimod:45 + uniprot.ptm:PTM-0196 + (2S)-2-amino-6-(tetradecanoylamino)hexanoic acid + 2-amino-6-(tetradecanamido)hexanoic acid + LIPID N6-myristoyl lysine + N(zeta)-myristoyllysine + N6-(1-oxotetradecyl)-L-lysine + N6-(C14:0 aliphatic acyl)lysine + N6-myristoyl-L-lysine + N6-myristoylated L-lysine + N6MyrLys + epsilon-myristoyllysine + myristoylationk + PSI-MOD + Myristoyl + Myristoylation + MOD:00087 + + N6-myristoyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-myristoyl-L-lysine. + OMSSA:81 + PubMed:1402651 + PubMed:8346241 + RESID:AA0078 + Unimod:45#K + + + + + (2S)-2-amino-6-(tetradecanoylamino)hexanoic acid + + + + + + 2-amino-6-(tetradecanamido)hexanoic acid + + + + + + LIPID N6-myristoyl lysine + + + + + + N(zeta)-myristoyllysine + + + + + + N6-(1-oxotetradecyl)-L-lysine + + + + + + N6-(C14:0 aliphatic acyl)lysine + + + + + + N6-myristoyl-L-lysine + + + + + + N6-myristoylated L-lysine + + + + + + N6MyrLys + + + + + + epsilon-myristoyllysine + + + + + + myristoylationk + + + + + + Myristoyl + + + + + + Myristoylation + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-palmitoyl-L-threonine. + 238.41 + C 16 H 30 N 0 O 1 + 238.22966 + C 20 H 37 N 1 O 3 + 339.52 + 339.27734 + T + natural + Unimod:47 + uniprot.ptm:PTM-0242 + (2S,3R)-2-amino-3-(hexadecanoyloxy)butanoic acid + L-threonine hexadecanoate ester + LIPID O-palmitoyl threonine + O-hexadecanoylated L-threonine + O-palmitoyl-L-threonine + O-palmitoylated L-threonine + O3-palmitoyl-threonine + OPamThr + palmitoylationt + threonine palmitate ester + PSI-MOD + Palmitoyl + Palmitoylation + MOD:00088 + + O-palmitoyl-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-palmitoyl-L-threonine. + OMSSA:95 + PubMed:6642431 + PubMed:8413602 + RESID:AA0079 + Unimod:47#T + + + + + (2S,3R)-2-amino-3-(hexadecanoyloxy)butanoic acid + + + + + + L-threonine hexadecanoate ester + + + + + + LIPID O-palmitoyl threonine + + + + + + O-hexadecanoylated L-threonine + + + + + + O-palmitoyl-L-threonine + + + + + + O-palmitoylated L-threonine + + + + + + O3-palmitoyl-threonine + + + + + + OPamThr + + + + + + palmitoylationt + + + + + + threonine palmitate ester + + + + + + Palmitoyl + + + + + + Palmitoylation + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-palmitoyl-L-serine. + 238.41 + C 16 H 30 N 0 O 1 + 238.22966 + C 19 H 35 N 1 O 3 + 325.49 + 325.2617 + S + natural + Unimod:47 + uniprot.ptm:PTM-0241 + (2S)-2-amino-3-(hexadecanoyloxy)propanoic acid + ACT_SITE O-palmitoyl serine intermediate + L-serine hexadecanoate ester + LIPID O-palmitoyl serine + O-hexadecanoylated L-serine + O-palmitoyl-L-serine + O-palmitoylated L-serine + O3-palmitoyl-serine + OPamSer + palmitoylations + serine palmitate ester + PSI-MOD + Palmitoyl + Palmitoylation + MOD:00089 + + O-palmitoyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-palmitoyl-L-serine. + OMSSA:94 + PubMed:3467339 + RESID:AA0080 + Unimod:47#S + + + + + (2S)-2-amino-3-(hexadecanoyloxy)propanoic acid + + + + + + ACT_SITE O-palmitoyl serine intermediate + + + + + + L-serine hexadecanoate ester + + + + + + LIPID O-palmitoyl serine + + + + + + O-hexadecanoylated L-serine + + + + + + O-palmitoyl-L-serine + + + + + + O-palmitoylated L-serine + + + + + + O3-palmitoyl-serine + + + + + + OPamSer + + + + + + palmitoylations + + + + + + serine palmitate ester + + + + + + Palmitoyl + + + + + + Palmitoylation + + + + + + + + + + + A protein modification that effectively converts an L-alanine residue to L-alanine amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 3 H 7 N 2 O 1 + 87.1 + 87.05584 + A + natural + C-term + uniprot.ptm:PTM-0057 + (2S)-2-aminopropanamide + AlaN + L-alanine amide + MOD_RES Alanine amide + alaninamide + amidated L-alanine + PSI-MOD + MOD:00090 + + L-alanine amide + + + + + A protein modification that effectively converts an L-alanine residue to L-alanine amide. + PubMed:1377792 + PubMed:2069951 + PubMed:8472537 + PubMed:952951 + RESID:AA0081 + + + + + (2S)-2-aminopropanamide + + + + + + AlaN + + + + + + L-alanine amide + + + + + + MOD_RES Alanine amide + + + + + + alaninamide + + + + + + amidated L-alanine + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to L-arginine amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 6 H 14 N 5 O 1 + 172.21 + 172.11984 + R + natural + C-term + uniprot.ptm:PTM-0060 + (2S)-2-amino-5-[(diaminomethylidene)amino]pentanamide + 2-amino-5-carbamimidamidopentanamide + 2-amino-5-guanidinopentanamide + ArgN + L-arginine amide + MOD_RES Arginine amide + amidated L-arginine + argininamide + PSI-MOD + MOD:00091 + + L-arginine amide + + + + + A protein modification that effectively converts an L-arginine residue to L-arginine amide. + ChEBI:145897 + PubMed:2229025 + PubMed:2753890 + PubMed:743209 + RESID:AA0082 + + + + + (2S)-2-amino-5-[(diaminomethylidene)amino]pentanamide + + + + + + 2-amino-5-carbamimidamidopentanamide + + + + + + 2-amino-5-guanidinopentanamide + + + + + + ArgN + + + + + + L-arginine amide + + + + + + MOD_RES Arginine amide + + + + + + amidated L-arginine + + + + + + argininamide + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to L-asparagine amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 4 H 8 N 3 O 2 + 130.13 + 130.06165 + N + natural + C-term + uniprot.ptm:PTM-0062 + (2S)-2-aminobutanediamide + AsnN + L-asparagine amide + MOD_RES Asparagine amide + amidated L-asparagine + asparaginamide + PSI-MOD + MOD:00092 + + L-asparagine amide + + + + + A protein modification that effectively converts an L-asparagine residue to L-asparagine amide. + ChEBI:145898 + PubMed:2753132 + PubMed:279902 + PubMed:3415690 + RESID:AA0083 + + + + + (2S)-2-aminobutanediamide + + + + + + AsnN + + + + + + L-asparagine amide + + + + + + MOD_RES Asparagine amide + + + + + + amidated L-asparagine + + + + + + asparaginamide + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-aspartic acid 1-amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 4 H 7 N 2 O 3 + 131.11 + 131.04567 + D + natural + C-term + uniprot.ptm:PTM-0063 + (2S)-2-amino-1-butanediamic acid + 1-amidated L-aspartic acid + 3,4-diamino-4-oxobutanoic acid + 3-amino-succinamic acid + AspN + L-aspartic acid 1-amide + MOD_RES Aspartic acid 1-amide + alpha-asparagine + isoasparagine + PSI-MOD + MOD:00093 + + L-aspartic acid 1-amide + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-aspartic acid 1-amide. + PubMed:2542051 + RESID:AA0084 + + + + + (2S)-2-amino-1-butanediamic acid + + + + + + 1-amidated L-aspartic acid + + + + + + 3,4-diamino-4-oxobutanoic acid + + + + + + 3-amino-succinamic acid + + + + + + AspN + + + + + + L-aspartic acid 1-amide + + + + + + MOD_RES Aspartic acid 1-amide + + + + + + alpha-asparagine + + + + + + isoasparagine + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteine amide. + -0.98 + C 0 H 1 N 1 O -1 S 0 + -0.984016 + C 3 H 7 N 2 O 1 S 1 + 119.16 + 119.02791 + C + natural + C-term + uniprot.ptm:PTM-0102 + (2R)-2-amino-3-sulfanylpropanamide + 2-amino-3-mercaptopropanamide + CysN + L-cysteine amide + MOD_RES Cysteine amide + amidated L-cysteine + cysteinamide + PSI-MOD + MOD:00094 + + L-cysteine amide + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteine amide. + PubMed:1892838 + PubMed:7149738 + RESID:AA0085 + + + + + (2R)-2-amino-3-sulfanylpropanamide + + + + + + 2-amino-3-mercaptopropanamide + + + + + + CysN + + + + + + L-cysteine amide + + + + + + MOD_RES Cysteine amide + + + + + + amidated L-cysteine + + + + + + cysteinamide + + + + + + + + + + + A protein modification that effectively converts an L-glutamine residue to L-glutamine amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 5 H 10 N 3 O 2 + 144.15 + 144.0773 + Q + natural + C-term + uniprot.ptm:PTM-0130 + (2S)-2-aminopentanediamide + GlnN + L-glutamine amide + MOD_RES Glutamine amide + amidated L-glutamine + glutaminamide + PSI-MOD + MOD:00095 + + L-glutamine amide + + + + + A protein modification that effectively converts an L-glutamine residue to L-glutamine amide. + PubMed:7673220 + PubMed:9048550 + RESID:AA0086 + + + + + (2S)-2-aminopentanediamide + + + + + + GlnN + + + + + + L-glutamine amide + + + + + + MOD_RES Glutamine amide + + + + + + amidated L-glutamine + + + + + + glutaminamide + + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-glutamic acid 1-amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 5 H 9 N 2 O 3 + 145.14 + 145.06131 + E + natural + C-term + uniprot.ptm:PTM-0129 + (2S)-2-amino-1-pentanediamic acid + 1-amidated L-glutamic acid + 4,5-diamino-5-oxopentanoic acid + GluN + L-glutamic acid 1-amide + MOD_RES Glutamic acid 1-amide + isoglutamine + PSI-MOD + MOD:00096 + + L-glutamic acid 1-amide + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-glutamic acid 1-amide. + PubMed:1093875 + PubMed:14550575 + RESID:AA0087 + + + + + (2S)-2-amino-1-pentanediamic acid + + + + + + 1-amidated L-glutamic acid + + + + + + 4,5-diamino-5-oxopentanoic acid + + + + + + GluN + + + + + + L-glutamic acid 1-amide + + + + + + MOD_RES Glutamic acid 1-amide + + + + + + isoglutamine + + + + + + + + + + + A protein modification that effectively converts a glycine residue to glycine amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 2 H 5 N 2 O 1 + 73.07 + 73.04019 + G + natural + C-term + uniprot.ptm:PTM-0132 + 2-aminoacetamide + 2-aminoethanamide + 2-azanylethanamide + GlyN + MOD_RES Glycine amide + amidated glycine + glycinamide + glycine amide + PSI-MOD + MOD:00097 + + glycine amide + + + + + A protein modification that effectively converts a glycine residue to glycine amide. + PubMed:13591312 + RESID:AA0088 + + + + + 2-aminoacetamide + + + + + + 2-aminoethanamide + + + + + + 2-azanylethanamide + + + + + + GlyN + + + + + + MOD_RES Glycine amide + + + + + + amidated glycine + + + + + + glycinamide + + + + + + glycine amide + + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to L-histidine amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 6 H 9 N 4 O 1 + 153.16 + 153.07764 + H + natural + C-term + uniprot.ptm:PTM-0148 + (2S)-2-amino-3-(1H-imidazol-4-yl)propanamide + HisN + L-histidine amide + MOD_RES Histidine amide + amidated L-histidine + histidinamide + PSI-MOD + MOD:00098 + + L-histidine amide + + + + + A protein modification that effectively converts an L-histidine residue to L-histidine amide. + PubMed:2153586 + PubMed:2307683 + PubMed:2839478 + RESID:AA0089 + + + + + (2S)-2-amino-3-(1H-imidazol-4-yl)propanamide + + + + + + HisN + + + + + + L-histidine amide + + + + + + MOD_RES Histidine amide + + + + + + amidated L-histidine + + + + + + histidinamide + + + + + + + + + + + A protein modification that effectively converts an L-isoleucine residue to L-isoleucine amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 6 H 13 N 2 O 1 + 129.18 + 129.10278 + I + natural + C-term + uniprot.ptm:PTM-0161 + (2S,3S)-2-amino-3-methylpentanamide + IleN + L-isoleucine amide + MOD_RES Isoleucine amide + amidated L-isoleucine + isoleucinamide + PSI-MOD + MOD:00099 + + L-isoleucine amide + + + + + A protein modification that effectively converts an L-isoleucine residue to L-isoleucine amide. + RESID:AA0090 + + + + + (2S,3S)-2-amino-3-methylpentanamide + + + + + + IleN + + + + + + L-isoleucine amide + + + + + + MOD_RES Isoleucine amide + + + + + + amidated L-isoleucine + + + + + + isoleucinamide + + + + + + + + + + + A protein modification that effectively converts an L-leucine residue to L-leucine amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 6 H 13 N 2 O 1 + 129.18 + 129.10278 + L + natural + C-term + uniprot.ptm:PTM-0166 + (2S)-2-amino-4-methylpentanamide + 2-amino-4-methylvaleramide + 2-azanyl-4-methylpentanamide + L-leucine amide + LeuN + MOD_RES Leucine amide + alpha-aminoisocaproamide + amidated L-leucine + leucinamide + PSI-MOD + MOD:00100 + + L-leucine amide + + + + + A protein modification that effectively converts an L-leucine residue to L-leucine amide. + PubMed:2578459 + RESID:AA0091 + + + + + (2S)-2-amino-4-methylpentanamide + + + + + + 2-amino-4-methylvaleramide + + + + + + 2-azanyl-4-methylpentanamide + + + + + + L-leucine amide + + + + + + LeuN + + + + + + MOD_RES Leucine amide + + + + + + alpha-aminoisocaproamide + + + + + + amidated L-leucine + + + + + + leucinamide + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to L-lysine amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 6 H 14 N 3 O 1 + 144.2 + 144.1137 + K + natural + C-term + uniprot.ptm:PTM-0168 + (2S)-2,6-diaminohexanamide + L-lysine amide + LysN + MOD_RES Lysine amide + amidated L-lysine + lysinamide + PSI-MOD + MOD:00101 + + L-lysine amide + + + + + A protein modification that effectively converts an L-lysine residue to L-lysine amide. + PubMed:6579533 + RESID:AA0092 + + + + + (2S)-2,6-diaminohexanamide + + + + + + L-lysine amide + + + + + + LysN + + + + + + MOD_RES Lysine amide + + + + + + amidated L-lysine + + + + + + lysinamide + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to L-methionine amide. + -0.98 + C 0 H 1 N 1 O -1 S 0 + -0.984016 + C 5 H 11 N 2 O 1 S 1 + 147.22 + 147.0592 + M + natural + C-term + uniprot.ptm:PTM-0164 + (2S)-2-amino-4-(methylsulfanyl)butanamide + 2-amino-4-(methylthio)butanamide + L-methionine amide + MOD_RES Methionine amide + MetN + amidated L-methionine + methioninamide + PSI-MOD + MOD:00102 + + L-methionine amide + + + + + methioninamide + + + + + + A protein modification that effectively converts an L-methionine residue to L-methionine amide. + PubMed:4375977 + RESID:AA0093 + + + + + (2S)-2-amino-4-(methylsulfanyl)butanamide + + + + + + 2-amino-4-(methylthio)butanamide + + + + + + L-methionine amide + + + + + + MOD_RES Methionine amide + + + + + + MetN + + + + + + amidated L-methionine + + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to L-phenylalanine amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 9 H 11 N 2 O 1 + 163.2 + 163.08714 + F + natural + C-term + uniprot.ptm:PTM-0248 + (2S)-2-amino-3-phenylpropanamide + L-phenylalanine amide + MOD_RES Phenylalanine amide + PheN + amidated L-phenylalanine + phenylalaninamide + PSI-MOD + MOD:00103 + + L-phenylalanine amide + + + + + A protein modification that effectively converts an L-phenylalanine residue to L-phenylalanine amide. + PubMed:2905621 + PubMed:8868490 + RESID:AA0094 + + + + + (2S)-2-amino-3-phenylpropanamide + + + + + + L-phenylalanine amide + + + + + + MOD_RES Phenylalanine amide + + + + + + PheN + + + + + + amidated L-phenylalanine + + + + + + phenylalaninamide + + + + + + + + + + + A protein modification that effectively converts an L-proline residue to L-proline amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 5 H 9 N 2 O 1 + 113.14 + 113.07149 + P + natural + C-term + uniprot.ptm:PTM-0257 + (2S)-pyrrolidine-2-carboxamide + L-proline amide + MOD_RES Proline amide + ProN + amidated L-proline + prolinamide + PSI-MOD + MOD:00104 + + L-proline amide + + + + + A protein modification that effectively converts an L-proline residue to L-proline amide. + PubMed:4982117 + PubMed:5760861 + RESID:AA0095 + + + + + (2S)-pyrrolidine-2-carboxamide + + + + + + L-proline amide + + + + + + MOD_RES Proline amide + + + + + + ProN + + + + + + amidated L-proline + + + + + + prolinamide + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to L-serine amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 3 H 7 N 2 O 2 + 103.1 + 103.05075 + S + natural + C-term + uniprot.ptm:PTM-0275 + (2S)-2-amino-3-hydroxypropanamide + L-serine amide + MOD_RES Serine amide + SerN + amidated L-serine + serinamide + PSI-MOD + MOD:00105 + + L-serine amide + + + + + A protein modification that effectively converts an L-serine residue to L-serine amide. + PubMed:743209 + RESID:AA0096 + + + + + (2S)-2-amino-3-hydroxypropanamide + + + + + + L-serine amide + + + + + + MOD_RES Serine amide + + + + + + SerN + + + + + + amidated L-serine + + + + + + serinamide + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to L-threonine amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 4 H 9 N 2 O 2 + 117.13 + 117.06641 + T + natural + C-term + uniprot.ptm:PTM-0293 + (2S,3R)-2-amino-3-hydroxybutanamide + L-threonine amide + MOD_RES Threonine amide + ThrN + amidated L-threonine + threoninamide + PSI-MOD + MOD:00106 + + L-threonine amide + + + + + A protein modification that effectively converts an L-threonine residue to L-threonine amide. + PubMed:1390774 + RESID:AA0097 + + + + + (2S,3R)-2-amino-3-hydroxybutanamide + + + + + + L-threonine amide + + + + + + MOD_RES Threonine amide + + + + + + ThrN + + + + + + amidated L-threonine + + + + + + threoninamide + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to L-tryptophan amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 11 H 12 N 3 O 1 + 202.24 + 202.09804 + W + natural + C-term + uniprot.ptm:PTM-0296 + (2S)-2-amino-3-(1H-indol-3-yl)propanamide + L-tryptophan amide + MOD_RES Tryptophan amide + TrpN + amidated L-tryptophan + tryptophanamide + PSI-MOD + MOD:00107 + + L-tryptophan amide + + + + + A protein modification that effectively converts an L-tryptophan residue to L-tryptophan amide. + PubMed:3947348 + RESID:AA0098 + + + + + (2S)-2-amino-3-(1H-indol-3-yl)propanamide + + + + + + L-tryptophan amide + + + + + + MOD_RES Tryptophan amide + + + + + + TrpN + + + + + + amidated L-tryptophan + + + + + + tryptophanamide + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to L-tyrosine amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 9 H 11 N 2 O 2 + 179.2 + 179.08205 + Y + natural + C-term + uniprot.ptm:PTM-0302 + (2S)-2-amino-3-(4-hydoxyphenyl)propanamide + L-tyrosine amide + MOD_RES Tyrosine amide + TyrN + amidated L-tyrosine + tyrosinamide + PSI-MOD + MOD:00108 + + L-tyrosine amide + + + + + A protein modification that effectively converts an L-tyrosine residue to L-tyrosine amide. + PubMed:1377792 + PubMed:3562898 + PubMed:6509012 + RESID:AA0099 + + + + + (2S)-2-amino-3-(4-hydoxyphenyl)propanamide + + + + + + L-tyrosine amide + + + + + + MOD_RES Tyrosine amide + + + + + + TyrN + + + + + + amidated L-tyrosine + + + + + + tyrosinamide + + + + + + + + + + + A protein modification that effectively converts an L-valine residue to L-valine amide. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 5 H 11 N 2 O 1 + 115.16 + 115.087135 + V + natural + C-term + uniprot.ptm:PTM-0303 + (2S)-2-amino-3-methylbutanamide + L-valine amide + MOD_RES Valine amide + ValN + valinamide + PSI-MOD + MOD:00109 + + L-valine amide + + + + + A protein modification that effectively converts an L-valine residue to L-valine amide. + PubMed:2578459 + PubMed:5465996 + RESID:AA0100 + + + + + (2S)-2-amino-3-methylbutanamide + + + + + + L-valine amide + + + + + + MOD_RES Valine amide + + + + + + ValN + + + + + + valinamide + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl disulfide. + 46.09 + C 1 H 2 N 0 O 0 S 1 + 45.98772 + C 4 H 7 N 1 O 1 S 2 + 149.23 + 148.9969 + C + natural + Unimod:39 + uniprot.ptm:PTM-0104 + (2R)-2-amino-3-(methyldisulfanediyl)propanoic acid + 2-amino-3-(methyldisulfanediyl)propanoic acid + 2-amino-3-(methyldithio)propanoic acid + 2-amino-3-methyldisulfanylpropanoic acid + 2-azanyl-3-(methyldisulfanediyl)-propanoic acid + L-3-(methyldithio)alanine + L-cysteine methyl disulfide + MOD_RES Cysteine methyl disulfide + S-methylthio-L-cysteine + S-methylthiocysteine + methyl methanethiolsulfonate derivatized cysteine + methyl methanethiosulfonate derivatized cysteine + mmts + PSI-MOD + Beta-methylthiolation + Methylthio + MOD:00110 + Produced artifactually by reaction of cysteine residues with methyl methanethiosulfonate (MMTS) [JSG], but also naturally in bacteria [PMT]. + L-cysteine methyl disulfide + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl disulfide. + OMSSA:179 + PubMed:10555576 + PubMed:163643 + PubMed:2056535 + PubMed:6381494 + RESID:AA0101 + Unimod:39#C + + + + + (2R)-2-amino-3-(methyldisulfanediyl)propanoic acid + + + + + + 2-amino-3-(methyldisulfanediyl)propanoic acid + + + + + + 2-amino-3-(methyldithio)propanoic acid + + + + + + 2-amino-3-methyldisulfanylpropanoic acid + + + + + + 2-azanyl-3-(methyldisulfanediyl)-propanoic acid + + + + + + L-3-(methyldithio)alanine + + + + + + L-cysteine methyl disulfide + + + + + + MOD_RES Cysteine methyl disulfide + + + + + + S-methylthio-L-cysteine + + + + + + S-methylthiocysteine + + + + + + methyl methanethiolsulfonate derivatized cysteine + + + + + + methyl methanethiosulfonate derivatized cysteine + + + + + + mmts + + + + + + Beta-methylthiolation + + + + + + Methylthio + + + + + + Methylthio + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine. + 204.36 + C 15 H 24 N 0 O 0 S 0 + 204.1878 + C 18 H 29 N 1 O 1 S 1 + 307.5 + 307.197 + C + natural + Unimod:44 + uniprot.ptm:PTM-0277 + (2R)-2-amino-3-([(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid + 2-amino-3-(3,7,11-trimethyl-2,6,10-dodecatrienylthio)propanoic acid + LIPID S-farnesyl cysteine + S-farnesyl Cystenyl + S-farnesyl-L-cysteine + SFarnCys + farnesylationc + PSI-MOD + Farnesyl + Farnesylation + MOD:00111 + + From DeltaMass: (name misspelled "S-farnesyl cystenyl") + S-farnesyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine. + DeltaMass:293 + OMSSA:42 + PubMed:1409665 + PubMed:15609361 + PubMed:1872463 + PubMed:2684976 + RESID:AA0102 + Unimod:44#C + + + + + (2R)-2-amino-3-([(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid + + + + + + 2-amino-3-(3,7,11-trimethyl-2,6,10-dodecatrienylthio)propanoic acid + + + + + + LIPID S-farnesyl cysteine + + + + + + S-farnesyl Cystenyl + + + + + + S-farnesyl-L-cysteine + + + + + + SFarnCys + + + + + + farnesylationc + + + + + + Farnesyl + + + + + + Farnesylation + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine. + 220.36 + C 15 H 24 N 0 O 1 S 0 + 220.18271 + C 18 H 29 N 1 O 2 S 1 + 323.5 + 323.1919 + C + natural + Unimod:376 + uniprot.ptm:PTM-0269 + (2R)-2-amino-3-([(2E,6E,10Z)-12-hydroxy-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid + 2-amino-3-(12-hydroxy-3,7,11-trimethyl-3,6,10-dodecatrienylthio)propanoic acid + LIPID S-12-hydroxyfarnesyl cysteine + S-12-hydroxyfarnesyl-L-cysteine + S12HyFarnCys + PSI-MOD + Hydroxyfarnesyl + hydroxyfarnesyl + MOD:00112 + S-12-hydroxyfarnesyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine. + PubMed:17790543 + RESID:AA0103 + Unimod:376 + + + + + (2R)-2-amino-3-([(2E,6E,10Z)-12-hydroxy-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid + + + + + + 2-amino-3-(12-hydroxy-3,7,11-trimethyl-3,6,10-dodecatrienylthio)propanoic acid + + + + + + LIPID S-12-hydroxyfarnesyl cysteine + + + + + + S-12-hydroxyfarnesyl-L-cysteine + + + + + + S12HyFarnCys + + + + + + Hydroxyfarnesyl + + + + + + hydroxyfarnesyl + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine. + 272.48 + C 20 H 32 N 0 O 0 S 0 + 272.2504 + C 23 H 37 N 1 O 1 S 1 + 375.62 + 375.25958 + C + natural + Unimod:48 + uniprot.ptm:PTM-0278 + (2R)-2-amino-3-([(2E,6E,10Z)-12-hydroxy-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid + 2-amino-3-(3,7,11,15-tetramethyl-2,6,10,14-hexadecatetraenylthio)propanoic acid + LIPID S-geranylgeranyl cysteine + S-geranylgeranyl + S-geranylgeranyl-L-cysteine + SGergerCys + geranylgeranylc + PSI-MOD + Geranyl-geranyl + GeranylGeranyl + MOD:00113 + + DeltaMass calculates the mass with two double bonds rather than four + S-geranylgeranyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine. + DeltaMass:0 + OMSSA:49 + PubMed:1483450 + PubMed:15609361 + RESID:AA0104 + Unimod:48#C + + + + + (2R)-2-amino-3-([(2E,6E,10Z)-12-hydroxy-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid + + + + + + 2-amino-3-(3,7,11,15-tetramethyl-2,6,10,14-hexadecatetraenylthio)propanoic acid + + + + + + LIPID S-geranylgeranyl cysteine + + + + + + S-geranylgeranyl + + + + + + S-geranylgeranyl-L-cysteine + + + + + + SGergerCys + + + + + + geranylgeranylc + + + + + + Geranyl-geranyl + + + + + + GeranylGeranyl + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl ester. + 14.03 + C 1 H 2 N 0 O 0 S 0 + 14.01565 + C 4 H 8 N 1 O 2 S 1 + 134.17 + 134.02757 + C + natural + C-term + Unimod:34 + uniprot.ptm:PTM-0105 + 2-amino-3-mercaptopropanoic methyl ester + 2-amino-3-sulfanylpropanoic methyl ester + L-cysteine methyl ester + MOD_RES Cysteine methyl ester + OMeCys + mecysteine + methyl (2R)-2-amino-3-sulfanylpropanoate + methyl L-cysteinate + methyl esterified L-cysteine + PSI-MOD + Methyl + Methylation + MOD:00114 + + Secondary to RESID:AA0102; secondary to RESID:AA0103; secondary to RESID:AA0104. + L-cysteine methyl ester + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl ester. + PubMed:11875433 + PubMed:1872463 + RESID:AA0105 + Unimod:34#C-term + + + + + 2-amino-3-mercaptopropanoic methyl ester + + + + + + 2-amino-3-sulfanylpropanoic methyl ester + + + + + + L-cysteine methyl ester + + + + + + MOD_RES Cysteine methyl ester + + + + + + OMeCys + + + + + + mecysteine + + + + + + methyl (2R)-2-amino-3-sulfanylpropanoate + + + + + + methyl L-cysteinate + + + + + + methyl esterified L-cysteine + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-palmitoyl-L-cysteine. + 238.41 + C 16 H 30 N 0 O 1 S 0 + 238.22966 + C 19 H 35 N 1 O 2 S 1 + 341.55 + 341.23886 + C + natural + Unimod:47 + uniprot.ptm:PTM-0281 + (2R)-2-amino-3-(hexadecanoylsulfanyl)propanoic acid + 2-amino-3-(hexadecanoylthio)propanoic acid + ACT_SITE S-palmitoyl cysteine intermediate + LIPID S-palmitoyl cysteine + S-hexadecanoylated L-cysteine + S-palmitoyl-L-cysteine + S-palmitoylated L-cysteine + S-palmityl Cystenyl + SPamCys + cysteine hexadecanoate thioester + cysteine palmitate thioester + PSI-MOD + Palmitoyl + Palmitoylation + MOD:00115 + + From DeltaMass: (name misspelled "S-palmityl Cystenyl" and formula incorrect, N and O reversed) Formula: C19H35O1N2S1 Monoisotopic Mass Change: 341.239 Average Mass Change: 341.556 + S-palmitoyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-palmitoyl-L-cysteine. + DeltaMass:303 + PubMed:1872406 + PubMed:3166978 + PubMed:8180229 + PubMed:8824274 + RESID:AA0106 + Unimod:47#C + + + + + (2R)-2-amino-3-(hexadecanoylsulfanyl)propanoic acid + + + + + + 2-amino-3-(hexadecanoylthio)propanoic acid + + + + + + ACT_SITE S-palmitoyl cysteine intermediate + + + + + + LIPID S-palmitoyl cysteine + + + + + + S-hexadecanoylated L-cysteine + + + + + + S-palmitoyl-L-cysteine + + + + + + S-palmitoylated L-cysteine + + + + + + S-palmityl Cystenyl + + + + + + SPamCys + + + + + + cysteine hexadecanoate thioester + + + + + + cysteine palmitate thioester + + + + + + Palmitoyl + + + + + + Palmitoylation + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-diacylglycerol-L-cysteine. + C + natural + uniprot.ptm:PTM-0274 + (2R)-2-amino-3-[(2S)-2-((9Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]sulfanylpropanoic acid + 2-amino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]thiopropanoic acid + LIPID S-diacylglycerol cysteine + S-(1-2'-oleoyl-3'-palmitoyl-glycerol)cysteine + S-(2',3'-diacylglycerol)-L-cysteine + S-diacylglycerol-L-cysteine + SAcyl2GlyceroCys + PSI-MOD + Diacylglycerol + diacylglycerol + MOD:00116 + + Incidental to RESID:AA0060. + S-diacylglycerol-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-diacylglycerol-L-cysteine. + PubMed:10896212 + PubMed:4575979 + PubMed:9056182 + RESID:AA0107 + Unimod:377#C + + + + + (2R)-2-amino-3-[(2S)-2-((9Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]sulfanylpropanoic acid + + + + + + 2-amino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]thiopropanoic acid + + + + + + LIPID S-diacylglycerol cysteine + + + + + + S-(1-2'-oleoyl-3'-palmitoyl-glycerol)cysteine + + + + + + S-(2',3'-diacylglycerol)-L-cysteine + + + + + + S-diacylglycerol-L-cysteine + + + + + + SAcyl2GlyceroCys + + + + + + Diacylglycerol + + + + + + diacylglycerol + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-glutamine residue by a thioester bond with the formation of S-(L-isoglutamyl)-L-cysteine and the release of ammonia. + -17.03 + C 0 H -3 N -1 O 0 S 0 + -17.026548 + C 8 H 10 N 2 O 3 S 1 + 214.24 + 214.04121 + C, Q + natural + uniprot.ptm:PTM-0156 + (2S)-2-amino-5-[(2R)-2-amino-2-carboxyethyl]sulfanyl-5-oxopentanoic acid + (S,R)-2-amino-4-[S-(2-amino-2-carboxyethyl)thiocarboxy]butanoic acid + 2-amino-5-(2-amino-2-carboxyethyl)thio-5-oxopentanoic acid + CROSSLNK Isoglutamyl cysteine thioester (Cys-Gln) + S-(L-isoglutamyl)-L-cysteine + S-gamma-glutamyl (crosslinked to cysteine) + XLNK-SCys-5Glu(Gln) + gamma-(S-cysteinyl)glutamic acid + PSI-MOD + MOD:00117 + + Cross-link 2; DeltaMass calculates the mass difference from glutamic acid rather than glutamine. + S-(L-isoglutamyl)-L-cysteine + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-glutamine residue by a thioester bond with the formation of S-(L-isoglutamyl)-L-cysteine and the release of ammonia. + ChEBI:22021 + DeltaMass:0 + PubMed:6838833 + RESID:AA0108 + + + + + (2S)-2-amino-5-[(2R)-2-amino-2-carboxyethyl]sulfanyl-5-oxopentanoic acid + + + + + + (S,R)-2-amino-4-[S-(2-amino-2-carboxyethyl)thiocarboxy]butanoic acid + + + + + + 2-amino-5-(2-amino-2-carboxyethyl)thio-5-oxopentanoic acid + + + + + + CROSSLNK Isoglutamyl cysteine thioester (Cys-Gln) + + + + + + S-(L-isoglutamyl)-L-cysteine + + + + + + S-gamma-glutamyl (crosslinked to cysteine) + + + + + + XLNK-SCys-5Glu(Gln) + + + + + + gamma-(S-cysteinyl)glutamic acid + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-histidine residue by a thioether bond to form 2'-(S-L-cysteinyl)-L-histidine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 9 H 10 N 4 O 2 S 1 + 238.26 + 238.05244 + C, H + natural + uniprot.ptm:PTM-0005 + (2R)-2-amino-3-[(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-2-yl)sulfanyl]propanoic acid + (2S)-2-amino-3-[2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-1H-imidazol-4-yl]propanoic acid + 2'-(L-cystein-S-yl)-L-histidine + CROSSLNK 2'-(S-cysteinyl)-histidine (Cys-His) + S-(2'-histidyl)cysteine + S-(2-histidyl)- (crosslinked to cysteine) + XLNK-SCys-2'His + PSI-MOD + MOD:00118 + Cross-link 2. + 2'-(S-L-cysteinyl)-L-histidine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-histidine residue by a thioether bond to form 2'-(S-L-cysteinyl)-L-histidine. + DeltaMass:0 + PubMed:6210696 + RESID:AA0109 + + + + + (2R)-2-amino-3-[(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-2-yl)sulfanyl]propanoic acid + + + + + + (2S)-2-amino-3-[2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-1H-imidazol-4-yl]propanoic acid + + + + + + 2'-(L-cystein-S-yl)-L-histidine + + + + + + CROSSLNK 2'-(S-cysteinyl)-histidine (Cys-His) + + + + + + S-(2'-histidyl)cysteine + + + + + + S-(2-histidyl)- (crosslinked to cysteine) + + + + + + XLNK-SCys-2'His + + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form L-lanthionine. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 6 H 8 N 2 O 2 S 1 + 172.2 + 172.03065 + C, S + artifact + (2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid) + (R)-S-(2-amino-2-carboxyethyl)-L-cysteine + (R,R)-2,6-diamino-4-thiaheptanedioic acid + (R,R)-3,3'-thiobis-(2-aminopropanoic acid) + (R,R)-bis(2-amino-2-carboxyethyl)sulfide + 2-amino-3-(2-amino-2-carboxyethyl)sulfanylpropanoic acid + 3,3'-thiobis-L-alanine + L-lanthionine + XLNK-SCys-(L)3Dha + PSI-MOD + MOD:00119 + Cross-link 2. The natural occurrence of this modification is rare. For the more common modification see MOD:00120 meso-lanthionine [JSG]. + L-lanthionine (Cys-Ser) + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form L-lanthionine. + ChEBI:21347 + DeltaMass:7 + RESID:AA0110#CSX + + + + + (2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid) + + + + + + (R)-S-(2-amino-2-carboxyethyl)-L-cysteine + + + + + + (R,R)-2,6-diamino-4-thiaheptanedioic acid + + + + + + (R,R)-3,3'-thiobis-(2-aminopropanoic acid) + + + + + + (R,R)-bis(2-amino-2-carboxyethyl)sulfide + + + + + + 2-amino-3-(2-amino-2-carboxyethyl)sulfanylpropanoic acid + + + + + + 3,3'-thiobis-L-alanine + + + + + + L-lanthionine + + + + + + XLNK-SCys-(L)3Dha + + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form meso-lanthionine. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 6 H 8 N 2 O 2 S 1 + 172.2 + 172.03065 + C, S + natural + uniprot.ptm:PTM-0164 + (2R,2'S)-3,3'-sulfanediylbis(2-aminopropanoic acid) + (2R,2'S)-3,3'-thiobis-(2-aminopropanoic acid) + (2R,6S)-2,6-diamino-4-thiaheptanedioic acid + (2R,6S)-meso-lanthionine + (2S)-2-amino-3-[[(2R)-2-amino-2-carboxyethyl]sulfanyl]propanoic acid + (R)-S-(2-amino-2-carboxyethyl)-D-cysteine + (R,S)-bis(2-amino-2-carboxyethyl)sulfide + 3,3'-thiobis-meso-alanine + CROSSLNK Lanthionine (Cys-Ser) + CROSSLNK Lanthionine (Ser-Cys) + XLNK-SCys-(D)3Dha + cysteine-3-D-alanine thioether + meso-lanthionine + PSI-MOD + (2S,6R)-meso-lanthionine + MOD:00120 + Cross-link 2. + meso-lanthionine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form meso-lanthionine. + PubMed:15023056 + PubMed:3769923 + RESID:AA0111 + + + + + (2R,2'S)-3,3'-sulfanediylbis(2-aminopropanoic acid) + + + + + + (2R,2'S)-3,3'-thiobis-(2-aminopropanoic acid) + + + + + + (2R,6S)-2,6-diamino-4-thiaheptanedioic acid + + + + + + (2R,6S)-meso-lanthionine + + + + + + (2S)-2-amino-3-[[(2R)-2-amino-2-carboxyethyl]sulfanyl]propanoic acid + + + + + + (R)-S-(2-amino-2-carboxyethyl)-D-cysteine + + + + + + (R,S)-bis(2-amino-2-carboxyethyl)sulfide + + + + + + 3,3'-thiobis-meso-alanine + + + + + + CROSSLNK Lanthionine (Cys-Ser) + + + + + + CROSSLNK Lanthionine (Ser-Cys) + + + + + + XLNK-SCys-(D)3Dha + + + + + + cysteine-3-D-alanine thioether + + + + + + meso-lanthionine + + + + + + (2S,6R)-meso-lanthionine + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form (2S,3S,2'R)-3-methyllanthionine. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 7 H 10 N 2 O 2 S 1 + 186.23 + 186.0463 + C, T + natural + uniprot.ptm:PTM-0067 + (2S,3S)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)butanoic acid + (2S,3S,2'R)-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid + (2S,3S,2'R)-3-methyllanthionine + (2S,3S,6R)-2,6-diamino-3-methyl-4-thiaheptanedioic acid + (2S,3S,6R)-3-methyllanthionine + (2S-[2R*,3R*(S*)])-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid + 3-methyl-D,L-lanthionine + CROSSLNK Beta-methyllanthionine (Cys-Thr) + CROSSLNK Beta-methyllanthionine (Thr-Cys) + XLNK-SCys-3Dhb + cysteine-3-D-butyrine thioether + PSI-MOD + MOD:00121 + Cross-link 2. + (2S,3S,2'R)-3-methyllanthionine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form (2S,3S,2'R)-3-methyllanthionine. + PubMed:3769923 + RESID:AA0112 + + + + + (2S,3S)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)butanoic acid + + + + + + (2S,3S,2'R)-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid + + + + + + (2S,3S,2'R)-3-methyllanthionine + + + + + + (2S,3S,6R)-2,6-diamino-3-methyl-4-thiaheptanedioic acid + + + + + + (2S,3S,6R)-3-methyllanthionine + + + + + + (2S-[2R*,3R*(S*)])-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid + + + + + + 3-methyl-D,L-lanthionine + + + + + + CROSSLNK Beta-methyllanthionine (Cys-Thr) + + + + + + CROSSLNK Beta-methyllanthionine (Thr-Cys) + + + + + + XLNK-SCys-3Dhb + + + + + + cysteine-3-D-butyrine thioether + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-tyrosine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 12 H 12 N 2 O 3 S 1 + 264.3 + 264.05685 + C, Y + natural + uniprot.ptm:PTM-0019 + (2S)-2-amino-3-(3-[(2R)2-amino-2-carboxyethylsulfanyl]-4-hydroxyphenyl)propanoic acid + 2-amino-3-[3-(2-amino-2-carboxyethylthio)-4-hydroxyphenyl]propanoic acid + 3'-(L-cystein-S-yl)-L-tyrosine + 3'-(cystein-S-yl)tyrosine + CROSSLNK 3'-(S-cysteinyl)-tyrosine (Cys-Tyr) + CROSSLNK 3'-(S-cysteinyl)-tyrosine (Tyr-Cys) + S-(3-Tyr) (Crosslinked to Cysteine) + S-(tyros-3'-yl)cysteine + XLNK-SCys-3'Tyr + PSI-MOD + MOD:00122 + Cross-link 2. + 3'-(S-L-cysteinyl)-L-tyrosine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-tyrosine. + DeltaMass:0 + PubMed:15917234 + PubMed:2002850 + RESID:AA0113 + + + + + (2S)-2-amino-3-(3-[(2R)2-amino-2-carboxyethylsulfanyl]-4-hydroxyphenyl)propanoic acid + + + + + + 2-amino-3-[3-(2-amino-2-carboxyethylthio)-4-hydroxyphenyl]propanoic acid + + + + + + 3'-(L-cystein-S-yl)-L-tyrosine + + + + + + 3'-(cystein-S-yl)tyrosine + + + + + + CROSSLNK 3'-(S-cysteinyl)-tyrosine (Cys-Tyr) + + + + + + CROSSLNK 3'-(S-cysteinyl)-tyrosine (Tyr-Cys) + + + + + + S-(3-Tyr) (Crosslinked to Cysteine) + + + + + + S-(tyros-3'-yl)cysteine + + + + + + XLNK-SCys-3'Tyr + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-carboxy-L-lysine. + 44.01 + C 1 H 0 N 0 O 2 + 43.98983 + C 7 H 12 N 2 O 3 + 172.18 + 172.0848 + K + natural + Unimod:299 + uniprot.ptm:PTM-0191 + (2S)-2-amino-6-(carboxyamino)hexanoic acid + 2-amino-6-carbamic hexanoic acid + MOD_RES N6-carboxylysine + N6-carboxy-L-lysine + N6-carboxylysine + N6CbxLys + lysine NZ-carboxylic acid + PSI-MOD + Carboxy + Carboxylation + N6-carbamyllysine + MOD:00123 + + N6-carboxy-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-carboxy-L-lysine. + PubMed:11369851 + PubMed:4436319 + PubMed:637859 + PubMed:7754395 + RESID:AA0114 + Unimod:299#K + + + + + (2S)-2-amino-6-(carboxyamino)hexanoic acid + + + + + + 2-amino-6-carbamic hexanoic acid + + + + + + MOD_RES N6-carboxylysine + + + + + + N6-carboxy-L-lysine + + + + + + N6-carboxylysine + + + + + + N6CbxLys + + + + + + lysine NZ-carboxylic acid + + + + + + Carboxy + + + + + + Carboxylation + + + + + + N6-carbamyllysine + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-1-carboxyethyl-L-lysine. + 72.06 + C 3 H 4 N 0 O 2 + 72.021126 + C 9 H 16 N 2 O 3 + 200.24 + 200.11609 + K + natural + Unimod:378 + uniprot.ptm:PTM-0189 + (2S)-2-amino-6-([(1S)-1-carboxyethyl]amino)hexanoic acid + MOD_RES N6-1-carboxyethyl lysine + N6-(1-carboxyethyl)-L-lysine + N6-(1-carboxyethyl)lysine + N6CbzEtLys + NZ-(1-carboxyethyl)lysine + PSI-MOD + Carboxyethyl + carboxyethyl + MOD:00124 + + N6-1-carboxyethyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-1-carboxyethyl-L-lysine. + PubMed:3123486 + PubMed:8253186 + PubMed:8421682 + RESID:AA0115 + Unimod:378#K + + + + + (2S)-2-amino-6-([(1S)-1-carboxyethyl]amino)hexanoic acid + + + + + + MOD_RES N6-1-carboxyethyl lysine + + + + + + N6-(1-carboxyethyl)-L-lysine + + + + + + N6-(1-carboxyethyl)lysine + + + + + + N6CbzEtLys + + + + + + NZ-(1-carboxyethyl)lysine + + + + + + Carboxyethyl + + + + + + carboxyethyl + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to hypusine, N6-(4-amino-2-hydroxybutyl)-L-lysine. + 87.12 + C 4 H 9 N 1 O 1 + 87.06841 + C 10 H 21 N 3 O 2 + 215.3 + 215.16338 + K + natural + Unimod:379 + uniprot.ptm:PTM-0150 + (2S)-2-amino-6-([(2R)-4-amino-2-hydroxybutyl]amino)hexanoic acid + (2S,9R)-2,11-diazanyl-9-hydroxy-7-azaundecanoic acid + (2S,9R)-hypusine + 2-azanyl-6-[(4-azanyl-2-hydroxybutyl)azanyl]hexanoic acid + Hypu + L-hypusine + MOD_RES Hypusine + N-(4-NH2-2-OH-butyl)- (of Lysine) + N6-(4-amino-2-hydroxybutyl)-L-lysine + PSI-MOD + Hypusine + hypusine + MOD:00125 + + This modification occurs uniquely in translation initiation factor eIF-5A [JSG]. + hypusine + + + + + A protein modification that effectively converts an L-lysine residue to hypusine, N6-(4-amino-2-hydroxybutyl)-L-lysine. + DeltaMass:0 + PubMed:6806267 + PubMed:8108861 + RESID:AA0116 + Unimod:379#K + + + + + (2S)-2-amino-6-([(2R)-4-amino-2-hydroxybutyl]amino)hexanoic acid + + + + + + (2S,9R)-2,11-diazanyl-9-hydroxy-7-azaundecanoic acid + + + + + + (2S,9R)-hypusine + + + + + + 2-azanyl-6-[(4-azanyl-2-hydroxybutyl)azanyl]hexanoic acid + + + + + + Hypu + + + + + + L-hypusine + + + + + + MOD_RES Hypusine + + + + + + N-(4-NH2-2-OH-butyl)- (of Lysine) + + + + + + N6-(4-amino-2-hydroxybutyl)-L-lysine + + + + + + Hypusine + + + + + + hypusine + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-biotinyl-L-lysine. + 226.29 + C 10 H 14 N 2 O 2 S 1 + 226.0776 + C 16 H 26 N 4 O 3 S 1 + 354.47 + 354.17258 + K + natural + Unimod:3 + uniprot.ptm:PTM-0382 + (2S)-2-amino-6-(5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoylamino)hexanoic acid + (3aS-(3aalpha,4beta,6aalpha))-N6-(5-(hexahydro-2-oxo-1H-thieno(3,4-d)imidazol-4-yl)-1-oxopentyl)-L-lysine + MOD_RES N6-biotinyllysine + N6-[5-((3aS,4S,6aR)-hexahydro-2-oxo-1H-thieno[3,4-d]imidazol-4-yl)-1-oxopentyl]-L-lysine + N6-biotinyl-L-lysine + N6-biotinyllysine + N6BtnLys + biocytin + biotinyl lysyl + epsilon-N-biotinyllysine + PSI-MOD + Biotin + Biotinylation + MOD:00126 + + From DeltaMass: Average Mass: 354 Formula:C 16 H 26 O 4 N 3 S 1 (formula incorrect, N and O reversed) Monoisotopic Mass Change:354.172 Average Mass Change:354.471 References:PE Sciex. + N6-biotinyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-biotinyl-L-lysine. + DeltaMass:305 + PubMed:16109483 + PubMed:3178228 + PubMed:7948875 + PubMed:8747466 + RESID:AA0117 + Unimod:3#K + + + + + (2S)-2-amino-6-(5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoylamino)hexanoic acid + + + + + + (3aS-(3aalpha,4beta,6aalpha))-N6-(5-(hexahydro-2-oxo-1H-thieno(3,4-d)imidazol-4-yl)-1-oxopentyl)-L-lysine + + + + + + MOD_RES N6-biotinyllysine + + + + + + N6-[5-((3aS,4S,6aR)-hexahydro-2-oxo-1H-thieno[3,4-d]imidazol-4-yl)-1-oxopentyl]-L-lysine + + + + + + N6-biotinyl-L-lysine + + + + + + N6-biotinyllysine + + + + + + N6BtnLys + + + + + + biocytin + + + + + + biotinyl lysyl + + + + + + epsilon-N-biotinyllysine + + + + + + Biotin + + + + + + Biotinylation + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-lipoyl-L-lysine. + 188.3 + C 8 H 12 N 0 O 1 S 2 + 188.03296 + C 14 H 24 N 2 O 2 S 2 + 316.48 + 316.12793 + K + natural + Unimod:42 + uniprot.ptm:PTM-0383 + (2S)-2-amino-6-(5-[(3R)-1,2-dithiolan-3-yl]pentanamido)hexanoic acid + (2S)-2-amino-6-[(5-[(3R)-1,2-dithiolan-3-yl]pentanoyl)amino]hexanoic acid + (2S,6'R)-2-amino-6-(6,8-dithiooctanamido)hexanoic acid + 2-amino-6-(5-[1,2-dithiolan-3-yl]-1-oxopentyl)aminohexanoic acid + MOD_RES N6-lipoyllysine + N-Lipoyl- (on Lysine) + N6-6,8-dithiooctanoyllysine + N6-lipoyl-L-lysine + N6-lipoyllysine + N6LipLys + lipoylk + PSI-MOD + Lipoyl + MOD:00127 + + N6-lipoyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-lipoyl-L-lysine. + DeltaMass:0 + OMSSA:67 + PubMed:3421911 + PubMed:3522581 + PubMed:7719855 + RESID:AA0118 + Unimod:42#K + + + + + (2S)-2-amino-6-(5-[(3R)-1,2-dithiolan-3-yl]pentanamido)hexanoic acid + + + + + + (2S)-2-amino-6-[(5-[(3R)-1,2-dithiolan-3-yl]pentanoyl)amino]hexanoic acid + + + + + + (2S,6'R)-2-amino-6-(6,8-dithiooctanamido)hexanoic acid + + + + + + 2-amino-6-(5-[1,2-dithiolan-3-yl]-1-oxopentyl)aminohexanoic acid + + + + + + MOD_RES N6-lipoyllysine + + + + + + N-Lipoyl- (on Lysine) + + + + + + N6-6,8-dithiooctanoyllysine + + + + + + N6-lipoyl-L-lysine + + + + + + N6-lipoyllysine + + + + + + N6LipLys + + + + + + lipoylk + + + + + + Lipoyl + + + + + + Lipoyl + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-pyridoxal phosphate-L-lysine. + 229.13 + C 8 H 8 N 1 O 5 P 1 + 229.014 + C 14 H 20 N 3 O 6 P 1 + 357.3 + 357.10898 + K + natural + Unimod:46 + uniprot.ptm:PTM-0387 + (2S)-2-amino-6-[([3-hydroxy-2-methyl-5-phosphonooxymethylpyridin-4-yl]methylidene)amino]hexanoic acid + MOD_RES N6-(pyridoxal phosphate)lysine + N6-pyridoxal phosphate-L-lysine + N6PydoxLys + Pyridoxal phosphate (Schiff Base formed to lysine) + PSI-MOD + Pyridoxal phosphate + PyridoxalPhosphate + MOD:00128 + + From DeltaMass: Average Mass: 231 + N6-pyridoxal phosphate-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-pyridoxal phosphate-L-lysine. + DeltaMass:0 + PubMed:1544460 + RESID:AA0119 + Unimod:46#K + + + + + (2S)-2-amino-6-[([3-hydroxy-2-methyl-5-phosphonooxymethylpyridin-4-yl]methylidene)amino]hexanoic acid + + + + + + MOD_RES N6-(pyridoxal phosphate)lysine + + + + + + N6-pyridoxal phosphate-L-lysine + + + + + + N6PydoxLys + + + + + + Pyridoxal phosphate (Schiff Base formed to lysine) + + + + + + Pyridoxal phosphate + + + + + + PyridoxalPhosphate + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine, the adduct of retinal. + 266.43 + C 20 H 26 N 0 O 0 + 266.20346 + C 26 H 38 N 2 O 1 + 394.6 + 394.2984 + K + natural + Unimod:380 + uniprot.ptm:PTM-0388 + (2S)-2-amino-6-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid + MOD_RES N6-(retinylidene)lysine + N6-retinal-L-lysine + N6-retinyl-lysine + N6-retinylidene-L-lysine + N6RetalLys + PSI-MOD + Retinylidene + retinal + MOD:00129 + + N6-retinylidene-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine, the adduct of retinal. + PubMed:6794028 + PubMed:6870827 + RESID:AA0120 + Unimod:380#K + + + + + (2S)-2-amino-6-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid + + + + + + MOD_RES N6-(retinylidene)lysine + + + + + + N6-retinal-L-lysine + + + + + + N6-retinyl-lysine + + + + + + N6-retinylidene-L-lysine + + + + + + N6RetalLys + + + + + + Retinylidene + + + + + + retinal + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to L-allysine. + -1.03 + C 0 H -3 N -1 O 1 + -1.031634 + C 6 H 9 N 1 O 2 + 127.14 + 127.06333 + K + natural + Unimod:352 + uniprot.ptm:PTM-0059 + (2S)-2-amino-6-oxohexanoic acid + 2-amino-5-formylvaleric acid + 2-amino-adipic acid semialdahyde + 2-aminoadipate 6-semialdehyde + 5-formyl-norvaline + 6-oxonorleucine + AASA + Allysine (from Lysine) + L-allysine + Lysal + MOD_RES Allysine + Oxidation of lysine (to aminoadipic semialdehyde) + alpha-amino-adipic acid delta-semialdahyde + PSI-MOD + Lys->Allysine + Lysine oxidation to aminoadipic semialdehyde + MOD:00130 + + From DeltaMass: Average Mass: -1 + L-allysine + + + + + A protein modification that effectively converts an L-lysine residue to L-allysine. + ChEBI:17917 + DeltaMass:0 + PubMed:11120890 + PubMed:11332453 + PubMed:358196 + PubMed:5337886 + PubMed:5529814 + RESID:AA0121 + Unimod:352#K + + + + + (2S)-2-amino-6-oxohexanoic acid + + + + + + 2-amino-5-formylvaleric acid + + + + + + 2-amino-adipic acid semialdahyde + + + + + + 2-aminoadipate 6-semialdehyde + + + + + + 5-formyl-norvaline + + + + + + 6-oxonorleucine + + + + + + AASA + + + + + + Allysine (from Lysine) + + + + + + L-allysine + + + + + + Lysal + + + + + + MOD_RES Allysine + + + + + + Oxidation of lysine (to aminoadipic semialdehyde) + + + + + + alpha-amino-adipic acid delta-semialdahyde + + + + + + Lys->Allysine + + + + + + Lysine oxidation to aminoadipic semialdehyde + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to L-2-aminoadipic acid. + 14.97 + C 0 H -3 N -1 O 2 + 14.96328 + C 6 H 9 N 1 O 3 + 143.14 + 143.05824 + K + natural + Unimod:381 + (2S)-2-aminohexanedioic acid + 2-amino-1,4-butanedicarboxylic acid + L-2-aminoadipic acid + L-alpha-aminoadipic acid + Lysoic + Oxidation of lysine (to aminoadipic acid) + PSI-MOD + Lys->AminoadipicAcid + alpha-amino adipic acid + MOD:00131 + + From DeltaMass: References:Amici A, Levine, RL, Tsai, L, and Stadtman, ER: Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. Journal of Biological Chemistry 264: 3341-3346 1989.Requena JR, Chao CC, Levine RL, and Stadtman ER: Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. Proceedings of the National Academy of Sciences USA 98: 69-74 2001. Notes:Expected reaction following oxidation of lysine to aminoadipic semialdehyde. Not proven experimentally but deduced by reference to the similar known reaction of oxidation of Arg to Glu via the semialdehyde. [This has been observed as a natural modification, see RESID:AA0122. JSG] + L-2-aminoadipic acid + + + + + A protein modification that effectively converts an L-lysine residue to L-2-aminoadipic acid. + DeltaMass:353 + PubMed:336041 + PubMed:358196 + PubMed:7419498 + RESID:AA0122 + Unimod:381#K + + + + + (2S)-2-aminohexanedioic acid + + + + + + 2-amino-1,4-butanedicarboxylic acid + + + + + + L-2-aminoadipic acid + + + + + + L-alpha-aminoadipic acid + + + + + + Lysoic + + + + + + Oxidation of lysine (to aminoadipic acid) + + + + + + Lys->AminoadipicAcid + + + + + + alpha-amino adipic acid + + + + + + + + + + + + + A protein modification that effectively crosslinks an L-serine residue and an L-lysine residue to release water and form 2-amino-6-(2-amino-2-carboxyethylamino)hexanoic acid. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 9 H 15 N 3 O 2 + 197.24 + 197.11642 + K, S + natural + uniprot.ptm:PTM-0172 + (2R,9S)-lysinoalanine + (2S)-2-amino-6-([(2R)-2-amino-2-carboxyethyl]amino)hexanoic acid + CROSSLNK Lysinoalanine (Ser-Lys) + L-lysinoalanine + LAL + Lysinoalanine (from Cysteine) + N-epsilon-(2-amino-2-carboxyethyl)-L-lysine + N6-(2-amino-2-carboxyethyl)-L-lysine + XLNK-N6Lys-3Dha(Ser) + alaninolysine + PSI-MOD + MOD:00132 + Cross-link 2. This entry is for the crosslink of peptidyl serine and peptidyl lysine. For the modification of peptidyl lysine by a free serine see MOD:01838. From DeltaMass: Average Mass: -34. + L-lysinoalanine (Lys-Ser) + + + + + A protein modification that effectively crosslinks an L-serine residue and an L-lysine residue to release water and form 2-amino-6-(2-amino-2-carboxyethylamino)hexanoic acid. + DeltaMass:0 + PubMed:2544544 + RESID:AA0123#KSX + + + + + (2R,9S)-lysinoalanine + + + + + + (2S)-2-amino-6-([(2R)-2-amino-2-carboxyethyl]amino)hexanoic acid + + + + + + CROSSLNK Lysinoalanine (Ser-Lys) + + + + + + L-lysinoalanine + + + + + + LAL + + + + + + Lysinoalanine (from Cysteine) + + + + + + N-epsilon-(2-amino-2-carboxyethyl)-L-lysine + + + + + + N6-(2-amino-2-carboxyethyl)-L-lysine + + + + + + XLNK-N6Lys-3Dha(Ser) + + + + + + alaninolysine + + + + + + + + + + + + A protein modification that effectively crosslinks an L-glutamine residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoglutamyl)-L-lysine and the release of ammonia. + -17.03 + C 0 H -3 N -1 O 0 + -17.026548 + C 11 H 17 N 3 O 3 + 239.27 + 239.12698 + K, Q + natural + uniprot.ptm:PTM-0158 + (2S)-2-amino-6-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid + 2-azanyl-6-([4-azanyl-4-carboxybutanoyl]azanyl)hexanoic acid + 5-glutamyl N6-lysine + CROSSLNK Isoglutamyl lysine isopeptide (Lys-Gln) + N alpha -(gamma-Glutamyl)-lysine + N(epsilon)-(gamma-glutamyl)lysine + N6-(L-isoglutamyl)-L-lysine + XLNK-N6Lys-5Glu(Gln) + PSI-MOD + MOD:00133 + + Cross-link 2. + N6-(L-isoglutamyl)-L-lysine (Gln) + + + + + A protein modification that effectively crosslinks an L-glutamine residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoglutamyl)-L-lysine and the release of ammonia. + ChEBI:21863 + DeltaMass:0 + PubMed:2461365 + PubMed:5637041 + PubMed:5656070 + PubMed:8598899 + RESID:AA0124#GLN + + + + + (2S)-2-amino-6-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid + + + + + + 2-azanyl-6-([4-azanyl-4-carboxybutanoyl]azanyl)hexanoic acid + + + + + + 5-glutamyl N6-lysine + + + + + + CROSSLNK Isoglutamyl lysine isopeptide (Lys-Gln) + + + + + + N alpha -(gamma-Glutamyl)-lysine + + + + + + N(epsilon)-(gamma-glutamyl)lysine + + + + + + N6-(L-isoglutamyl)-L-lysine + + + + + + XLNK-N6Lys-5Glu(Gln) + + + + + + + + + + + + + + A protein modification that effectively crosslinks an L-lysine residue and a glycine residue by an isopeptide bond to form N6-glycyl-L-lysine. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 8 H 14 N 3 O 2 + 184.22 + 184.1086 + G, K + natural + C-term + uniprot.ptm:PTM-0134 + (2S)-2-amino-6-[(aminoacetyl)amino]hexanoic acid + CROSSLNK Glycyl lysine isopeptide (Gly-Lys) (interchain with K-...) + CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-...) + N6-(glycyl)-L-lysine + N6-glycyllysine + XLNK-N6Lys-1Gly + PSI-MOD + MOD:00134 + + Cross-link 2; this is the common crosslink structure formed by ubiquitin, SUMO, and similar proteins. + N6-glycyl-L-lysine + + + + + A protein modification that effectively crosslinks an L-lysine residue and a glycine residue by an isopeptide bond to form N6-glycyl-L-lysine. + ChEBI:21885 + RESID:AA0125 + + + + + (2S)-2-amino-6-[(aminoacetyl)amino]hexanoic acid + + + + + + CROSSLNK Glycyl lysine isopeptide (Gly-Lys) (interchain with K-...) + + + + + + CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-...) + + + + + + N6-(glycyl)-L-lysine + + + + + + N6-glycyllysine + + + + + + XLNK-N6Lys-1Gly + + + + + + + + + + + + A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue by an isopeptide bond with formation of N-(L-isoaspartyl)glycine and the release of ammonia. + -17.03 + C 0 H -3 N -1 O 0 + -17.026548 + C 6 H 7 N 2 O 3 + 155.13 + 155.04567 + G, N + natural + N-term + uniprot.ptm:PTM-0489 + (2S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid + 2-amino-N4-(carboxymethyl)-butanediamic acid + CROSSLNK Isoaspartyl glycine isopeptide (Asn-Gly) + CROSSLNK Isoaspartyl glycine isopeptide (Gly-Asn) + N-(L-isoaspartyl)-glycine + N-beta-aspartylglycine + N4-(carboxymethyl)-asparagine + XLNK-4Asp-NGly(Asn) + isoaspartyl glycine + PSI-MOD + MOD:00135 + Cross-link 2. + N-(L-isoaspartyl)-glycine (Asn) + + + + + A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue by an isopeptide bond with formation of N-(L-isoaspartyl)glycine and the release of ammonia. + ChEBI:21479 + PubMed:1826288 + RESID:AA0126 + + + + + (2S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid + + + + + + 2-amino-N4-(carboxymethyl)-butanediamic acid + + + + + + CROSSLNK Isoaspartyl glycine isopeptide (Asn-Gly) + + + + + + CROSSLNK Isoaspartyl glycine isopeptide (Gly-Asn) + + + + + + N-(L-isoaspartyl)-glycine + + + + + + N-beta-aspartylglycine + + + + + + N4-(carboxymethyl)-asparagine + + + + + + XLNK-4Asp-NGly(Asn) + + + + + + isoaspartyl glycine + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to pyruvic acid. + -33.09 + C 0 H -3 N -1 O 1 S -1 + -33.003704 + C 3 H 3 O 2 + 71.06 + 71.013306 + C + natural + N-term + Unimod:382 + uniprot.ptm:PTM-0265 + 2-oxopropanoic acid + MOD_RES Pyruvic acid (Cys) + Pyruv(Cys) + pyruvic acid + PSI-MOD + MOD:00136 + + pyruvic acid (Cys) + + + + + A protein modification that effectively converts an L-cysteine residue to pyruvic acid. + PubMed:10085076 + PubMed:3042771 + PubMed:8464063 + RESID:AA0127#CYS + Unimod:382 + + + + + 2-oxopropanoic acid + + + + + + MOD_RES Pyruvic acid (Cys) + + + + + + Pyruv(Cys) + + + + + + pyruvic acid + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue into L-3-phenyllactic acid. + 0.98 + C 0 H -1 N -1 O 1 + 0.984016 + C 9 H 9 O 2 + 149.17 + 149.06026 + F + N-term + Unimod:7 + uniprot.ptm:PTM-0035 + (2S)-2-hydroxy-3-phenylpropanoic acid + L-3-phenyllactic acid + MOD_RES 3-phenyllactic acid + PSI-MOD + Deamidated + Deamidation + MOD:00137 + This modification is not the result of deamidation, instead the alpha amino group is replaced with an hydroxyl group. + L-3-phenyllactic acid + + + + + A protein modification that effectively converts an L-phenylalanine residue into L-3-phenyllactic acid. + PubMed:1973541 + RESID:AA0128 + Unimod:7#F + + + + + (2S)-2-hydroxy-3-phenylpropanoic acid + + + + + + L-3-phenyllactic acid + + + + + + MOD_RES 3-phenyllactic acid + + + + + + Deamidated + + + + + + Deamidation + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue into 2-oxobutanoic acid. + -17.03 + C 0 H -3 N -1 O 0 + -17.026548 + C 4 H 5 O 2 + 85.08 + 85.02895 + T + N-term + Unimod:385 + uniprot.ptm:PTM-0017 + 2-ketobutyric acid + 2-oxobutanoic acid + 2-oxobutyric acid + MOD_RES 2-oxobutanoic acid + PSI-MOD + Ammonia-loss + Loss of ammonia + MOD:00138 + 2-oxobutanoic acid + + + + + A protein modification that effectively converts an L-threonine residue into 2-oxobutanoic acid. + ChEBI:149508 + PubMed:15023056 + PubMed:1680314 + PubMed:2253617 + PubMed:2764678 + RESID:AA0129 + Unimod:385#T + + + + + 2-ketobutyric acid + + + + + + 2-oxobutanoic acid + + + + + + 2-oxobutanoic acid + + + + + + 2-oxobutyric acid + + + + + + MOD_RES 2-oxobutanoic acid + + + + + + Ammonia-loss + + + + + + Loss of ammonia + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to N2-succinyl-L-tryptophan. + 100.07 + C 4 H 4 N 0 O 3 + 100.016045 + C 15 H 15 N 2 O 4 + 287.29 + 287.10318 + W + natural + N-term + Unimod:64 + uniprot.ptm:PTM-0181 + (2S)-2-(3-carboxypropanoyl)amino-3-(1H-indol-3-yl)propanoic acid + (2S)-2-amino-(6,7-dihydro-6,7-dioxo-1H-indole)-3-propanoic acid + MOD_RES N2-succinyltryptophan + N2-succinyl-L-tryptophan + PSI-MOD + Succinic anhydride labeling reagent light form (N-term) + Succinyl + MOD:00139 + N2-succinyl-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to N2-succinyl-L-tryptophan. + PubMed:11857757 + PubMed:12175151 + PubMed:8471040 + RESID:AA0130 + Unimod:64#N-term + + + + + (2S)-2-(3-carboxypropanoyl)amino-3-(1H-indol-3-yl)propanoic acid + + + + + + (2S)-2-amino-(6,7-dihydro-6,7-dioxo-1H-indole)-3-propanoic acid + + + + + + MOD_RES N2-succinyltryptophan + + + + + + N2-succinyl-L-tryptophan + + + + + + Succinic anhydride labeling reagent light form (N-term) + + + + + + Succinyl + + + + + + + + + + + A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycocyanobilin. + 586.69 + C 33 H 38 N 4 O 6 S 0 + 586.2791 + C 36 H 43 N 5 O 7 S 1 + 689.83 + 689.2883 + C + natural + Unimod:387 + (2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-18-ethyl-1,2,3,19,21,22,24-heptahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid + (2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-2,7,13,17-tetramethyl-1,2,3,19,21,22,24-heptahydrobilin-1,19(21H,22H,24H)-dione + BINDING Phycocyanobilin chromophore (covalent; via 1 link) + PCB + S-Phycocyanobilin (on Cysteine) + S-phycocyanobilin-L-cysteine + phycobilin cysteine + phycocyanobilin cysteine adduct + PSI-MOD + Phycocyanobilin + phycocyanobilin + MOD:00140 + From DeltaMass: Average Mass: 587. + S-phycocyanobilin-L-cysteine + + + + + A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycocyanobilin. + ChEBI:15617 + DeltaMass:0 + PubMed:16644722 + PubMed:3208761 + PubMed:3838747 + PubMed:7918400 + RESID:AA0131 + Unimod:387#C + + + + + (2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-18-ethyl-1,2,3,19,21,22,24-heptahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid + + + + + + (2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-2,7,13,17-tetramethyl-1,2,3,19,21,22,24-heptahydrobilin-1,19(21H,22H,24H)-dione + + + + + + BINDING Phycocyanobilin chromophore (covalent; via 1 link) + + + + + + PCB + + + + + + S-Phycocyanobilin (on Cysteine) + + + + + + S-phycocyanobilin-L-cysteine + + + + + + phycobilin cysteine + + + + + + phycocyanobilin cysteine adduct + + + + + + Phycocyanobilin + + + + + + phycocyanobilin + + + + + + + + + + + A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoerythrobilin. + 588.7 + C 33 H 40 N 4 O 6 S 0 + 588.2948 + C 36 H 45 N 5 O 7 S 1 + 691.84 + 691.30396 + C + natural + Unimod:388 + (2S,3R,16R)-18-ethenyl-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-2,3,15,16-tetrahydrobilin-1,19(21H,22H,24H)-dione + 18-ethenyl-3-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,3,15,16-tetrahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid + BINDING Phycoerythrobilin chromophore (covalent; via 1 link) + PEB + S-phycoerythrobilin-L-cysteine + phycoerythrobilin cysteine adduct + PSI-MOD + Phycoerythrobilin + phycoerythrobilin + MOD:00141 + S-phycoerythrobilin-L-cysteine + + + + + A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoerythrobilin. + ChEBI:15618 + PubMed:14588022 + PubMed:3208761 + PubMed:3838747 + PubMed:8876649 + RESID:AA0132 + Unimod:388#C + + + + + (2S,3R,16R)-18-ethenyl-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-2,3,15,16-tetrahydrobilin-1,19(21H,22H,24H)-dione + + + + + + 18-ethenyl-3-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,3,15,16-tetrahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid + + + + + + BINDING Phycoerythrobilin chromophore (covalent; via 1 link) + + + + + + PEB + + + + + + S-phycoerythrobilin-L-cysteine + + + + + + phycoerythrobilin cysteine adduct + + + + + + Phycoerythrobilin + + + + + + phycoerythrobilin + + + + + + + + + + + A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phytochromobilin. + 584.67 + C 33 H 36 N 4 O 6 S 0 + 584.2635 + C 36 H 41 N 5 O 7 S 1 + 687.81 + 687.27264 + C + natural + Unimod:389 + (2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-2,7,13,17-tetramethyl-1,2,3,19,21,22,24-heptahydrobilin-1,19(21H,22H,24H)-dione + 18-ethenyl-3-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-1,2,3,19,22,24-hexahydro-2,7,13,17-tetramethyl-1,19-dioxo-21H-biline-8,12-dipropanoic acid + BINDING Phytochromobilin chromophore (covalent; via 1 link) + S-phytochromobilin-L-cysteine + phytochrome chromophore + phytochromobilin cysteine adduct + PSI-MOD + Phytochromobilin + phytochromobilin + MOD:00142 + S-phytochromobilin-L-cysteine + + + + + A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phytochromobilin. + ChEBI:15619 + PubMed:1634523 + PubMed:16593380 + PubMed:3208761 + PubMed:7918400 + RESID:AA0133 + Unimod:389#C + + + + + (2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-2,7,13,17-tetramethyl-1,2,3,19,21,22,24-heptahydrobilin-1,19(21H,22H,24H)-dione + + + + + + 18-ethenyl-3-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-1,2,3,19,22,24-hexahydro-2,7,13,17-tetramethyl-1,19-dioxo-21H-biline-8,12-dipropanoic acid + + + + + + BINDING Phytochromobilin chromophore (covalent; via 1 link) + + + + + + S-phytochromobilin-L-cysteine + + + + + + phytochrome chromophore + + + + + + phytochromobilin cysteine adduct + + + + + + Phytochromobilin + + + + + + phytochromobilin + + + + + + + + + + + A protein modification that effectively results from forming an adduct between two cysteine residues and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + 616.5 + C 34 Fe 1 H 32 N 4 O 4 S 0 + 616.1773 + C 40 Fe 1 H 42 N 6 O 6 S 2 + 822.78 + 822.1957 + C, C + natural + (7,12-bis[(1S)-1-([(2R)-2-amino-2-carboxyethyl]sulfanyl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis[2-carboxyethyl]-N21,N22,N23,N24)-ferrate + 2,4-bis[1-(S-cysteinyl)ethyl]protoporphyrin IX + BINDING Heme (covalent) + HemeCys2 + biscysteinyl heme + heme-bis-L-cysteine + PSI-MOD + MOD:00143 + + Cross-link 2. + heme-bis-L-cysteine + + + + + A protein modification that effectively results from forming an adduct between two cysteine residues and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + ChEBI:17627 + PubMed:5545094 + PubMed:8827449 + RESID:AA0134 + + + + + (7,12-bis[(1S)-1-([(2R)-2-amino-2-carboxyethyl]sulfanyl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis[2-carboxyethyl]-N21,N22,N23,N24)-ferrate + + + + + + 2,4-bis[1-(S-cysteinyl)ethyl]protoporphyrin IX + + + + + + BINDING Heme (covalent) + + + + + + HemeCys2 + + + + + + biscysteinyl heme + + + + + + heme-bis-L-cysteine + + + + + + + + + + + A protein modification that effectively results from forming an adduct between a cysteine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + 616.5 + C 34 Fe 1 H 32 N 4 O 4 S 0 + 616.1773 + C 37 Fe 1 H 37 N 5 O 5 S 1 + 719.64 + 719.18646 + C + natural + Unimod:390 + (12-ethenyl-7-[(1S)-1-([(2R)-2-amino-2-carboxyethyl]sulfanyl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis[2-carboxyethyl]-N21,N22,N23,N24)-ferrate + 4-[1-(S-cysteinyl)ethyl]protoporphyrin IX + BINDING Heme (covalent; via 1 link) + HemeCys1 + S-Heme (on Cysteine) + cysteinyl heme + heme-L-cysteine + PSI-MOD + Heme + heme + MOD:00144 + + From DeltaMass: Average Mass: 617. + heme-L-cysteine + + + + + A protein modification that effectively results from forming an adduct between a cysteine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + ChEBI:17627 + DeltaMass:0 + PubMed:170910 + PubMed:192772 + PubMed:2536325 + PubMed:9535866 + RESID:AA0135 + Unimod:390#C + + + + + (12-ethenyl-7-[(1S)-1-([(2R)-2-amino-2-carboxyethyl]sulfanyl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis[2-carboxyethyl]-N21,N22,N23,N24)-ferrate + + + + + + 4-[1-(S-cysteinyl)ethyl]protoporphyrin IX + + + + + + BINDING Heme (covalent; via 1 link) + + + + + + HemeCys1 + + + + + + S-Heme (on Cysteine) + + + + + + cysteinyl heme + + + + + + heme-L-cysteine + + + + + + Heme + + + + + + heme + + + + + + + + + + + A protein modification that effectively converts four L-cysteine residues iron atom to tetrakis-L-cysteinyl iron. + 51.81 + C 0 Fe 1 H -4 N 0 O 0 S 0 + 51.904736 + 2- + C 12 Fe 1 H 16 N 4 O 4 S 4 + 464.37 + 463.94147 + C, C, C, C + natural + METAL Iron + tetrakis(cysteinato-kappaS)-iron + tetrakis-L-cysteinyl iron + PSI-MOD + MOD:00145 + Cross-link 4. + tetrakis-L-cysteinyl iron + + + + + A protein modification that effectively converts four L-cysteine residues iron atom to tetrakis-L-cysteinyl iron. + PubMed:1303768 + PubMed:2244884 + RESID:AA0136 + + + + + METAL Iron + + + + + + tetrakis(cysteinato-kappaS)-iron + + + + + + tetrakis-L-cysteinyl iron + + + + + + + + + + + A protein modification that effectively converts four L-cysteine residues and a two-iron two-sulfur cluster to tetrakis-L-cysteinyl diiron disulfide. + 171.78 + C 0 Fe 2 H -4 N 0 O 0 S 2 + 171.78381 + 2- + C 12 Fe 2 H 16 N 4 O 4 S 6 + 584.34 + 583.82056 + C, C, C, C + natural + METAL Iron-sulfur (2Fe-2S) + METAL Iron-sulfur (2Fe-2S); shared with dimeric partner + tetrakis-L-cysteinyl diiron disulfide + tetrakiscysteinato-1kappa(2)S,2kappa(2)S-di-mu-sulfido-diiron + PSI-MOD + MOD:00146 + Cross-link 4. + tetrakis-L-cysteinyl diiron disulfide + + + + + A protein modification that effectively converts four L-cysteine residues and a two-iron two-sulfur cluster to tetrakis-L-cysteinyl diiron disulfide. + PubMed:2123937 + PubMed:6801028 + PubMed:7763242 + PubMed:8688437 + RESID:AA0137 + + + + + METAL Iron-sulfur (2Fe-2S) + + + + + + METAL Iron-sulfur (2Fe-2S); shared with dimeric partner + + + + + + tetrakis-L-cysteinyl diiron disulfide + + + + + + tetrakiscysteinato-1kappa(2)S,2kappa(2)S-di-mu-sulfido-diiron + + + + + + + + + + + A protein modification that effectively converts six L-cysteine residues and a three-iron three-sulfur cluster to hexakis-L-cysteinyl triiron trisulfide. + 257.67 + C 0 Fe 3 H -6 N 0 O 0 S 3 + 257.67572 + 3- + C 18 Fe 3 H 24 N 6 O 6 S 9 + 876.5 + 875.73083 + C, C, C, C, C, C + hypothetical + hexakis-L-cysteinyl triiron trisulfide + tri-mu-sulfido-hexakiscysteinato-1kappa(2)S,2kappa(2)S,3kappa(2)S-triiron + tri-mu-sulfidotris(biscysteinato-kappaS-iron) + PSI-MOD + MOD:00147 + Cross-link 6. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. + hexakis-L-cysteinyl triiron trisulfide + + + + + A protein modification that effectively converts six L-cysteine residues and a three-iron three-sulfur cluster to hexakis-L-cysteinyl triiron trisulfide. + PubMed:3379067 + PubMed:3932661 + PubMed:7354058 + RESID:AA0138 + + + + + hexakis-L-cysteinyl triiron trisulfide + + + + + + tri-mu-sulfido-hexakiscysteinato-1kappa(2)S,2kappa(2)S,3kappa(2)S-triiron + + + + + + tri-mu-sulfidotris(biscysteinato-kappaS-iron) + + + + + + + + + + + A protein modification that effectively converts three L-cysteine residues and a three-iron four-sulfur cluster to tris-L-cysteinyl triiron tetrasulfide. + 292.75 + C 0 Fe 3 H -3 N 0 O 0 S 4 + 292.67126 + 3- + C 9 Fe 3 H 12 N 3 O 3 S 7 + 602.17 + 601.6988 + C, C, C + natural + METAL Iron-sulfur (3Fe-4S) + mu3-sulfido tri-mu-sulfido tris-S-L-cysteinyl triiron + mu3-sulfido-tri-mu-sulfido-triscysteinato-1kappaS,2kappaS,3kappaS-triiron + tris-L-cysteinyl triiron tetrasulfide + tris-L-cysteinyl triiron tetrasulfide C3 cluster + tris-L-cysteinyl triiron tetrasulfide cubane form + tris-L-cysteinyl triiron tetrasulfide cuboid cluster + tris-L-cysteinyl triiron tetrasulfide trigonal cluster + PSI-MOD + MOD:00148 + Cross-link 3. + tris-L-cysteinyl triiron tetrasulfide + + + + + A protein modification that effectively converts three L-cysteine residues and a three-iron four-sulfur cluster to tris-L-cysteinyl triiron tetrasulfide. + PubMed:10555576 + PubMed:2056535 + PubMed:3422475 + PubMed:6848518 + PubMed:7819255 + PubMed:9063899 + RESID:AA0139 + + + + + METAL Iron-sulfur (3Fe-4S) + + + + + + mu3-sulfido tri-mu-sulfido tris-S-L-cysteinyl triiron + + + + + + mu3-sulfido-tri-mu-sulfido-triscysteinato-1kappaS,2kappaS,3kappaS-triiron + + + + + + tris-L-cysteinyl triiron tetrasulfide + + + + + + tris-L-cysteinyl triiron tetrasulfide C3 cluster + + + + + + tris-L-cysteinyl triiron tetrasulfide cubane form + + + + + + tris-L-cysteinyl triiron tetrasulfide cuboid cluster + + + + + + tris-L-cysteinyl triiron tetrasulfide trigonal cluster + + + + + + + + + + + A protein modification that effectively converts four L-cysteine residues and a four-iron four-sulfur cluster to tetrakis-L-cysteinyl tetrairon tetrasulfide. + 347.59 + C 0 Fe 4 H -4 N 0 O 0 S 4 + 347.59784 + 2- + C 12 Fe 4 H 16 N 4 O 4 S 8 + 760.15 + 759.6346 + C, C, C, C + natural + METAL Iron-sulfur (4Fe-4S) + METAL Iron-sulfur (4Fe-4S); shared with dimeric partner + tetra-mu3-sulfido-tetrakis(cysteinato)-1kappaS,2kappaS,3kappaS,4kappaS-tetrahedro-tetrairon + tetra-mu3-sulfidotetrakis(S-cysteinyliron) + tetrakis-L-cysteinyl tetrairon tetrasulfide + PSI-MOD + MOD:00149 + Cross-link 4. + tetrakis-L-cysteinyl tetrairon tetrasulfide + + + + + A protein modification that effectively converts four L-cysteine residues and a four-iron four-sulfur cluster to tetrakis-L-cysteinyl tetrairon tetrasulfide. + PubMed:3351918 + PubMed:7803404 + PubMed:7819196 + PubMed:932007 + RESID:AA0140 + + + + + METAL Iron-sulfur (4Fe-4S) + + + + + + METAL Iron-sulfur (4Fe-4S); shared with dimeric partner + + + + + + tetra-mu3-sulfido-tetrakis(cysteinato)-1kappaS,2kappaS,3kappaS,4kappaS-tetrahedro-tetrairon + + + + + + tetra-mu3-sulfidotetrakis(S-cysteinyliron) + + + + + + tetrakis-L-cysteinyl tetrairon tetrasulfide + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and a one-molybdenum seven-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide. + 991.53 + C 7 Fe 7 H 6 Mo 1 N 1 O 7 S 9 + 993.213 + C 16 Fe 7 H 18 Mo 1 N 5 O 9 S 10 + 1231.81 + 1233.2811 + C, H + natural + L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide carbide + cysteinato-8kappaS-histidino-1kappaN(tau)-[(2R)-4-carboxy-2-(carboxymethyl)-2-oxidobutanoate-1kappaO(1),1kappaO(2)]-mu6-carbido-2:3:4:5:6:7kappa(6)C-hexa-mu3-sulfido-1:2:3kappa(3)S;1:2:4kappa(3)S;1:3:4kappa(3)S;5:6:8kappa(3)S;5:7:8kappa(3)S;6:7:8kappa(3)S-tri-mu2-sulfido-2:5kappa(2)S;3:6kappa(2)S;4:7kappa(2)S molybdenum heptairon + nitrogenase iron-molybdenum cofactor + PSI-MOD + MOD:00150 + Cross-link 2; incidental to RESID:AA0300. + L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide + + + + + A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and a one-molybdenum seven-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide. + PubMed:10525412 + PubMed:12215645 + PubMed:12733878 + PubMed:1529354 + PubMed:8027059 + RESID:AA0141 + + + + + L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide carbide + + + + + + cysteinato-8kappaS-histidino-1kappaN(tau)-[(2R)-4-carboxy-2-(carboxymethyl)-2-oxidobutanoate-1kappaO(1),1kappaO(2)]-mu6-carbido-2:3:4:5:6:7kappa(6)C-hexa-mu3-sulfido-1:2:3kappa(3)S;1:2:4kappa(3)S;1:3:4kappa(3)S;5:6:8kappa(3)S;5:7:8kappa(3)S;6:7:8kappa(3)S-tri-mu2-sulfido-2:5kappa(2)S;3:6kappa(2)S;4:7kappa(2)S molybdenum heptairon + + + + + + nitrogenase iron-molybdenum cofactor + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteinyl molybdopterin. + 520.27 + C 10 H 11 Mo 1 N 5 O 8 P 1 S 2 + 521.8841 + C 13 H 16 Mo 1 N 6 O 9 P 1 S 3 + 623.41 + 624.89325 + C + natural + Unimod:391 + (4R,5aR,11aR)-8-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-4,5a,6,9,10,11,11a-heptahydro-4-(phosphoric acid)methyl-2,2,10-trioxo-pteridino[6,7-5,6]pyrano[3,4-4,3][1,2,5]molybdadithiolene + L-cysteinyl molybdopterin + METAL Molybdenum-pterin + MoPterCys + cysteinyl Mo-molybdopterin + cysteinyl Mo-pterin + molybdoenzyme molybdenum cofactor + PSI-MOD + Molybdopterin + molybdopterin + MOD:00151 + + L-cysteinyl molybdopterin + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteinyl molybdopterin. + PubMed:14527393 + PubMed:7878465 + PubMed:9428520 + RESID:AA0142 + Unimod:391#C + + + + + (4R,5aR,11aR)-8-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-4,5a,6,9,10,11,11a-heptahydro-4-(phosphoric acid)methyl-2,2,10-trioxo-pteridino[6,7-5,6]pyrano[3,4-4,3][1,2,5]molybdadithiolene + + + + + + L-cysteinyl molybdopterin + + + + + + METAL Molybdenum-pterin + + + + + + MoPterCys + + + + + + cysteinyl Mo-molybdopterin + + + + + + cysteinyl Mo-pterin + + + + + + molybdoenzyme molybdenum cofactor + + + + + + Molybdopterin + + + + + + molybdopterin + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S'-(8alpha-FAD)-L-cystine. + 783.54 + C 27 H 31 N 9 O 15 P 2 S 0 + 783.1415 + C 30 H 36 N 10 O 16 P 2 S 1 + 886.68 + 886.1507 + C + natural + Unimod:50 + uniprot.ptm:PTM-0272 + (2R)-2-amino-3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]sulfanylpropanoic acid + 8alpha-(S-cysteinyl)FAD + MOD_RES S-8alpha-FAD cysteine + S-(8alpha-FAD)-L-cysteine + S8aFADCys + PSI-MOD + FAD + Flavin adenine dinucleotide + MOD:00152 + + S-(8alpha-FAD)-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S'-(8alpha-FAD)-L-cystine. + PubMed:10220347 + RESID:AA0143 + Unimod:50#C + + + + + (2R)-2-amino-3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]sulfanylpropanoic acid + + + + + + 8alpha-(S-cysteinyl)FAD + + + + + + MOD_RES S-8alpha-FAD cysteine + + + + + + S-(8alpha-FAD)-L-cysteine + + + + + + S8aFADCys + + + + + + FAD + + + + + + Flavin adenine dinucleotide + + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FAD)-L-histidine. + 783.54 + C 27 H 31 N 9 O 15 P 2 + 783.1415 + C 33 H 38 N 12 O 16 P 2 + 920.68 + 920.2004 + H + natural + Unimod:50 + uniprot.ptm:PTM-0258 + (2S)-2-amino-3-(3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid + 3'-(8alpha-FAD)-L-histidine + 8alpha-(N(delta)-histidyl)FAD + 8alpha-(N3'-histidyl)FAD + MOD_RES Pros-8alpha-FAD histidine + N(pi)-(8alpha-FAD)-histidine + Np8aFADHis + pros-(8alpha-FAD)-histidine + PSI-MOD + 8alpha-N1-histidyl FAD + FAD + Flavin adenine dinucleotide + MOD:00153 + + 3'-(8alpha-FAD)-L-histidine + + + + + A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FAD)-L-histidine. + PubMed:241294 + PubMed:8076 + RESID:AA0144 + Unimod:50#H + + + + + (2S)-2-amino-3-(3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid + + + + + + 3'-(8alpha-FAD)-L-histidine + + + + + + 8alpha-(N(delta)-histidyl)FAD + + + + + + 8alpha-(N3'-histidyl)FAD + + + + + + MOD_RES Pros-8alpha-FAD histidine + + + + + + N(pi)-(8alpha-FAD)-histidine + + + + + + Np8aFADHis + + + + + + pros-(8alpha-FAD)-histidine + + + + + + 8alpha-N1-histidyl FAD + + + + + + FAD + + + + + + Flavin adenine dinucleotide + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to O4'-(8alpha-FAD)-L-tyrosine. + 783.54 + C 27 H 31 N 9 O 15 P 2 + 783.1415 + C 36 H 40 N 10 O 17 P 2 + 946.72 + 946.20483 + Y + natural + Unimod:50 + uniprot.ptm:PTM-0231 + (2S)-2-amino-3-(4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxyphenyl)propanoic acid + 8alpha-(O4'-tyrosyl)FAD + MOD_RES O-8alpha-FAD tyrosine + O-8 alpha-Flavin [FAD])- (of Tyrosine) + O4'-(8alpha-FAD)-L-tyrosine + O8aFADTyr + PSI-MOD + FAD + Flavin adenine dinucleotide + MOD:00154 + + From DeltaMass: Average Mass: 783 + O4'-(8alpha-FAD)-L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to O4'-(8alpha-FAD)-L-tyrosine. + DeltaMass:0 + PubMed:7391034 + RESID:AA0145 + Unimod:50#Y + + + + + (2S)-2-amino-3-(4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxyphenyl)propanoic acid + + + + + + 8alpha-(O4'-tyrosyl)FAD + + + + + + MOD_RES O-8alpha-FAD tyrosine + + + + + + O-8 alpha-Flavin [FAD])- (of Tyrosine) + + + + + + O4'-(8alpha-FAD)-L-tyrosine + + + + + + O8aFADTyr + + + + + + FAD + + + + + + Flavin adenine dinucleotide + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to L-3',4'-dihydroxyphenylalanine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 9 H 9 N 1 O 3 + 179.18 + 179.05824 + Y + natural + Unimod:35 + uniprot.ptm:PTM-0023 + (2S)-2-amino-3-(3,4-dihydroxyphenyl)propanoic acid + 3,4-Dihydroxy-Phenylalanine (from Tyrosine) (DOPA) + 3HyTyr + L-3',4'-dihydroxyphenylalanine + L-3'-hydroxytyrosine + L-DOPA + MOD_RES 3',4'-dihydroxyphenylalanine + hydroxylationy + levodopa + mod194 + PSI-MOD + MOD:00155 + + incidental to RESID:AA0368 From DeltaMass: Average Mass: 16 + L-3',4'-dihydroxyphenylalanine + + + + + A protein modification that effectively converts an L-tyrosine residue to L-3',4'-dihydroxyphenylalanine. + ChEBI:141815 + DeltaMass:0 + OMSSA:194 + OMSSA:64 + PubMed:1610822 + PubMed:1903612 + PubMed:3734192 + RESID:AA0146 + Unimod:35#Y + + + + + (2S)-2-amino-3-(3,4-dihydroxyphenyl)propanoic acid + + + + + + 3,4-Dihydroxy-Phenylalanine (from Tyrosine) (DOPA) + + + + + + 3HyTyr + + + + + + L-3',4'-dihydroxyphenylalanine + + + + + + L-3'-hydroxytyrosine + + + + + + L-DOPA + + + + + + MOD_RES 3',4'-dihydroxyphenylalanine + + + + + + hydroxylationy + + + + + + levodopa + + + + + + mod194 + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to an L-2',4',5'-topaquinone. + 29.98 + C 0 H -2 N 0 O 2 + 29.974178 + C 9 H 7 N 1 O 4 + 193.16 + 193.0375 + Y + natural + Unimod:392 + uniprot.ptm:PTM-0009 + (2S)-2-amino-3-(5-hydroxy-2,5-cyclohexadien-1,4-dion-2-yl)propanoic acid + 2,4,5-trihydroxyphenylalanine quinone + 5-(2-carboxy-2-aminoethyl)-2-hydroxy-1,4-benzoquinone + L-2',4',5'-topaquinone + L-2,4,5-TOPAquinone + MOD_RES 2',4',5'-topaquinone + TPQ + TopaQ + PSI-MOD + Quinone + quinone + MOD:00156 + + L-2',4',5'-topaquinone + + + + + A protein modification that effectively converts an L-tyrosine residue to an L-2',4',5'-topaquinone. + ChEBI:21187 + PubMed:10387067 + PubMed:1457410 + PubMed:1569055 + PubMed:2111581 + RESID:AA0147 + Unimod:392#Y + + + + + (2S)-2-amino-3-(5-hydroxy-2,5-cyclohexadien-1,4-dion-2-yl)propanoic acid + + + + + + 2,4,5-trihydroxyphenylalanine quinone + + + + + + 5-(2-carboxy-2-aminoethyl)-2-hydroxy-1,4-benzoquinone + + + + + + L-2',4',5'-topaquinone + + + + + + L-2,4,5-TOPAquinone + + + + + + MOD_RES 2',4',5'-topaquinone + + + + + + TPQ + + + + + + TopaQ + + + + + + Quinone + + + + + + quinone + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to an L-tryptophan quinone. + 29.98 + C 0 H -2 N 0 O 2 + 29.974178 + C 11 H 8 N 2 O 3 + 216.2 + 216.0535 + W + natural + Unimod:392 + uniprot.ptm:PTM-0299 + (2S)-2-amino-3-(6,7-dioxo-1H-indol-3-yl)propanoic acid + 2-amino-3-(6,7-dioxo-6,7-dihydro-1H-indol-3-yl)-propionic acid + 3-[(2S)-2-amino-2-carboxyethyl]-6,7-indolinedione + 6,7 Dione (from Tryptophan) + L-tryptophyl quinone + MOD_RES Tryptophylquinone + N-(3-carboxy-1-oxopropyl)-L-tryptophan + TrpQ + PSI-MOD + Quinone + quinone + MOD:00157 + + incidental to RESID:AA0149; incidental to RESID:AA0313; From DeltaMass: Average Mass: 30. + L-tryptophyl quinone + + + + + A protein modification that effectively converts an L-tryptophan residue to an L-tryptophan quinone. + DeltaMass:0 + PubMed:2028257 + RESID:AA0148 + Unimod:392#W + + + + + (2S)-2-amino-3-(6,7-dioxo-1H-indol-3-yl)propanoic acid + + + + + + 2-amino-3-(6,7-dioxo-6,7-dihydro-1H-indol-3-yl)-propionic acid + + + + + + 3-[(2S)-2-amino-2-carboxyethyl]-6,7-indolinedione + + + + + + 6,7 Dione (from Tryptophan) + + + + + + L-tryptophyl quinone + + + + + + MOD_RES Tryptophylquinone + + + + + + N-(3-carboxy-1-oxopropyl)-L-tryptophan + + + + + + TrpQ + + + + + + Quinone + + + + + + quinone + + + + + + + + + + + A protein modification that effectively cross-links two L-tryptophan residues by a carbon-carbon bond to form 4'-(L-tryptophan)-L-tryptophyl quinone. + 27.97 + C 0 H -4 N 0 O 2 + 27.958529 + C 22 H 16 N 4 O 4 + 400.39 + 400.11716 + W, W + natural + uniprot.ptm:PTM-0298 + 2,4-BisTrp-6,7-dione (from Tryptophan) + 2-amino-3-[2-[2-amino-3-(2-carboxyethyl)-6,7-dioxo-1H-indol-4-yl]-1H-indol-3-yl]propanoic acid + 3-[(2S)-2-amino-2-carboxyethyl]-4-(3-[(2S)-2-amino-2-carboxyethyl]-1H-indol-2-yl)-6,7-indolinedione + 4'-tryptophan-tryptophylquinone + 4-(2'-tryptophyl)tryptophan-6,7-dione + 4-(L-tryptophan-2-yl)-L-tryptophyl quinone + CROSSLNK Tryptophan tryptophylquinone (Trp-Trp) + TTQ + XLNK-4'Trp-TrpQ + alpha,alpha'-diamino-6',7'-dihydro-6',7'-dioxo-(2,4'-bi-1H-indole)-3,3'-dipropanoic acid + PSI-MOD + MOD:00158 + + Cross-link 2; secondary to RESID:AA0148; From DeltaMass: Average Mass: 28. + 4'-(L-tryptophan)-L-tryptophyl quinone + + + + + A protein modification that effectively cross-links two L-tryptophan residues by a carbon-carbon bond to form 4'-(L-tryptophan)-L-tryptophyl quinone. + ChEBI:20251 + DeltaMass:0 + PubMed:2028257 + RESID:AA0149 + + + + + 2,4-BisTrp-6,7-dione (from Tryptophan) + + + + + + 2-amino-3-[2-[2-amino-3-(2-carboxyethyl)-6,7-dioxo-1H-indol-4-yl]-1H-indol-3-yl]propanoic acid + + + + + + 3-[(2S)-2-amino-2-carboxyethyl]-4-(3-[(2S)-2-amino-2-carboxyethyl]-1H-indol-2-yl)-6,7-indolinedione + + + + + + 4'-tryptophan-tryptophylquinone + + + + + + 4-(2'-tryptophyl)tryptophan-6,7-dione + + + + + + 4-(L-tryptophan-2-yl)-L-tryptophyl quinone + + + + + + CROSSLNK Tryptophan tryptophylquinone (Trp-Trp) + + + + + + TTQ + + + + + + XLNK-4'Trp-TrpQ + + + + + + alpha,alpha'-diamino-6',7'-dihydro-6',7'-dioxo-(2,4'-bi-1H-indole)-3,3'-dipropanoic acid + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-phosphopantetheine-L-serine. + 340.33 + C 11 H 21 N 2 O 6 P 1 S 1 + 340.0858 + C 14 H 26 N 3 O 8 P 1 S 1 + 427.41 + 427.11783 + S + natural + Unimod:49 + uniprot.ptm:PTM-0391 + (2R)-2-hydroxy-3,3-dimethyl-4-[(2S)-2-amino-2-carboxyethyl]phosphonato-N-(3-oxo-3-[(2-sulfanylethyl)amino]propyl)butanamide + 4'-Phosphopantetheine + MOD_RES O-(pantetheine 4'-phosphoryl)serine + O-phosphopantetheine-L-serine + OPpantSer + PSI-MOD + Phosphopantetheine + MOD:00159 + + Unimod has DiffFormula C 11 H 20 N 2 O 6 P 1 S 1 From DeltaMass: Average Mass: 339 + O-phosphopantetheine-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-phosphopantetheine-L-serine. + DeltaMass:0 + PubMed:10320345 + PubMed:10997907 + PubMed:12057197 + PubMed:12869567 + PubMed:4568609 + RESID:AA0150 + Unimod:49#S + + + + + (2R)-2-hydroxy-3,3-dimethyl-4-[(2S)-2-amino-2-carboxyethyl]phosphonato-N-(3-oxo-3-[(2-sulfanylethyl)amino]propyl)butanamide + + + + + + 4'-Phosphopantetheine + + + + + + MOD_RES O-(pantetheine 4'-phosphoryl)serine + + + + + + O-phosphopantetheine-L-serine + + + + + + OPpantSer + + + + + + Phosphopantetheine + + + + + + Phosphopantetheine + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to an N4-glycosyl-L-asparagine. + N + natural + N4GlycoAsn + PSI-MOD + MOD:00160 + + N4-glycosyl-L-asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to an N4-glycosyl-L-asparagine. + PubMed:111247 + PubMed:1694179 + PubMed:5490222 + RESID:AA0151#var + + + + + N4GlycoAsn + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-glucosylated L-cysteine. + 162.14 + C 6 H 10 N 0 O 5 S 0 + 162.05283 + C 9 H 15 N 1 O 6 S 1 + 265.28 + 265.062 + C + natural + Unimod:41 + uniprot.ptm:PTM-0626 + (2R)-2-amino-3-[(beta-D-glucopyranosyl)sulfanyl]propanoic acid + CARBOHYD S-linked (Glc) cysteine + S-(beta-D-glucopyranosyl)cysteine + S-glucosyl-L-cysteine + S-glycosyl-cysteine + SGlcCys + PSI-MOD + Hex + Hexose + MOD:00161 + S-glucosyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-glucosylated L-cysteine. + PubMed:1145128 + PubMed:15279557 + PubMed:5286858 + RESID:AA0152 + Unimod:41#C + + + + + (2R)-2-amino-3-[(beta-D-glucopyranosyl)sulfanyl]propanoic acid + + + + + + CARBOHYD S-linked (Glc) cysteine + + + + + + S-(beta-D-glucopyranosyl)cysteine + + + + + + S-glucosyl-L-cysteine + + + + + + S-glycosyl-cysteine + + + + + + SGlcCys + + + + + + Hex + + + + + + Hexose + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to O5-glucosylgalactosyl-L-hydroxylysine. + 340.28 + C 12 H 20 N 0 O 11 + 340.10056 + C 18 H 32 N 2 O 12 + 468.46 + 468.19553 + K + natural + Unimod:393 + (2S,5R)-2,6-diamino-5-[2-O-(alpha-D-glucopyranosyl)-beta-D-galactopyranosyloxy]hexanoic acid + 5-(2-O-alpha-D-glucopyranosyl-beta-D-galactopyranosyl)oxy-L-lysine + O5-glucosylgalactosyl-L-hydroxylysine + OGlcGal5HyLys + PSI-MOD + Glucosylgalactosyl + glucosylgalactosyl hydroxylysine + MOD:00162 + + Secondary to RESID:AA0028. + O5-glucosylgalactosyl-L-hydroxylysine + + + + + A protein modification that effectively converts an L-lysine residue to O5-glucosylgalactosyl-L-hydroxylysine. + PubMed:15149698 + PubMed:4288358 + PubMed:4319110 + RESID:AA0153 + Unimod:393 + + + + + (2S,5R)-2,6-diamino-5-[2-O-(alpha-D-glucopyranosyl)-beta-D-galactopyranosyloxy]hexanoic acid + + + + + + 5-(2-O-alpha-D-glucopyranosyl-beta-D-galactopyranosyl)oxy-L-lysine + + + + + + O5-glucosylgalactosyl-L-hydroxylysine + + + + + + OGlcGal5HyLys + + + + + + Glucosylgalactosyl + + + + + + glucosylgalactosyl hydroxylysine + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-(N-acetylaminogalactosyl)-L-serine. + 203.19 + C 8 H 13 N 1 O 5 + 203.07938 + C 11 H 18 N 2 O 7 + 290.27 + 290.1114 + S + natural + uniprot.ptm:PTM-0564 + (2S)-2-amino-3-(2-acetamido-2-deoxy-alpha-D-galactopyranosyloxy)propanoic acid + CARBOHYD O-linked (GalNAc) serine + O-(N-acetylamino)galactosyl-L-serine + O3-(N-acetylgalactosaminyl)serine + OGalNAcSer + mucin type O-glycosylserine + PSI-MOD + HexNAc + MOD:00163 + + O-(N-acetylamino)galactosyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-(N-acetylaminogalactosyl)-L-serine. + PubMed:115869 + PubMed:16005634 + PubMed:3086323 + PubMed:8948436 + PubMed:9092502 + RESID:AA0154 + + + + + (2S)-2-amino-3-(2-acetamido-2-deoxy-alpha-D-galactopyranosyloxy)propanoic acid + + + + + + CARBOHYD O-linked (GalNAc) serine + + + + + + O-(N-acetylamino)galactosyl-L-serine + + + + + + O3-(N-acetylgalactosaminyl)serine + + + + + + OGalNAcSer + + + + + + mucin type O-glycosylserine + + + + + + HexNAc + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to O-(N-acetylaminogalactosyl)-L-threonine. + 203.19 + C 8 H 13 N 1 O 5 + 203.07938 + C 12 H 20 N 2 O 7 + 304.3 + 304.12704 + T + natural + uniprot.ptm:PTM-0567 + (2S,3R)-2-amino-3-(2-acetamido-2-deoxy-alpha-D-galactopyranosyloxy)butanoic acid + CARBOHYD O-linked (GalNAc) threonine + CARBOHYD O-linked (HexNAc) + O-(N-acetylamino)galactosyl-L-threonine + O3-(N-acetylgalactosaminyl)threonine + OGalNAcThr + mucin type O-glycosylthreonine + PSI-MOD + HexNAc + MOD:00164 + + O-(N-acetylamino)galactosyl-L-threonine + + + + + A protein modification that effectively converts an L-asparagine residue to O-(N-acetylaminogalactosyl)-L-threonine. + PubMed:16005634 + PubMed:1997327 + PubMed:3086323 + PubMed:8948436 + PubMed:9092502 + RESID:AA0155 + + + + + (2S,3R)-2-amino-3-(2-acetamido-2-deoxy-alpha-D-galactopyranosyloxy)butanoic acid + + + + + + CARBOHYD O-linked (GalNAc) threonine + + + + + + CARBOHYD O-linked (HexNAc) + + + + + + O-(N-acetylamino)galactosyl-L-threonine + + + + + + O3-(N-acetylgalactosaminyl)threonine + + + + + + OGalNAcThr + + + + + + mucin type O-glycosylthreonine + + + + + + HexNAc + + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to 1'-mannosyl-L-tryptophan. + 162.14 + C 6 H 10 N 0 O 5 + 162.05283 + C 17 H 20 N 2 O 6 + 348.36 + 348.13214 + W + natural + uniprot.ptm:PTM-0535 + (2S)-2-amino-3-(1-D-mannopyranosyloxy-1H-indol-3-yl)propanoic acid + 1'-glycosyl-L-tryptophan + 1'-mannosyl-L-tryptophan + CARBOHYD N-linked (Man) tryptophan + N-mannosyl-tryptophan + N1'ManTrp + N1-mannosyl-tryptophan + PSI-MOD + MOD:00165 + + 1'-mannosyl-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to 1'-mannosyl-L-tryptophan. + PubMed:1482345 + PubMed:16150691 + RESID:AA0156 + + + + + (2S)-2-amino-3-(1-D-mannopyranosyloxy-1H-indol-3-yl)propanoic acid + + + + + + 1'-glycosyl-L-tryptophan + + + + + + 1'-mannosyl-L-tryptophan + + + + + + CARBOHYD N-linked (Man) tryptophan + + + + + + N-mannosyl-tryptophan + + + + + + N1'ManTrp + + + + + + N1-mannosyl-tryptophan + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to O4'-glucosyl-tyrosine. + 162.14 + C 6 H 10 N 0 O 5 + 162.05283 + C 15 H 19 N 1 O 7 + 325.32 + 325.11615 + Y + natural + Unimod:41 + uniprot.ptm:PTM-0575 + (2S)-2-amino-3-(4-alpha-D-glucopyranosyloxy)phenylpropanoic acid + CARBOHYD O-linked (Glc) tyrosine + O4'-glucosyl-L-tyrosine + O4'-glycosyl-L-tyrosine + O4GlcTyr + PSI-MOD + Hex + Hexose + MOD:00166 + O4'-glucosyl-L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to O4'-glucosyl-tyrosine. + PubMed:15279557 + PubMed:3181138 + RESID:AA0157 + Unimod:41#Y + + + + + (2S)-2-amino-3-(4-alpha-D-glucopyranosyloxy)phenylpropanoic acid + + + + + + CARBOHYD O-linked (Glc) tyrosine + + + + + + O4'-glucosyl-L-tyrosine + + + + + + O4'-glycosyl-L-tyrosine + + + + + + O4GlcTyr + + + + + + Hex + + + + + + Hexose + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylphosphatidylinositolethanolamine. + 123.05 + C 2 H 6 N 1 O 3 P 1 + 123.00853 + C 6 H 13 N 3 O 6 P 1 + 254.16 + 254.0542 + N + natural + C-term + uniprot.ptm:PTM-0137 + GPIAsn + LIPID GPI-anchor amidated asparagine + N-asparaginyl-glycosylphosphatidylinositolethanolamine + PSI-MOD + MOD:00167 + N-asparaginyl-glycosylphosphatidylinositolethanolamine + + + + + A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylphosphatidylinositolethanolamine. + PubMed:1824714 + PubMed:8276756 + RESID:AA0158 + + + + + GPIAsn + + + + + + LIPID GPI-anchor amidated asparagine + + + + + + N-asparaginyl-glycosylphosphatidylinositolethanolamine + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to N-(aspart-1-yl)-glycosylphosphatidylinositolethanolamine. + 123.05 + C 2 H 6 N 1 O 3 P 1 + 123.00853 + C 6 H 12 N 2 O 7 P 1 + 255.14 + 255.03821 + D + natural + C-term + uniprot.ptm:PTM-0138 + GPIAsp + LIPID GPI-anchor amidated aspartate + N-aspartyl-glycosylphosphatidylinositolethanolamine + PSI-MOD + MOD:00168 + N-aspartyl-glycosylphosphatidylinositolethanolamine + + + + + A protein modification that effectively converts an L-aspartic acid residue to N-(aspart-1-yl)-glycosylphosphatidylinositolethanolamine. + PubMed:7120400 + RESID:AA0159 + + + + + GPIAsp + + + + + + LIPID GPI-anchor amidated aspartate + + + + + + N-aspartyl-glycosylphosphatidylinositolethanolamine + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to N-cysteinyl-glycosylphosphatidylinositolethanolamine. + 123.05 + C 2 H 6 N 1 O 3 P 1 S 0 + 123.00853 + C 5 H 12 N 2 O 5 P 1 S 1 + 243.19 + 243.02045 + C + natural + C-term + uniprot.ptm:PTM-0140 + GPICys + LIPID GPI-anchor amidated cysteine + N-cysteinyl-glycosylphosphatidylinositolethanolamine + PSI-MOD + MOD:00169 + N-cysteinyl-glycosylphosphatidylinositolethanolamine + + + + + A protein modification that effectively converts an L-cysteine residue to N-cysteinyl-glycosylphosphatidylinositolethanolamine. + PubMed:2897081 + RESID:AA0160 + + + + + GPICys + + + + + + LIPID GPI-anchor amidated cysteine + + + + + + N-cysteinyl-glycosylphosphatidylinositolethanolamine + + + + + + + + + + + A protein modification that effectively converts a glycine residue to N-glycyl-glycosylphosphatidylinositolethanolamine. + 123.05 + C 2 H 6 N 1 O 3 P 1 + 123.00853 + C 4 H 10 N 2 O 5 P 1 + 197.11 + 197.03273 + G + natural + C-term + uniprot.ptm:PTM-0141 + GPIGly + LIPID GPI-anchor amidated glycine + N-glycyl-glycosylphosphatidylinositolethanolamine + PSI-MOD + MOD:00170 + N-glycyl-glycosylphosphatidylinositolethanolamine + + + + + A protein modification that effectively converts a glycine residue to N-glycyl-glycosylphosphatidylinositolethanolamine. + PubMed:2341397 + RESID:AA0161 + + + + + GPIGly + + + + + + LIPID GPI-anchor amidated glycine + + + + + + N-glycyl-glycosylphosphatidylinositolethanolamine + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to N-seryl-glycosylphosphatidylinositolethanolamine. + 123.05 + C 2 H 6 N 1 O 3 P 1 + 123.00853 + C 5 H 12 N 2 O 6 P 1 + 227.13 + 227.0433 + S + natural + C-term + uniprot.ptm:PTM-0142 + GPISer + LIPID GPI-anchor amidated serine + N-seryl-glycosylphosphatidylinositolethanolamine + PSI-MOD + MOD:00171 + N-seryl-glycosylphosphatidylinositolethanolamine + + + + + A protein modification that effectively converts an L-serine residue to N-seryl-glycosylphosphatidylinositolethanolamine. + PubMed:2111324 + PubMed:8448158 + RESID:AA0162 + + + + + GPISer + + + + + + LIPID GPI-anchor amidated serine + + + + + + N-seryl-glycosylphosphatidylinositolethanolamine + + + + + + + + + + + A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylphosphatidylinositolethanolamine. + 123.05 + C 2 H 6 N 1 O 3 P 1 + 123.00853 + C 5 H 12 N 2 O 5 P 1 + 211.13 + 211.04839 + A + natural + C-term + uniprot.ptm:PTM-0136 + GPIAla + LIPID GPI-anchor amidated alanine + N-alanyl-glycosylphosphatidylinositolethanolamine + PSI-MOD + MOD:00172 + N-alanyl-glycosylphosphatidylinositolethanolamine + + + + + A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylphosphatidylinositolethanolamine. + PubMed:7682556 + PubMed:7744038 + RESID:AA0163 + + + + + GPIAla + + + + + + LIPID GPI-anchor amidated alanine + + + + + + N-alanyl-glycosylphosphatidylinositolethanolamine + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to N-threonyl-glycosylphosphatidylinositolethanolamine. + 123.05 + C 2 H 6 N 1 O 3 P 1 + 123.00853 + C 6 H 14 N 2 O 6 P 1 + 241.16 + 241.05894 + T + hypothetical + C-term + uniprot.ptm:PTM-0143 + GPIThr + LIPID GPI-anchor amidated threonine + N-threonyl-glycosylphosphatidylinositolethanolamine + PSI-MOD + MOD:00173 + N-threonyl-glycosylphosphatidylinositolethanolamine + + + + + A protein modification that effectively converts an L-threonine residue to N-threonyl-glycosylphosphatidylinositolethanolamine. + RESID:AA0164 + + + + + GPIThr + + + + + + LIPID GPI-anchor amidated threonine + + + + + + N-threonyl-glycosylphosphatidylinositolethanolamine + + + + + + + + + + + A protein modification that effectively converts a glycine residue to N-glycyl-glycosylsphingolipidinositolethanolamine. + 123.05 + C 2 H 6 N 1 O 3 P 1 + 123.00853 + C 4 H 10 N 2 O 5 P 1 + 197.11 + 197.03273 + G + hypothetical + C-term + uniprot.ptm:PTM-0146 + GSIGly + LIPID GPI-like-anchor amidated glycine + N-glycyl-glycosylsphingolipidinositolethanolamine + PSI-MOD + MOD:00174 + N-glycyl-glycosylsphingolipidinositolethanolamine + + + + + A protein modification that effectively converts a glycine residue to N-glycyl-glycosylsphingolipidinositolethanolamine. + PubMed:12626404 + PubMed:8404891 + RESID:AA0165 + + + + + GSIGly + + + + + + LIPID GPI-like-anchor amidated glycine + + + + + + N-glycyl-glycosylsphingolipidinositolethanolamine + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to N-seryl-glycosylsphingolipidinositolethanolamine. + 123.05 + C 2 H 6 N 1 O 3 P 1 + 123.00853 + C 5 H 12 N 2 O 6 P 1 + 227.13 + 227.0433 + S + natural + C-term + uniprot.ptm:PTM-0147 + GSISer + LIPID GPI-like-anchor amidated serine + N-seryl-glycosylsphingolipidinositolethanolamine + PSI-MOD + MOD:00175 + N-seryl-glycosylsphingolipidinositolethanolamine + + + + + A protein modification that effectively converts an L-serine residue to N-seryl-glycosylsphingolipidinositolethanolamine. + PubMed:12626404 + PubMed:2721485 + PubMed:8269952 + RESID:AA0166 + + + + + GSISer + + + + + + LIPID GPI-like-anchor amidated serine + + + + + + N-seryl-glycosylsphingolipidinositolethanolamine + + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-(phosphoribosyl dephospho-coenzyme A)-L-serine. + 881.63 + C 26 H 42 N 7 O 19 P 3 S 1 + 881.1469 + C 29 H 47 N 8 O 21 P 3 S 1 + 968.71 + 968.17896 + S + natural + Unimod:395 + uniprot.ptm:PTM-0389 + MOD_RES O-(phosphoribosyl dephospho-coenzyme A)serine + O-(phosphoribosyl dephospho-coenzyme A)-L-serine + O3-(phosphate-5-ribosyl-alpha-2-adenosine-5-diphosphate pantetheine)-L-serine + O3-(phosphoribosyl dephospho-coenzyme A)-L-serine + O3-2'-(5''-phosphoribosyl-3'-dephosphocoenzyme A)-L-serine + OPRibdPCoASer + PSI-MOD + PhosphoribosyldephosphoCoA + phosphoribosyl dephospho-coenzyme A + MOD:00176 + + pRibodePcoA + O-(phosphoribosyl dephospho-coenzyme A)-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-(phosphoribosyl dephospho-coenzyme A)-L-serine. + PubMed:10924139 + PubMed:11052675 + PubMed:179809 + PubMed:180526 + PubMed:368065 + RESID:AA0167 + Unimod:395#S + + + + + MOD_RES O-(phosphoribosyl dephospho-coenzyme A)serine + + + + + + O-(phosphoribosyl dephospho-coenzyme A)-L-serine + + + + + + O3-(phosphate-5-ribosyl-alpha-2-adenosine-5-diphosphate pantetheine)-L-serine + + + + + + O3-(phosphoribosyl dephospho-coenzyme A)-L-serine + + + + + + O3-2'-(5''-phosphoribosyl-3'-dephosphocoenzyme A)-L-serine + + + + + + OPRibdPCoASer + + + + + + PhosphoribosyldephosphoCoA + + + + + + phosphoribosyl dephospho-coenzyme A + + + + + + + + + + + A protein modification that effectively converts an L-argininine residue to omega-N-(ADP-ribosyl)-L-arginine. + 541.3 + C 15 H 21 N 5 O 13 P 2 + 541.0611 + C 21 H 33 N 9 O 14 P 2 + 697.49 + 697.16223 + R + natural + Unimod:213 + uniprot.ptm:PTM-0053 + (S)-2-amino-5-([imino([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)methyl]amino)pentanoic acid + ADPRibArg + MOD_RES ADP-ribosylarginine + N(omega)-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-arginine + N(omega)-alpha-D-ribofuranosyl-L-arginine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) + N-(ADP-ribosyl)- (on Arginine) + omega-N-(ADP-ribosyl)-L-arginine + PSI-MOD + ADP Ribose addition + ADP-Ribosyl + MOD:00177 + + From DeltaMass: Average Mass: 541. + omega-N-(ADP-ribosyl)-L-arginine + + + + + A protein modification that effectively converts an L-argininine residue to omega-N-(ADP-ribosyl)-L-arginine. + DeltaMass:0 + PubMed:15842200 + PubMed:209022 + PubMed:3090031 + PubMed:3923473 + PubMed:6582062 + RESID:AA0168 + Unimod:213#R + + + + + (S)-2-amino-5-([imino([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)methyl]amino)pentanoic acid + + + + + + ADPRibArg + + + + + + MOD_RES ADP-ribosylarginine + + + + + + N(omega)-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-arginine + + + + + + N(omega)-alpha-D-ribofuranosyl-L-arginine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) + + + + + + N-(ADP-ribosyl)- (on Arginine) + + + + + + omega-N-(ADP-ribosyl)-L-arginine + + + + + + ADP Ribose addition + + + + + + ADP-Ribosyl + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-(ADP-ribosyl)-L-cysteine. + 541.3 + C 15 H 21 N 5 O 13 P 2 S 0 + 541.0611 + C 18 H 26 N 6 O 14 P 2 S 1 + 644.44 + 644.0703 + C + natural + Unimod:213 + uniprot.ptm:PTM-0055 + (R)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]sulfanyl)propanoic acid + ADPRibCys + MOD_RES ADP-ribosylcysteine + S-(ADP-ribosyl)- (on Cysteine) + S-(ADP-ribosyl)-L-cysteine + S-L-cysteine alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) + S-alpha-D-ribofuranosyl-L-cysteine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) + PSI-MOD + ADP Ribose addition + ADP-Ribosyl + MOD:00178 + + From DeltaMass: Average Mass: 541. + S-(ADP-ribosyl)-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-(ADP-ribosyl)-L-cysteine. + DeltaMass:0 + PubMed:15842200 + PubMed:3863818 + RESID:AA0169 + Unimod:213#C + + + + + (R)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]sulfanyl)propanoic acid + + + + + + ADPRibCys + + + + + + MOD_RES ADP-ribosylcysteine + + + + + + S-(ADP-ribosyl)- (on Cysteine) + + + + + + S-(ADP-ribosyl)-L-cysteine + + + + + + S-L-cysteine alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) + + + + + + S-alpha-D-ribofuranosyl-L-cysteine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) + + + + + + ADP Ribose addition + + + + + + ADP-Ribosyl + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-glycerylphosphorylethanolamine. + 197.13 + C 5 H 12 N 1 O 5 P 1 + 197.0453 + C 10 H 19 N 2 O 8 P 1 + 326.24 + 326.0879 + E + natural + Unimod:396 + uniprot.ptm:PTM-0403 + (S)-2-amino-5-[2-([([2,3-dihydroxypropyl]oxy)(hydroxy)phosphoryl]oxy)ethyl]amino-5-oxopentanoic acid + 5-L-glutamyl glycerylphosphorylethanolamine + 5GlyceroPEtAGlu + L-glutamyl 5-glycerophosphoethanolamine + L-glutamyl 5-glycerophosphorylethanolamine + L-glutamyl 5-glycerylphosphorylethanolamine + MOD_RES 5-glutamyl glycerylphosphorylethanolamine + PSI-MOD + GlycerylPE + glycerylphosphorylethanolamine + MOD:00179 + + glycerylPE + L-glutamyl 5-glycerylphosphorylethanolamine + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-glycerylphosphorylethanolamine. + PubMed:2511205 + PubMed:2569467 + PubMed:9662537 + RESID:AA0170 + Unimod:396#E + + + + + (S)-2-amino-5-[2-([([2,3-dihydroxypropyl]oxy)(hydroxy)phosphoryl]oxy)ethyl]amino-5-oxopentanoic acid + + + + + + 5-L-glutamyl glycerylphosphorylethanolamine + + + + + + 5GlyceroPEtAGlu + + + + + + L-glutamyl 5-glycerophosphoethanolamine + + + + + + L-glutamyl 5-glycerophosphorylethanolamine + + + + + + L-glutamyl 5-glycerylphosphorylethanolamine + + + + + + MOD_RES 5-glutamyl glycerylphosphorylethanolamine + + + + + + GlycerylPE + + + + + + glycerylphosphorylethanolamine + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-sulfo-L-cysteine. + 80.06 + C 0 H 0 N 0 O 3 S 1 + 79.95682 + C 3 H 5 N 1 O 4 S 2 + 183.2 + 182.966 + C + natural + Unimod:40 + (2R)-2-amino-3-(sulfosulfanyl)propanoic acid + 2-amino-3-(sulfothio)propanoic acid + 3-(sulfosulfanyl)-L-alanine + S-sulfo-L-cysteine + S-sulfocysteine + SSulfCys + cysteine sulfate thioester + cysteine-S-sulfonic acid + PSI-MOD + O-Sulfonation + Sulfo + MOD:00180 + S-sulfo-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-sulfo-L-cysteine. + PubMed:12876326 + PubMed:14752058 + PubMed:643076 + RESID:AA0171 + Unimod:40#C + + + + + (2R)-2-amino-3-(sulfosulfanyl)propanoic acid + + + + + + 2-amino-3-(sulfothio)propanoic acid + + + + + + 3-(sulfosulfanyl)-L-alanine + + + + + + S-sulfo-L-cysteine + + + + + + S-sulfocysteine + + + + + + S-sulfocysteine + + + + + + SSulfCys + + + + + + cysteine sulfate thioester + + + + + + cysteine-S-sulfonic acid + + + + + + O-Sulfonation + + + + + + Sulfo + + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to O4'-sulfo-L-tyrosine. + 80.06 + C 0 H 0 N 0 O 3 S 1 + 79.95682 + C 9 H 9 N 1 O 5 S 1 + 243.23 + 243.02014 + Y + natural + Unimod:40 + uniprot.ptm:PTM-0286 + (S)-2-amino-3-(4-sulfooxyphenyl)propanoic acid + 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-sulfate + MOD_RES Sulfotyrosine + O4'-sulfo-L-tyrosine + O4-sulfotyrosine + OSulfTyr + Sulphation (of O of Tyrosine) + Tyrosinyl Sulphate + sulfationy + tyrosine sulfate + tyrosine-O-sulfonic acid + tyrosine-O-sulphonic acid + PSI-MOD + O-Sulfonation + Sulfo + MOD:00181 + + From DeltaMass: Average Mass: 80 Average Mass Change:80 PubMed:9624161. + O4'-sulfo-L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to O4'-sulfo-L-tyrosine. + DeltaMass:88 + OMSSA:114 + PubMed:10226369 + PubMed:14752058 + PubMed:2303439 + PubMed:3778455 + PubMed:3801003 + RESID:AA0172 + Unimod:40#Y + + + + + (S)-2-amino-3-(4-sulfooxyphenyl)propanoic acid + + + + + + 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-sulfate + + + + + + MOD_RES Sulfotyrosine + + + + + + O4'-sulfo-L-tyrosine + + + + + + O4-sulfotyrosine + + + + + + OSulfTyr + + + + + + Sulphation (of O of Tyrosine) + + + + + + Tyrosinyl Sulphate + + + + + + sulfationy + + + + + + tyrosine sulfate + + + + + + tyrosine-O-sulfonic acid + + + + + + tyrosine-O-sulphonic acid + + + + + + O-Sulfonation + + + + + + Sulfo + + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to L-bromohistidine. + 78.9 + Br 1 C 0 H -1 N 0 O 0 + 77.910515 + Br 1 C 6 H 6 N 3 O 1 + 216.04 + 214.96942 + H + natural + Unimod:340 + uniprot.ptm:PTM-0089 + Br1His + L-bromohistidine + MOD_RES Bromohistidine + PSI-MOD + Bromo + bromination + MOD:00182 + L-bromohistidine + + + + + A protein modification that effectively converts an L-histidine residue to L-bromohistidine. + PubMed:2076468 + PubMed:9033387 + RESID:AA0173 + Unimod:340#H + + + + + Br1His + + + + + + L-bromohistidine + + + + + + MOD_RES Bromohistidine + + + + + + Bromo + + + + + + bromination + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to L-2'-bromophenylalanine. + 78.9 + Br 1 C 0 H -1 N 0 O 0 + 77.910515 + Br 1 C 9 H 8 N 1 O 1 + 226.07 + 224.97893 + F + natural + (S)-2-amino-3-(2-bromophenyl)propanoic acid + 2'BrPhe + L-2'-bromophenylalanine + L-o-bromination of Phe with 79Br + o-bromophenylalanine + ortho-bromophenylalanine + PSI-MOD + Bromo + bromination + MOD:00183 + From DeltaMass: Average Mass: 78 Average Mass Change:78 References:Yoshino,K et.al. Biochemistry Vol. 30 pg 6203-9 (1991) Identifidation of a novel amino acid, o-bromo-L-phenylananine, in egg-associated peptides that activate spermatozoa. + L-2'-bromophenylalanine + + + + + A protein modification that effectively converts an L-phenylalanine residue to L-2'-bromophenylalanine. + DeltaMass:83 + PubMed:2059627 + PubMed:2076468 + PubMed:9033387 + RESID:AA0174 + + + + + (S)-2-amino-3-(2-bromophenyl)propanoic acid + + + + + + 2'BrPhe + + + + + + L-2'-bromophenylalanine + + + + + + L-o-bromination of Phe with 79Br + + + + + + o-bromophenylalanine + + + + + + ortho-bromophenylalanine + + + + + + Bromo + + + + + + bromination + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to L-3'-bromophenylalanine. + 78.9 + Br 1 C 0 H -1 N 0 O 0 + 77.910515 + Br 1 C 9 H 8 N 1 O 1 + 226.07 + 224.97893 + F + natural + (S)-2-amino-3-(3-bromophenyl)propanoic acid + 3'BrPhe + L-3'-bromophenylalanine + m-bromophenylalanine + meta-bromophenylalanine + PSI-MOD + Bromo + bromination + MOD:00184 + L-3'-bromophenylalanine + + + + + A protein modification that effectively converts an L-phenylalanine residue to L-3'-bromophenylalanine. + PubMed:2076468 + PubMed:9033387 + RESID:AA0175 + + + + + (S)-2-amino-3-(3-bromophenyl)propanoic acid + + + + + + 3'BrPhe + + + + + + L-3'-bromophenylalanine + + + + + + m-bromophenylalanine + + + + + + meta-bromophenylalanine + + + + + + Bromo + + + + + + bromination + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to L-4'-bromophenylalanine. + 78.9 + Br 1 C 0 H -1 N 0 O 0 + 77.910515 + Br 1 C 9 H 8 N 1 O 1 + 226.07 + 224.97893 + F + natural + (2S)-2-amino-3-(4-bromophenyl)propanoic acid + 4'BrPhe + L-4'-bromophenylalanine + p-bromophenylalanine + para-bromophenylalanine + PSI-MOD + Bromo + bromination + MOD:00185 + L-4'-bromophenylalanine + + + + + A protein modification that effectively converts an L-phenylalanine residue to L-4'-bromophenylalanine. + PubMed:2076468 + PubMed:9033387 + RESID:AA0176 + + + + + (2S)-2-amino-3-(4-bromophenyl)propanoic acid + + + + + + 4'BrPhe + + + + + + L-4'-bromophenylalanine + + + + + + p-bromophenylalanine + + + + + + para-bromophenylalanine + + + + + + Bromo + + + + + + bromination + + + + + + + + + + A protein modification that effectively substitutes an L-tyrosine residue with 3,3',5-triiodo-L-thyronine. + 469.79 + C 6 H 1 I 3 N 0 O 1 + 469.71616 + C 15 H 10 I 3 N 1 O 3 + 632.96 + 632.7795 + Y + natural + Unimod:397 + uniprot.ptm:PTM-0295 + (S)-2-amino-3-[4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl]propanoic acid + 3',3'',5'-triiodo-L-thyronine + 3,3',5-triiodo-L-thyronine + 3,5,3'-Triiodothyronine (from Tyrosine) + 3,5,3'-triiodo-L-thyronine + 4-(4-hydroxy-3-iodophenoxy)-3,5-diiodo-L-phenylalanine + I3Thy + MOD_RES Triiodothyronine + O-(4-hydroxy-3-iodophenyl)-3,5-diiodo-L-tyrosine + T3 + liothyronine + PSI-MOD + Triiodothyronine + triiodo + MOD:00186 + + From DeltaMass: Average Mass: 470. + 3,3',5-triiodo-L-thyronine + + + + + A protein modification that effectively substitutes an L-tyrosine residue with 3,3',5-triiodo-L-thyronine. + ChEBI:18258 + DeltaMass:0 + RESID:AA0177 + Unimod:397 + + + + + (S)-2-amino-3-[4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl]propanoic acid + + + + + + 3',3'',5'-triiodo-L-thyronine + + + + + + 3,3',5-triiodo-L-thyronine + + + + + + 3,5,3'-Triiodothyronine (from Tyrosine) + + + + + + 3,5,3'-triiodo-L-thyronine + + + + + + 4-(4-hydroxy-3-iodophenoxy)-3,5-diiodo-L-phenylalanine + + + + + + I3Thy + + + + + + MOD_RES Triiodothyronine + + + + + + O-(4-hydroxy-3-iodophenyl)-3,5-diiodo-L-tyrosine + + + + + + T3 + + + + + + liothyronine + + + + + + Triiodothyronine + + + + + + triiodo + + + + + + + + + + A protein modification that effectively substitutes an L-tyrosine residue with L-thyroxine. + 595.68 + C 6 H 0 I 4 N 0 O 1 + 595.6128 + C 15 H 9 I 4 N 1 O 3 + 758.86 + 758.67615 + Y + natural + Unimod:398 + uniprot.ptm:PTM-0294 + (S)-2-amino-3-[4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodophenyl]propanoic acid + 3',3'',5',5''-tetraiodo-L-thyronine + 3,3',5,5'-tetraiodo-L-thyronine + 3,5,3',5'-tetraiodo-L-thyronine + 4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodo-L-phenylalanine + I4Thy + L-thyroxine + MOD_RES Thyroxine + O-(4-hydroxy-3,5-diiodophenyl)-3,5-diiodo-L-tyrosine + T4 + PSI-MOD + Thyroxine + tetraiodo + MOD:00187 + + L-thyroxine + + + + + A protein modification that effectively substitutes an L-tyrosine residue with L-thyroxine. + ChEBI:18332 + PubMed:6704086 + RESID:AA0178 + Unimod:398 + + + + + (S)-2-amino-3-[4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodophenyl]propanoic acid + + + + + + 3',3'',5',5''-tetraiodo-L-thyronine + + + + + + 3,3',5,5'-tetraiodo-L-thyronine + + + + + + 3,5,3',5'-tetraiodo-L-thyronine + + + + + + 4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodo-L-phenylalanine + + + + + + I4Thy + + + + + + L-thyroxine + + + + + + MOD_RES Thyroxine + + + + + + O-(4-hydroxy-3,5-diiodophenyl)-3,5-diiodo-L-tyrosine + + + + + + T4 + + + + + + Thyroxine + + + + + + tetraiodo + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to 6'-bromo-L-tryptophan. + 78.9 + Br 1 C 0 H -1 N 0 O 0 + 77.910515 + Br 1 C 11 H 9 N 2 O 1 + 265.11 + 263.98984 + W + natural + Unimod:398 + uniprot.ptm:PTM-0051 + (2S)-2-amino-3-(6-bromo-1H-indol-3-yl)propanoic acid + 6'-BrTrp + 6'-bromo-L-tryptophan + MOD_RES 6'-bromotryptophan + PSI-MOD + Bromo + bromination + MOD:00188 + 6'-bromo-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to 6'-bromo-L-tryptophan. + PubMed:12118011 + PubMed:9030520 + PubMed:9033387 + PubMed:9434739 + RESID:AA0179 + Unimod:340#W + + + + + (2S)-2-amino-3-(6-bromo-1H-indol-3-yl)propanoic acid + + + + + + 6'-BrTrp + + + + + + 6'-bromo-L-tryptophan + + + + + + MOD_RES 6'-bromotryptophan + + + + + + Bromo + + + + + + bromination + + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to dehydroalanine. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 3 H 3 N 1 O 1 + 69.06 + 69.02146 + S + natural + Unimod:23 + uniprot.ptm:PTM-0006 + 2,3-didehydroalanine + 2-aminoacrylic acid + 2-aminopropenoic acid + 4-methylidene-imidazole-5-one (MIO) active site + Dha + Dha(Ser) + MOD_RES 2,3-didehydroalanine (Ser) + anhydroserine + beta-elim-s + dehydro + dehydroalanine + phospholosss + PSI-MOD + Dehydrated + MOD:00189 + + dehydroalanine (Ser) + + + + + A protein modification that effectively converts an L-serine residue to dehydroalanine. + DeltaMass:0 + OMSSA:140 + OMSSA:164 + OMSSA:96 + PubMed:10220322 + PubMed:1547888 + PubMed:1815586 + PubMed:2914619 + PubMed:7947813 + PubMed:8239649 + RESID:AA0181#SER + Unimod:23#S + + + + + 2,3-didehydroalanine + + + + + + 2-aminoacrylic acid + + + + + + 2-aminopropenoic acid + + + + + + 4-methylidene-imidazole-5-one (MIO) active site + + + + + + Dha + + + + + + Dha(Ser) + + + + + + MOD_RES 2,3-didehydroalanine (Ser) + + + + + + anhydroserine + + + + + + beta-elim-s + + + + + + dehydro + + + + + + dehydroalanine + + + + + + phospholosss + + + + + + Dehydrated + + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to dehydrobutyrine. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 4 H 5 N 1 O 1 + 83.09 + 83.03712 + T + natural + Unimod:23 + uniprot.ptm:PTM-0007 + (2Z)-2-aminobut-2-enoic acid + (Z)-2-amino-2-butenoic acid + (Z)-2-aminobutenoic acid + (Z)-dehydrobutyrine + 2,3-didehydrobutyrine + 3-methyldehydroalanine + Dehydroamino butyric acid + Dhb + Dhb(Thr) + MOD_RES 2,3-didehydrobutyrine + alpha,beta-dehydroaminobutyric acid + anhydrothreonine + beta-elim-t + dehydro + methyl-dehydroalanine + phospholosst + PSI-MOD + Dehydrated + Dehydration + MOD:00190 + + dehydrobutyrine (Thr) + + + + + A protein modification that effectively converts an L-threonine residue to dehydrobutyrine. + DeltaMass:0 + OMSSA:141 + OMSSA:164 + OMSSA:97 + PubMed:1547888 + PubMed:3769923 + RESID:AA0182 + Unimod:23#T + + + + + (2Z)-2-aminobut-2-enoic acid + + + + + + (Z)-2-amino-2-butenoic acid + + + + + + (Z)-2-aminobutenoic acid + + + + + + (Z)-dehydrobutyrine + + + + + + 2,3-didehydrobutyrine + + + + + + 3-methyldehydroalanine + + + + + + Dehydroamino butyric acid + + + + + + Dhb + + + + + + Dhb(Thr) + + + + + + MOD_RES 2,3-didehydrobutyrine + + + + + + alpha,beta-dehydroaminobutyric acid + + + + + + anhydrothreonine + + + + + + beta-elim-t + + + + + + dehydro + + + + + + methyl-dehydroalanine + + + + + + phospholosst + + + + + + Dehydrated + + + + + + Dehydrated + + + + + + Dehydration + + + + + + + + + + A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine. + -2.02 + C 0 H -2 N 0 O 0 + -2.01565 + C 9 H 7 N 1 O 2 + 161.16 + 161.04768 + Y + natural + uniprot.ptm:PTM-0002 + (2Z)-2-amino-3-(4-hydroxyphenyl)prop-2-enoic acid + (Z)-2,3-didehydrogenated tyrosine + (Z)-2,3-didehydrotyrosine + MOD_RES (Z)-2,3-didehydrotyrosine + Z-dHTyr + amino-(para-hydroxybenzylidenyl)acetic acid + cis-dehydrotyrosine + green fluorescent protein chromophore + para-hydroxybenzylidene-imidazolidinone chromophore + red fluorescent protein chromophore + PSI-MOD + 2-amino-3-oxo-butanoic_acid + Didehydro + MOD:00191 + + incidental to RESID:AA0184; incidental to RESID:AA0187; incidental to RESID:AA0188; incidental to RESID:AA0189; incidental to RESID:AA0378; incidental to RESID:AA0379; incidental to RESID:AA0380; incidental to RESID:AA0381 + (Z)-2,3-didehydrotyrosine + + + + + A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine. + PubMed:1347277 + PubMed:9631087 + RESID:AA0183 + + + + + (2Z)-2-amino-3-(4-hydroxyphenyl)prop-2-enoic acid + + + + + + (Z)-2,3-didehydrogenated tyrosine + + + + + + (Z)-2,3-didehydrotyrosine + + + + + + MOD_RES (Z)-2,3-didehydrotyrosine + + + + + + Z-dHTyr + + + + + + amino-(para-hydroxybenzylidenyl)acetic acid + + + + + + cis-dehydrotyrosine + + + + + + green fluorescent protein chromophore + + + + + + para-hydroxybenzylidene-imidazolidinone chromophore + + + + + + red fluorescent protein chromophore + + + + + + 2-amino-3-oxo-butanoic_acid + + + + + + Didehydro + + + + + + + + + + + + + A protein modification that effectively crosslinks an L-serine residue and a glycine residue to form L-serine 5-imidazolinone glycine. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 5 H 6 N 2 O 2 + 126.11 + 126.04293 + G, S + natural + uniprot.ptm:PTM-0049 + (2-[(1R)-1-amino-2-hydroxyethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid + 2-[1-amino-2-hydroxyethyl]-1-carboxymethyl-1-imidazolin-5-one + 4-methylidene-imidazole-5-one (MIO) active site + CROSSLNK 5-imidazolinone (Ser-Gly) + L-serine 5-imidazolinone glycine + green fluorescent protein chromophore + para-hydroxybenzylidene-imidazolidinone chromophore + seryl-5-imidazolinone glycine + PSI-MOD + MOD:00192 + Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365. + L-serine 5-imidazolinone glycine + + + + + A protein modification that effectively crosslinks an L-serine residue and a glycine residue to form L-serine 5-imidazolinone glycine. + ChEBI:21393 + PubMed:1347277 + PubMed:9631087 + RESID:AA0184 + + + + + (2-[(1R)-1-amino-2-hydroxyethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid + + + + + + 2-[1-amino-2-hydroxyethyl]-1-carboxymethyl-1-imidazolin-5-one + + + + + + 4-methylidene-imidazole-5-one (MIO) active site + + + + + + CROSSLNK 5-imidazolinone (Ser-Gly) + + + + + + L-serine 5-imidazolinone glycine + + + + + + green fluorescent protein chromophore + + + + + + para-hydroxybenzylidene-imidazolidinone chromophore + + + + + + seryl-5-imidazolinone glycine + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to L-oxoalanine. + -18.08 + C 0 H -2 N 0 O 1 S -1 + -17.992805 + C 3 H 3 N 1 O 2 + 85.06 + 85.01638 + C + natural + Unimod:402 + uniprot.ptm:PTM-0034 + (S)-2-amino-3-oxopropanoic acid + 2-amino-3-oxopropionic acid + L-3-oxoalanine + L-amino-malonic acid semialdehyde + L-aminomalonaldehydic acid + MOD_RES 3-oxoalanine (Cys) + Oxala(Cys) + PSI-MOD + C(alpha)-formylglycine + L-serinesemialdehyde + MOD:00193 + + L-3-oxoalanine (Cys) + + + + + A protein modification that effectively converts an L-cysteine residue to L-oxoalanine. + DeltaMass:350 + PubMed:14563551 + PubMed:7628016 + PubMed:8681943 + PubMed:9478923 + RESID:AA0185#CYS + Unimod:402#C + + + + + (S)-2-amino-3-oxopropanoic acid + + + + + + 2-amino-3-oxopropionic acid + + + + + + L-3-oxoalanine + + + + + + L-amino-malonic acid semialdehyde + + + + + + L-aminomalonaldehydic acid + + + + + + MOD_RES 3-oxoalanine (Cys) + + + + + + Oxala(Cys) + + + + + + C(alpha)-formylglycine + + + + + + L-serinesemialdehyde + + + + + + + + + + A protein modification that effectively converts an L-serine residue to an amino-terminal lactic acid. + -15.02 + C 0 H -1 N -1 O 0 + -15.010899 + C 3 H 5 O 2 + 73.07 + 73.02895 + S + N-term + Unimod:403 + uniprot.ptm:PTM-0163 + (2R)-2-hydroxypropanoic acid + 2-hydroxypropionic acid + Lac(Ser) + MOD_RES Lactic acid + alpha-hydroxypropionic acid + lactic acid + PSI-MOD + Ser->LacticAcid + lactic acid from N-term Ser + MOD:00194 + lactic acid + + + + + A protein modification that effectively converts an L-serine residue to an amino-terminal lactic acid. + PubMed:7607233 + RESID:AA0186 + Unimod:403#S + + + + + (2R)-2-hydroxypropanoic acid + + + + + + 2-hydroxypropionic acid + + + + + + Lac(Ser) + + + + + + MOD_RES Lactic acid + + + + + + alpha-hydroxypropionic acid + + + + + + lactic acid + + + + + + Ser->LacticAcid + + + + + + lactic acid from N-term Ser + + + + + + + + + + + + + A protein modification that effectively crosslinks an L-alanine residue and a glycine residue to form L-alanine 5-imidazolinone glycine. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 5 H 6 N 2 O 1 + 110.12 + 110.04801 + A, G + natural + uniprot.ptm:PTM-0045 + (2-[(1S)-1-aminoethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid + 2-[1-aminoethyl]-1-carboxymethyl-1-imidazolin-5-one + 4-methylidene-imidazole-5-one active site + CROSSLNK 5-imidazolinone (Ala-Gly) + L-alanine 5-imidazolinone glycine + XLNK-1Ala-NGly(Imidazole) + alanyl-5-imidazolinone glycine + para-hydroxybenzylidene-imidazolidinone chromophore + PSI-MOD + MOD:00195 + Cross-link 2; carboxamidine; incidental to RESID:AA0181; incidental to RESID:AA0183; incidental to RESID:AA0365. + L-alanine 5-imidazolinone glycine + + + + + A protein modification that effectively crosslinks an L-alanine residue and a glycine residue to form L-alanine 5-imidazolinone glycine. + PubMed:10220322 + RESID:AA0187 + + + + + (2-[(1S)-1-aminoethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid + + + + + + 2-[1-aminoethyl]-1-carboxymethyl-1-imidazolin-5-one + + + + + + 4-methylidene-imidazole-5-one active site + + + + + + CROSSLNK 5-imidazolinone (Ala-Gly) + + + + + + L-alanine 5-imidazolinone glycine + + + + + + XLNK-1Ala-NGly(Imidazole) + + + + + + alanyl-5-imidazolinone glycine + + + + + + para-hydroxybenzylidene-imidazolidinone chromophore + + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form L-cysteine 5-imidazolinone glycine. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 5 H 6 N 2 O 1 S 1 + 142.18 + 142.02008 + C, G + natural + uniprot.ptm:PTM-0047 + (2-[(1R)-1-amino-2-sulfanylethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid + 2-[1-amino-2-sulfanylethyl]-1-carboxymethyl-1-imidazolin-5-one + 4-methylidene-imidazole-5-one (MIO) active site + CROSSLNK 5-imidazolinone (Cys-Gly) + L-cysteine 5-imidazolinone glycine + XLNK-1Cys-NGly(Imidazole) + cysteinyl-5-imidazolinone glycine + para-hydroxybenzylidene-imidazolidinone chromophore + PSI-MOD + MOD:00196 + Cross-link 2; carboxamidine; incidental to RESID:AA0181; incidental to RESID:AA0183; incidental to RESID:AA0365. + L-cysteine 5-imidazolinone glycine + + + + + A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form L-cysteine 5-imidazolinone glycine. + PubMed:1537807 + RESID:AA0188 + + + + + (2-[(1R)-1-amino-2-sulfanylethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid + + + + + + 2-[1-amino-2-sulfanylethyl]-1-carboxymethyl-1-imidazolin-5-one + + + + + + 4-methylidene-imidazole-5-one (MIO) active site + + + + + + CROSSLNK 5-imidazolinone (Cys-Gly) + + + + + + L-cysteine 5-imidazolinone glycine + + + + + + XLNK-1Cys-NGly(Imidazole) + + + + + + cysteinyl-5-imidazolinone glycine + + + + + + para-hydroxybenzylidene-imidazolidinone chromophore + + + + + + + + + + + + A protein modification that effectively crosslinks an L-glutamine residue and a glycine residue to form 2-imino-glutamine 5-imidazolinone glycine. + -20.03 + C 0 H -4 N 0 O -1 + -20.026215 + C 7 H 7 N 3 O 2 + 165.15 + 165.05383 + G, Q + natural + uniprot.ptm:PTM-0013 + 2,N-didehydroglutaminyl-5-imidazolinone glycine + 2-(3-carbamoyl-1-imino-propyl)-1-carboxymethyl-1-imidazolin-5-one + 2-imino-glutamine 5-imidazolinone glycine + CROSSLNK 2-iminomethyl-5-imidazolinone (Gln-Gly) + [2-(3-carbamoyl-1-imino-propyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid + [2-(4-amino-4-oxobutanimidoyl)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid + fluorescent protein FP583 chromophore + para-hydroxybenzylidene-imidazolidinone chromophore + red fluorescent protein chromophore + PSI-MOD + MOD:00197 + Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365. + 2-imino-glutamine 5-imidazolinone glycine + + + + + A protein modification that effectively crosslinks an L-glutamine residue and a glycine residue to form 2-imino-glutamine 5-imidazolinone glycine. + PubMed:11050230 + PubMed:11209050 + RESID:AA0189 + + + + + 2,N-didehydroglutaminyl-5-imidazolinone glycine + + + + + + 2-(3-carbamoyl-1-imino-propyl)-1-carboxymethyl-1-imidazolin-5-one + + + + + + 2-imino-glutamine 5-imidazolinone glycine + + + + + + CROSSLNK 2-iminomethyl-5-imidazolinone (Gln-Gly) + + + + + + [2-(3-carbamoyl-1-imino-propyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid + + + + + + [2-(4-amino-4-oxobutanimidoyl)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid + + + + + + fluorescent protein FP583 chromophore + + + + + + para-hydroxybenzylidene-imidazolidinone chromophore + + + + + + red fluorescent protein chromophore + + + + + + + + + + + + A protein modification that effectively converts an L-alanine residue to D-alanine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 3 H 5 N 1 O 1 + 71.08 + 71.03712 + A + natural + uniprot.ptm:PTM-0112 + (R)-2-aminopropanoic acid + D-Ala(Ala) + D-alanine + MOD_RES D-alanine (Ala) + PSI-MOD + MOD:00198 + D-alanine (Ala) + + + + + A protein modification that effectively converts an L-alanine residue to D-alanine. + PubMed:15023056 + PubMed:7287302 + PubMed:7961627 + RESID:AA0191#ALA + + + + + (R)-2-aminopropanoic acid + + + + + + D-Ala(Ala) + + + + + + D-alanine + + + + + + MOD_RES D-alanine (Ala) + + + + + + + + + + + + A protein modification that effectively converts an L-isoleucine residue to a D-allo-isoleucine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 6 H 11 N 1 O 1 + 113.16 + 113.08406 + I + natural + uniprot.ptm:PTM-0114 + (2R,3S)-2-amino-3-methylpentanoic acid + 2-azanyl-3-methylpentanoic acid + 3-methyl-norvaline + D-Ile + D-allo-isoleucine + D-threo-isoleucine + MOD_RES D-allo-isoleucine + allo-D-isoleucine + alpha-amino-beta-methylvaleric acid + PSI-MOD + MOD:00199 + D-allo-isoleucine + + + + + A protein modification that effectively converts an L-isoleucine residue to a D-allo-isoleucine. + ChEBI:30007 + PubMed:8223491 + RESID:AA0192 + + + + + (2R,3S)-2-amino-3-methylpentanoic acid + + + + + + 2-azanyl-3-methylpentanoic acid + + + + + + 3-methyl-norvaline + + + + + + D-Ile + + + + + + D-allo-isoleucine + + + + + + D-threo-isoleucine + + + + + + MOD_RES D-allo-isoleucine + + + + + + allo-D-isoleucine + + + + + + alpha-amino-beta-methylvaleric acid + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to D-methionine. + 0.0 + C 0 H 0 N 0 O 0 S 0 + 0.0 + C 5 H 9 N 1 O 1 S 1 + 131.19 + 131.04048 + M + natural + uniprot.ptm:PTM-0120 + (2R)-2-amino-4-(methylsulfanyl)butanoic acid + 2-amino-4-(methylthio)butanoic acid + 2-amino-4-(methylthio)butyric acid + D-Met + D-methionine + MOD_RES D-methionine + PSI-MOD + MOD:00200 + D-methionine + + + + + A protein modification that effectively converts an L-methionine residue to D-methionine. + ChEBI:29984 + PubMed:16033333 + PubMed:2542051 + RESID:AA0193 + + + + + (2R)-2-amino-4-(methylsulfanyl)butanoic acid + + + + + + 2-amino-4-(methylthio)butanoic acid + + + + + + 2-amino-4-(methylthio)butyric acid + + + + + + D-Met + + + + + + D-methionine + + + + + + MOD_RES D-methionine + + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to D-phenylalanine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 9 H 9 N 1 O 1 + 147.18 + 147.06842 + F + natural + uniprot.ptm:PTM-0121 + (R)-2-amino-3-phenylpropanoic acid + D-Phe + D-phenylalanine + MOD_RES D-phenylalanine + PSI-MOD + MOD:00201 + D-phenylalanine + + + + + A protein modification that effectively converts an L-phenylalanine residue to D-phenylalanine. + ChEBI:29996 + PubMed:1548227 + PubMed:1644179 + PubMed:2597281 + RESID:AA0194 + + + + + (R)-2-amino-3-phenylpropanoic acid + + + + + + D-Phe + + + + + + D-phenylalanine + + + + + + MOD_RES D-phenylalanine + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to D-serine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 3 H 5 N 1 O 2 + 87.08 + 87.03203 + S + natural + uniprot.ptm:PTM-0308 + (R)-2-amino-3-hydroxypropanoic acid + D-Ser(Ser) + D-serine + MOD_RES D-serine (Ser) + PSI-MOD + MOD:00202 + D-serine (Ser) + + + + + A protein modification that effectively converts an L-serine residue to D-serine. + PubMed:7973665 + RESID:AA0195#SER + + + + + (R)-2-amino-3-hydroxypropanoic acid + + + + + + D-Ser(Ser) + + + + + + D-serine + + + + + + MOD_RES D-serine (Ser) + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to D-asparagine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 4 H 6 N 2 O 2 + 114.1 + 114.04293 + N + natural + uniprot.ptm:PTM-0115 + (R)-2-amino-4-butanediamic acid + D-Asn + D-alpha-aminosuccinamic acid + D-asparagine + D-aspartic acid beta-amide + MOD_RES D-asparagine + PSI-MOD + MOD:00203 + D-asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to D-asparagine. + ChEBI:29957 + PubMed:1859408 + RESID:AA0196 + + + + + (R)-2-amino-4-butanediamic acid + + + + + + D-Asn + + + + + + D-alpha-aminosuccinamic acid + + + + + + D-asparagine + + + + + + D-aspartic acid beta-amide + + + + + + MOD_RES D-asparagine + + + + + + + + + + + + A protein modification that effectively converts an L-leucine residue to D-leucine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 6 H 11 N 1 O 1 + 113.16 + 113.08406 + L + natural + uniprot.ptm:PTM-0119 + (2R)-2-amino-4-methylpentanoic acid + D-Leu + D-leucine + MOD_RES D-leucine + alpha-aminoisocaproic acid + PSI-MOD + MOD:00204 + D-leucine + + + + + A protein modification that effectively converts an L-leucine residue to D-leucine. + ChEBI:30005 + PubMed:10461743 + PubMed:12135762 + PubMed:1358533 + PubMed:1548227 + RESID:AA0197 + + + + + (2R)-2-amino-4-methylpentanoic acid + + + + + + D-Leu + + + + + + D-leucine + + + + + + MOD_RES D-leucine + + + + + + alpha-aminoisocaproic acid + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to D-tryptophan. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 11 H 10 N 2 O 1 + 186.21 + 186.07932 + W + natural + uniprot.ptm:PTM-0123 + (R)-2-amino-3-(1H-indol-3-yl)propanoic acid + D-Trp + D-tryptophan + MOD_RES D-tryptophan + alpha-amino-beta-(3-indolyl)propionoic acid + PSI-MOD + MOD:00205 + D-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to D-tryptophan. + ChEBI:29955 + PubMed:8910408 + RESID:AA0198 + + + + + (R)-2-amino-3-(1H-indol-3-yl)propanoic acid + + + + + + D-Trp + + + + + + D-tryptophan + + + + + + MOD_RES D-tryptophan + + + + + + alpha-amino-beta-(3-indolyl)propionoic acid + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-isoglutamyl-polyglycine. + E + natural + uniprot.ptm:PTM-0394 + L-isoglutamyl-polyglycine + MOD_RES 5-glutamyl polyglycine + gamma-glutamylpolyglycine + PSI-MOD + MOD:00206 + L-isoglutamyl-polyglycine + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-isoglutamyl-polyglycine. + ChEBI:21343 + PubMed:10074368 + PubMed:16368691 + PubMed:7992051 + RESID:AA0201 + + + + + L-isoglutamyl-polyglycine + + + + + + MOD_RES 5-glutamyl polyglycine + + + + + + gamma-glutamylpolyglycine + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl-polyglutamic acid, forming an isopeptide bond with a polyglutamic acid. + E + natural + uniprot.ptm:PTM-0395 + L-isoglutamyl-polyglutamic acid + gamma-glutamylpolyglutamic acid + PSI-MOD + MOD:00207 + L-isoglutamyl-polyglutamic acid + + + + + A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl-polyglutamic acid, forming an isopeptide bond with a polyglutamic acid. + PubMed:10747868 + PubMed:1680872 + RESID:AA0202 + + + + + L-isoglutamyl-polyglutamic acid + + + + + + gamma-glutamylpolyglutamic acid + + + + + + + + + + + A protein modification that effectively crosslinks an L-tyrosine residue and 5'-phosphoadenosine through a phosphodiester bond to form O4'-(phospho-5'-adenosine)-L-tyrosine. + 329.21 + C 10 H 12 N 5 O 6 P 1 + 329.05252 + C 19 H 21 N 6 O 8 P 1 + 492.38 + 492.11584 + Y + natural + Unimod:405 + uniprot.ptm:PTM-0332 + (2S)-2-amino-3-[4-(5'-adenosine phosphonoxy)phenyl]propanoic acid + 5'-adenylic-O-tyrosine + MOD_RES O-AMP-tyrosine + O-5'-Adenosylation ( of Tyrosine) + O4'-(phospho-5'-adenosine)-L-tyrosine + O4'-L-tyrosine 5'-adenosine phosphodiester + OAMPTyr + hydrogen 5'-adenylate tyrosine ester + PSI-MOD + AMP binding site + Phosphoadenosine + MOD:00208 + + From DeltaMass: Average Mass: 329. + O4'-(phospho-5'-adenosine)-L-tyrosine + + + + + A protein modification that effectively crosslinks an L-tyrosine residue and 5'-phosphoadenosine through a phosphodiester bond to form O4'-(phospho-5'-adenosine)-L-tyrosine. + DeltaMass:0 + PubMed:5543675 + RESID:AA0203 + Unimod:405#Y + + + + + (2S)-2-amino-3-[4-(5'-adenosine phosphonoxy)phenyl]propanoic acid + + + + + + 5'-adenylic-O-tyrosine + + + + + + MOD_RES O-AMP-tyrosine + + + + + + O-5'-Adenosylation ( of Tyrosine) + + + + + + O4'-(phospho-5'-adenosine)-L-tyrosine + + + + + + O4'-L-tyrosine 5'-adenosine phosphodiester + + + + + + OAMPTyr + + + + + + hydrogen 5'-adenylate tyrosine ester + + + + + + AMP binding site + + + + + + Phosphoadenosine + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form S-(2-aminovinyl)-D-cysteine. + -64.04 + C -1 H -4 N 0 O -3 S 0 + -64.016045 + C 5 H 7 N 2 O 1 S 1 + 143.18 + 143.02791 + C, S + C-term + uniprot.ptm:PTM-0268 + (2S)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid + (S,Z)-S-(2-aminovinyl)cysteine + CROSSLNK S-(2-aminovinyl)-D-cysteine (Ser-Cys) + S-(2-aminovinyl)-D-cysteine + XLNK-(D)SCys-VinAm + PSI-MOD + MOD:00209 + Cross-link 2. + S-(2-aminovinyl)-D-cysteine (Cys-Ser) + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form S-(2-aminovinyl)-D-cysteine. + PubMed:3181159 + PubMed:3769923 + RESID:AA0204#SER + + + + + (2S)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid + + + + + + (S,Z)-S-(2-aminovinyl)cysteine + + + + + + CROSSLNK S-(2-aminovinyl)-D-cysteine (Ser-Cys) + + + + + + S-(2-aminovinyl)-D-cysteine + + + + + + XLNK-(D)SCys-VinAm + + + + + + + + + + + A protein modification that effectively monooxygenates an L-cysteine residue to L-cysteine sulfenic acid. + 16.0 + C 0 H 0 N 0 O 1 S 0 + 15.994915 + C 3 H 5 N 1 O 2 S 1 + 119.14 + 119.0041 + C + natural + Unimod:35 + uniprot.ptm:PTM-0107 + (2R)-2-amino-3-(hydroxysulfanyl)propanoic acid + (2R)-2-amino-3-(oxido-lambda(4)-sulfanyl)propanoic acid [tautomer] + 2-amino-2-carboxyethanesulfenic acid + 2-amino-3-sulfinylpropanoic acid [tautomer] + 3-sulfenoalanine + ACT_SITE Cysteine sulfenic acid (-SOH) intermediate + CysOH + L-cysteine sulfenic acid + MOD_RES Cysteine sulfenic acid (-SOH) + S-hydroxycysteine + S-oxocysteine [tautomer] + S-oxycysteine [tautomer] + Sulfenic Acid (from Cysteine) + cysteine S-oxide [tautomer] + cysteine sulfoxide [tautomer] + cysteine sulphenic acid + mod193 + PSI-MOD + Oxidation + MOD:00210 + + From DeltaMass: Average Mass: 16 Average Mass Change:16 Notes:Green et al. in J. B. C. 270, 18209-18211 (1995) quote Kim and Raines in Eur. J. Biochem. 224, 109-114 (1994). Kim and Raines using ESI-MS and sulfhydryl group titration found that bovine seminal ribonuclease contains a single oxidized sulfhydryl group, which cannot participate in a disulfide bond. This form of cysteine is called sulfenic acid (-SOH). + L-cysteine sulfenic acid + + + + + A protein modification that effectively monooxygenates an L-cysteine residue to L-cysteine sulfenic acid. + DeltaMass:41 + OMSSA:193 + PubMed:10964927 + PubMed:2501303 + PubMed:8756456 + PubMed:9214307 + PubMed:9586994 + PubMed:9587003 + RESID:AA0205 + Unimod:35#C + + + + + (2R)-2-amino-3-(hydroxysulfanyl)propanoic acid + + + + + + (2R)-2-amino-3-(oxido-lambda(4)-sulfanyl)propanoic acid [tautomer] + + + + + + 2-amino-2-carboxyethanesulfenic acid + + + + + + 2-amino-3-sulfinylpropanoic acid [tautomer] + + + + + + 3-sulfenoalanine + + + + + + ACT_SITE Cysteine sulfenic acid (-SOH) intermediate + + + + + + CysOH + + + + + + L-cysteine sulfenic acid + + + + + + MOD_RES Cysteine sulfenic acid (-SOH) + + + + + + S-hydroxycysteine + + + + + + S-oxocysteine [tautomer] + + + + + + S-oxycysteine [tautomer] + + + + + + Sulfenic Acid (from Cysteine) + + + + + + cysteine S-oxide [tautomer] + + + + + + cysteine sulfoxide [tautomer] + + + + + + cysteine sulphenic acid + + + + + + mod193 + + + + + + Oxidation + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a thioester bond to form S-glycyl-L-cysteine. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 5 H 7 N 2 O 2 S 1 + 159.18 + 159.02283 + C, G + C-term + uniprot.ptm:PTM-0429 + (2R)-2-amino-3-[(aminoacetyl)sulfanyl]propanoic acid + 1-(cystein-S-yl)-glycinate + ACT_SITE Glycyl thioester intermediate + S-(2-amino-1-oxoethyl)cysteine + S-(glycyl)-L-cysteine + XLNK-SCys-1Gly + glycine cysteine thioester + PSI-MOD + MOD:00211 + + Cross-link 2. For the modification of a C-terminal glycine by formation of a thioester bond with free L-cysteine see MOD:01777 [JSG]. + S-(glycyl)-L-cysteine (Cys-Gly) + + + + + A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a thioester bond to form S-glycyl-L-cysteine. + ChEBI:22050 + PubMed:3306404 + RESID:AA0206 + + + + + (2R)-2-amino-3-[(aminoacetyl)sulfanyl]propanoic acid + + + + + + 1-(cystein-S-yl)-glycinate + + + + + + ACT_SITE Glycyl thioester intermediate + + + + + + S-(2-amino-1-oxoethyl)cysteine + + + + + + S-(glycyl)-L-cysteine + + + + + + XLNK-SCys-1Gly + + + + + + glycine cysteine thioester + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-4-hydroxycinnamyl-L-cysteine. + 146.14 + C 9 H 6 N 0 O 2 S 0 + 146.03677 + C 12 H 11 N 1 O 3 S 1 + 249.28 + 249.04596 + C + natural + Unimod:407 + uniprot.ptm:PTM-0414 + (2R)-2-amino-3-([(2E)-3-(4-hydroxyphenyl)prop-2-enoyl]sulfanyl)propanoic acid + MOD_RES S-(4-hydroxycinnamyl)cysteine + S-4-hydroxycinnamyl-L-cysteine + S-para-coumaryl-L-cysteine + cinnamate cysteine thioester + PSI-MOD + Hydroxycinnamyl + hydroxycinnamyl + MOD:00212 + S-4-hydroxycinnamyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-4-hydroxycinnamyl-L-cysteine. + PubMed:7947803 + PubMed:7981196 + RESID:AA0207 + Unimod:407 + + + + + (2R)-2-amino-3-([(2E)-3-(4-hydroxyphenyl)prop-2-enoyl]sulfanyl)propanoic acid + + + + + + MOD_RES S-(4-hydroxycinnamyl)cysteine + + + + + + S-4-hydroxycinnamyl-L-cysteine + + + + + + S-para-coumaryl-L-cysteine + + + + + + cinnamate cysteine thioester + + + + + + Hydroxycinnamyl + + + + + + hydroxycinnamyl + + + + + + + + + + A protein modification that effectively cross-links an L-serine residue to the polymer chondroitin sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide. + S + natural + chondroitin 4-sulfate (chondroitin sulfate A) + chondroitin 6-sulfate (chondroitin sulfate C) + chondroitin sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine + poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate-D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine; poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-6-sulfate D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine + PSI-MOD + MOD:00213 + chondroitin sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine + + + + + A protein modification that effectively cross-links an L-serine residue to the polymer chondroitin sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide. + PubMed:1794445 + PubMed:1898736 + PubMed:3472204 + RESID:AA0208 + + + + + chondroitin 4-sulfate (chondroitin sulfate A) + + + + + + chondroitin 6-sulfate (chondroitin sulfate C) + + + + + + chondroitin sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine + + + + + + poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate-D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine; poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-6-sulfate D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine + + + + + + + + + + A protein modification that effectively cross-links an L-serine residue to the polymer dermatan 4-sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide. + S + natural + beta-heparin + chondroitin sulfate B + dermatan 4-sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine + poly[beta-1,4-L-idopyranuronosyl-alpha-1,3-(2-acetamido-2-deoxy-4-sulfate D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine + PSI-MOD + MOD:00214 + dermatan 4-sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine + + + + + A protein modification that effectively cross-links an L-serine residue to the polymer dermatan 4-sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide. + PubMed:2914936 + PubMed:3472204 + RESID:AA0209 + + + + + beta-heparin + + + + + + chondroitin sulfate B + + + + + + dermatan 4-sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine + + + + + + poly[beta-1,4-L-idopyranuronosyl-alpha-1,3-(2-acetamido-2-deoxy-4-sulfate D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine + + + + + + + + + + A protein modification that effectively cross-links an L-serine residue to the polymer heparan sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide. + S + natural + heparan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine + heparin + heparitin sulfate + poly[alpha-1,4-(2-sulfate D-glucopyranuronosyl)-beta-1,4-(2-sulfamino-2-deoxy-6-sulfate D-glucosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine + PSI-MOD + MOD:00215 + heparan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine + + + + + A protein modification that effectively cross-links an L-serine residue to the polymer heparan sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide. + PubMed:3472204 + RESID:AA0210 + + + + + heparan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine + + + + + + heparin + + + + + + heparitin sulfate + + + + + + poly[alpha-1,4-(2-sulfate D-glucopyranuronosyl)-beta-1,4-(2-sulfamino-2-deoxy-6-sulfate D-glucosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-formyl-L-lysine. + 28.01 + C 1 H 0 N 0 O 1 + 27.994915 + C 7 H 12 N 2 O 2 + 156.19 + 156.08987 + K + natural + Unimod:122 + uniprot.ptm:PTM-0192 + (2S)-2-amino-6-(formylamino)hexanoic acid + MOD_RES N6-formyllysine + N(zeta)-formyllysine + N6-formyl-L-lysine + N6-formylated L-lysine + N6FoLys + epsilon-formyllysine + formylk + PSI-MOD + Formyl + Formylation + MOD:00216 + + N6-formyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-formyl-L-lysine. + OMSSA:43 + PubMed:15799070 + RESID:AA0211 + Unimod:122#K + + + + + (2S)-2-amino-6-(formylamino)hexanoic acid + + + + + + MOD_RES N6-formyllysine + + + + + + N(zeta)-formyllysine + + + + + + N6-formyl-L-lysine + + + + + + N6-formylated L-lysine + + + + + + N6FoLys + + + + + + epsilon-formyllysine + + + + + + formylk + + + + + + Formyl + + + + + + Formylation + + + + + + + + + + + A protein modification that effectively converts an L-proline residue to O4-arabinosyl-L-hydroxyproline. + 148.11 + C 5 H 8 N 0 O 5 + 148.03717 + C 10 H 15 N 1 O 6 + 245.23 + 245.08994 + P + natural + Unimod:408 + uniprot.ptm:PTM-0545 + (2S,4R)-4-(beta-L-arabinofuranosyloxy)pyrrolidine-2-carboxylic acid + 4-(beta-L-arabinofuranosyloxy)proline + 4-Glycosyloxy- (pentosyl,C5) (of Proline) + O4-arabinosyl-L-hydroxyproline + O4-glycosyl-hydroxyproline + OAra4HyPro + beta-arabinofuranosyl-4-hydroxyproline + PSI-MOD + Glycosyl + glycosyl-L-hydroxyproline + MOD:00217 + + secondary to RESID:AA0030; From DeltaMass: Average Mass: 147. + O4-arabinosyl-L-hydroxyproline + + + + + A protein modification that effectively converts an L-proline residue to O4-arabinosyl-L-hydroxyproline. + DeltaMass:0 + PubMed:666730 + PubMed:7852316 + RESID:AA0212 + Unimod:408 + + + + + (2S,4R)-4-(beta-L-arabinofuranosyloxy)pyrrolidine-2-carboxylic acid + + + + + + 4-(beta-L-arabinofuranosyloxy)proline + + + + + + 4-Glycosyloxy- (pentosyl,C5) (of Proline) + + + + + + O4-arabinosyl-L-hydroxyproline + + + + + + O4-glycosyl-hydroxyproline + + + + + + OAra4HyPro + + + + + + beta-arabinofuranosyl-4-hydroxyproline + + + + + + Glycosyl + + + + + + glycosyl-L-hydroxyproline + + + + + + + + + + + A protein modification that effectively crosslinks an L-serine residue and the 5'-end of RNA through a phosphodiester to form O4'-(phospho-5'-RNA)-L-serine. + S + natural + uniprot.ptm:PTM-0227 + (S)-2-amino-3-(5'-ribonucleic acid phosphonoxy)propanoic acid + MOD_RES O-(5'-phospho-RNA)-serine + O-(phospho-5'-RNA)-L-serine + O3-(phospho-5'-RNA)-L-serine + O3-L-serine 5'-RNA phosphodiester + PSI-MOD + MOD:00218 + O-(phospho-5'-RNA)-L-serine + + + + + A protein modification that effectively crosslinks an L-serine residue and the 5'-end of RNA through a phosphodiester to form O4'-(phospho-5'-RNA)-L-serine. + PubMed:1705009 + RESID:AA0213 + + + + + (S)-2-amino-3-(5'-ribonucleic acid phosphonoxy)propanoic acid + + + + + + MOD_RES O-(5'-phospho-RNA)-serine + + + + + + O-(phospho-5'-RNA)-L-serine + + + + + + O3-(phospho-5'-RNA)-L-serine + + + + + + O3-L-serine 5'-RNA phosphodiester + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to L-citrulline. + 0.98 + C 0 H -1 N -1 O 1 + 0.984016 + C 6 H 11 N 3 O 2 + 157.17 + 157.08513 + R + natural + Unimod:7 + uniprot.ptm:PTM-0092 + (S)-2-amino-5-(carbamoylamino)pentanoic acid + 2-amino-5-(aminocarbonyl)aminopentanoic acid + Cit + Citrulline + L-citrulline + MOD_RES Citrulline + N5-(aminocarbonyl)ornithine + N5-carbamoylornithine + N5-carbamylornithine + alpha-amino-delta-ureidovaleric acid + citrullinationr + delta-ureidonorvaline + PSI-MOD + Deamidated + Deamidation + MOD:00219 + + This modification is not the result of deamidation, instead the guanidino group is replaced with an ureido group. + L-citrulline + + + + + A protein modification that effectively converts an L-arginine residue to L-citrulline. + DeltaMass:0 + OMSSA:33 + PubMed:2466844 + RESID:AA0214 + Unimod:7#R + + + + + (S)-2-amino-5-(carbamoylamino)pentanoic acid + + + + + + 2-amino-5-(aminocarbonyl)aminopentanoic acid + + + + + + Cit + + + + + + Citrulline + + + + + + L-citrulline + + + + + + MOD_RES Citrulline + + + + + + N5-(aminocarbonyl)ornithine + + + + + + N5-carbamoylornithine + + + + + + N5-carbamylornithine + + + + + + alpha-amino-delta-ureidovaleric acid + + + + + + citrullinationr + + + + + + delta-ureidonorvaline + + + + + + Deamidated + + + + + + Deamidated + + + + + + Deamidation + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to a 4-hydroxy-L-arginine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 6 H 12 N 4 O 2 + 172.19 + 172.09602 + R + natural + uniprot.ptm:PTM-0042 + (2S,4Xi)-2-amino-5-[(diaminomethylidene)amino]-4-hydroxypentanoic acid + 2-amino-5-(carbamimidamido)-4-hydroxypentanoic acid [tautomer] + 2-amino-5-[(aminoiminomethyl)amino]-4-hydroxypentanoic acid [tautomer] + 2-amino-5-guanidino-4-hydroxypentanoic acid + 4-hydroxy-L-arginine + 4-hydroxylated L-arginine + 4HyArg + C(gamma)-hydroxyarginine + MOD_RES 4-hydroxyarginine + gamma-hydroxyarginine + PSI-MOD + MOD:00220 + 4-hydroxy-L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to a 4-hydroxy-L-arginine. + PubMed:10966817 + PubMed:7650037 + RESID:AA0215 + + + + + (2S,4Xi)-2-amino-5-[(diaminomethylidene)amino]-4-hydroxypentanoic acid + + + + + + 2-amino-5-(carbamimidamido)-4-hydroxypentanoic acid [tautomer] + + + + + + 2-amino-5-[(aminoiminomethyl)amino]-4-hydroxypentanoic acid [tautomer] + + + + + + 2-amino-5-guanidino-4-hydroxypentanoic acid + + + + + + 4-hydroxy-L-arginine + + + + + + 4-hydroxylated L-arginine + + + + + + 4HyArg + + + + + + C(gamma)-hydroxyarginine + + + + + + MOD_RES 4-hydroxyarginine + + + + + + gamma-hydroxyarginine + + + + + + + + + + + + + A protein modification that effectively crosslinks L-aspartic acid and L-cysteine residues via an isopeptide bond to form N-(L-isoaspartyl)-L-cysteine. + -17.03 + C 0 H -3 N -1 O 0 S 0 + -17.026548 + C 7 H 9 N 2 O 3 S 1 + 201.22 + 201.03339 + C, N + natural + N-term + uniprot.ptm:PTM-0151 + (S)-2-amino-4-((R)-1-carboxy-2-sulfanylethyl)amino-4-oxobutanoic acid + 2-(3-amino-3-carboxypropanoyl)amino-3-mercaptopropanoic acid + 2-amino-N4-(1-carboxy-2-mercaptoethyl)butanediamic acid + CROSSLNK Isoaspartyl cysteine isopeptide (Cys-Asn) + N-(L-isoaspartyl)-L-cysteine + N-beta-aspartylcysteine + N-isoaspartyl cysteine + PSI-MOD + MOD:00221 + Cross-link 2. + N-(L-isoaspartyl)-L-cysteine + + + + + A protein modification that effectively crosslinks L-aspartic acid and L-cysteine residues via an isopeptide bond to form N-(L-isoaspartyl)-L-cysteine. + PubMed:8286361 + RESID:AA0216 + + + + + (S)-2-amino-4-((R)-1-carboxy-2-sulfanylethyl)amino-4-oxobutanoic acid + + + + + + 2-(3-amino-3-carboxypropanoyl)amino-3-mercaptopropanoic acid + + + + + + 2-amino-N4-(1-carboxy-2-mercaptoethyl)butanediamic acid + + + + + + CROSSLNK Isoaspartyl cysteine isopeptide (Cys-Asn) + + + + + + N-(L-isoaspartyl)-L-cysteine + + + + + + N-beta-aspartylcysteine + + + + + + N-isoaspartyl cysteine + + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to 2'-alpha-mannosyl-L-tryptophan. + 162.14 + C 6 H 10 N 0 O 5 + 162.05283 + C 17 H 20 N 2 O 6 + 348.36 + 348.13214 + W + natural + Unimod:41 + uniprot.ptm:PTM-0505 + (2S)-2-amino-3-(2-beta-D-mannopyranosyl-1H-indol-3-yl)propanoic acid + 2'-mannosyl-L-tryptophan + 2'-tryptophan C-mannoside + C2'ManTrp + CARBOHYD C-linked (Man) tryptophan + PSI-MOD + Hex + Hexose + MOD:00222 + 2'-alpha-mannosyl-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to 2'-alpha-mannosyl-L-tryptophan. + PubMed:15279557 + PubMed:7547911 + PubMed:7947762 + RESID:AA0217 + Unimod:41#W + + + + + (2S)-2-amino-3-(2-beta-D-mannopyranosyl-1H-indol-3-yl)propanoic acid + + + + + + 2'-mannosyl-L-tryptophan + + + + + + 2'-tryptophan C-mannoside + + + + + + C2'ManTrp + + + + + + CARBOHYD C-linked (Man) tryptophan + + + + + + Hex + + + + + + Hexose + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-mureinyl-L-lysine. + K + natural + uniprot.ptm:PTM-0195 + MOD_RES N6-murein peptidoglycan lysine + N6-[(2R,6S)-2-(N-(N-mureinyl-(R)-alanyl)-(S)-glutamyl)amino-6-amino-6-carboxy-1-oxohex-1-yl]lysine + N6-mureinyl-L-lysine + PSI-MOD + MOD:00223 + N6-mureinyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-mureinyl-L-lysine. + PubMed:4261992 + RESID:AA0218 + + + + + MOD_RES N6-murein peptidoglycan lysine + + + + + + N6-[(2R,6S)-2-(N-(N-mureinyl-(R)-alanyl)-(S)-glutamyl)amino-6-amino-6-carboxy-1-oxohex-1-yl]lysine + + + + + + N6-mureinyl-L-lysine + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to 1-chondroitin sulfate-L-aspartic acid ester + D + C-term + uniprot.ptm:PTM-0334 + 1-aspartic acid ester with 6-chondroitin 4-sulfate + 1-chondroitin sulfate-L-aspartic acid ester + MOD_RES Aspartate 1-(chondroitin 4-sulfate)-ester + poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate D-galactosyl)]beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate-6-(1-L-aspartyl)-D-galactose) + protein-glycosaminoglycan-protein cross-link + PSI-MOD + MOD:00224 + 1-chondroitin sulfate-L-aspartic acid ester + + + + + A protein modification that effectively converts an L-aspartic acid residue to 1-chondroitin sulfate-L-aspartic acid ester + PubMed:1898736 + RESID:AA0219 + + + + + 1-aspartic acid ester with 6-chondroitin 4-sulfate + + + + + + 1-chondroitin sulfate-L-aspartic acid ester + + + + + + MOD_RES Aspartate 1-(chondroitin 4-sulfate)-ester + + + + + + poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate D-galactosyl)]beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate-6-(1-L-aspartyl)-D-galactose) + + + + + + protein-glycosaminoglycan-protein cross-link + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-(6-FMN)-L-cysteine. + 454.33 + C 17 H 19 N 4 O 9 P 1 S 0 + 454.08896 + C 20 H 24 N 5 O 10 P 1 S 1 + 557.47 + 557.09814 + C + natural + Unimod:409 + uniprot.ptm:PTM-0271 + (R)-2-amino-3-[6-riboflavin 5'-dihydrogen phosphate]sulfanylpropanoic acid + 6-[S-cysteinyl]FMN + 6-[S-cysteinyl]flavin mononucleotide + MOD_RES S-6-FMN cysteine + S-(6-FMN)-L-cysteine + S6FMNCys + PSI-MOD + FMNH + flavin mononucleotide + MOD:00225 + + S-(6-FMN)-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-(6-FMN)-L-cysteine. + PubMed:10869173 + PubMed:1551870 + PubMed:620783 + RESID:AA0220 + Unimod:409#C + + + + + (R)-2-amino-3-[6-riboflavin 5'-dihydrogen phosphate]sulfanylpropanoic acid + + + + + + 6-[S-cysteinyl]FMN + + + + + + 6-[S-cysteinyl]flavin mononucleotide + + + + + + MOD_RES S-6-FMN cysteine + + + + + + S-(6-FMN)-L-cysteine + + + + + + S6FMNCys + + + + + + FMNH + + + + + + flavin mononucleotide + + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FAD)-L-histidine. + 783.54 + C 27 H 31 N 9 O 15 P 2 + 783.1415 + C 33 H 38 N 12 O 16 P 2 + 920.68 + 920.2004 + H + natural + Unimod:50 + uniprot.ptm:PTM-0288 + (S)-2-amino-3-(1-[8alpha riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid + 1'-(8alpha-FAD)-L-histidine + 8alpha-(N(epsilon)-histidyl)FAD + 8alpha-(N1'-histidyl)FAD + MOD_RES Tele-8alpha-FAD histidine + N theta and N pi-(8alpha-Flavin) (on Histidine) + N(tau)-(8alpha-FAD)-histidine + Nt8aFADHis + tele-(8alpha-FAD)-histidine + PSI-MOD + 8alpha-N3-histidyl FAD + FAD + Flavin adenine dinucleotide + MOD:00226 + + From DeltaMass: Average Mass: 784 + 1'-(8alpha-FAD)-L-histidine + + + + + A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FAD)-L-histidine. + DeltaMass:0 + PubMed:10585424 + PubMed:1396672 + PubMed:4339951 + PubMed:9261083 + RESID:AA0221 + Unimod:50#H + + + + + (S)-2-amino-3-(1-[8alpha riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid + + + + + + 1'-(8alpha-FAD)-L-histidine + + + + + + 8alpha-(N(epsilon)-histidyl)FAD + + + + + + 8alpha-(N1'-histidyl)FAD + + + + + + MOD_RES Tele-8alpha-FAD histidine + + + + + + N theta and N pi-(8alpha-Flavin) (on Histidine) + + + + + + N(tau)-(8alpha-FAD)-histidine + + + + + + Nt8aFADHis + + + + + + tele-(8alpha-FAD)-histidine + + + + + + 8alpha-N3-histidyl FAD + + + + + + FAD + + + + + + Flavin adenine dinucleotide + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to omega-N-phospho-L-arginine. + 79.98 + C 0 H 1 N 0 O 3 P 1 + 79.96633 + C 6 H 13 N 4 O 4 P 1 + 236.17 + 236.06744 + R + natural + Unimod:21 + uniprot.ptm:PTM-0250 + (2S)-2-amino-5-(N'-phosphonocarbamimidamido)pentanoic acid + (2S)-2-amino-5-([amino(phosphonoamino)methylidene]amino)pentanoic acid + MOD_RES Phosphoarginine + N(gamma)-phosphoarginine + N(omega)-phosphono-L-arginine + N5-[imino(phosphonoamino)methyl]-L-ornithine + PArg + alpha-amino-delta-phosphonoguanidinovaleric acid + omega-N-phospho-L-arginine + phosphoarginine + PSI-MOD + Phospho + Phosphorylation + MOD:00227 + + omega-N-phospho-L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to omega-N-phospho-L-arginine. + PubMed:8300603 + RESID:AA0222 + Unimod:21#R + + + + + (2S)-2-amino-5-(N'-phosphonocarbamimidamido)pentanoic acid + + + + + + (2S)-2-amino-5-([amino(phosphonoamino)methylidene]amino)pentanoic acid + + + + + + MOD_RES Phosphoarginine + + + + + + N(gamma)-phosphoarginine + + + + + + N(omega)-phosphono-L-arginine + + + + + + N5-[imino(phosphonoamino)methyl]-L-ornithine + + + + + + PArg + + + + + + alpha-amino-delta-phosphonoguanidinovaleric acid + + + + + + omega-N-phospho-L-arginine + + + + + + phosphoarginine + + + + + + Phospho + + + + + + Phosphorylation + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-diphytanylglycerol diether-L-cysteine. + 635.16 + C 43 H 86 N 0 O 2 S 0 + 634.6628 + C 46 H 91 N 1 O 3 S 1 + 738.3 + 737.672 + C + natural + Unimod:410 + uniprot.ptm:PTM-0273 + (2R)-2-amino-3-([(2S)-2,3-bis(3,7,11,15-tetramethylhexadecanyloxy)propyl]sulfanyl)propanoic acid + LIPID S-archaeol cysteine + S-(diphytanylglyceryl)-L-cysteine + S-[2',3'-bis(phytanyloxy)propyl]cysteine + S-archaeol cysteine + SPhyt2GlyceroCys + PSI-MOD + Archaeol + S-diphytanylglycerol diether + MOD:00228 + + incidental to RESID:AA0043. + S-diphytanylglycerol diether-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-diphytanylglycerol diether-L-cysteine. + PubMed:7797461 + PubMed:8195126 + RESID:AA0223 + Unimod:410 + + + + + (2R)-2-amino-3-([(2S)-2,3-bis(3,7,11,15-tetramethylhexadecanyloxy)propyl]sulfanyl)propanoic acid + + + + + + LIPID S-archaeol cysteine + + + + + + S-(diphytanylglyceryl)-L-cysteine + + + + + + S-[2',3'-bis(phytanyloxy)propyl]cysteine + + + + + + S-archaeol cysteine + + + + + + SPhyt2GlyceroCys + + + + + + Archaeol + + + + + + S-diphytanylglycerol diether + + + + + + + + + + A protein modification that effectively converts two L-cysteine residues to form alpha-1-microglobulin-Ig alpha complex chromophore. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 6 H 8 N 2 O 2 S 2 + 204.26 + 204.00272 + C, C + natural + BINDING Multimeric 3-hydroxykynurenine chromophore (covalent) + alpha-1-microglobulin-Ig alpha complex chromophore + PSI-MOD + MOD:00229 + Cross-link 2. + alpha-1-microglobulin-Ig alpha complex chromophore + + + + + A protein modification that effectively converts two L-cysteine residues to form alpha-1-microglobulin-Ig alpha complex chromophore. + PubMed:11058759 + PubMed:11877257 + PubMed:7506257 + PubMed:7535251 + RESID:AA0224 + + + + + BINDING Multimeric 3-hydroxykynurenine chromophore (covalent) + + + + + + alpha-1-microglobulin-Ig alpha complex chromophore + + + + + + + + + + + + A protein modification that effectively converts two L-cysteine residues, two L-histidine residues and a two-iron two-sulfur cluster to bis-L-cysteinyl bis-L-histidino diiron disulfide. + 171.78 + C 0 Fe 2 H -4 N 0 O 0 S 2 + 171.78381 + 2- + C 18 Fe 2 H 20 N 8 O 4 S 4 + 652.34 + 651.92 + C, C, H, H + natural + METAL Iron-sulfur (2Fe-2S) + METAL Iron-sulfur (2Fe-2S); via pros nitrogen + Rieske iron-sulfur cofactor + bis-L-cysteinyl bis-L-histidino diiron disulfide + di-mu-sulfido(bis-S-cysteinyliron)(bis-N3'-histidinoiron) + PSI-MOD + MOD:00230 + Cross-link 4. + bis-L-cysteinyl bis-L-histidino diiron disulfide + + + + + A protein modification that effectively converts two L-cysteine residues, two L-histidine residues and a two-iron two-sulfur cluster to bis-L-cysteinyl bis-L-histidino diiron disulfide. + PubMed:2765515 + PubMed:9651245 + RESID:AA0225 + + + + + METAL Iron-sulfur (2Fe-2S) + + + + + + METAL Iron-sulfur (2Fe-2S); via pros nitrogen + + + + + + Rieske iron-sulfur cofactor + + + + + + bis-L-cysteinyl bis-L-histidino diiron disulfide + + + + + + di-mu-sulfido(bis-S-cysteinyliron)(bis-N3'-histidinoiron) + + + + + + + + + + + A protein modification that effectively converts six L-cysteine residues and a six-iron six-sulfur cluster to hexakis-L-cysteinyl hexairon hexasulfide. + 521.38 + C 0 Fe 6 H -6 N 0 O 0 S 6 + 521.3956 + 1- + C 18 Fe 6 H 24 N 6 O 6 S 12 + 1140.22 + 1139.4508 + C, C, C, C, C, C + hypothetical + hexa-mu3-sulfido-hexakis(S-cysteinyliron) + hexa-mu3-sulfido-hexakis(cysteinato-kappaS)-hexairon + hexakis-L-cysteinyl hexairon hexasulfide + prismane iron-sulfur cofactor + PSI-MOD + MOD:00231 + Cross-link 6. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. + hexakis-L-cysteinyl hexairon hexasulfide + + + + + A protein modification that effectively converts six L-cysteine residues and a six-iron six-sulfur cluster to hexakis-L-cysteinyl hexairon hexasulfide. + PubMed:1311311 + PubMed:1318833 + RESID:AA0226 + + + + + hexa-mu3-sulfido-hexakis(S-cysteinyliron) + + + + + + hexa-mu3-sulfido-hexakis(cysteinato-kappaS)-hexairon + + + + + + hexakis-L-cysteinyl hexairon hexasulfide + + + + + + prismane iron-sulfur cofactor + + + + + + + + + + + A protein modification that effectively crosslinks an L-lysine residue and 5'-phosphoadenosine through a phosphoramide ester bond to form N6-(phospho-5'-adenosine)-L-lysine. + 329.21 + C 10 H 12 N 5 O 6 P 1 + 329.05252 + C 16 H 24 N 7 O 7 P 1 + 457.38 + 457.1475 + K + natural + Unimod:405 + (2S)-2-amino-6-(5'-adenosine phosphonamino)hexanoic acid + 5'-adenylic-N6-L-lysine + ACT_SITE N6-AMP-lysine intermediate + AMP Lysyl + L-lysine monoanhydride with 5'-adenylic acid + N(zeta)-5'-adenylic-L-lysine + N6-(phospho-5'-adenosine)-L-lysine + N6-L-lysine 5'-adenosine phosphoramidester + N6AMPLys + epsilon-5'-adenylic-L-lysine + PSI-MOD + AMP binding site + Phosphoadenosine + MOD:00232 + + N6-(phospho-5'-adenosine)-L-lysine + + + + + A protein modification that effectively crosslinks an L-lysine residue and 5'-phosphoadenosine through a phosphoramide ester bond to form N6-(phospho-5'-adenosine)-L-lysine. + DeltaMass:316 + PubMed:3882425 + PubMed:4944632 + RESID:AA0227 + Unimod:405#K + + + + + (2S)-2-amino-6-(5'-adenosine phosphonamino)hexanoic acid + + + + + + 5'-adenylic-N6-L-lysine + + + + + + ACT_SITE N6-AMP-lysine intermediate + + + + + + AMP Lysyl + + + + + + L-lysine monoanhydride with 5'-adenylic acid + + + + + + N(zeta)-5'-adenylic-L-lysine + + + + + + N6-(phospho-5'-adenosine)-L-lysine + + + + + + N6-L-lysine 5'-adenosine phosphoramidester + + + + + + N6AMPLys + + + + + + epsilon-5'-adenylic-L-lysine + + + + + + AMP binding site + + + + + + Phosphoadenosine + + + + + + + + + + + A protein modification that effectively crosslinks an L-lysine residue and 5'-phosphoguanosine through a phosphoramide ester bond to form N6-(phospho-5'-guanosine)-L-lysine. + 345.21 + C 10 H 12 N 5 O 7 P 1 + 345.04742 + C 16 H 24 N 7 O 8 P 1 + 473.38 + 473.1424 + K + natural + Unimod:413 + (2S)-2-amino-6-(5'-guanosine phosphonamino)hexanoic acid + 5'-guanylic-N6-L-lysine + 5'phos Guanosyl + ACT_SITE N6-GMP-lysine intermediate + L-lysine monoanhydride with 5'-guanylic acid + N(zeta)-5'-guanylic-lysine + N6-(5'-guanylyl)-lysine + N6-(phospho-5'-guanosine)-L-lysine + N6-L-lysine 5'-guanosine phosphoramidester + N6GMPLys + epsilon-5'-guanylic-L-lysine + lysine guanosine-5'-monophosphate + PSI-MOD + Phosphoguanosine + phospho-guanosine + MOD:00233 + + From DeltaMass: Average Mass: 345 Formula:C10H12O5N7P1 Monoisotopic Mass Change:345.047 Average Mass Change:345.209 References:PE Sciex + N6-(phospho-5'-guanosine)-L-lysine + + + + + A protein modification that effectively crosslinks an L-lysine residue and 5'-phosphoguanosine through a phosphoramide ester bond to form N6-(phospho-5'-guanosine)-L-lysine. + DeltaMass:304 + PubMed:6092377 + PubMed:6264433 + RESID:AA0228 + Unimod:413#K + + + + + (2S)-2-amino-6-(5'-guanosine phosphonamino)hexanoic acid + + + + + + 5'-guanylic-N6-L-lysine + + + + + + 5'phos Guanosyl + + + + + + ACT_SITE N6-GMP-lysine intermediate + + + + + + L-lysine monoanhydride with 5'-guanylic acid + + + + + + N(zeta)-5'-guanylic-lysine + + + + + + N6-(5'-guanylyl)-lysine + + + + + + N6-(phospho-5'-guanosine)-L-lysine + + + + + + N6-L-lysine 5'-guanosine phosphoramidester + + + + + + N6GMPLys + + + + + + epsilon-5'-guanylic-L-lysine + + + + + + lysine guanosine-5'-monophosphate + + + + + + Phosphoguanosine + + + + + + phospho-guanosine + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-glutathionyl-L-cysteine. + 305.3 + C 10 H 15 N 3 O 6 S 1 + 305.06815 + C 13 H 20 N 4 O 7 S 2 + 408.44 + 408.07733 + C + natural + Unimod:55 + uniprot.ptm:PTM-0311 + (2S)-2-amino-3-((2S)-2-((4R)-4-amino-4-carboxyl-1-oxobutyl)amino-3-(carboxylmethyl)amino-3-oxo-propyl)dithio-propanoic acid + Glutathionation + L-cysteine glutathione disulfide + L-gamma-glutamyl-L-cysteinyl-glycine (2-1')-disulfide with L-cysteine + MOD_RES S-glutathionyl cysteine + N-(N-gamma-glutamyl-cystinyl)-glycine + SGltCys + cysteinyl glutathione + glutathionec + PSI-MOD + Glutathione + glutathione disulfide + MOD:00234 + + From DeltaMass: Average Mass: 305 + Glutamyl-transpeptidase cleaves glutathione into cysteinylglycine (Cys-Gly) and a Glu residue. [PubMed: 28537416] + L-cysteine glutathione disulfide + + + + + A protein modification that effectively converts an L-cysteine residue to S-glutathionyl-L-cysteine. + ChEBI:21264 + DeltaMass:0 + OMSSA:51 + PubMed:3083866 + PubMed:8344916 + RESID:AA0229 + Unimod:55 + + + + + (2S)-2-amino-3-((2S)-2-((4R)-4-amino-4-carboxyl-1-oxobutyl)amino-3-(carboxylmethyl)amino-3-oxo-propyl)dithio-propanoic acid + + + + + + Glutathionation + + + + + + L-cysteine glutathione disulfide + + + + + + L-gamma-glutamyl-L-cysteinyl-glycine (2-1')-disulfide with L-cysteine + + + + + + MOD_RES S-glutathionyl cysteine + + + + + + N-(N-gamma-glutamyl-cystinyl)-glycine + + + + + + SGltCys + + + + + + cysteinyl glutathione + + + + + + glutathionec + + + + + + Glutathione + + + + + + glutathione disulfide + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-nitrosyl-L-cysteine. + 29.0 + C 0 H -1 N 1 O 1 S 0 + 28.990164 + C 3 H 4 N 2 O 2 S 1 + 132.14 + 131.99934 + C + natural + Unimod:275 + uniprot.ptm:PTM-0280 + (2R)-2-amino-3-nitrososulfanyl-propanoic acid + L-cysteine nitrite ester + MOD_RES S-nitrosocysteine + S-nitrosocysteine + S-nitrosyl-L-cysteine + SNOCys + PSI-MOD + Nitrosyl + S-nitrosylation + MOD:00235 + + S-nitrosyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-nitrosyl-L-cysteine. + PubMed:10442087 + PubMed:11562475 + PubMed:15688001 + PubMed:8626764 + PubMed:8637569 + RESID:AA0230 + Unimod:275 + + + + + (2R)-2-amino-3-nitrososulfanyl-propanoic acid + + + + + + L-cysteine nitrite ester + + + + + + MOD_RES S-nitrosocysteine + + + + + + S-nitrosocysteine + + + + + + S-nitrosyl-L-cysteine + + + + + + SNOCys + + + + + + Nitrosyl + + + + + + S-nitrosylation + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to N4-(ADP-ribosyl)-L-asparagine. + 541.3 + C 15 H 21 N 5 O 13 P 2 + 541.0611 + C 19 H 27 N 7 O 15 P 2 + 655.41 + 655.10406 + N + natural + Unimod:213 + uniprot.ptm:PTM-0054 + (S)-2-amino-4-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)-4-oxobutanoic acid + MOD_RES ADP-ribosylasparagine + N4-(ADP-ribosyl)-L-asparagine + N4-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-asparagine + N4-alpha-D-ribofuranosyl-L-asparagine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) + PSI-MOD + ADP Ribose addition + ADP-Ribosyl + MOD:00236 + N4-(ADP-ribosyl)-L-asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to N4-(ADP-ribosyl)-L-asparagine. + PubMed:15842200 + PubMed:2498316 + RESID:AA0231 + Unimod:213#N + + + + + (S)-2-amino-4-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)-4-oxobutanoic acid + + + + + + MOD_RES ADP-ribosylasparagine + + + + + + N4-(ADP-ribosyl)-L-asparagine + + + + + + N4-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-asparagine + + + + + + N4-alpha-D-ribofuranosyl-L-asparagine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) + + + + + + ADP Ribose addition + + + + + + ADP-Ribosyl + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-beta-methylthioaspartic acid. + 46.09 + C 1 H 2 N 0 O 0 S 1 + 45.98772 + C 5 H 7 N 1 O 3 S 1 + 161.18 + 161.01466 + D + natural + Unimod:39 + uniprot.ptm:PTM-0032 + (2R,3Xi)-2-amino-3-(methylsulfanyl)butanedioic acid + 3-(methylthio)-L-aspartic acid + 3-carboxy-S-methyl-cysteine + 3-methylthio-aspartic acid + 3MeSAsp + MOD_RES 3-methylthioaspartic acid + beta-Methylthio-aspartic acid + beta-methylthio-aspartic acid + bmethylthiold + methythiold + PSI-MOD + Beta-methylthiolation + Methylthio + MOD:00237 + + L-beta-methylthioaspartic acid + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-beta-methylthioaspartic acid. + ChEBI:73599 + DeltaMass:61 + OMSSA:13 + OMSSA:26 + PubMed:15473684 + PubMed:8844851 + RESID:AA0232 + Unimod:39#D + + + + + (2R,3Xi)-2-amino-3-(methylsulfanyl)butanedioic acid + + + + + + 3-(methylthio)-L-aspartic acid + + + + + + 3-carboxy-S-methyl-cysteine + + + + + + 3-methylthio-aspartic acid + + + + + + 3MeSAsp + + + + + + MOD_RES 3-methylthioaspartic acid + + + + + + beta-Methylthio-aspartic acid + + + + + + beta-methylthio-aspartic acid + + + + + + bmethylthiold + + + + + + methythiold + + + + + + Beta-methylthiolation + + + + + + Methylthio + + + + + + + + + + + + A protein modification that effectively cross-links an L-lysine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 5'-(N6-L-lysine)-L-topaquinone. + 11.97 + C 0 H -4 N 0 O 1 + 11.963614 + C 15 H 17 N 3 O 4 + 303.32 + 303.12192 + K, Y + natural + uniprot.ptm:PTM-0171 + 1-[(S)-5-amino-5-carboxypentyl]amino-2-[(S)-2-amino-2-carboxyethyl]-2,6-cyclohexadien-4,5-dione + 2'-(L-lys-N6-yl)-L-4',5'-topaquinone + 2'-(L-lysine)-L-tyrosyl-4',5'-quinone + CROSSLNK Lysine tyrosylquinone (Lys-Tyr) + CROSSLNK Lysine tyrosylquinone (Tyr-Lys) + LTQ + lysyl oxidase cofactor + PSI-MOD + MOD:00238 + Cross-link 2; secondary to RESID:AA0147. + 5'-(N6-L-lysine)-L-topaquinone + + + + + A protein modification that effectively cross-links an L-lysine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 5'-(N6-L-lysine)-L-topaquinone. + PubMed:8688089 + RESID:AA0233 + + + + + 1-[(S)-5-amino-5-carboxypentyl]amino-2-[(S)-2-amino-2-carboxyethyl]-2,6-cyclohexadien-4,5-dione + + + + + + 2'-(L-lys-N6-yl)-L-4',5'-topaquinone + + + + + + 2'-(L-lysine)-L-tyrosyl-4',5'-quinone + + + + + + CROSSLNK Lysine tyrosylquinone (Lys-Tyr) + + + + + + CROSSLNK Lysine tyrosylquinone (Tyr-Lys) + + + + + + LTQ + + + + + + lysyl oxidase cofactor + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-methyl-L-cysteine. + 14.03 + C 1 H 2 N 0 O 0 S 0 + 14.01565 + C 4 H 7 N 1 O 1 S 1 + 117.17 + 117.02483 + C + natural + Unimod:34 + uniprot.ptm:PTM-0636 + (R)-2-amino-3-(methylsulfanyl)propanoic acid + ACT_SITE S-methylcysteine intermediate + L-3-(methylthio)alanine + MOD_RES S-methylcysteine + S-methyl-L-cysteine + S-methylated L-cysteine + SMeCys + PSI-MOD + Methyl + Methylation + MOD:00239 + + S-methyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-methyl-L-cysteine. + PubMed:10660523 + PubMed:11875433 + PubMed:1339288 + RESID:AA0234 + Unimod:34#C + + + + + (R)-2-amino-3-(methylsulfanyl)propanoic acid + + + + + + ACT_SITE S-methylcysteine intermediate + + + + + + L-3-(methylthio)alanine + + + + + + MOD_RES S-methylcysteine + + + + + + S-methyl-L-cysteine + + + + + + S-methylated L-cysteine + + + + + + SMeCys + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 4-hydroxy-L-lysine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 6 H 12 N 2 O 2 + 144.17 + 144.08987 + K + artifact + uniprot.ptm:PTM-0664 + (2S,4R)-2,6-diamino-4-hydroxyhexanoic acid + 4-hydroxy-L-lysine + 4-hydroxylated L-lysine + 4HyLys + L-threo-gamma-hydroxylysine + MOD_RES 4-hydroxylysine + alpha,epsilon-diamino-gamma-hydroxycaproic acid + PSI-MOD + MOD:00240 + This modification was not structurally confirmed. Later 5-hydroxy-L-lysine was found at a homologous position in the same protein from closely related species. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. + 4-hydroxy-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to 4-hydroxy-L-lysine. + ChEBI:141495 + PubMed:4005040 + RESID:AA0235 + + + + + (2S,4R)-2,6-diamino-4-hydroxyhexanoic acid + + + + + + 4-hydroxy-L-lysine + + + + + + 4-hydroxylated L-lysine + + + + + + 4HyLys + + + + + + L-threo-gamma-hydroxylysine + + + + + + MOD_RES 4-hydroxylysine + + + + + + alpha,epsilon-diamino-gamma-hydroxycaproic acid + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to N4-hydroxymethyl-L-asparagine. + 30.03 + C 1 H 2 N 0 O 1 + 30.010565 + C 5 H 8 N 2 O 3 + 144.13 + 144.0535 + N + artifact + Unimod:414 + (2S)-2-amino-4-[(hydroxymethyl)amino]-4-oxobutanoic acid + 2-amino-N4-hydroxymethylbutanediamic acid + N(gamma)-hydroxymethylasparagine + N4-hydroxymethyl-L-asparagine + N4-hydroxymethylasparagine + beta-hydroxymethylasparagine + PSI-MOD + Hydroxymethyl + hydroxymethyl + MOD:00241 + N4-methyl-L-asparagine, see MOD:0079, was found at a homologous position of the same protein in a closely related species. Since the peptide containing this modification was obtained by enzymatic cleavage, not cyanogen bromide cleavage, it could have experienced oxidation of the following methionine residue, leading to the erroneous attribution of a mass of 29 for the modification rather than 14. comment: This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. + N4-hydroxymethyl-L-asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to N4-hydroxymethyl-L-asparagine. + RESID:AA0236 + Unimod:414 + + + + + (2S)-2-amino-4-[(hydroxymethyl)amino]-4-oxobutanoic acid + + + + + + 2-amino-N4-hydroxymethylbutanediamic acid + + + + + + N(gamma)-hydroxymethylasparagine + + + + + + N4-hydroxymethyl-L-asparagine + + + + + + N4-hydroxymethylasparagine + + + + + + beta-hydroxymethylasparagine + + + + + + Hydroxymethyl + + + + + + hydroxymethyl + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-(ADP-ribosyl)-L-serine. + 541.3 + C 15 H 21 N 5 O 13 P 2 + 541.0611 + C 18 H 26 N 6 O 15 P 2 + 628.38 + 628.09314 + S + natural + Unimod:213 + uniprot.ptm:PTM-0056 + (S)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]oxy)-propanoic acid + MOD_RES ADP-ribosylserine + O-(ADP-ribosyl)-L-serine + O3-(ADP-ribosyl)-L-serine + O3-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-serine + O3-alpha-D-ribofuranosyl-L-serine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) + OADPRibSer + PSI-MOD + ADP Ribose addition + ADP-Ribosyl + MOD:00242 + + O-(ADP-ribosyl)-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-(ADP-ribosyl)-L-serine. + PubMed:15842200 + PubMed:3141412 + RESID:AA0237 + Unimod:213#S + + + + + (S)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]oxy)-propanoic acid + + + + + + MOD_RES ADP-ribosylserine + + + + + + O-(ADP-ribosyl)-L-serine + + + + + + O3-(ADP-ribosyl)-L-serine + + + + + + O3-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-serine + + + + + + O3-alpha-D-ribofuranosyl-L-serine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) + + + + + + OADPRibSer + + + + + + ADP Ribose addition + + + + + + ADP-Ribosyl + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 S 0 + -20.026215 + C 6 H 6 N 2 O 2 S 1 + 170.19 + 170.015 + C, S + natural + uniprot.ptm:PTM-0376 + 2-(1-azanyl-2-sulfanylethyl)-4-oxazolecarboxylic acid + 2-[(1R)-1-amino-2-sulfanylethyl]-1,3-oxazole-4-carboxylic acid + CROSSLNK Oxazole-4-carboxylic acid (Cys-Ser) + L-cysteine oxazole-4-carboxylic acid + PSI-MOD + MOD:00243 + Cross-link 2. + L-cysteine oxazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid. + PubMed:8183941 + PubMed:8895467 + RESID:AA0238 + + + + + 2-(1-azanyl-2-sulfanylethyl)-4-oxazolecarboxylic acid + + + + + + 2-[(1R)-1-amino-2-sulfanylethyl]-1,3-oxazole-4-carboxylic acid + + + + + + CROSSLNK Oxazole-4-carboxylic acid (Cys-Ser) + + + + + + L-cysteine oxazole-4-carboxylic acid + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazoline-4-carboxylic acid. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 6 H 8 N 2 O 2 S 1 + 172.2 + 172.03065 + C, S + natural + uniprot.ptm:PTM-0381 + (4S)-2-[(1R)-1-amino-2-sulfanylethyl]-4,5-dihydro-1,3-oxazole-4-carboxylic acid + 2-[1-azanyl-2-sulfanylethyl]-4,5-dihydro-1,3-oxazole-4-carboxylic acid + CROSSLNK Oxazoline-4-carboxylic acid (Cys-Ser) + L-cysteine oxazoline-4-carboxylic acid + PSI-MOD + MOD:00244 + Cross-link 2. + L-cysteine oxazoline-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazoline-4-carboxylic acid. + PubMed:1880060 + RESID:AA0239 + + + + + (4S)-2-[(1R)-1-amino-2-sulfanylethyl]-4,5-dihydro-1,3-oxazole-4-carboxylic acid + + + + + + 2-[1-azanyl-2-sulfanylethyl]-4,5-dihydro-1,3-oxazole-4-carboxylic acid + + + + + + CROSSLNK Oxazoline-4-carboxylic acid (Cys-Ser) + + + + + + L-cysteine oxazoline-4-carboxylic acid + + + + + + + + + + + + A protein modification that effectively crosslinks a glycine residue and an L-serine residue to form glycine oxazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 + -20.026215 + C 5 H 4 N 2 O 2 + 124.1 + 124.027275 + G, S + natural + uniprot.ptm:PTM-0377 + 2-aminomethyl-1,3-oxazole-4-carboxylic acid + 2-azanylmethyl-1,3-oxazole-4-carboxylic acid + CROSSLNK Oxazole-4-carboxylic acid (Gly-Ser) + glycine oxazole-4-carboxylic acid + PSI-MOD + MOD:00245 + Cross-link 2. + glycine oxazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks a glycine residue and an L-serine residue to form glycine oxazole-4-carboxylic acid. + PubMed:8183941 + PubMed:8895467 + RESID:AA0240 + + + + + 2-aminomethyl-1,3-oxazole-4-carboxylic acid + + + + + + 2-azanylmethyl-1,3-oxazole-4-carboxylic acid + + + + + + CROSSLNK Oxazole-4-carboxylic acid (Gly-Ser) + + + + + + glycine oxazole-4-carboxylic acid + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form glycine thiazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 S 0 + -20.026215 + C 5 H 4 N 2 O 1 S 1 + 140.16 + 140.00444 + C, G + natural + uniprot.ptm:PTM-0378 + 2-(aminomethyl)-1,3-thiazole-4-carboxylic acid + 2-(azanylmethyl)-1,3-thiazole-4-carboxylic acid + CROSSLNK Thiazole-4-carboxylic acid (Gly-Cys) + glycine thiazole-4-carboxylic acid + PSI-MOD + MOD:00246 + Cross-link 2. + glycine thiazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form glycine thiazole-4-carboxylic acid. + ChEBI:21276 + PubMed:8183941 + PubMed:8895467 + RESID:AA0241 + + + + + 2-(aminomethyl)-1,3-thiazole-4-carboxylic acid + + + + + + 2-(azanylmethyl)-1,3-thiazole-4-carboxylic acid + + + + + + CROSSLNK Thiazole-4-carboxylic acid (Gly-Cys) + + + + + + glycine thiazole-4-carboxylic acid + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-serine thiazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 S 0 + -20.026215 + C 6 H 6 N 2 O 2 S 1 + 170.19 + 170.015 + C, S + natural + uniprot.ptm:PTM-0363 + 2-[(1S)-1-amino-2-hydroxyethyl]-1,3-thiazole-4-carboxylic acid + 2-[1-azanyl-2-hydroxyethyl]-1,3-thiazole-4-carboxylic acid + CROSSLNK Thiazole-4-carboxylic acid (Ser-Cys) + L-serine thiazole-4-carboxylic acid + PSI-MOD + MOD:00247 + Cross-link 2. + L-serine thiazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-serine thiazole-4-carboxylic acid. + PubMed:8183941 + PubMed:8895467 + RESID:AA0242 + + + + + 2-[(1S)-1-amino-2-hydroxyethyl]-1,3-thiazole-4-carboxylic acid + + + + + + 2-[1-azanyl-2-hydroxyethyl]-1,3-thiazole-4-carboxylic acid + + + + + + CROSSLNK Thiazole-4-carboxylic acid (Ser-Cys) + + + + + + L-serine thiazole-4-carboxylic acid + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 S 0 + -20.026215 + C 12 H 10 N 2 O 1 S 1 + 230.29 + 230.05139 + C, F + natural + uniprot.ptm:PTM-0375 + 2-[(1S)-1-amino-2-phenylethyl]-1,3-thiazole-4-carboxylic acid + 2-[1-azanyl-2-phenylethyl]-1,3-thiazole-4-carboxylic acid + CROSSLNK Thiazole-4-carboxylic acid (Phe-Cys) + L-phenylalanine thiazole-4-carboxylic acid + PSI-MOD + MOD:00248 + Cross-link 2. + L-phenylalanine thiazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazole-4-carboxylic acid. + PubMed:1880060 + RESID:AA0243 + + + + + 2-[(1S)-1-amino-2-phenylethyl]-1,3-thiazole-4-carboxylic acid + + + + + + 2-[1-azanyl-2-phenylethyl]-1,3-thiazole-4-carboxylic acid + + + + + + CROSSLNK Thiazole-4-carboxylic acid (Phe-Cys) + + + + + + L-phenylalanine thiazole-4-carboxylic acid + + + + + + + + + + + A protein modification that effectively crosslinks two L-cysteine residues to form L-cysteine thiazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 S 0 + -20.026215 + C 6 H 6 N 2 O 1 S 2 + 186.25 + 185.99216 + C, C + natural + uniprot.ptm:PTM-0360 + 2-[(1S)-1-amino-2-sulfanylethyl]-1,3-thiazole-4-carboxylic acid + 2-[1-azanyl-2-sulfanylethyl]-1,3-thiazole-4-carboxylic acid + CROSSLNK Thiazole-4-carboxylic acid (Cys-Cys) + L-cysteine thiazole-4-carboxylic acid + PSI-MOD + MOD:00249 + Cross-link 2. + L-cysteine thiazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks two L-cysteine residues to form L-cysteine thiazole-4-carboxylic acid. + PubMed:1880060 + RESID:AA0244 + + + + + 2-[(1S)-1-amino-2-sulfanylethyl]-1,3-thiazole-4-carboxylic acid + + + + + + 2-[1-azanyl-2-sulfanylethyl]-1,3-thiazole-4-carboxylic acid + + + + + + CROSSLNK Thiazole-4-carboxylic acid (Cys-Cys) + + + + + + L-cysteine thiazole-4-carboxylic acid + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-lysine residue to form L-lysine thiazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 S 0 + -20.026215 + C 9 H 13 N 3 O 1 S 1 + 211.28 + 211.07793 + C, K + hypothetical + 2-[(1S)-1,5-diaminopentyl]-1,3-thiazole-4-carboxylic acid + 2-[1,5-bis(azanyl)pentyl]-1,3-thiazole-4-carboxylic acid + L-lysine thiazole-4-carboxylic acid + PSI-MOD + MOD:00250 + Cross-link 2. Lysine is now thought not to be encoded in the peptide sequence modified to produce GE2270. See RESID:AA0470. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. + L-lysine thiazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-lysine residue to form L-lysine thiazole-4-carboxylic acid. + PubMed:1880060 + RESID:AA0245 + + + + + 2-[(1S)-1,5-diaminopentyl]-1,3-thiazole-4-carboxylic acid + + + + + + 2-[1,5-bis(azanyl)pentyl]-1,3-thiazole-4-carboxylic acid + + + + + + L-lysine thiazole-4-carboxylic acid + + + + + + + + + + + A protein modification that effectively crosslinks an L-serine residue and the 5'-end of DNA through a phosphodiester bond to form O-(phospho-5'-DNA)-L-serine. + S + natural + uniprot.ptm:PTM-0226 + (S)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)propanoic acid + ACT_SITE O-(5'-phospho-DNA)-serine intermediate + MOD_RES O-(5'-phospho-DNA)-serine + O-(phospho-5'-DNA)-L-serine + O3-(phospho-5'-DNA)-L-serine + O3-L-serine 5'-DNA phosphodiester + PSI-MOD + MOD:00251 + O-(phospho-5'-DNA)-L-serine + + + + + A protein modification that effectively crosslinks an L-serine residue and the 5'-end of DNA through a phosphodiester bond to form O-(phospho-5'-DNA)-L-serine. + PubMed:7142163 + PubMed:7265205 + RESID:AA0246 + + + + + (S)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)propanoic acid + + + + + + ACT_SITE O-(5'-phospho-DNA)-serine intermediate + + + + + + MOD_RES O-(5'-phospho-DNA)-serine + + + + + + O-(phospho-5'-DNA)-L-serine + + + + + + O3-(phospho-5'-DNA)-L-serine + + + + + + O3-L-serine 5'-DNA phosphodiester + + + + + + + + + + A protein modification that effectively cross-links an L-threonine residue to the polymer keratan sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide. + T + natural + keratan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-threonine + keratosulfate + poly[beta-1,4-(2-acetamido-2-deoxy-6-sulfate D-glucosyl)-beta-1,3-D-galactosyl]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-threonine + PSI-MOD + MOD:00252 + keratan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-threonine + + + + + A protein modification that effectively cross-links an L-threonine residue to the polymer keratan sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide. + PubMed:1417734 + PubMed:3472204 + RESID:AA0247 + + + + + keratan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-threonine + + + + + + keratosulfate + + + + + + poly[beta-1,4-(2-acetamido-2-deoxy-6-sulfate D-glucosyl)-beta-1,3-D-galactosyl]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-threonine + + + + + + + + + + + A protein modification that effectively converts an L-selenocysteine residue to L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide). + 1572.02 + C 40 H 47 Mo 1 N 20 O 26 P 4 S 4 Se 0 + 1572.9857 + C 43 H 52 Mo 1 N 21 O 27 P 4 S 4 Se 1 + 1722.07 + 1723.9395 + U + natural + Unimod:415 + PSI-MOD + MOD:00253 + L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) (Sec) + + + + + A protein modification that effectively converts an L-selenocysteine residue to L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide). + PubMed:14235557 + PubMed:2211698 + PubMed:8052647 + PubMed:9036855 + RESID:AA0248#SEC + Unimod:415 + + + + + + + + + + A protein modification that effectively crosslinks an L-tyrosine residue and the 5'-end of RNA through a phosphodiester to form O4'-(phospho-5'-RNA)-L-tyrosine. + Y + natural + uniprot.ptm:PTM-0229 + (S)-2-amino-3-[4-(5'-ribonucleic acid phosphonoxy)phenyl]propanoic acid + MOD_RES O-(5'-phospho-RNA)-tyrosine + O4'-(phospho-5'-RNA)-L-tyrosine + O4'-L-tyrosine 5'-RNA phosphodiester + PSI-MOD + MOD:00254 + O4'-(phospho-5'-RNA)-L-tyrosine + + + + + A protein modification that effectively crosslinks an L-tyrosine residue and the 5'-end of RNA through a phosphodiester to form O4'-(phospho-5'-RNA)-L-tyrosine. + PubMed:1702164 + PubMed:209034 + PubMed:217003 + PubMed:6264310 + RESID:AA0249 + + + + + (S)-2-amino-3-[4-(5'-ribonucleic acid phosphonoxy)phenyl]propanoic acid + + + + + + MOD_RES O-(5'-phospho-RNA)-tyrosine + + + + + + O4'-(phospho-5'-RNA)-L-tyrosine + + + + + + O4'-L-tyrosine 5'-RNA phosphodiester + + + + + + + + + + + + A protein modification that effectively cross-links an L-histidine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 3-(3'-L-histidyl)-L-tyrosine. + -2.02 + C 0 H -2 N 0 O 0 + -2.01565 + C 15 H 14 N 4 O 3 + 298.3 + 298.1066 + H, Y + natural + uniprot.ptm:PTM-0027 + (2S,3R)-2-amino-3-(5-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl)-3-(4-hydroxyphenyl)propanoic acid + 3-(3'-L-histidyl)-L-tyrosine + 3-(N3'-histidyl)tyrosine + 3-(pi-histidyl)tyrosine + 3-(pros-histidyl)tyrosine + CROSSLNK 3'-histidyl-3-tyrosine (His-Tyr) + beta-(N(delta)-histidyl)tyrosine + beta-(N3'-histidyl)tyrosine + PSI-MOD + MOD:00255 + Cross-link 2. + 3-(3'-L-histidyl)-L-tyrosine + + + + + A protein modification that effectively cross-links an L-histidine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 3-(3'-L-histidyl)-L-tyrosine. + PubMed:9144772 + RESID:AA0250 + + + + + (2S,3R)-2-amino-3-(5-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl)-3-(4-hydroxyphenyl)propanoic acid + + + + + + 3-(3'-L-histidyl)-L-tyrosine + + + + + + 3-(N3'-histidyl)tyrosine + + + + + + 3-(pi-histidyl)tyrosine + + + + + + 3-(pros-histidyl)tyrosine + + + + + + CROSSLNK 3'-histidyl-3-tyrosine (His-Tyr) + + + + + + beta-(N(delta)-histidyl)tyrosine + + + + + + beta-(N3'-histidyl)tyrosine + + + + + + + + + + + A protein modification that dioxygenates an L-methionine residue to L-methionine sulfone. + 32.0 + C 0 H 0 N 0 O 2 S 0 + 31.989828 + C 5 H 9 N 1 O 3 S 1 + 163.19 + 163.03032 + M + natural + Unimod:425 + uniprot.ptm:PTM-0175 + (2S)-2-amino-4-(methylsulfonyl)butanoic acid + L-methionine S,S-dioxide + L-methionine sulfone + MOD_RES Methionine sulfone + MetO2 + MethionylSulphone + Oxidation of Methionine (to Sulphone) + S,S-dioxymethionine + suphonem + PSI-MOD + Dioxidation + dihydroxy + MOD:00256 + + DeltaMass gives the formula C 5 H 9 N 3 O 1 S 1 with mass 163 + L-methionine sulfone + + + + + A protein modification that dioxygenates an L-methionine residue to L-methionine sulfone. + DeltaMass:205 + OMSSA:115 + PubMed:12686488 + PubMed:7786407 + PubMed:7791219 + PubMed:9252331 + RESID:AA0251 + Unimod:425#M + + + + + (2S)-2-amino-4-(methylsulfonyl)butanoic acid + + + + + + L-methionine S,S-dioxide + + + + + + L-methionine sulfone + + + + + + MOD_RES Methionine sulfone + + + + + + MetO2 + + + + + + MethionylSulphone + + + + + + Oxidation of Methionine (to Sulphone) + + + + + + S,S-dioxymethionine + + + + + + suphonem + + + + + + Dioxidation + + + + + + dihydroxy + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to dipyrrolylmethanemethyl-L-cysteine. + 418.4 + C 20 H 22 N 2 O 8 S 0 + 418.1376 + C 23 H 27 N 3 O 9 S 1 + 521.54 + 521.1468 + C + natural + Unimod:416 + uniprot.ptm:PTM-0421 + (2S)-3-[5-[4-(2-carboxy)ethyl-3-carboxymethyl-1-pyrrol-2-yl]methyl-4-(2-carboxy)ethyl-3-carboxymethyl-1-pyrrol-2-yl]methylthio-2-aminopropanoic acid + 3-[5-(3-acetic acid-4-propanoic acid-1-pyrrol-2-yl)methyl-3-acetic acid-4-propanoic acid-1-pyrrol-2-yl]methylthio-2-aminopropanoic acid + MOD_RES S-(dipyrrolylmethanemethyl)cysteine + dipyrrole cofactor + dipyrrolylmethanemethyl-L-cysteine + dipyrrolylmethyl-L-cysteine + dipyrromethane cofactor + pyrromethane cofactor + PSI-MOD + Dipyrrolylmethanemethyl + dipyrrolylmethanemethyl + MOD:00257 + dipyrrolylmethanemethyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to dipyrrolylmethanemethyl-L-cysteine. + PubMed:3042456 + PubMed:3196304 + PubMed:3421931 + PubMed:8727319 + RESID:AA0252 + Unimod:416 + + + + + (2S)-3-[5-[4-(2-carboxy)ethyl-3-carboxymethyl-1-pyrrol-2-yl]methyl-4-(2-carboxy)ethyl-3-carboxymethyl-1-pyrrol-2-yl]methylthio-2-aminopropanoic acid + + + + + + 3-[5-(3-acetic acid-4-propanoic acid-1-pyrrol-2-yl)methyl-3-acetic acid-4-propanoic acid-1-pyrrol-2-yl]methylthio-2-aminopropanoic acid + + + + + + MOD_RES S-(dipyrrolylmethanemethyl)cysteine + + + + + + dipyrrole cofactor + + + + + + dipyrrolylmethanemethyl-L-cysteine + + + + + + dipyrrolylmethyl-L-cysteine + + + + + + dipyrromethane cofactor + + + + + + pyrromethane cofactor + + + + + + Dipyrrolylmethanemethyl + + + + + + dipyrrolylmethanemethyl + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form S-(2-aminovinyl)-3-methyl-D-cysteine. + -64.04 + C -1 H -4 N 0 O -3 S 0 + -64.016045 + C 6 H 9 N 2 O 1 S 1 + 157.21 + 157.04356 + C, T + natural + C-term + uniprot.ptm:PTM-0267 + (2S,3S)-2-amino-3-[((Z)-2-aminoethenyl)sulfanyl]butanoic acid + 2-amino-3-[(2-aminovinyl)sulfanyl]butanoic acid + CROSSLNK S-(2-aminovinyl)-3-methyl-D-cysteine (Thr-Cys) + S-(2-aminovinyl)-3-methyl-D-cysteine + decarboxylated methyllanthionine + PSI-MOD + MOD:00258 + Cross-link 2. + S-(2-aminovinyl)-3-methyl-D-cysteine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form S-(2-aminovinyl)-3-methyl-D-cysteine. + PubMed:9119018 + RESID:AA0253 + + + + + (2S,3S)-2-amino-3-[((Z)-2-aminoethenyl)sulfanyl]butanoic acid + + + + + + 2-amino-3-[(2-aminovinyl)sulfanyl]butanoic acid + + + + + + CROSSLNK S-(2-aminovinyl)-3-methyl-D-cysteine (Thr-Cys) + + + + + + S-(2-aminovinyl)-3-methyl-D-cysteine + + + + + + decarboxylated methyllanthionine + + + + + + + + + + + A protein modification that effectively crosslinks an L-tyrosine residue and the 5'-end of DNA through a phosphodiester bond to form O4'-(phospho-5'-DNA)-L-tyrosine. + Y + natural + uniprot.ptm:PTM-0228 + (S)-2-amino-3-[4-(5'-deoxyribonucleic acid phosphonoxy)phenyl]propanoic acid + ACT_SITE O-(5'-phospho-DNA)-tyrosine intermediate + MOD_RES O-(5'-phospho-DNA)-tyrosine + O4'-(phospho-5'-DNA)-L-tyrosine + O4'-L-tyrosine 5'-DNA phosphodiester + PSI-MOD + MOD:00259 + O4'-(phospho-5'-DNA)-L-tyrosine + + + + + A protein modification that effectively crosslinks an L-tyrosine residue and the 5'-end of DNA through a phosphodiester bond to form O4'-(phospho-5'-DNA)-L-tyrosine. + PubMed:1861973 + PubMed:2940511 + PubMed:3684578 + RESID:AA0254 + + + + + (S)-2-amino-3-[4-(5'-deoxyribonucleic acid phosphonoxy)phenyl]propanoic acid + + + + + + ACT_SITE O-(5'-phospho-DNA)-tyrosine intermediate + + + + + + MOD_RES O-(5'-phospho-DNA)-tyrosine + + + + + + O4'-(phospho-5'-DNA)-L-tyrosine + + + + + + O4'-L-tyrosine 5'-DNA phosphodiester + + + + + + + + + + + A protein modification that effectively crosslinks an L-threonine residue and the 5'-end of DNA through a phosphodiester bond to form O-(phospho-5'-DNA)-L-threonine. + 78.97 + C 0 H 0 N 0 O 3 P 1 + 78.9585 + C 4 H 7 N 1 O 5 P 1 + 180.08 + 180.00618 + T + natural + (S)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)butanoic acid + O-(phospho-5'-DNA)-L-threonine + O3-(phospho-5'-DNA)-L-threonine + O3-L-threonine 5'-DNA phosphodiester + PSI-MOD + MOD:00260 + O-(phospho-5'-DNA)-L-threonine + + + + + A protein modification that effectively crosslinks an L-threonine residue and the 5'-end of DNA through a phosphodiester bond to form O-(phospho-5'-DNA)-L-threonine. + PubMed:3081736 + RESID:AA0255 + + + + + (S)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)butanoic acid + + + + + + O-(phospho-5'-DNA)-L-threonine + + + + + + O3-(phospho-5'-DNA)-L-threonine + + + + + + O3-L-threonine 5'-DNA phosphodiester + + + + + + + + + + + A protein modification that effectively crosslinks an L-tyrosine residue and 5'-phosphouridine through a phosphodiester bond to form O4'-(phospho-5'-uridine)-L-tyrosine. + 306.17 + C 9 H 11 N 2 O 8 P 1 + 306.0253 + C 18 H 20 N 3 O 10 P 1 + 469.34 + 469.08862 + Y + natural + Unimod:417 + uniprot.ptm:PTM-0333 + (S)-2-amino-3-[4-(5'-uridine phosphonoxy)phenyl]propanoic acid + 5'-uridylic-O-tyrosine + MOD_RES O-UMP-tyrosine + O-Uridinylylation (of Tyrosine) + O4'-(phospho-5'-uridine)-L-tyrosine + O4'-L-tyrosine 5'-uridine phosphodiester + OUMPTyr + hydrogen 5'-uridylate tyrosine ester + PSI-MOD + PhosphoUridine + uridine phosphodiester + MOD:00261 + + From DeltaMass: Average Mass: 306. + O4'-(phospho-5'-uridine)-L-tyrosine + + + + + A protein modification that effectively crosslinks an L-tyrosine residue and 5'-phosphouridine through a phosphodiester bond to form O4'-(phospho-5'-uridine)-L-tyrosine. + DeltaMass:0 + PubMed:11467524 + PubMed:2885322 + RESID:AA0256 + Unimod:417#Y + + + + + (S)-2-amino-3-[4-(5'-uridine phosphonoxy)phenyl]propanoic acid + + + + + + 5'-uridylic-O-tyrosine + + + + + + MOD_RES O-UMP-tyrosine + + + + + + O-Uridinylylation (of Tyrosine) + + + + + + O4'-(phospho-5'-uridine)-L-tyrosine + + + + + + O4'-L-tyrosine 5'-uridine phosphodiester + + + + + + OUMPTyr + + + + + + hydrogen 5'-uridylate tyrosine ester + + + + + + PhosphoUridine + + + + + + uridine phosphodiester + + + + + + + + + + + A protein modification that effectively forms a peptide bond between a C-terminal L-glutamic acid residue and a free L-tyrosine. + -17.01 + C 0 H -1 N 0 O -1 + -17.00274 + C 14 H 16 N 2 O 5 + 292.29 + 292.10593 + E, Y + natural + C-term + (S,S)-2-(2-aminopentanedio-1-yl)amino-3-(4-hydoxyphenyl)propanoic acid + L-glutamyl L-tyrosine + N-(L-glutamyl)-L-tyrosine + SITE Involved in polymerization + PSI-MOD + MOD:00262 + Cross-link 2. + N-(L-glutamyl)-L-tyrosine + + + + + A protein modification that effectively forms a peptide bond between a C-terminal L-glutamic acid residue and a free L-tyrosine. + ChEBI:21477 + PubMed:6387372 + PubMed:8093886 + RESID:AA0257 + + + + + (S,S)-2-(2-aminopentanedio-1-yl)amino-3-(4-hydoxyphenyl)propanoic acid + + + + + + L-glutamyl L-tyrosine + + + + + + N-(L-glutamyl)-L-tyrosine + + + + + + SITE Involved in polymerization + + + + + + + + + + + A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoviolobilin. + 586.69 + C 33 H 38 N 4 O 6 S 0 + 586.2791 + C 36 H 43 N 5 O 7 S 1 + 689.83 + 689.2883 + C + natural + Unimod:387 + (4S)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-4,5-dihydro-2,7,13,17-tetramethyl-(21H,22H,24H)-biladiene-bc-1,19-dione + BINDING Phycoviolobilin chromophore (covalent; via 1 link) + PBV + PVB + PXB + S-phycobiliviolin-L-cysteine + S-phycoviolobilin-L-cysteine + cryptobiliviolin + cryptoviolin + cryptoviolobilin + PSI-MOD + Phycocyanobilin + phycocyanobilin + MOD:00263 + S-phycoviolobilin-L-cysteine + + + + + A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoviolobilin. + PubMed:2106585 + PubMed:3208761 + RESID:AA0258 + Unimod:387 + + + + + (4S)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-4,5-dihydro-2,7,13,17-tetramethyl-(21H,22H,24H)-biladiene-bc-1,19-dione + + + + + + BINDING Phycoviolobilin chromophore (covalent; via 1 link) + + + + + + PBV + + + + + + PVB + + + + + + PXB + + + + + + S-phycobiliviolin-L-cysteine + + + + + + S-phycoviolobilin-L-cysteine + + + + + + cryptobiliviolin + + + + + + cryptoviolin + + + + + + cryptoviolobilin + + + + + + Phycocyanobilin + + + + + + phycocyanobilin + + + + + + + + + + + A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycoerythrobilin. + 586.69 + C 33 H 38 N 4 O 6 S 0 + 586.2791 + C 39 H 48 N 6 O 8 S 2 + 792.97 + 792.2975 + C, C + natural + (2S,3R,16R)-3,18-bis-[(R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-2,3,15,16-tetrahydrobilin-1,19(21H,22H,24H)-dione + 3,18-bis-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,3,15,16-tetrahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-biladiene-ab-8,12-dipropanoic acid + BINDING Phycoerythrobilin chromophore (covalent; via 2 links) + PEB + phycoerythrobilin biscysteine adduct + phycoerythrobilin-bis-L-cysteine + PSI-MOD + MOD:00264 + Cross-link 2. + phycoerythrobilin-bis-L-cysteine + + + + + A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycoerythrobilin. + PubMed:3208761 + PubMed:3838747 + RESID:AA0259 + + + + + (2S,3R,16R)-3,18-bis-[(R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-2,3,15,16-tetrahydrobilin-1,19(21H,22H,24H)-dione + + + + + + 3,18-bis-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,3,15,16-tetrahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-biladiene-ab-8,12-dipropanoic acid + + + + + + BINDING Phycoerythrobilin chromophore (covalent; via 2 links) + + + + + + PEB + + + + + + phycoerythrobilin biscysteine adduct + + + + + + phycoerythrobilin-bis-L-cysteine + + + + + + + + + + + A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycourobilin. + 586.69 + C 33 H 38 N 4 O 6 S 0 + 586.2791 + C 39 H 48 N 6 O 8 S 2 + 792.97 + 792.2975 + C, C + natural + 3,18-bis(1-[(R)-2-amino-2-carboxyethyl]sulfanylethyl)-2,7,13,17-tetramethyl-1,19-dioxo-4,5,15,16-tetrahydro-(21H,22H,24H)-bilene-b-8,12-dipropanoic acid + 3,18-bis(1-[(R)-2-amino-2-carboxyethyl]sulfanylethyl)-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-4,5,15,16-tetrahydro-(21H,22H,24H)-bilene-b-1,19(4H,16H)-dione + BINDING Phycourobilin chromophore (covalent; via 2 links) + PUB + phycourobilin biscysteine adduct + phycourobilin-bis-L-cysteine + PSI-MOD + MOD:00265 + Cross-link 2. + phycourobilin-bis-L-cysteine + + + + + A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycourobilin. + PubMed:3208761 + PubMed:3838665 + PubMed:3838747 + PubMed:8876649 + RESID:AA0260 + + + + + 3,18-bis(1-[(R)-2-amino-2-carboxyethyl]sulfanylethyl)-2,7,13,17-tetramethyl-1,19-dioxo-4,5,15,16-tetrahydro-(21H,22H,24H)-bilene-b-8,12-dipropanoic acid + + + + + + 3,18-bis(1-[(R)-2-amino-2-carboxyethyl]sulfanylethyl)-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-4,5,15,16-tetrahydro-(21H,22H,24H)-bilene-b-1,19(4H,16H)-dione + + + + + + BINDING Phycourobilin chromophore (covalent; via 2 links) + + + + + + PUB + + + + + + phycourobilin biscysteine adduct + + + + + + phycourobilin-bis-L-cysteine + + + + + + + + + + A protein modification that effectively forms a peptide bond between a C-terminal L-glutamic acid residue and one or more free L-glutamic acid molecules to form N-(L-glutamyl)-poly-L-glutamic acid. + E + natural + C-term + PSI-MOD + MOD:00266 + N-L-glutamyl-poly-L-glutamic acid + + + + + A protein modification that effectively forms a peptide bond between a C-terminal L-glutamic acid residue and one or more free L-glutamic acid molecules to form N-(L-glutamyl)-poly-L-glutamic acid. + PubMed:2570347 + PubMed:328274 + RESID:AA0261 + + + + + + + + + + A protein modification that effectively dioxygenates an L-cysteine residue to L-cysteine sulfinic acid. + 32.0 + C 0 H 0 N 0 O 2 S 0 + 31.989828 + C 3 H 5 N 1 O 3 S 1 + 135.14 + 134.99901 + C + natural + Unimod:425 + uniprot.ptm:PTM-0108 + (2R)-2-amino-3-sulfinopropanoic acid + 2-amino-2-carboxyethanesulfinic acid + 2-amino-3-(dioxido-lambda(6)-sulfanyl)propanoic acid [tautomer] + 2-amino-3-sulfonylpropanoic acid [tautomer] + 3-sulfinoalanine + 3-sulphinoalanine + CysO2H + L-cysteine sulfinic acid + MOD_RES Cysteine sulfinic acid (-SO2H) + S-cysteinesulfinic acid + S-sulfinocysteine + cysteine sulphinic acid + cysteine-S,S-dioxide [tautomer] + sulfinicacid + PSI-MOD + Dioxidation + dihydroxy + MOD:00267 + + "Hyun Ae Woo, et. al., Science 300 (5619), 653-656" + L-cysteine sulfinic acid + + + + + A protein modification that effectively dioxygenates an L-cysteine residue to L-cysteine sulfinic acid. + ChEBI:16345 + OMSSA:162 + PubMed:12686488 + PubMed:9252331 + PubMed:9586994 + RESID:AA0262 + Unimod:425#C + + + + + (2R)-2-amino-3-sulfinopropanoic acid + + + + + + 2-amino-2-carboxyethanesulfinic acid + + + + + + 2-amino-3-(dioxido-lambda(6)-sulfanyl)propanoic acid [tautomer] + + + + + + 2-amino-3-sulfonylpropanoic acid [tautomer] + + + + + + 3-sulfinoalanine + + + + + + 3-sulphinoalanine + + + + + + CysO2H + + + + + + L-cysteine sulfinic acid + + + + + + MOD_RES Cysteine sulfinic acid (-SO2H) + + + + + + S-cysteinesulfinic acid + + + + + + S-sulfinocysteine + + + + + + cysteine sulphinic acid + + + + + + cysteine-S,S-dioxide [tautomer] + + + + + + sulfinicacid + + + + + + Dioxidation + + + + + + dihydroxy + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to L-3',4',5'-trihydroxyphenylalanine. + 32.0 + C 0 H 0 N 0 O 2 + 31.989828 + C 9 H 9 N 1 O 4 + 195.17 + 195.05316 + Y + natural + Unimod:425 + uniprot.ptm:PTM-0667 + (S)-2-amino-3-(3,4,5-trihydroxyphenyl)propanoic acid + 3,4,6-Trihydroxy-Phenylalanine (from Tyrosine) (TOPA) + 35Hy2Tyr + L-3',4',5'-trihydroxyphenylalanine + L-3,4,5-TOPA + MOD_RES 3',4',5'-trihydroxyphenylalanine + PSI-MOD + Dioxidation + dihydroxy + MOD:00268 + From DeltaMass: Average Mass: 32 + L-3',4',5'-trihydroxyphenylalanine + + + + + A protein modification that effectively converts an L-tyrosine residue to L-3',4',5'-trihydroxyphenylalanine. + ChEBI:141811 + DeltaMass:0 + PubMed:12686488 + PubMed:12771378 + PubMed:8554314 + PubMed:9252331 + PubMed:9434739 + RESID:AA0263 + Unimod:425#Y + + + + + (S)-2-amino-3-(3,4,5-trihydroxyphenyl)propanoic acid + + + + + + 3,4,6-Trihydroxy-Phenylalanine (from Tyrosine) (TOPA) + + + + + + 35Hy2Tyr + + + + + + L-3',4',5'-trihydroxyphenylalanine + + + + + + L-3,4,5-TOPA + + + + + + MOD_RES 3',4',5'-trihydroxyphenylalanine + + + + + + Dioxidation + + + + + + dihydroxy + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-(sn-1-glycerophosphoryl)-L-serine. + 154.06 + C 3 H 7 N 0 O 5 P 1 + 154.00311 + C 6 H 12 N 1 O 7 P 1 + 241.14 + 241.03514 + S + natural + Unimod:419 + uniprot.ptm:PTM-0230 + (2S)-2-amino-3-[(2Xi)-2,3-dihydroxypropyl]phosphonoxypropanoic acid + MOD_RES O-(sn-1-glycerophosphoryl)serine + O-(sn-1-glycerophosphoryl)-L-serine + O3-(sn-1-glycerophosphoryl)-L-serine + O3-2,3-dihydroxypropyl hydrogen phosphate-L-serine ester + O3-L-serine glyceryl-1-phosphodiester + alpha-glycerophosphoryl serine + glycerophosphoserine + PSI-MOD + Glycerophospho + glycerophospho + MOD:00269 + + O-(sn-1-glycerophosphoryl)-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-(sn-1-glycerophosphoryl)-L-serine. + PubMed:8645220 + RESID:AA0264 + Unimod:419#S + + + + + (2S)-2-amino-3-[(2Xi)-2,3-dihydroxypropyl]phosphonoxypropanoic acid + + + + + + MOD_RES O-(sn-1-glycerophosphoryl)serine + + + + + + O-(sn-1-glycerophosphoryl)-L-serine + + + + + + O3-(sn-1-glycerophosphoryl)-L-serine + + + + + + O3-2,3-dihydroxypropyl hydrogen phosphate-L-serine ester + + + + + + O3-L-serine glyceryl-1-phosphodiester + + + + + + alpha-glycerophosphoryl serine + + + + + + glycerophosphoserine + + + + + + Glycerophospho + + + + + + glycerophospho + + + + + + + + + + A protein modification that effectively converts a glycine residue to an internal 1-thioglycine. + 16.06 + C 0 H 0 N 0 O -1 S 1 + 15.977156 + C 2 H 3 N 1 S 1 + 73.11 + 72.99862 + G + natural + uniprot.ptm:PTM-0004 + 1-thioglycine + 2-amino-1-sulfanylethanone + MOD_RES 1-thioglycine + S(O)Gly + aminoethanethioic O-acid + aminoethanethioic acid + aminoethanethionic acid + aminothioacetic acid + PSI-MOD + Carboxy->Thiocarboxy + thiocarboxylic acid + MOD:00270 + + This modification occurs naturally in two forms. At an interior peptide location it exists as aminoethanethionic acid (or aminoethanethioic O-acid). At the carboxyl-terminal it exists as aminoethanethiolic acid (or aminoethanethioic S-acid). + 1-thioglycine (internal) + + + + + A protein modification that effectively converts a glycine residue to an internal 1-thioglycine. + PubMed:11463785 + PubMed:9367957 + RESID:AA0265#INT + + + + + 1-thioglycine + + + + + + 2-amino-1-sulfanylethanone + + + + + + MOD_RES 1-thioglycine + + + + + + S(O)Gly + + + + + + aminoethanethioic O-acid + + + + + + aminoethanethioic acid + + + + + + aminoethanethionic acid + + + + + + aminothioacetic acid + + + + + + Carboxy->Thiocarboxy + + + + + + thiocarboxylic acid + + + + + + + + + + + + A protein modification that effectively results from forming an adduct between two cysteine residues, the C-3' of a tyrosine residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + 614.48 + C 34 Fe 1 H 30 N 4 O 4 S 0 + 614.1616 + C 49 Fe 1 H 49 N 7 O 8 S 2 + 983.94 + 983.24335 + C, C, Y + natural + (10S,11S)-[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-10-(2-hydroxy-5-[(S)-2-amino-2-carboxy]ethylphenyl)-3,8,13,17-tetramethyl-21H,23H-10,11-dihydroporphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate + BINDING Heme (covalent; via 3 links) + bis(S-cysteinyl)-(tyros-3'-yl)-heme + heme P460-bis-L-cysteine-L-tyrosine + PSI-MOD + MOD:00271 + Cross-link 3. + heme P460-bis-L-cysteine-L-tyrosine + + + + + A protein modification that effectively results from forming an adduct between two cysteine residues, the C-3' of a tyrosine residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + PubMed:8325841 + PubMed:9095195 + RESID:AA0266 + + + + + (10S,11S)-[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-10-(2-hydroxy-5-[(S)-2-amino-2-carboxy]ethylphenyl)-3,8,13,17-tetramethyl-21H,23H-10,11-dihydroporphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate + + + + + + BINDING Heme (covalent; via 3 links) + + + + + + bis(S-cysteinyl)-(tyros-3'-yl)-heme + + + + + + heme P460-bis-L-cysteine-L-tyrosine + + + + + + + + + + + A protein modification that effectively crosslinks an L-threonine residue and 5'-phosphoadenosine through a phosphodiester bond to form O-(phospho-5'-adenosine)-L-threonine. + 329.21 + C 10 H 12 N 5 O 6 P 1 + 329.05252 + C 14 H 19 N 6 O 8 P 1 + 430.31 + 430.1002 + T + natural + Unimod:405 + uniprot.ptm:PTM-0393 + (2S,3R)-2-amino-3-(5'-adenosine phosphonoxy)butanoic acid + 5'-adenylic-O3-L-threonine + ACT_SITE O-AMP-threonine intermediate + L-threonine monoanhydride with 5'-adenylic acid + MOD_RES O-AMP-threonine + O(gamma)-5'-adenylic-L-threonine + O-(phospho-5'-adenosine)-L-threonine + O3-(phospho-5'-adenosine)-L-threonine + O3-L-threonine 5'-adenosine phosphodiester + beta-5'-adenylic-L-threonine + PSI-MOD + AMP binding site + Phosphoadenosine + MOD:00272 + + O-(phospho-5'-adenosine)-L-threonine + + + + + A protein modification that effectively crosslinks an L-threonine residue and 5'-phosphoadenosine through a phosphodiester bond to form O-(phospho-5'-adenosine)-L-threonine. + PubMed:2989287 + PubMed:8917428 + RESID:AA0267 + Unimod:405#T + + + + + (2S,3R)-2-amino-3-(5'-adenosine phosphonoxy)butanoic acid + + + + + + 5'-adenylic-O3-L-threonine + + + + + + ACT_SITE O-AMP-threonine intermediate + + + + + + L-threonine monoanhydride with 5'-adenylic acid + + + + + + MOD_RES O-AMP-threonine + + + + + + O(gamma)-5'-adenylic-L-threonine + + + + + + O-(phospho-5'-adenosine)-L-threonine + + + + + + O3-(phospho-5'-adenosine)-L-threonine + + + + + + O3-L-threonine 5'-adenosine phosphodiester + + + + + + beta-5'-adenylic-L-threonine + + + + + + AMP binding site + + + + + + Phosphoadenosine + + + + + + + + + + + + + A protein modification that effectively converts four L-cysteine residues, two L-glutamic acid residues, an L-histidine residue and a four-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide. + 360.5 + C 0 Fe 4 H -7 N 0 O 3 S 3 + 360.58594 + C 28 Fe 4 H 34 N 9 O 14 S 7 + 1168.43 + 1167.7667 + C, C, C, C, E, E, H + natural + 4Fe-2S-3O cluster + METAL Iron-oxo-sulfur (4Fe-2O-2S) + METAL Iron-oxo-sulfur (4Fe-2O-2S); via persulfide group + METAL Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogen + hybrid four iron cluster 2 + mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O5-glutamato 2-iron-3,4-bis-(S-cysteinyl iron) + tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide + PSI-MOD + prismane iron-sulfur cofactor + MOD:00273 + Cross-link 7; secondary to RESID:AA0269. + tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide + + + + + A protein modification that effectively converts four L-cysteine residues, two L-glutamic acid residues, an L-histidine residue and a four-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide. + PubMed:12764602 + RESID:AA0268 + + + + + 4Fe-2S-3O cluster + + + + + + METAL Iron-oxo-sulfur (4Fe-2O-2S) + + + + + + METAL Iron-oxo-sulfur (4Fe-2O-2S); via persulfide group + + + + + + METAL Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogen + + + + + + hybrid four iron cluster 2 + + + + + + mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O5-glutamato 2-iron-3,4-bis-(S-cysteinyl iron) + + + + + + tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide + + + + + + prismane iron-sulfur cofactor + + + + + + + + + + + A protein modification that effectively replaces the hydrogen atom of a cysteine sulfanyl group with a sulfanyl group, forming a disulfanyl group, and converting an L-cysteine residue to L-cysteine persulfide. + 32.06 + C 0 H 0 N 0 O 0 S 1 + 31.97207 + C 3 H 5 N 1 O 1 S 2 + 135.2 + 134.98126 + C + natural + Unimod:421 + uniprot.ptm:PTM-0106 + (R)-2-amino-3-disulfanylpropanoic acid + 2-amino-3-disulfanylpropanoic acid + 2-amino-3-hydrodisulfidopropanoic acid + 2-amino-3-hydropersulfidopropanoic acid + 2-amino-3-persulfhydrylpropanoic acid + 3-(thiosulfeno)-alanine + 3-disulfanylalanine + ACT_SITE Cysteine persulfide intermediate + L-cysteine persulfide + MOD_RES Cysteine persulfide + S-mercaptocysteine + S-sulfanylcysteine + thiocysteine + PSI-MOD + Sulfide + persulfide + MOD:00274 + + L-cysteine persulfide + + + + + A protein modification that effectively replaces the hydrogen atom of a cysteine sulfanyl group with a sulfanyl group, forming a disulfanyl group, and converting an L-cysteine residue to L-cysteine persulfide. + ChEBI:28839 + PubMed:15096637 + PubMed:4276457 + PubMed:8161529 + RESID:AA0269 + Unimod:421 + + + + + (R)-2-amino-3-disulfanylpropanoic acid + + + + + + 2-amino-3-disulfanylpropanoic acid + + + + + + 2-amino-3-hydrodisulfidopropanoic acid + + + + + + 2-amino-3-hydropersulfidopropanoic acid + + + + + + 2-amino-3-persulfhydrylpropanoic acid + + + + + + 3-(thiosulfeno)-alanine + + + + + + 3-disulfanylalanine + + + + + + ACT_SITE Cysteine persulfide intermediate + + + + + + L-cysteine persulfide + + + + + + MOD_RES Cysteine persulfide + + + + + + S-mercaptocysteine + + + + + + S-sulfanylcysteine + + + + + + thiocysteine + + + + + + Sulfide + + + + + + persulfide + + + + + + + + + + + + A protein modification that effectively cross-links an L-histidine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 3'-(1'-L-histidyl)-L-tyrosine. + -2.02 + C 0 H -2 N 0 O 0 + -2.01565 + C 15 H 14 N 4 O 3 + 298.3 + 298.1066 + H, Y + natural + uniprot.ptm:PTM-0003 + (2S)-2-amino-3-[1-(5-[(2S)-2-amino-2-carboxyethyl]-2-hydroxyphenyl)-1H-imidazol-4-yl]propanoic acid + 3'-(1'-L-histidyl)-L-tyrosine + 3'-(N(epsilon)-histidyl)tyrosine + 3'-(N1'-histidyl)tyrosine + 3'-(tau-histidyl)tyrosine + 3'-(tele-histidyl)tyrosine + CROSSLNK 1'-histidyl-3'-tyrosine (His-Tyr) + PSI-MOD + MOD:00275 + + Cross-link 2. + 3'-(1'-L-histidyl)-L-tyrosine + + + + + A protein modification that effectively cross-links an L-histidine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 3'-(1'-L-histidyl)-L-tyrosine. + ChEBI:19837 + PubMed:10338009 + RESID:AA0270 + + + + + (2S)-2-amino-3-[1-(5-[(2S)-2-amino-2-carboxyethyl]-2-hydroxyphenyl)-1H-imidazol-4-yl]propanoic acid + + + + + + 3'-(1'-L-histidyl)-L-tyrosine + + + + + + 3'-(N(epsilon)-histidyl)tyrosine + + + + + + 3'-(N1'-histidyl)tyrosine + + + + + + 3'-(tau-histidyl)tyrosine + + + + + + 3'-(tele-histidyl)tyrosine + + + + + + CROSSLNK 1'-histidyl-3'-tyrosine (His-Tyr) + + + + + + + + + + + + A protein modification that effectively results from forming an adduct between two cysteine residues, a lysine residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + 614.48 + C 34 Fe 1 H 30 N 4 O 4 S 0 + 614.1616 + C 46 Fe 1 H 52 N 8 O 7 S 2 + 948.94 + 948.27496 + C, C, K + natural + (19S,20S)-[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-20-([(S)-5-amino-5-carboxypentyl]amino)-3,8,13,17-tetramethyl-21H,23H-19,20-dihydroporphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate + BINDING Heme (covalent; via 3 links) + bis(S-cysteinyl)-N6-lysino-heme + heme P460-bis-L-cysteine-L-lysine + PSI-MOD + MOD:00276 + Cross-link 3. + heme P460-bis-L-cysteine-L-lysine + + + + + A protein modification that effectively results from forming an adduct between two cysteine residues, a lysine residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + PubMed:12709052 + PubMed:9237682 + RESID:AA0271 + + + + + (19S,20S)-[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-20-([(S)-5-amino-5-carboxypentyl]amino)-3,8,13,17-tetramethyl-21H,23H-19,20-dihydroporphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate + + + + + + BINDING Heme (covalent; via 3 links) + + + + + + bis(S-cysteinyl)-N6-lysino-heme + + + + + + heme P460-bis-L-cysteine-L-lysine + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to 5-methyl-L-arginine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 7 H 14 N 4 O 1 + 170.22 + 170.11676 + R + natural + uniprot.ptm:PTM-0050 + (2S,5S)-2-amino-5-carbamimidamidohexanoic acid + 2-amino-5-guanidinohexanoic acid + 5-methyl-L-arginine + 5-methylated L-arginine + C5Me1Arg + MOD_RES 5-methylarginine + delta-methylarginine + PSI-MOD + 4-methylarginine + Methyl + Methylation + MOD:00277 + 5-methyl-L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to 5-methyl-L-arginine. + PubMed:10660523 + PubMed:11875433 + PubMed:9367957 + RESID:AA0272 + + + + + (2S,5S)-2-amino-5-carbamimidamidohexanoic acid + + + + + + 2-amino-5-guanidinohexanoic acid + + + + + + 5-methyl-L-arginine + + + + + + 5-methylated L-arginine + + + + + + C5Me1Arg + + + + + + MOD_RES 5-methylarginine + + + + + + delta-methylarginine + + + + + + 4-methylarginine + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + A protein modification that effectively converts an L-glutamine residue to 2-methyl-L-glutamine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 6 H 10 N 2 O 2 + 142.16 + 142.07423 + Q + natural + uniprot.ptm:PTM-0016 + (S)-2-amino-2-methylpentanediamic acid + 2-methyl-L-glutamine + 2-methylated L-glutamine + 2-methylglutamine + C2MeGln + MOD_RES 2-methylglutamine + alpha-methylglutamine + PSI-MOD + Methyl + Methylation + MOD:00278 + 2-methyl-L-glutamine + + + + + A protein modification that effectively converts an L-glutamine residue to 2-methyl-L-glutamine. + PubMed:10660523 + PubMed:11875433 + PubMed:9367957 + RESID:AA0273 + + + + + (S)-2-amino-2-methylpentanediamic acid + + + + + + 2-methyl-L-glutamine + + + + + + 2-methylated L-glutamine + + + + + + 2-methylglutamine + + + + + + C2MeGln + + + + + + MOD_RES 2-methylglutamine + + + + + + alpha-methylglutamine + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to N-pyruvic acid 2-iminyl-L-cysteine. + 70.05 + C 3 H 2 N 0 O 2 S 0 + 70.00548 + C 6 H 8 N 1 O 3 S 1 + 174.19 + 174.02249 + C + natural + N-term + Unimod:422 + uniprot.ptm:PTM-0224 + (R)-2-(1-carboxy-2-sulfanylethanimino)propanoic acid + MOD_RES N-pyruvate 2-iminyl-cysteine + N-pyruvic acid 2-iminyl-L-cysteine + PSI-MOD + N-pyruvic acid 2-iminyl + PyruvicAcidIminyl + MOD:00279 + + N-pyruvic acid 2-iminyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to N-pyruvic acid 2-iminyl-L-cysteine. + PubMed:1388164 + RESID:AA0274 + Unimod:422#C + + + + + (R)-2-(1-carboxy-2-sulfanylethanimino)propanoic acid + + + + + + MOD_RES N-pyruvate 2-iminyl-cysteine + + + + + + N-pyruvic acid 2-iminyl-L-cysteine + + + + + + N-pyruvic acid 2-iminyl + + + + + + PyruvicAcidIminyl + + + + + + + + + + + A protein modification that effectively converts an L-valine residue to N-pyruvic acid 2-iminyl-L-valine. + 70.05 + C 3 H 2 N 0 O 2 + 70.00548 + C 8 H 12 N 1 O 3 + 170.19 + 170.08171 + V + natural + N-term + Unimod:422 + uniprot.ptm:PTM-0225 + (S)-2-(1-carboxy-2-methylpropanimino)propanoic acid + MOD_RES N-pyruvate 2-iminyl-valine + N-pyruvic acid 2-iminyl-L-valine + PSI-MOD + N-pyruvic acid 2-iminyl + PyruvicAcidIminyl + MOD:00280 + + N-pyruvic acid 2-iminyl-L-valine + + + + + A protein modification that effectively converts an L-valine residue to N-pyruvic acid 2-iminyl-L-valine. + PubMed:2071591 + RESID:AA0275 + Unimod:422#V + + + + + (S)-2-(1-carboxy-2-methylpropanimino)propanoic acid + + + + + + MOD_RES N-pyruvate 2-iminyl-valine + + + + + + N-pyruvic acid 2-iminyl-L-valine + + + + + + N-pyruvic acid 2-iminyl + + + + + + PyruvicAcidIminyl + + + + + + + + + + + A protein modification that effectively results from forming an adduct between the pros nitrogen of a histidine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + 616.5 + C 34 Fe 1 H 32 N 4 O 4 + 616.1773 + C 40 Fe 1 H 39 N 7 O 5 + 753.64 + 753.2362 + H + natural + 2-[1-(N3'-histidyl)ethyl]protoporphyrin IX + 3'-heme-L-histidine + BINDING Heme (covalent; via pros nitrogen) + N(delta)-histidyl heme + N(pi)-histidyl heme + N3'-histidyl heme + [7-ethenyl-12-((S)-1-[((R)-2-amino-2-carboxyethyl)-3H-imidazol-3-yl]ethyl)-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate + pros-histidyl heme + PSI-MOD + MOD:00281 + 3'-heme-L-histidine + + + + + A protein modification that effectively results from forming an adduct between the pros nitrogen of a histidine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + PubMed:12119398 + PubMed:12429096 + PubMed:12486054 + PubMed:9712585 + RESID:AA0276 + + + + + 2-[1-(N3'-histidyl)ethyl]protoporphyrin IX + + + + + + 3'-heme-L-histidine + + + + + + BINDING Heme (covalent; via pros nitrogen) + + + + + + N(delta)-histidyl heme + + + + + + N(pi)-histidyl heme + + + + + + N3'-histidyl heme + + + + + + [7-ethenyl-12-((S)-1-[((R)-2-amino-2-carboxyethyl)-3H-imidazol-3-yl]ethyl)-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate + + + + + + pros-histidyl heme + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-selenyl-L-cysteine. + 78.97 + C 0 H 0 N 0 O 0 S 0 Se 1 + 79.91652 + C 3 H 5 N 1 O 1 S 1 Se 1 + 182.11 + 182.9257 + C + hypothetical + Unimod:423 + uniprot.ptm:PTM-0282 + (R)-2-amino-3-(selanylsulfanyl)propanoic acid + 2-amino-3-hydroselenosulfidopropanoic acid + 2-amino-3-hydroselenylsulfidopropanoic acid + 2-amino-3-hydroselenylthiopropanoic acid + ACT_SITE S-selanylcysteine intermediate + MOD_RES S-selenylcysteine + S-selanyl-L-cysteine + S-selanylcysteine + S-selenylcysteine + PSI-MOD + Delta:Se(1) + cysteine perselenide + selenyl + MOD:00282 + S-selenyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-selenyl-L-cysteine. + PubMed:10430865 + PubMed:10966817 + PubMed:11827487 + PubMed:12716131 + PubMed:14594807 + RESID:AA0277 + Unimod:423#C + + + + + (R)-2-amino-3-(selanylsulfanyl)propanoic acid + + + + + + 2-amino-3-hydroselenosulfidopropanoic acid + + + + + + 2-amino-3-hydroselenylsulfidopropanoic acid + + + + + + 2-amino-3-hydroselenylthiopropanoic acid + + + + + + ACT_SITE S-selanylcysteine intermediate + + + + + + MOD_RES S-selenylcysteine + + + + + + S-selanyl-L-cysteine + + + + + + S-selanylcysteine + + + + + + S-selenylcysteine + + + + + + Delta:Se(1) + + + + + + cysteine perselenide + + + + + + selenyl + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to an N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine. + K + natural + uniprot.ptm:PTM-0198 + (alpha)- ([([(5S)-5-amino-5-carboxypentyl]amino)propyl][(methyl)amino])-(omega)-methyl poly[propane-1,3-diyl(methylimino)] + MOD_RES N6-poly(methylaminopropyl)lysine + N6-[3-([(omega)-(dimethyl)aminopropyl-poly(3-[methylamino]propyl)]amino)propyl]lysine + N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine + lysine derivative Lys(x) + silaffin polycationic lysine derivative + PSI-MOD + MOD:00283 + N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to an N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine. + PubMed:10550045 + PubMed:11349130 + RESID:AA0278 + + + + + (alpha)- ([([(5S)-5-amino-5-carboxypentyl]amino)propyl][(methyl)amino])-(omega)-methyl poly[propane-1,3-diyl(methylimino)] + + + + + + MOD_RES N6-poly(methylaminopropyl)lysine + + + + + + N6-[3-([(omega)-(dimethyl)aminopropyl-poly(3-[methylamino]propyl)]amino)propyl]lysine + + + + + + N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine + + + + + + lysine derivative Lys(x) + + + + + + silaffin polycationic lysine derivative + + + + + + + + + + + + A protein modification that effectively results from forming an adduct between an aspartic acid residue, a glutamic acid residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + 612.47 + C 34 Fe 1 H 28 N 4 O 4 + 612.146 + C 43 Fe 1 H 40 N 6 O 10 + 856.67 + 856.2155 + D, E + hypothetical + 1,5-bishydroxymethyl protoporphyrin IX 1-glutamate ester 5-aspartate ester + BINDING Heme (covalent; via 2 links) + [13-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-3-[(S)-(3-amino-3-carboxy)propanoyloxymethyl]-7,12-diethenyl-8,17-dimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate + dihydroxyheme-L-aspartate ester-L-glutamate ester + peroxidase heme cofactor + PSI-MOD + MOD:00284 + Cross-link 2. + dihydroxyheme-L-aspartate ester-L-glutamate ester + + + + + A protein modification that effectively results from forming an adduct between an aspartic acid residue, a glutamic acid residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + PubMed:10447690 + RESID:AA0279 + + + + + 1,5-bishydroxymethyl protoporphyrin IX 1-glutamate ester 5-aspartate ester + + + + + + BINDING Heme (covalent; via 2 links) + + + + + + [13-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-3-[(S)-(3-amino-3-carboxy)propanoyloxymethyl]-7,12-diethenyl-8,17-dimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate + + + + + + dihydroxyheme-L-aspartate ester-L-glutamate ester + + + + + + peroxidase heme cofactor + + + + + + + + + + + + + A protein modification that effectively results from forming an adduct between an aspartic acid residue, a glutamic acid residue, a methionine residue (forming a sulfonium ether), and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + 613.47 + C 34 Fe 1 H 29 N 4 O 4 S 0 + 613.15326 + 1+ + C 48 Fe 1 H 50 N 7 O 11 S 1 + 988.87 + 988.2633 + D, E, M + natural + 1,5-bishydroxymethyl protoporphyrin IX 1-glutamate ester 5-aspartate ester 2-methionine sulfonium + BINDING Heme (covalent; via 3 links) + [13-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-3-[(S)-(3-amino-3-carboxy)propanoyloxymethyl]-12-[(S)-(3-amino-3-carboxy)propylsulfoniumethyl]-7-ethenyl-8,17-dimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate + dihydroxyheme-L-aspartate ester-L-glutamate ester-L-methionine sulfonium + myeloperoxidase heme cofactor + PSI-MOD + MOD:00285 + Cross-link 3. + dihydroxyheme-L-aspartate ester-L-glutamate ester-L-methionine sulfonium + + + + + A protein modification that effectively results from forming an adduct between an aspartic acid residue, a glutamic acid residue, a methionine residue (forming a sulfonium ether), and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + PubMed:10447690 + PubMed:10480885 + PubMed:1320128 + PubMed:7840679 + RESID:AA0280 + + + + + 1,5-bishydroxymethyl protoporphyrin IX 1-glutamate ester 5-aspartate ester 2-methionine sulfonium + + + + + + BINDING Heme (covalent; via 3 links) + + + + + + [13-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-3-[(S)-(3-amino-3-carboxy)propanoyloxymethyl]-12-[(S)-(3-amino-3-carboxy)propylsulfoniumethyl]-7-ethenyl-8,17-dimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate + + + + + + dihydroxyheme-L-aspartate ester-L-glutamate ester-L-methionine sulfonium + + + + + + myeloperoxidase heme cofactor + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide). + 1572.02 + C 40 H 47 Mo 1 N 20 O 26 P 4 S 4 + 1572.9857 + C 43 H 52 Mo 1 N 21 O 27 P 4 S 5 + 1675.15 + 1675.995 + C + hypothetical + Unimod:424 + 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide + L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide) + bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-cystein-S-yl-molybdenum + PSI-MOD + MolybdopterinGD + molybdenum bis(molybdopterin guanine dinucleotide) + MOD:00286 + L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide) + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide). + RESID:AA0281 + Unimod:424#C + + + + + 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide + + + + + + L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide) + + + + + + bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-cystein-S-yl-molybdenum + + + + + + MolybdopterinGD + + + + + + molybdenum bis(molybdopterin guanine dinucleotide) + + + + + + + + + + A protein modification that effectively converts an L-proline residue to a (2S,3R,4S)-3,4-dihydroxyproline. + 32.0 + C 0 H 0 N 0 O 2 + 31.989828 + C 5 H 7 N 1 O 3 + 129.12 + 129.04259 + P + natural + Unimod:425 + uniprot.ptm:PTM-0306 + (2S,3R,4S)-3,4-dihydroxyproline + (2S,3R,4S)-3,4-dihydroxypyrrolidine-2-carboxylic acid + 2,3-trans-3,4-cis-3,4-dihydroxy-L-proline + 2-alpha-3-beta-4-beta-3,4-dihydroxyproline + 3,4-Dihydroxylation (of Proline) + 3,4-dihydroxylated L-proline + 34Hy2Pro + MOD_RES (3R,4S)-3,4-dihydroxyproline + trans-2,3-cis-3,4-dihydroxy-L-proline + PSI-MOD + Dioxidation + dihydroxy + MOD:00287 + From DeltaMass: Average Mass: 32. + (2S,3R,4S)-3,4-dihydroxyproline + + + + + A protein modification that effectively converts an L-proline residue to a (2S,3R,4S)-3,4-dihydroxyproline. + ChEBI:141803 + DeltaMass:0 + PubMed:12686488 + RESID:AA0282 + Unimod:425#P + + + + + (2S,3R,4S)-3,4-dihydroxyproline + + + + + + (2S,3R,4S)-3,4-dihydroxypyrrolidine-2-carboxylic acid + + + + + + 2,3-trans-3,4-cis-3,4-dihydroxy-L-proline + + + + + + 2-alpha-3-beta-4-beta-3,4-dihydroxyproline + + + + + + 3,4-Dihydroxylation (of Proline) + + + + + + 3,4-dihydroxylated L-proline + + + + + + 34Hy2Pro + + + + + + MOD_RES (3R,4S)-3,4-dihydroxyproline + + + + + + trans-2,3-cis-3,4-dihydroxy-L-proline + + + + + + Dioxidation + + + + + + dihydroxy + + + + + + + + + + + + A protein modification that effectively doubly cross-links an L-glutamic acid residue and an L-tyrosine residue with a carbon-carbon bond and a carbon-nitrogen bond to form pyrroloquinoline quinone. + 37.92 + C 0 H -10 N 0 O 3 + 37.906494 + C 14 H 6 N 2 O 8 + 330.21 + 330.01242 + E, Y + natural + uniprot.ptm:PTM-0263 + 2,4,6-tricarboxylic-pyrrolo[2,3-5,6]quinoline 8,9-quinone + 2,7,9-tricarboxy-1H-pyrrolo(2,3-f)quinoline-4,5-dione + 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-5,6]quinoline-2,7,9-tricarboxylic acid + CROSSLNK Pyrroloquinoline quinone (Glu-Tyr) + coenzyme PQQ + methoxatin + pyrroloquinoline quinone + PSI-MOD + MOD:00288 + Cross-link 2. + pyrroloquinoline quinone + + + + + A protein modification that effectively doubly cross-links an L-glutamic acid residue and an L-tyrosine residue with a carbon-carbon bond and a carbon-nitrogen bond to form pyrroloquinoline quinone. + ChEBI:18315 + PubMed:1310505 + PubMed:7665488 + RESID:AA0283 + + + + + 2,4,6-tricarboxylic-pyrrolo[2,3-5,6]quinoline 8,9-quinone + + + + + + 2,7,9-tricarboxy-1H-pyrrolo(2,3-f)quinoline-4,5-dione + + + + + + 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-5,6]quinoline-2,7,9-tricarboxylic acid + + + + + + CROSSLNK Pyrroloquinoline quinone (Glu-Tyr) + + + + + + coenzyme PQQ + + + + + + methoxatin + + + + + + pyrroloquinoline quinone + + + + + + + + + + + + A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide. + 347.59 + C 0 Fe 4 H -4 N 0 O 0 S 4 + 347.59784 + 2- + C 15 Fe 4 H 18 N 6 O 4 S 7 + 794.15 + 793.6843 + C, C, C, H + natural + METAL Iron-sulfur (4Fe-4S) + METAL Iron-sulfur (4Fe-4S); via tele nitrogen + tetra-mu3-sulfidotris(S-cysteinyliron)(N1'-histidinoiron) + tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide + PSI-MOD + MOD:00289 + Cross-link 4. + tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide + + + + + A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide. + PubMed:9836629 + RESID:AA0284 + + + + + METAL Iron-sulfur (4Fe-4S) + + + + + + METAL Iron-sulfur (4Fe-4S); via tele nitrogen + + + + + + tetra-mu3-sulfidotris(S-cysteinyliron)(N1'-histidinoiron) + + + + + + tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide + + + + + + + + + + + + A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide. + 347.59 + C 0 Fe 4 H -4 N 0 O 0 S 4 + 347.59784 + 2- + C 15 Fe 4 H 18 N 6 O 4 S 7 + 794.15 + 793.6843 + C, C, C, H + natural + METAL Iron-sulfur (4Fe-4S) + METAL Iron-sulfur (4Fe-4S); via pros nitrogen + tetra-mu3-sulfidotris(S-cysteinyliron)(N3'-histidinoiron) + tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide + PSI-MOD + MOD:00290 + Cross-link 4. + tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide + + + + + A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide. + PubMed:7854413 + RESID:AA0285 + + + + + METAL Iron-sulfur (4Fe-4S) + + + + + + METAL Iron-sulfur (4Fe-4S); via pros nitrogen + + + + + + tetra-mu3-sulfidotris(S-cysteinyliron)(N3'-histidinoiron) + + + + + + tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide + + + + + + + + + + + + A protein modification that effectively converts three L-cysteine residues, an L-aspartic acid residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-aspartato tetrairon tetrasulfide. + 347.59 + C 0 Fe 4 H -4 N 0 O 0 S 4 + 347.59784 + 2- + C 13 Fe 4 H 16 N 4 O 6 S 7 + 772.09 + 771.65234 + C, C, C, D + natural + METAL Iron-sulfur (4Fe-4S) + tetra-mu3-sulfidotris(S-cysteinyliron)(O4-aspartatoiron) + tris-L-cysteinyl L-aspartato tetrairon tetrasulfide + PSI-MOD + MOD:00291 + Cross-link 4. + tris-L-cysteinyl L-aspartato tetrairon tetrasulfide + + + + + A protein modification that effectively converts three L-cysteine residues, an L-aspartic acid residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-aspartato tetrairon tetrasulfide. + PubMed:7819255 + PubMed:9283079 + RESID:AA0286 + + + + + METAL Iron-sulfur (4Fe-4S) + + + + + + tetra-mu3-sulfidotris(S-cysteinyliron)(O4-aspartatoiron) + + + + + + tris-L-cysteinyl L-aspartato tetrairon tetrasulfide + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-pyruvic acid 2-iminyl-L-lysine. + 70.05 + C 3 H 2 N 0 O 2 + 70.00548 + C 9 H 14 N 2 O 3 + 198.22 + 198.10045 + K + natural + Unimod:422 + (2S)-2-amino-6-([1-carboxyethylidene]amino)hexanoic acid + ACT_SITE Schiff-base intermediate with substrate + N6-pyruvic acid 2-iminyl-L-lysine + PSI-MOD + N-pyruvic acid 2-iminyl + PyruvicAcidIminyl + MOD:00292 + N6-pyruvic acid 2-iminyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-pyruvic acid 2-iminyl-L-lysine. + PubMed:1463470 + PubMed:7853400 + PubMed:9047371 + RESID:AA0287 + Unimod:422#K + + + + + (2S)-2-amino-6-([1-carboxyethylidene]amino)hexanoic acid + + + + + + ACT_SITE Schiff-base intermediate with substrate + + + + + + N6-pyruvic acid 2-iminyl-L-lysine + + + + + + N-pyruvic acid 2-iminyl + + + + + + PyruvicAcidIminyl + + + + + + + + + + + + A protein modification that effectively converts three L-cysteine residues, an L-serine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-serinyl tetrairon tetrasulfide. + 347.59 + C 0 Fe 4 H -4 N 0 O 0 S 4 + 347.59784 + 2- + C 12 Fe 4 H 16 N 4 O 5 S 7 + 744.08 + 743.6574 + C, C, C, S + hypothetical + tetra-mu3-sulfidotris(S-cysteinyliron)(O3-serinyliron) + tris-L-cysteinyl L-serinyl tetrairon tetrasulfide + PSI-MOD + MOD:00293 + Cross-link 4. + tris-L-cysteinyl L-serinyl tetrairon tetrasulfide + + + + + A protein modification that effectively converts three L-cysteine residues, an L-serine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-serinyl tetrairon tetrasulfide. + RESID:AA0288 + + + + + tetra-mu3-sulfidotris(S-cysteinyliron)(O3-serinyliron) + + + + + + tris-L-cysteinyl L-serinyl tetrairon tetrasulfide + + + + + + + + + + + + + A protein modification that effectively converts two L-cysteine residues, an L-histidine residues, an L-serine residue and a four-iron four-sulfur cluster to bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide. + 347.59 + C 0 Fe 4 H -4 N 0 O 0 S 4 + 347.59784 + 2- + C 15 Fe 4 H 18 N 6 O 5 S 6 + 778.09 + 777.70715 + C, C, H, S + hypothetical + METAL Iron-sulfur (4Fe-4S) + METAL Iron-sulfur (4Fe-4S); via pros nitrogen + bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide + tetra-mu3-sulfidobis(S-cysteinyliron)(N3'-histidinoiron)(O3-serinyliron) + PSI-MOD + MOD:00294 + Cross-link 4. + bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide + + + + + A protein modification that effectively converts two L-cysteine residues, an L-histidine residues, an L-serine residue and a four-iron four-sulfur cluster to bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide. + RESID:AA0289 + + + + + METAL Iron-sulfur (4Fe-4S) + + + + + + METAL Iron-sulfur (4Fe-4S); via pros nitrogen + + + + + + bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide + + + + + + tetra-mu3-sulfidobis(S-cysteinyliron)(N3'-histidinoiron)(O3-serinyliron) + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-octanoyl-L-serine. + 126.2 + C 8 H 14 N 0 O 1 + 126.10446 + C 11 H 19 N 1 O 3 + 213.28 + 213.13649 + S + natural + Unimod:426 + uniprot.ptm:PTM-0239 + (2S)-2-amino-3-(octanoyloxy)propanoic acid + L-serine octanoate ester + LIPID O-octanoyl serine + O-octanoyl-L-serine + O-octanoylated L-serine + O3-octanoyl-L-serine + OOctSer + PSI-MOD + Octanoyl + octanoyl + MOD:00295 + + O-octanoyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-octanoyl-L-serine. + PubMed:10604470 + PubMed:12716131 + RESID:AA0290 + Unimod:426#S + + + + + (2S)-2-amino-3-(octanoyloxy)propanoic acid + + + + + + L-serine octanoate ester + + + + + + LIPID O-octanoyl serine + + + + + + O-octanoyl-L-serine + + + + + + O-octanoylated L-serine + + + + + + O3-octanoyl-L-serine + + + + + + OOctSer + + + + + + Octanoyl + + + + + + octanoyl + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-D-glucuronosyl-L-serine. + 176.12 + C 6 H 8 N 0 O 6 + 176.03209 + C 9 H 13 N 1 O 8 + 263.2 + 263.06412 + S + natural + Unimod:54 + uniprot.ptm:PTM-0577 + (2S)-2-amino-3-(beta-D-glucopyranuronosyl)propanoic acid + CARBOHYD O-linked (GlcA) serine + O-D-glucuronosyl-L-serine + O3-D-glucuronosyl-L-serine + PSI-MOD + Glucuronyl + N-glucuronylation + MOD:00296 + + O-D-glucuronosyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-D-glucuronosyl-L-serine. + PubMed:10858503 + PubMed:12716131 + PubMed:7398618 + RESID:AA0291 + Unimod:54#S + + + + + (2S)-2-amino-3-(beta-D-glucopyranuronosyl)propanoic acid + + + + + + CARBOHYD O-linked (GlcA) serine + + + + + + O-D-glucuronosyl-L-serine + + + + + + O3-D-glucuronosyl-L-serine + + + + + + Glucuronyl + + + + + + N-glucuronylation + + + + + + + + + + + + + + A protein modification that effectively converts four L-cysteine residues, two L-glutamic acid residues, an L-histidine residue and a three-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide. + 363.35 + C 0 Fe 3 H -7 N 0 Ni 1 O 3 S 3 + 362.58633 + C 28 Fe 3 H 34 N 9 Ni 1 O 14 S 7 + 1171.28 + 1169.7672 + C, C, C, C, E, E, H + artifact + Ni-3Fe-2S-3O cluster + carbon monoxide dehydrogenase nickel-iron cofactor + hybrid nickel-triiron cluster + mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O5-glutamato 2-nickel-3,4-bis-(S-cysteinyl iron) + tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide + PSI-MOD + MOD:00297 + Cross-link 7; secondary to RESID:AA0269. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. + tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide + + + + + A protein modification that effectively converts four L-cysteine residues, two L-glutamic acid residues, an L-histidine residue and a three-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide. + RESID:AA0292 + + + + + Ni-3Fe-2S-3O cluster + + + + + + carbon monoxide dehydrogenase nickel-iron cofactor + + + + + + hybrid nickel-triiron cluster + + + + + + mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O5-glutamato 2-nickel-3,4-bis-(S-cysteinyl iron) + + + + + + tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide + + + + + + + + + + + + + + + A protein modification that effectively converts four L-cysteine residues, an L-glutamic acid residue, an L-histidine residue, an L-serine residue and a one-nickel three-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide. + 363.35 + C 0 Fe 3 H -7 N 0 Ni 1 O 3 S 3 + 362.58633 + C 26 Fe 3 H 32 N 9 Ni 1 O 13 S 7 + 1129.24 + 1127.7566 + C, C, C, C, E, H, S + artifact + Ni-3Fe-2S-3O cluster + carbon monoxide dehydrogenase nickel-iron cofactor + hybrid nickel-triiron cluster + mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O3-serinyl 2-nickel-3,4-bis-(S-cysteinyl iron) + tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide + PSI-MOD + MOD:00298 + Cross-link 7; secondary to RESID:AA0269. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. + tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide + + + + + A protein modification that effectively converts four L-cysteine residues, an L-glutamic acid residue, an L-histidine residue, an L-serine residue and a one-nickel three-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide. + PubMed:2550436 + RESID:AA0293 + + + + + Ni-3Fe-2S-3O cluster + + + + + + carbon monoxide dehydrogenase nickel-iron cofactor + + + + + + hybrid nickel-triiron cluster + + + + + + mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O3-serinyl 2-nickel-3,4-bis-(S-cysteinyl iron) + + + + + + tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide + + + + + + + + + + + + A protein modification that effectively crosslinks an L-asparagine residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoaspartyl)-L-lysine and the release of ammonia. + -17.03 + C 0 H -3 N -1 O 0 + -17.026548 + C 10 H 15 N 3 O 3 + 225.25 + 225.11134 + K, N + natural + uniprot.ptm:PTM-0153 + (2S)-2-amino-6-([(3S)-3-amino-3-carboxypropanoyl]amino)hexanoic acid + CROSSLNK Isoaspartyl lysine isopeptide (Lys-Asn) + N(epsilon)-(beta-aspartyl)lysine + N-(beta-Aspartyl)-Lysine (Crosslink) + N6-(L-isoaspartyl)-L-lysine + XLNK-4Asp-N6Lys(Asn) + beta-(N6-lysyl)aspartyl acid + isoaspartyl N6-lysine + PSI-MOD + MOD:00299 + Cross-link 2. + N6-(L-isoaspartyl)-L-lysine (Asn) + + + + + A protein modification that effectively crosslinks an L-asparagine residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoaspartyl)-L-lysine and the release of ammonia. + ChEBI:21862 + DeltaMass:0 + PubMed:11000116 + PubMed:6503713 + RESID:AA0294 + + + + + (2S)-2-amino-6-([(3S)-3-amino-3-carboxypropanoyl]amino)hexanoic acid + + + + + + CROSSLNK Isoaspartyl lysine isopeptide (Lys-Asn) + + + + + + N(epsilon)-(beta-aspartyl)lysine + + + + + + N-(beta-Aspartyl)-Lysine (Crosslink) + + + + + + N6-(L-isoaspartyl)-L-lysine + + + + + + XLNK-4Asp-N6Lys(Asn) + + + + + + beta-(N6-lysyl)aspartyl acid + + + + + + isoaspartyl N6-lysine + + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl-5-poly(ADP-ribose). + E + natural + Unimod:213 + (S)-2-amino-5-poly[2'-adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with 1alpha-D-ribofuranosyl]oxy-5-oxopentanoic acid + L-glutamyl-5-poly(ADP-ribose) + L-isoglutamyl-poly(ADP-ribose) + MOD_RES PolyADP-ribosyl glutamic acid + O-ADP-ribosylation (on Glutamate or C terminus) + PSI-MOD + ADP Ribose addition + ADP-Ribosyl + MOD:00300 + L-glutamyl-5-poly(ADP-ribose) + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl-5-poly(ADP-ribose). + DeltaMass:0 + PubMed:11246023 + PubMed:15842200 + PubMed:8533153 + RESID:AA0295 + Unimod:213#E + + + + + (S)-2-amino-5-poly[2'-adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with 1alpha-D-ribofuranosyl]oxy-5-oxopentanoic acid + + + + + + L-glutamyl-5-poly(ADP-ribose) + + + + + + L-isoglutamyl-poly(ADP-ribose) + + + + + + MOD_RES PolyADP-ribosyl glutamic acid + + + + + + O-ADP-ribosylation (on Glutamate or C terminus) + + + + + + ADP Ribose addition + + + + + + ADP-Ribosyl + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-(N-acetylglucosamine-1-phosphoryl)-L-serine. + 283.17 + C 8 H 14 N 1 O 8 P 1 + 283.04572 + C 11 H 19 N 2 O 10 P 1 + 370.25 + 370.07773 + S + natural + Unimod:428 + uniprot.ptm:PTM-0586 + (2S)-2-amino-3-[([(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)oxy][hydroxy]phosphoryl)oxy]propanoic acid + CARBOHYD O-linked (GalNAcP) serine + O-(N-acetylglucosamine-1-phosphoryl)-L-serine + O-GlcNAc-1-phosphorylation (of Serine) + O-beta(N-acetyl-glucosamine-alpha1-phosphate)serine + O3-(N-acetylglucosamine-1-phosphoryl)-L-serine + O3-L-serine 2-(acetylamino)-2-deoxy-D-glucopyranose 1-phosphodiester + PSI-MOD + N-acetylglucosamine-1-phosphoryl + PhosphoHexNAc + MOD:00301 + O-(N-acetylglucosamine-1-phosphoryl)-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-(N-acetylglucosamine-1-phosphoryl)-L-serine. + DeltaMass:0 + PubMed:6438439 + PubMed:6993483 + PubMed:8631906 + RESID:AA0296 + Unimod:428 + + + + + (2S)-2-amino-3-[([(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)oxy][hydroxy]phosphoryl)oxy]propanoic acid + + + + + + CARBOHYD O-linked (GalNAcP) serine + + + + + + O-(N-acetylglucosamine-1-phosphoryl)-L-serine + + + + + + O-GlcNAc-1-phosphorylation (of Serine) + + + + + + O-beta(N-acetyl-glucosamine-alpha1-phosphate)serine + + + + + + O3-(N-acetylglucosamine-1-phosphoryl)-L-serine + + + + + + O3-L-serine 2-(acetylamino)-2-deoxy-D-glucopyranose 1-phosphodiester + + + + + + N-acetylglucosamine-1-phosphoryl + + + + + + PhosphoHexNAc + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-(phosphoglycosyl-D-mannose-1-phosphoryl)-L-serine. + 242.12 + C 6 H 11 N 0 O 8 P 1 + 242.01915 + C 9 H 16 N 1 O 10 P 1 + 329.2 + 329.05118 + S + natural + Unimod:429 + uniprot.ptm:PTM-0594 + CARBOHYD O-linked (Man1P) serine + O-(D-mannose-1-phosphoryl)-L-serine + O-(alpha-D-mannosyl-1-phosphoryl)-L-serine + O-[alpha-D-mannopyranosyloxy(hydroxy)phosphoryl]-L-serine + O3-(D-mannose-1-phosphoryl)-L-serine + O3-L-serine alpha-D-mannopyranose 1-phosphodiester + PSI-MOD + PhosphoHex + phosphoglycosyl-D-mannose-1-phosphoryl + MOD:00302 + O-(phosphoglycosyl-D-mannose-1-phosphoryl)-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-(phosphoglycosyl-D-mannose-1-phosphoryl)-L-serine. + PubMed:10037765 + PubMed:15649890 + RESID:AA0297 + Unimod:429 + + + + + CARBOHYD O-linked (Man1P) serine + + + + + + O-(D-mannose-1-phosphoryl)-L-serine + + + + + + O-(alpha-D-mannosyl-1-phosphoryl)-L-serine + + + + + + O-[alpha-D-mannopyranosyloxy(hydroxy)phosphoryl]-L-serine + + + + + + O3-(D-mannose-1-phosphoryl)-L-serine + + + + + + O3-L-serine alpha-D-mannopyranose 1-phosphodiester + + + + + + PhosphoHex + + + + + + phosphoglycosyl-D-mannose-1-phosphoryl + + + + + + + + + + + + A protein modification that effectively converts seven L-histidinine residues and a four-copper one-sulfur one-hydroxide cluster to heptakis-L-histidino tetracopper mu4-sulfide hydroxide. + 296.19 + C 0 Cu 4 H -6 N 0 O 1 S 1 + 293.63843 + C 42 Cu 4 H 43 N 21 O 8 S 1 + 1256.19 + 1253.0508 + H, H, H, H, H, H, H + natural + heptakis-L-histidino tetracopper mu4-sulfide hydroxide + mu4-sulfido bis(bis-N1'-histidino copper)(N1'-histidino-N3'-histidino copper)(N3'-histidino hydroxide copper) + nitrous oxide reductase nosZ CuZ cluster + pentakis-L-N1'-histidino-bis-L-N3'-histidino tetracopper sulfide hydroxide + PSI-MOD + MOD:00303 + Cross-link 7. + heptakis-L-histidino tetracopper mu4-sulfide hydroxide + + + + + A protein modification that effectively converts seven L-histidinine residues and a four-copper one-sulfur one-hydroxide cluster to heptakis-L-histidino tetracopper mu4-sulfide hydroxide. + PubMed:11024061 + PubMed:11041839 + RESID:AA0298 + + + + + heptakis-L-histidino tetracopper mu4-sulfide hydroxide + + + + + + mu4-sulfido bis(bis-N1'-histidino copper)(N1'-histidino-N3'-histidino copper)(N3'-histidino hydroxide copper) + + + + + + nitrous oxide reductase nosZ CuZ cluster + + + + + + pentakis-L-N1'-histidino-bis-L-N3'-histidino tetracopper sulfide hydroxide + + + + + + + + + + + + A protein modification that effectively converts an L-leucine residue to L-leucine methyl ester. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 7 H 14 N 1 O 2 + 144.19 + 144.10245 + L + natural + C-term + Unimod:34 + uniprot.ptm:PTM-0167 + 2-amino-4-methylpentanoic methyl ester + L-leucine methyl ester + MOD_RES Leucine methyl ester + OMeLeu + alpha-aminoisocaproic methyl ester + methyl (2S)-2-amino-4-methylpentanoate + methyl L-leucinate + methyl esterified L-leucine + PSI-MOD + Methyl + Methylation + MOD:00304 + + incidental to RESID:AA0039 + L-leucine methyl ester + + + + + A protein modification that effectively converts an L-leucine residue to L-leucine methyl ester. + PubMed:10191253 + PubMed:11875433 + PubMed:8206937 + RESID:AA0299 + Unimod:34#C-term + + + + + 2-amino-4-methylpentanoic methyl ester + + + + + + L-leucine methyl ester + + + + + + MOD_RES Leucine methyl ester + + + + + + OMeLeu + + + + + + alpha-aminoisocaproic methyl ester + + + + + + methyl (2S)-2-amino-4-methylpentanoate + + + + + + methyl L-leucinate + + + + + + methyl esterified L-leucine + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + + A protein modification that effectively converts six L-cysteine residues, an L-serine residue and a eight-iron seven-sulfur cluster to hexakis-L-cysteinyl L-serinyl octairon heptasulfide. + 663.12 + C 0 Fe 8 H -8 N 0 O 0 S 7 + 663.223 + 3- + C 21 Fe 8 H 27 N 7 O 8 S 13 + 1369.03 + 1368.3102 + C, C, C, C, C, C, S + natural + Cys6Ser-[8Fe7S] + METAL Iron-sulfur (8Fe-7S) + hexakis-L-cysteinyl L-serinyl octairon heptasulfide + nitrogenase P-cluster + PSI-MOD + MOD:00305 + Cross-link 7; incidental to RESID:AA0141. + hexakis-L-cysteinyl L-serinyl octairon heptasulfide + + + + + A protein modification that effectively converts six L-cysteine residues, an L-serine residue and a eight-iron seven-sulfur cluster to hexakis-L-cysteinyl L-serinyl octairon heptasulfide. + PubMed:10525412 + PubMed:12215645 + PubMed:9063865 + RESID:AA0300 + + + + + Cys6Ser-[8Fe7S] + + + + + + METAL Iron-sulfur (8Fe-7S) + + + + + + hexakis-L-cysteinyl L-serinyl octairon heptasulfide + + + + + + nitrogenase P-cluster + + + + + + + + + + + Natural or modified residues with a mass of 113.084064 Da. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 6 H 11 N 1 O 1 + 113.16 + 113.08406 + X + L-isoleucine or L-leucine + Xle + PSI-MOD + MOD:00306 + + residues isobaric at 113.084064 Da + + + + + Natural or modified residues with a mass of 113.084064 Da. + PubMed:10523135 + RESID:AA0301 + + + + + L-isoleucine or L-leucine + + + + + + Xle + + + + + + + + + + + + A protein modification that effectively cyclizes an L-asparagine residue to form a carboxyl-terminal L-aspartimide. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 4 H 5 N 2 O 2 + 113.1 + 113.0351 + N + natural + C-term + Unimod:23 + (3S)-3-amino-2,5-pyrrolidinedione + 2-amino-butanimide + ASI + L-2-aminosuccinimide + L-asparaginimide + L-aspartimide + Succinimide formation from asparagine + alpha-aminosuccinimide + PSI-MOD + Dehydrated + Dehydration + L-3-aminosuccinimide + MOD:00307 + From DeltaMass: Average Mass: -17 Average Mass Change:-17 References:Clarke, S., Lability of Aspargine and Aspartic Acid Residues in Protein and Peptides, in: Stability of Protein Pharmaceuticals : Chemical and Physical Paths of Protein Degradation, Part A (T.J. Ahern and M.C. Manning, eds.), 1992,Plenum Press, New York, pp.1-29Xie, M.; Vander Velde, D.; Morton, M.; Borchardt, R.T.; Schowen,R.L.: pH-Induced Change in the Rate-Determining Step for the Hydrolysis of the Asp/Asn-Derived Cyclic-Imide Intermediate in Protein Degradation. (1996) J. Am. Chem. Soc. 118: 8955-8956. + L-aspartimide + + + + + A protein modification that effectively cyclizes an L-asparagine residue to form a carboxyl-terminal L-aspartimide. + DeltaMass:18 + PubMed:12771378 + PubMed:2378679 + PubMed:7662664 + PubMed:7988548 + PubMed:9309583 + RESID:AA0302 + Unimod:23#N + + + + + (3S)-3-amino-2,5-pyrrolidinedione + + + + + + 2-amino-butanimide + + + + + + ASI + + + + + + L-2-aminosuccinimide + + + + + + L-asparaginimide + + + + + + L-aspartimide + + + + + + Succinimide formation from asparagine + + + + + + alpha-aminosuccinimide + + + + + + Dehydrated + + + + + + Dehydration + + + + + + L-3-aminosuccinimide + + + + + + + + + + + + A protein modification that effectively cyclizes an L-glutamine residue to form a carboxyl-terminal L-glutamimide. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 5 H 7 N 2 O 2 + 127.12 + 127.05075 + Q + hypothetical + C-term + Unimod:23 + (3S)-3-aminopiperidine-2,6-dione + 2-aminopentanimide + 3-amino-2,6-piperidinedione + L-glutamimide + alpha-aminoglutarimide + PSI-MOD + Dehydrated + Dehydration + MOD:00308 + L-glutamimide + + + + + A protein modification that effectively cyclizes an L-glutamine residue to form a carboxyl-terminal L-glutamimide. + PubMed:12771378 + PubMed:14593103 + RESID:AA0303 + Unimod:23#Q + + + + + (3S)-3-aminopiperidine-2,6-dione + + + + + + 2-aminopentanimide + + + + + + 3-amino-2,6-piperidinedione + + + + + + L-glutamimide + + + + + + alpha-aminoglutarimide + + + + + + Dehydrated + + + + + + Dehydration + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-beta-carboxyaspartic acid. + 44.01 + C 1 H 0 N 0 O 2 + 43.98983 + C 5 H 5 N 1 O 5 + 159.1 + 159.01677 + D + hypothetical + Unimod:299 + (2S)-2-aminoethane-1,1,2-tricarboxylic acid + 2-amino-3-carboxybutanedioic acid + 3-carboxy-L-aspartic acid + 3-carboxyaspartic acid + 3CbxAsp + beta-carboxyaspartic acid + gammacarboxyld + PSI-MOD + Carboxy + Carboxylation + MOD:00309 + References to this modification as a gamma-carboxylation are in error [JSG]. + L-beta-carboxyaspartic acid + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-beta-carboxyaspartic acid. + OMSSA:47 + PubMed:6390094 + PubMed:7138832 + PubMed:7457858 + PubMed:8135347 + RESID:AA0304 + Unimod:299#D + + + + + (2S)-2-aminoethane-1,1,2-tricarboxylic acid + + + + + + 2-amino-3-carboxybutanedioic acid + + + + + + 3-carboxy-L-aspartic acid + + + + + + 3-carboxyaspartic acid + + + + + + 3CbxAsp + + + + + + beta-carboxyaspartic acid + + + + + + gammacarboxyld + + + + + + Carboxy + + + + + + Carboxy + + + + + + Carboxylation + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to N5-methyl-L-arginine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 7 H 14 N 4 O 1 + 170.22 + 170.11676 + R + hypothetical + uniprot.ptm:PTM-0185 + (2S)-2-amino-5-(N-methylcarbamimidamido)pentanoic acid + MOD_RES N5-methylarginine + N5-carbamimidoyl-N5-methyl-L-ornithine + N5-methyl-L-arginine + N5-methylated L-arginine + N5Me1Arg + delta-N-methylarginine + PSI-MOD + Methyl + Methylation + MOD:00310 + N5-methyl-L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to N5-methyl-L-arginine. + PubMed:11875433 + PubMed:9792625 + PubMed:9873020 + RESID:AA0305 + + + + + (2S)-2-amino-5-(N-methylcarbamimidamido)pentanoic acid + + + + + + MOD_RES N5-methylarginine + + + + + + N5-carbamimidoyl-N5-methyl-L-ornithine + + + + + + N5-methyl-L-arginine + + + + + + N5-methylated L-arginine + + + + + + N5Me1Arg + + + + + + delta-N-methylarginine + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteine coenzyme A disulfide. + 765.52 + C 21 H 34 N 7 O 16 P 3 S 1 + 765.09955 + C 24 H 39 N 8 O 17 P 3 S 2 + 868.66 + 868.10876 + C + hypothetical + Unimod:281 + (2R)-2-amino-3-(2-((3-(((2R)-2,4-dihydroxy-3,3-dimethyl-1-oxobutyl)amino)-1-oxopropyl)amino)ethyl)dithio-propanoic acid 4'-ester with adenosine 5'-(trihydrogen diphosphate) 3'-(dihydrogen phosphate) + L-cysteine coenzyme A disulfide + SCoACys + coenzyme A L-cysteine mixed disulfide + PSI-MOD + CoenzymeA + Cysteine modified Coenzyme A + MOD:00311 + DeltaMass gives no formula with mass as 454. + L-cysteine coenzyme A disulfide + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteine coenzyme A disulfide. + DeltaMass:0 + PubMed:1734967 + RESID:AA0306 + Unimod:281#C + + + + + (2R)-2-amino-3-(2-((3-(((2R)-2,4-dihydroxy-3,3-dimethyl-1-oxobutyl)amino)-1-oxopropyl)amino)ethyl)dithio-propanoic acid 4'-ester with adenosine 5'-(trihydrogen diphosphate) 3'-(dihydrogen phosphate) + + + + + + L-cysteine coenzyme A disulfide + + + + + + SCoACys + + + + + + coenzyme A L-cysteine mixed disulfide + + + + + + CoenzymeA + + + + + + Cysteine modified Coenzyme A + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-myristoyl-L-cysteine. + 210.36 + C 14 H 26 N 0 O 1 S 0 + 210.19836 + C 17 H 31 N 1 O 2 S 1 + 313.5 + 313.20755 + C + hypothetical + Unimod:45 + (R)-2-amino-3-(tetradecanoylsulfanyl)propanoic acid + LIPID S-myristoyl cysteine + S-(C14:1 aliphatic acyl)cysteine + S-myristoyl-L-cysteine + S-myristoylated L-cysteine + SMyrCys + tetradecanoate cysteine thioester + PSI-MOD + Myristoyl + Myristoylation + MOD:00312 + S-myristoyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-myristoyl-L-cysteine. + PubMed:10026218 + PubMed:10080938 + PubMed:8824274 + RESID:AA0307 + Unimod:45#C + + + + + (R)-2-amino-3-(tetradecanoylsulfanyl)propanoic acid + + + + + + LIPID S-myristoyl cysteine + + + + + + S-(C14:1 aliphatic acyl)cysteine + + + + + + S-myristoyl-L-cysteine + + + + + + S-myristoylated L-cysteine + + + + + + SMyrCys + + + + + + tetradecanoate cysteine thioester + + + + + + Myristoyl + + + + + + Myristoylation + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-palmitoleyl-L-cysteine. + 236.4 + C 16 H 28 N 0 O 1 S 0 + 236.21402 + C 19 H 33 N 1 O 2 S 1 + 339.54 + 339.2232 + C + hypothetical + Unimod:431 + uniprot.ptm:PTM-0645 + (R)-2-amino-3-((Z)-9-hexadecenoylsulfanyl)propanoic acid + S-palmitoleyl-L-cysteine + S-palmitoleylated L-cysteine + SPamD1Cys + cis-9-hexadecenoate cysteine thioester + mod187 + PSI-MOD + Palmitoleyl + palmitoleyl + MOD:00313 + S-palmitoleyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-palmitoleyl-L-cysteine. + OMSSA:187 + PubMed:8294460 + RESID:AA0308 + Unimod:431#C + + + + + (R)-2-amino-3-((Z)-9-hexadecenoylsulfanyl)propanoic acid + + + + + + S-palmitoleyl-L-cysteine + + + + + + S-palmitoleylated L-cysteine + + + + + + SPamD1Cys + + + + + + cis-9-hexadecenoate cysteine thioester + + + + + + mod187 + + + + + + Palmitoleyl + + + + + + palmitoleyl + + + + + + + + + + + A protein modification that effectively converts a glycine residue to glycine cholesterol ester. + 368.65 + C 27 H 44 N 0 O 0 + 368.3443 + C 29 H 48 N 1 O 2 + 442.71 + 442.3685 + G + natural + C-term + Unimod:432 + uniprot.ptm:PTM-0090 + LIPID Cholesterol glycine ester + cholesteryl glycinate + glycine cholest-5-en-3beta-ol ester + glycine cholesterol ester + hedgehog lipophilic adduct + PSI-MOD + C-cholesterol + cholesterol ester + MOD:00314 + + Incidental to RESID:AA0060. Unimod origin corrected [JSG]. + glycine cholesterol ester + + + + + A protein modification that effectively converts a glycine residue to glycine cholesterol ester. + ChEBI:143135 + PubMed:11111088 + PubMed:8824192 + RESID:AA0309 + Unimod:432#C-term + + + + + LIPID Cholesterol glycine ester + + + + + + cholesteryl glycinate + + + + + + glycine cholest-5-en-3beta-ol ester + + + + + + glycine cholesterol ester + + + + + + hedgehog lipophilic adduct + + + + + + C-cholesterol + + + + + + cholesterol ester + + + + + + + + + + + + + A protein modification that effectively converts five L-cysteine residues, an L-histidine residue and a one-nickel four-iron five-sulfur cluster to pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide. + 436.33 + C 0 Fe 4 H -6 N 0 Ni 1 O 0 S 5 + 435.4885 + C 21 Fe 4 H 26 N 8 Ni 1 O 6 S 10 + 1089.16 + 1087.5934 + C, C, C, C, C, H + natural + METAL Nickel-iron-sulfur (Ni-4Fe-5S) + METAL Nickel-iron-sulfur (Ni-4Fe-5S); via tele nitrogen + Ni-4Fe-5S cluster + carbon monoxide dehydrogenase nickel-iron cofactor + mu-1:2kappaS-sulfido-mu3-1:3:5kappaS-sulfido-mu3-2:3:4kappaS-sulfido-mu3-2:4:5kappaS-sulfido-mu3-3:4:5kappaS-sulfido-N1'-histidino-S-cysteinyl-1-iron-S-cysteinyl-2-nickel-3,4,5-tris-(S-cysteinyl iron) + pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide + PSI-MOD + MOD:00315 + Cross-link 6. + pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide + + + + + A protein modification that effectively converts five L-cysteine residues, an L-histidine residue and a one-nickel four-iron five-sulfur cluster to pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide. + PubMed:11509720 + PubMed:2550436 + RESID:AA0310 + + + + + METAL Nickel-iron-sulfur (Ni-4Fe-5S) + + + + + + METAL Nickel-iron-sulfur (Ni-4Fe-5S); via tele nitrogen + + + + + + Ni-4Fe-5S cluster + + + + + + carbon monoxide dehydrogenase nickel-iron cofactor + + + + + + mu-1:2kappaS-sulfido-mu3-1:3:5kappaS-sulfido-mu3-2:3:4kappaS-sulfido-mu3-2:4:5kappaS-sulfido-mu3-3:4:5kappaS-sulfido-N1'-histidino-S-cysteinyl-1-iron-S-cysteinyl-2-nickel-3,4,5-tris-(S-cysteinyl iron) + + + + + + pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide + + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to N4,N4-dimethyl-L-asparagine. + 28.05 + C 2 H 4 N 0 O 0 + 28.0313 + C 6 H 10 N 2 O 2 + 142.16 + 142.07423 + N + hypothetical + Unimod:36 + uniprot.ptm:PTM-0182 + (2S)-2-amino-4-(dimethylamino)-4-oxobutanoic acid + 2-amino-N4,N4-dimethylbutanediamic acid + MOD_RES N4,N4-dimethylasparagine + N(gamma),N(gamma)-dimethylasparagine + N4,N4-dimethyl-L-asparagine + N4,N4-dimethylated L-asparagine + N4Me2Asn + PSI-MOD + Dimethyl + beta-dimethylasparagine + di-Methylation + MOD:00316 + N4,N4-dimethyl-L-asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to N4,N4-dimethyl-L-asparagine. + PubMed:12964758 + PubMed:14570711 + PubMed:8783012 + RESID:AA0311 + Unimod:36#N + + + + + (2S)-2-amino-4-(dimethylamino)-4-oxobutanoic acid + + + + + + 2-amino-N4,N4-dimethylbutanediamic acid + + + + + + MOD_RES N4,N4-dimethylasparagine + + + + + + N(gamma),N(gamma)-dimethylasparagine + + + + + + N4,N4-dimethyl-L-asparagine + + + + + + N4,N4-dimethylated L-asparagine + + + + + + N4Me2Asn + + + + + + Dimethyl + + + + + + beta-dimethylasparagine + + + + + + di-Methylation + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-3,4-didehydroretinylidene-L-lysine. + 264.41 + C 20 H 24 N 0 O 0 + 264.1878 + C 26 H 36 N 2 O 1 + 392.59 + 392.28278 + K + natural + Unimod:433 + (S)-2-amino-6-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohexa-1,3-dien-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid + N6-(3,4-didehydroretinylidene)-L-lysine + N6-3-dehydroretinal-L-lysine + N6-3-dehydroretinyl-lysine + PSI-MOD + 3,4-didehydroretinylidene + Didehydroretinylidene + MOD:00317 + N6-3,4-didehydroretinylidene-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-3,4-didehydroretinylidene-L-lysine. + PubMed:10717661 + PubMed:3257009 + PubMed:4056688 + RESID:AA0312 + Unimod:433#K + + + + + (S)-2-amino-6-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohexa-1,3-dien-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid + + + + + + N6-(3,4-didehydroretinylidene)-L-lysine + + + + + + N6-3-dehydroretinal-L-lysine + + + + + + N6-3-dehydroretinyl-lysine + + + + + + 3,4-didehydroretinylidene + + + + + + Didehydroretinylidene + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-tryptophan residue by a thioether bond to form 4'-(S-L-cysteinyl)-L-tryptophyl quinone. + 27.97 + C 0 H -4 N 0 O 2 S 0 + 27.958529 + C 14 H 11 N 3 O 4 S 1 + 317.32 + 317.04703 + C, W + natural + uniprot.ptm:PTM-0041 + (2R)-2-amino-3-[(3-[(2S)-2-amino-2-carboxyethyl]-6,7-dioxo-6,7-dihydro-1H-indol-4-yl)sulfanyl]propanoic acid + 3-(2-amino-2-carboxyethyl)-4-[2-amino-2-carboxyethyl]sulfanyl-6,7-indolinedione + 4'-(L-cystein-S-yl)-L-tryptophyl quinone + 4-(S-cysteinyl)tryptophan-6,7-dione + CROSSLNK 4'-cysteinyl-tryptophylquinone (Cys-Trp) + CTQ + cysteine tryptophylquinone + PSI-MOD + MOD:00318 + Cross-link 2; secondary to RESID:AA0148. + 4'-(S-L-cysteinyl)-L-tryptophyl quinone + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-tryptophan residue by a thioether bond to form 4'-(S-L-cysteinyl)-L-tryptophyl quinone. + PubMed:11555656 + PubMed:11717396 + RESID:AA0313 + + + + + (2R)-2-amino-3-[(3-[(2S)-2-amino-2-carboxyethyl]-6,7-dioxo-6,7-dihydro-1H-indol-4-yl)sulfanyl]propanoic acid + + + + + + 3-(2-amino-2-carboxyethyl)-4-[2-amino-2-carboxyethyl]sulfanyl-6,7-indolinedione + + + + + + 4'-(L-cystein-S-yl)-L-tryptophyl quinone + + + + + + 4-(S-cysteinyl)tryptophan-6,7-dione + + + + + + CROSSLNK 4'-cysteinyl-tryptophylquinone (Cys-Trp) + + + + + + CTQ + + + + + + cysteine tryptophylquinone + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-aspartic acid residue by a thioether bond to form 2-(S-L-cysteinyl)-L-aspartic acid. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 7 H 8 N 2 O 4 S 1 + 216.21 + 216.02048 + C, D + natural + uniprot.ptm:PTM-0025 + (2R,3S)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)butanedioic acid + (2R,3S,6R)-2,6-diamino-3-carboxy-4-thiaheptanedioic acid + 3-(L-cystein-S-yl)-L-aspartic acid + 3-carboxy-L-lanthionine + CROSSLNK 3-cysteinyl-aspartic acid (Cys-Asp) + PSI-MOD + MOD:00319 + Cross-link 2. + 3-(S-L-cysteinyl)-L-aspartic acid + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-aspartic acid residue by a thioether bond to form 2-(S-L-cysteinyl)-L-aspartic acid. + PubMed:11555656 + PubMed:11717396 + RESID:AA0314 + + + + + (2R,3S)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)butanedioic acid + + + + + + (2R,3S,6R)-2,6-diamino-3-carboxy-4-thiaheptanedioic acid + + + + + + 3-(L-cystein-S-yl)-L-aspartic acid + + + + + + 3-carboxy-L-lanthionine + + + + + + CROSSLNK 3-cysteinyl-aspartic acid (Cys-Asp) + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-glutamic acid residue by a thioether bond to form 4-(S-L-cysteinyl)-L-glutamic acid. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 8 H 10 N 2 O 4 S 1 + 230.24 + 230.03613 + C, E + natural + uniprot.ptm:PTM-0040 + (2S,3S,7R)-2,7-diamino-4-carboxy-5-thiaoctanedioic acid + (2S,4S)-2-amino-4-[(R)-2-amino-2-carboxyethyl]sulfanylpentanedioic acid + 4-(L-cystein-S-yl)-L-glutamic acid + CROSSLNK 4-cysteinyl-glutamic acid (Cys-Glu) + PSI-MOD + MOD:00320 + Cross-link 2. + 4-(S-L-cysteinyl)-L-glutamic acid + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-glutamic acid residue by a thioether bond to form 4-(S-L-cysteinyl)-L-glutamic acid. + ChEBI:20293 + PubMed:11555656 + PubMed:11717396 + RESID:AA0315 + + + + + (2S,3S,7R)-2,7-diamino-4-carboxy-5-thiaoctanedioic acid + + + + + + (2S,4S)-2-amino-4-[(R)-2-amino-2-carboxyethyl]sulfanylpentanedioic acid + + + + + + 4-(L-cystein-S-yl)-L-glutamic acid + + + + + + CROSSLNK 4-cysteinyl-glutamic acid (Cys-Glu) + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester. + 294.39 + C 17 H 26 N 0 O 4 + 294.1831 + C 21 H 31 N 1 O 7 + 409.48 + 409.21005 + D + natural + Unimod:434 + uniprot.ptm:PTM-0091 + (7Z,14Xi)-14-[(S)-3-amino-3-carboxy-propanoyl]oxy-10,13-dioxo-7-heptadecenoic acid + LIPID Cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid aspartate ester + barley lipid transfer protein modification + cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester + PSI-MOD + CHDH + cis-14-hydroxy-10,13-dioxo-7-heptadecenoic ester + MOD:00321 + cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester + + + + + A protein modification that effectively converts an L-aspartic acid residue to cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester. + PubMed:11435437 + PubMed:7949339 + RESID:AA0316 + Unimod:434#D + + + + + (7Z,14Xi)-14-[(S)-3-amino-3-carboxy-propanoyl]oxy-10,13-dioxo-7-heptadecenoic acid + + + + + + LIPID Cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid aspartate ester + + + + + + barley lipid transfer protein modification + + + + + + cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester + + + + + + CHDH + + + + + + cis-14-hydroxy-10,13-dioxo-7-heptadecenoic ester + + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to tele-methyl-L-histidine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 7 H 9 N 3 O 1 + 151.17 + 151.07455 + H + natural + uniprot.ptm:PTM-0290 + (S)-2-amino-3-(1-methyl-1H-imidazol-4-yl)propanoic acid + 1'-methyl-L-histidine + MOD_RES Tele-methylhistidine + N(epsilon)-methylhistidine + N(tau)-methylhistidine + NteleMeHis + tele-methylated L-histidine + tele-methylhistidine + PSI-MOD + 3-methylhistidine + 4-methyl-histidine + Methyl + Methylation + MOD:00322 + + 1'-methyl-L-histidine + + + + + A protein modification that effectively converts an L-histidine residue to tele-methyl-L-histidine. + PubMed:10601317 + PubMed:11474090 + PubMed:11875433 + PubMed:6692818 + PubMed:8076 + PubMed:8645219 + RESID:AA0317 + + + + + (S)-2-amino-3-(1-methyl-1H-imidazol-4-yl)propanoic acid + + + + + + 1'-methyl-L-histidine + + + + + + MOD_RES Tele-methylhistidine + + + + + + N(epsilon)-methylhistidine + + + + + + N(tau)-methylhistidine + + + + + + NteleMeHis + + + + + + tele-methylated L-histidine + + + + + + tele-methylhistidine + + + + + + 3-methylhistidine + + + + + + 4-methyl-histidine + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to L-lysine methyl ester. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 7 H 15 N 2 O 2 + 159.21 + 159.11336 + K + natural + C-term + Unimod:34 + uniprot.ptm:PTM-0170 + 2,6-diaminohexanoic methyl ester + L-lysine methyl ester + MOD_RES Lysine methyl ester + OMeLys + alpha,epsilon-diaminocaproic methyl ester + methyl (S)-2,6-diaminohexanoate + methyl L-lysinate + methyl esterified L-lysine + PSI-MOD + Methyl + Methylation + MOD:00323 + + L-lysine methyl ester + + + + + A protein modification that effectively converts an L-lysine residue to L-lysine methyl ester. + PubMed:10973948 + PubMed:11875433 + RESID:AA0318 + Unimod:34#C-term + + + + + 2,6-diaminohexanoic methyl ester + + + + + + L-lysine methyl ester + + + + + + MOD_RES Lysine methyl ester + + + + + + OMeLys + + + + + + alpha,epsilon-diaminocaproic methyl ester + + + + + + methyl (S)-2,6-diaminohexanoate + + + + + + methyl L-lysinate + + + + + + methyl esterified L-lysine + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to L-serinyl molybdenum bis(molybdopterin guanine dinucleotide). + 1588.01 + C 40 H 47 Mo 1 N 20 O 27 P 4 S 4 + 1588.9807 + C 43 H 52 Mo 1 N 21 O 29 P 4 S 4 + 1675.09 + 1676.0127 + S + natural + 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide + L-serinyl molybdenum bis(molybdopterin guanine dinucleotide) + bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-O3-serinyl-molybdenum oxide + PSI-MOD + MOD:00324 + L-serinyl molybdenum bis(molybdopterin guanine dinucleotide) + + + + + A protein modification that effectively converts an L-serine residue to L-serinyl molybdenum bis(molybdopterin guanine dinucleotide). + PubMed:8658132 + PubMed:8658134 + RESID:AA0319 + + + + + 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide + + + + + + L-serinyl molybdenum bis(molybdopterin guanine dinucleotide) + + + + + + bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-O3-serinyl-molybdenum oxide + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to L-beta-methylthioasparagine. + 46.09 + C 1 H 2 N 0 O 0 S 1 + 45.98772 + C 5 H 8 N 2 O 2 S 1 + 160.19 + 160.03065 + N + hypothetical + Unimod:39 + (2R,3Xi)-2-amino-3-(methylsulfanyl)-4-butanediamic acid + 2,4-diamino-3-(methylsulfanyl)-4-oxobutanoic acid + 3-(methylthio)-L-asparagine + 3-carboxamido-S-methyl-cysteine + beta-(methylthio)asparagine + PSI-MOD + Beta-methylthiolation + Methylthio + MOD:00325 + This modification was predicted for ribosomal protein S12 in Bacillus subtilis when the sequence in the original version of the genome was reported to have asparagine rather than aspartic acid at the position of the methylthioaspartic acid modification (see MOD:00237). Two groups independently confirmed that the genome sequence was incorrect. The sequence in the revised genome has aspartic acid at that position. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. + L-beta-methylthioasparagine + + + + + A protein modification that effectively converts an L-asparagine residue to L-beta-methylthioasparagine. + RESID:AA0320 + Unimod:39#N + + + + + (2R,3Xi)-2-amino-3-(methylsulfanyl)-4-butanediamic acid + + + + + + 2,4-diamino-3-(methylsulfanyl)-4-oxobutanoic acid + + + + + + 3-(methylthio)-L-asparagine + + + + + + 3-carboxamido-S-methyl-cysteine + + + + + + beta-(methylthio)asparagine + + + + + + Beta-methylthiolation + + + + + + Methylthio + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to L-pyrrolysine (not known as a natural, post-translational modification process). + 109.13 + C 6 H 7 N 1 O 1 + 109.052765 + C 12 H 19 N 3 O 2 + 237.3 + 237.14772 + K + artifact + Unimod:435 + (2S)-2-amino-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]aminohexanoic acid + 2-azanyl-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]azanylhexanoic acid + L-pyrrolysine + N6-(4-methyl-1,2-didehydropyrrolidine-5-carboxyl)-L-lysine + N6-(4-methyl-delta-1-pyrroline-5-carboxyl)-L-lysine + N6-([(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-yl]carbonyl)-L-lysine + NON_STD Pyrrolysine + Pyl(Lys) + monomethylamine methyltransferase cofactor lysine adduct + PSI-MOD + MOD:00326 + This entry is for the artifactual formation of L-pyrrolysine from lysine. For encoded L-pyrrolysine, use MOD:01187 [JSG]. + L-pyrrolysine (Lys) + + + + + A protein modification that effectively converts an L-lysine residue to L-pyrrolysine (not known as a natural, post-translational modification process). + PubMed:11435424 + PubMed:12029131 + PubMed:12029132 + PubMed:15314242 + PubMed:16096277 + RESID:AA0321#LYS + Unimod:435#K + + + + + (2S)-2-amino-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]aminohexanoic acid + + + + + + 2-azanyl-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]azanylhexanoic acid + + + + + + L-pyrrolysine + + + + + + N6-(4-methyl-1,2-didehydropyrrolidine-5-carboxyl)-L-lysine + + + + + + N6-(4-methyl-delta-1-pyrroline-5-carboxyl)-L-lysine + + + + + + N6-([(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-yl]carbonyl)-L-lysine + + + + + + NON_STD Pyrrolysine + + + + + + Pyl(Lys) + + + + + + monomethylamine methyltransferase cofactor lysine adduct + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to a 3-hydroxy-L-tryptophan. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 11 H 10 N 2 O 2 + 202.21 + 202.07423 + W + hypothetical + uniprot.ptm:PTM-0031 + (2S,3S)-2-amino-3-hydroxy-3-(1H-indol-3-yl)propanoic acid + 3-hydroxy-L-tryptophan + 3-hydroxylated L-tryptophan + 3-hydroxytryptophan + 3HyTrp + MOD_RES 3-hydroxytryptophan + beta-hydroxytryptophan + PSI-MOD + MOD:00327 + 3-hydroxy-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to a 3-hydroxy-L-tryptophan. + ChEBI:141794 + PubMed:10024453 + PubMed:11457355 + RESID:AA0322 + + + + + (2S,3S)-2-amino-3-hydroxy-3-(1H-indol-3-yl)propanoic acid + + + + + + 3-hydroxy-L-tryptophan + + + + + + 3-hydroxylated L-tryptophan + + + + + + 3-hydroxytryptophan + + + + + + 3HyTrp + + + + + + MOD_RES 3-hydroxytryptophan + + + + + + beta-hydroxytryptophan + + + + + + + + + + + A protein modification that effectively crosslinks an L-tyrosine residue and the 3'-end of DNA through a phosphodiester bond to form O4'-(phospho-3'-DNA)-L-tyrosine. + Y + natural + (S)-2-amino-3-[4-(3'-deoxyribonucleic acid phosphonoxy)phenyl]propanoic acid + ACT_SITE O-(3'-phospho-DNA)-tyrosine intermediate + O4'-(phospho-3'-DNA)-L-tyrosine + O4'-L-tyrosine 3'-DNA phosphodiester + PSI-MOD + MOD:00328 + O4'-(phospho-3'-DNA)-L-tyrosine + + + + + A protein modification that effectively crosslinks an L-tyrosine residue and the 3'-end of DNA through a phosphodiester bond to form O4'-(phospho-3'-DNA)-L-tyrosine. + PubMed:2211714 + RESID:AA0323 + + + + + (S)-2-amino-3-[4-(3'-deoxyribonucleic acid phosphonoxy)phenyl]propanoic acid + + + + + + ACT_SITE O-(3'-phospho-DNA)-tyrosine intermediate + + + + + + O4'-(phospho-3'-DNA)-L-tyrosine + + + + + + O4'-L-tyrosine 3'-DNA phosphodiester + + + + + + + + + + + A protein modification that effectively results from forming an adduct between a glutamic acid residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + 614.48 + C 34 Fe 1 H 30 N 4 O 4 + 614.1616 + C 39 Fe 1 H 37 N 5 O 7 + 743.6 + 743.2042 + E + natural + Unimod:436 + 5-hydroxymethyl protoporphyrin IX 5-glutamate ester + BINDING Heme (covalent; via 1 link) + [3-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-7,12-diethenyl-8,13,17-trimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate + cytochrome P450 CYP4A family heme cofactor + hydroxyheme-L-glutamate ester + PSI-MOD + Hydroxyheme + hydroxyheme + MOD:00329 + hydroxyheme-L-glutamate ester + + + + + A protein modification that effectively results from forming an adduct between a glutamic acid residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + PubMed:11139583 + PubMed:11821421 + PubMed:11980497 + RESID:AA0324 + Unimod:436#E + + + + + 5-hydroxymethyl protoporphyrin IX 5-glutamate ester + + + + + + BINDING Heme (covalent; via 1 link) + + + + + + [3-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-7,12-diethenyl-8,13,17-trimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate + + + + + + cytochrome P450 CYP4A family heme cofactor + + + + + + hydroxyheme-L-glutamate ester + + + + + + Hydroxyheme + + + + + + hydroxyheme + + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to a (phospho-5'-guanosine)-L-histidine. + 345.21 + C 10 H 12 N 5 O 7 P 1 + 345.04742 + C 16 H 19 N 8 O 8 P 1 + 482.35 + 482.10635 + H + natural + Unimod:413 + (2S)-2-amino-3-(1-(5'-adenosine phosphono)imidazol-4-yl)propanoic acid + 1'-(phospho-5'-guanosine)-L-histidine + ACT_SITE GMP-histidine intermediate + L-histidine 5'-guanosine phosphoramidester + L-histidine monoanhydride with 5'-guanylic acid + N(tau)-5'-guanylic-L-histidine + N1'-guanylylated histidine + tele-5'-guanylic-L-histidine + PSI-MOD + Phosphoguanosine + phospho-guanosine + MOD:00330 + (phospho-5'-guanosine)-L-histidine + + + + + A protein modification that effectively converts an L-histidine residue to a (phospho-5'-guanosine)-L-histidine. + PubMed:10529169 + PubMed:10869342 + PubMed:7559521 + RESID:AA0325 + Unimod:413#H + + + + + (2S)-2-amino-3-(1-(5'-adenosine phosphono)imidazol-4-yl)propanoic acid + + + + + + 1'-(phospho-5'-guanosine)-L-histidine + + + + + + ACT_SITE GMP-histidine intermediate + + + + + + L-histidine 5'-guanosine phosphoramidester + + + + + + L-histidine monoanhydride with 5'-guanylic acid + + + + + + N(tau)-5'-guanylic-L-histidine + + + + + + N1'-guanylylated histidine + + + + + + tele-5'-guanylic-L-histidine + + + + + + Phosphoguanosine + + + + + + phospho-guanosine + + + + + + + + + + + A protein modification that effectively converts four L-cysteine residues and a three-iron four-sulfur cluster to tetrakis-L-cysteinyl triiron tetrasulfide. + 291.74 + C 0 Fe 3 H -4 N 0 O 0 S 4 + 291.66345 + 3- + C 12 Fe 3 H 16 N 4 O 4 S 8 + 704.3 + 703.7002 + C, C, C, C + hypothetical + bis[bis-L-cysteinyl iron disulfido]iron + di-mu-1:2kappaS-sulfido di-mu-2:3kappaS-sulfido iron bis(bis-S-cysteinyliron) + tetra-mu-sulfido tetrakis-S-L-cysteinyl triiron + tetrakis-L-cysteinyl linear [3Fe-4S] cluster + tetrakis-L-cysteinyl triiron tetrasulfide + tetrakis-L-cysteinyl triiron tetrasulfide D2 cluster + PSI-MOD + MOD:00331 + Cross-link 4. + tetrakis-L-cysteinyl triiron tetrasulfide + + + + + A protein modification that effectively converts four L-cysteine residues and a three-iron four-sulfur cluster to tetrakis-L-cysteinyl triiron tetrasulfide. + PubMed:11592901 + PubMed:11941493 + PubMed:2511202 + PubMed:6094558 + RESID:AA0326 + + + + + bis[bis-L-cysteinyl iron disulfido]iron + + + + + + di-mu-1:2kappaS-sulfido di-mu-2:3kappaS-sulfido iron bis(bis-S-cysteinyliron) + + + + + + tetra-mu-sulfido tetrakis-S-L-cysteinyl triiron + + + + + + tetrakis-L-cysteinyl linear [3Fe-4S] cluster + + + + + + tetrakis-L-cysteinyl triiron tetrasulfide + + + + + + tetrakis-L-cysteinyl triiron tetrasulfide D2 cluster + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to N4-glucosyl-arginine. + 162.14 + C 6 H 10 N 0 O 5 + 162.05283 + C 12 H 22 N 4 O 6 + 318.33 + 318.15393 + R + natural + Unimod:41 + uniprot.ptm:PTM-0515 + (2S)-2-amino-5-(beta-D-glucopyranosyl[imino(methylamino)methyl]amino)pentanoic acid + CARBOHYD N-linked (Glc) arginine + NG-beta-D-glucosylarginine + omega-N-(beta-D-glucosyl)-L-arginine + omega-N-glucosyl-L-arginine + omega-N-glycosyl-L-arginine + PSI-MOD + Hex + Hexose + MOD:00332 + omega-N-glucosyl-L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to N4-glucosyl-arginine. + PubMed:15279557 + PubMed:8521968 + PubMed:9536051 + RESID:AA0327 + Unimod:41#R + + + + + (2S)-2-amino-5-(beta-D-glucopyranosyl[imino(methylamino)methyl]amino)pentanoic acid + + + + + + CARBOHYD N-linked (Glc) arginine + + + + + + NG-beta-D-glucosylarginine + + + + + + omega-N-(beta-D-glucosyl)-L-arginine + + + + + + omega-N-glucosyl-L-arginine + + + + + + omega-N-glycosyl-L-arginine + + + + + + Hex + + + + + + Hexose + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine. + 386.3 + C 13 H 19 N 6 O 6 P 1 + 386.11038 + C 17 H 26 N 8 O 9 P 1 + 517.42 + 517.156 + N + natural + C-term + Unimod:437 + uniprot.ptm:PTM-0335 + (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine + 5'-O-[(3-aminopropoxy)(L-aspart-1-ylamino)phosphoryl]adenosine + 9-(5'-O-[(3-aminopropoxy)(L-aspart-1-ylamino)phosphoryl]-beta-D-ribofuranosyl)adenine + MOD_RES Aspartic acid 1-[(3-aminopropyl)(5'-adenosyl)phosphono]amide + N-(aspart-1-yl)-O-(3-aminopropyl)-O-(5'-adenosyl)phosphoramide + microcin C7 asparagine modification + PSI-MOD + (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5-adenosine + C-Asn-deriv + MOD:00333 + Unimod origin shown as C-term [JSG]. + (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine + + + + + A protein modification that effectively converts an L-asparagine residue to (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine. + PubMed:7559516 + PubMed:7835418 + PubMed:8183363 + RESID:AA0328 + Unimod:437#C-term + + + + + (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine + + + + + + 5'-O-[(3-aminopropoxy)(L-aspart-1-ylamino)phosphoryl]adenosine + + + + + + 9-(5'-O-[(3-aminopropoxy)(L-aspart-1-ylamino)phosphoryl]-beta-D-ribofuranosyl)adenine + + + + + + MOD_RES Aspartic acid 1-[(3-aminopropyl)(5'-adenosyl)phosphono]amide + + + + + + N-(aspart-1-yl)-O-(3-aminopropyl)-O-(5'-adenosyl)phosphoramide + + + + + + microcin C7 asparagine modification + + + + + + (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5-adenosine + + + + + + C-Asn-deriv + + + + + + + + + + + A protein modification that effectively results from forming an adduct between the tele nitrogen of a histidine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + 616.5 + C 34 Fe 1 H 32 N 4 O 4 + 616.1773 + C 40 Fe 1 H 39 N 7 O 5 + 753.64 + 753.2362 + H + hypothetical + Unimod:390 + (S)-[7-ethenyl-12-[1-((2-amino-2-carboxyethyl)-1H-imidazol-1-yl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate + 1'-heme-L-histidine + 2-[1-(N1'-histidyl)ethyl]protoporphyrin IX + BINDING Heme (covalent; via tele nitrogen) + N(epsilon)-histidyl heme + N(tau)-histidyl heme + N1'-histidyl heme + tele-histidyl heme + PSI-MOD + Heme + heme + MOD:00334 + 1'-heme-L-histidine + + + + + A protein modification that effectively results from forming an adduct between the tele nitrogen of a histidine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. + PubMed:12033922 + PubMed:12121092 + RESID:AA0329 + Unimod:390#H + + + + + (S)-[7-ethenyl-12-[1-((2-amino-2-carboxyethyl)-1H-imidazol-1-yl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate + + + + + + 1'-heme-L-histidine + + + + + + 2-[1-(N1'-histidyl)ethyl]protoporphyrin IX + + + + + + BINDING Heme (covalent; via tele nitrogen) + + + + + + N(epsilon)-histidyl heme + + + + + + N(tau)-histidyl heme + + + + + + N1'-histidyl heme + + + + + + tele-histidyl heme + + + + + + Heme + + + + + + heme + + + + + + + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form (2S,3S,2'R)-3-methyllanthionine sulfoxide. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 7 H 10 N 2 O 3 S 1 + 202.23 + 202.04121 + C, T + natural + uniprot.ptm:PTM-0069 + (2S,3S,4Xi,6R)-2,6-diamino-3-methyl-4-oxo-4-thiaheptanedioic acid + (2S,3S,SXi)-2-amino-3-([(R)-2-amino-2-carboxyethyl]sulfinyl)butanoic acid + 3-methyl-L-lanthionine S-oxide + 3-methyl-L-lanthionine sulfoxide + CROSSLNK Beta-methyllanthionine sulfoxide (Thr-Cys) + S-oxy-3-methyllanthionine + PSI-MOD + MOD:00335 + Cross-link 2. + (2S,3S,2'R)-3-methyllanthionine sulfoxide + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form (2S,3S,2'R)-3-methyllanthionine sulfoxide. + PubMed:7737178 + PubMed:9219543 + RESID:AA0330 + + + + + (2S,3S,4Xi,6R)-2,6-diamino-3-methyl-4-oxo-4-thiaheptanedioic acid + + + + + + (2S,3S,SXi)-2-amino-3-([(R)-2-amino-2-carboxyethyl]sulfinyl)butanoic acid + + + + + + 3-methyl-L-lanthionine S-oxide + + + + + + 3-methyl-L-lanthionine sulfoxide + + + + + + CROSSLNK Beta-methyllanthionine sulfoxide (Thr-Cys) + + + + + + S-oxy-3-methyllanthionine + + + + + + + + + + + + A protein modification that effectively converts three L-cysteine residues, an L-aspartic acid residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-aspartato diiron disulfide. + 171.78 + C 0 Fe 2 H -4 N 0 O 0 S 2 + 171.78381 + 2- + C 13 Fe 2 H 16 N 4 O 6 S 5 + 596.28 + 595.8383 + C, C, C, D + hypothetical + METAL Iron-sulfur (2Fe-2S) + di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-O4-aspartatoiron) + tris-L-cysteinyl L-aspartato diiron disulfide + PSI-MOD + MOD:00336 + Cross-link 4. + tris-L-cysteinyl L-aspartato diiron disulfide + + + + + A protein modification that effectively converts three L-cysteine residues, an L-aspartic acid residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-aspartato diiron disulfide. + PubMed:10968624 + PubMed:1312028 + PubMed:7947772 + RESID:AA0331 + + + + + METAL Iron-sulfur (2Fe-2S) + + + + + + di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-O4-aspartatoiron) + + + + + + tris-L-cysteinyl L-aspartato diiron disulfide + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-carbamoyl-L-cysteine. + 43.02 + C 1 H 1 N 1 O 1 S 0 + 43.005814 + C 4 H 6 N 2 O 2 S 1 + 146.16 + 146.015 + C + natural + Unimod:5 + uniprot.ptm:PTM-0649 + (R)-2-amino-3-(carbamoylsulfanyl)propanoic acid + 2-amino-3-(aminocarbonyl)sulfanylpropanoic acid + 2-amino-3-(aminocarbonyl)thiopropanoic acid + MOD_RES S-carbamoylcysteine + S-(aminocarbonyl)cysteine + S-carbamoyl-L-cysteine + S-carbamoylcysteine + S-carbamylcysteine + S-cysteinyl carbamate ester + SCbmCys + alpha-amino-beta-carbamylthiopropionic acid + beta-carbamylthioalanine + PSI-MOD + MOD:00337 + S-carbamoyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-carbamoyl-L-cysteine. + PubMed:12586941 + PubMed:240389 + RESID:AA0332 + Unimod:5#C + + + + + (R)-2-amino-3-(carbamoylsulfanyl)propanoic acid + + + + + + 2-amino-3-(aminocarbonyl)sulfanylpropanoic acid + + + + + + 2-amino-3-(aminocarbonyl)thiopropanoic acid + + + + + + MOD_RES S-carbamoylcysteine + + + + + + S-(aminocarbonyl)cysteine + + + + + + S-carbamoyl-L-cysteine + + + + + + S-carbamoylcysteine + + + + + + S-carbamylcysteine + + + + + + S-cysteinyl carbamate ester + + + + + + SCbmCys + + + + + + alpha-amino-beta-carbamylthiopropionic acid + + + + + + beta-carbamylthioalanine + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-cyano-L-cysteine. + 25.01 + C 1 H -1 N 1 O 0 S 0 + 24.995249 + C 4 H 4 N 2 O 1 S 1 + 128.15 + 128.00444 + C + natural + Unimod:438 + uniprot.ptm:PTM-0650 + (2R)-2-amino-3-thiocyanatopropanoic acid + MOD_RES S-cyanocysteine + S-cyano-L-cysteine + S-cyanocysteine + alpha-amino-beta-thiocyanatopropionic acid + beta-thiocyanatoalanine + serine thiocyanic acid ester + PSI-MOD + Cyano + cyano + MOD:00338 + S-cyano-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-cyano-L-cysteine. + PubMed:12586941 + PubMed:4808702 + RESID:AA0333 + Unimod:438#C + + + + + (2R)-2-amino-3-thiocyanatopropanoic acid + + + + + + MOD_RES S-cyanocysteine + + + + + + S-cyano-L-cysteine + + + + + + S-cyanocysteine + + + + + + alpha-amino-beta-thiocyanatopropionic acid + + + + + + beta-thiocyanatoalanine + + + + + + serine thiocyanic acid ester + + + + + + Cyano + + + + + + cyano + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteinyl hydrogenase diiron subcluster. + 342.87 + C 5 Fe 2 H -1 N 2 O 5 S 2 + 342.78693 + C 8 Fe 2 H 4 N 3 O 6 S 3 + 446.01 + 445.7961 + C + natural + Unimod:439 + 1,7-biscarbonyl-1-(cystein-S-yl)-8-oxo-4-aza-2lambda(3),6 lambda(3)-dithia-1,7-diferratricyclo[4.2.0.0(2,7)]octane-1,7-dicarbonitrile + L-cysteinyl hydrogenase diiron subcluster + METAL Diiron subcluster + mu-carbonyl-dicarbonyl-1kappaC,2kappaC-dicyanido-1kappaC,2kappaC-cysteinato-1kS-1,2-azadimethanthiol-1kS,2kS'-diiron + PSI-MOD + Diironsubcluster + hydrogenase diiron subcluster + MOD:00339 + incidental to RESID:AA0140. + L-cysteinyl hydrogenase diiron subcluster + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteinyl hydrogenase diiron subcluster. + PubMed:10694885 + PubMed:9836629 + RESID:AA0334 + Unimod:439#C + + + + + 1,7-biscarbonyl-1-(cystein-S-yl)-8-oxo-4-aza-2lambda(3),6 lambda(3)-dithia-1,7-diferratricyclo[4.2.0.0(2,7)]octane-1,7-dicarbonitrile + + + + + + L-cysteinyl hydrogenase diiron subcluster + + + + + + METAL Diiron subcluster + + + + + + mu-carbonyl-dicarbonyl-1kappaC,2kappaC-dicyanido-1kappaC,2kappaC-cysteinato-1kS-1,2-azadimethanthiol-1kS,2kS'-diiron + + + + + + Diironsubcluster + + + + + + hydrogenase diiron subcluster + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-amidino-L-cysteine. + 42.04 + C 1 H 2 N 2 O 0 S 0 + 42.021797 + C 4 H 7 N 3 O 1 S 1 + 145.18 + 145.03099 + C + natural + Unimod:440 + (2R)-2-amino-3-(carbamimidoylsulfanyl)propanoic acid + 2-amino-3-amidinosulfanylpropanoic acid + 2-amino-3-amidinothiopropanoic acid + ACT_SITE Amidino-cysteine intermediate + S-amidino-L-cysteine + S-amidinocysteine + alpha-amino-beta-amidinothiopropionic acid + beta-(S-isothiourea)alanine + beta-amidinothioalanine + PSI-MOD + Amidino + amidino + MOD:00340 + S-amidino-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-amidino-L-cysteine. + PubMed:9148748 + RESID:AA0335 + Unimod:440#C + + + + + (2R)-2-amino-3-(carbamimidoylsulfanyl)propanoic acid + + + + + + 2-amino-3-amidinosulfanylpropanoic acid + + + + + + 2-amino-3-amidinothiopropanoic acid + + + + + + ACT_SITE Amidino-cysteine intermediate + + + + + + S-amidino-L-cysteine + + + + + + S-amidinocysteine + + + + + + alpha-amino-beta-amidinothiopropionic acid + + + + + + beta-(S-isothiourea)alanine + + + + + + beta-amidinothioalanine + + + + + + Amidino + + + + + + amidino + + + + + + + + + + + A protein modification that effectively converts an L-isoleucine residue to N-methyl-L-isoleucine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 7 H 13 N 1 O 1 + 127.19 + 127.09972 + I + hypothetical + uniprot.ptm:PTM-0215 + (2S,3S)-2-methylamino-3-methylpentanoic acid + MOD_RES N-methylisoleucine + N-methyl-L-isoleucine + N-methylated L-isoleucine + N-methylisoleucine + NMe1Ile + PSI-MOD + Methyl + Methylation + MOD:00341 + Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG]. + N-methyl-L-isoleucine + + + + + A protein modification that effectively converts an L-isoleucine residue to N-methyl-L-isoleucine. + PubMed:11875433 + RESID:AA0336 + + + + + (2S,3S)-2-methylamino-3-methylpentanoic acid + + + + + + MOD_RES N-methylisoleucine + + + + + + N-methyl-L-isoleucine + + + + + + N-methylated L-isoleucine + + + + + + N-methylisoleucine + + + + + + NMe1Ile + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + A protein modification that effectively converts an L-leucine residue to N-methyl-L-leucine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 7 H 13 N 1 O 1 + 127.19 + 127.09972 + L + hypothetical + uniprot.ptm:PTM-0216 + (S)-2-methylamino-4-methylpentanoic acid + 2-(methylamino)-4-methyl-valeric acid + MOD_RES N-methylleucine + N-methyl-L-leucine + N-methylated L-leucine + N-methylleucine + NMe1Leu + PSI-MOD + Methyl + Methylation + MOD:00342 + Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG]. + N-methyl-L-leucine + + + + + A protein modification that effectively converts an L-leucine residue to N-methyl-L-leucine. + PubMed:11875433 + RESID:AA0337 + + + + + (S)-2-methylamino-4-methylpentanoic acid + + + + + + 2-(methylamino)-4-methyl-valeric acid + + + + + + MOD_RES N-methylleucine + + + + + + N-methyl-L-leucine + + + + + + N-methylated L-leucine + + + + + + N-methylleucine + + + + + + NMe1Leu + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to N-methyl-L-tyrosine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 10 H 11 N 1 O 2 + 177.2 + 177.07898 + Y + hypothetical + uniprot.ptm:PTM-0220 + (2S)-3-(4-hydroxyphenyl)-2-(methylamino)propanoic acid + MOD_RES N-methyltyrosine + N-methyl Tyrosinyl + N-methyl-L-tyrosine + N-methylated L-tyrosine + N-methyltyrosine + NMe1Tyr + PSI-MOD + Methyl + MOD:00343 + Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG]. + N-methyl-L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to N-methyl-L-tyrosine. + DeltaMass:0 + RESID:AA0338 + + + + + (2S)-3-(4-hydroxyphenyl)-2-(methylamino)propanoic acid + + + + + + MOD_RES N-methyltyrosine + + + + + + N-methyl Tyrosinyl + + + + + + N-methyl-L-tyrosine + + + + + + N-methylated L-tyrosine + + + + + + N-methyltyrosine + + + + + + NMe1Tyr + + + + + + Methyl + + + + + + + + + + + A protein modification that effectively converts a glycine residue to N-palmitoylglycine. + 238.41 + C 16 H 30 N 0 O 1 S 0 + 238.22966 + C 18 H 34 N 1 O 2 + 296.47 + 296.25894 + G + natural + N-term + uniprot.ptm:PTM-0223 + (hexadecanamido)acetic acid + (hexadecanoylamino)acetic acid + (hexadecanoylamino)ethanoic acid + LIPID N-palmitoyl glycine + N-(1-oxohexadecyl)glycine + N-hexadecanoylated glycine + N-palmitoyl-glycine + N-palmitoylated glycine + NPamGly + PSI-MOD + MOD:00344 + + incidental to RESID:AA0060 + N-palmitoylglycine + + + + + A protein modification that effectively converts a glycine residue to N-palmitoylglycine. + PubMed:12574119 + RESID:AA0339 + + + + + (hexadecanamido)acetic acid + + + + + + (hexadecanoylamino)acetic acid + + + + + + (hexadecanoylamino)ethanoic acid + + + + + + LIPID N-palmitoyl glycine + + + + + + N-(1-oxohexadecyl)glycine + + + + + + N-hexadecanoylated glycine + + + + + + N-palmitoyl-glycine + + + + + + N-palmitoylated glycine + + + + + + NPamGly + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-phenylalanine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-phenylalanine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 12 H 12 N 2 O 2 S 1 + 248.3 + 248.06195 + C, F + natural + uniprot.ptm:PTM-0012 + (2R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylpropanoic acid + (2R,5R)-2,5-diamino-3-thia-2-phenylmethylhexanedioic acid + 2-(L-cystein-S-yl)-L-phenylalanine + CROSSLNK 2-cysteinyl-L-phenylalanine (Cys-Phe) + alpha-(L-cystein-S-yl)-L-phenylalanine + PSI-MOD + MOD:00345 + Cross-link 2. + 2-(S-L-cysteinyl)-L-phenylalanine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-phenylalanine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-phenylalanine. + PubMed:12696888 + PubMed:3936839 + RESID:AA0340 + + + + + (2R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylpropanoic acid + + + + + + (2R,5R)-2,5-diamino-3-thia-2-phenylmethylhexanedioic acid + + + + + + 2-(L-cystein-S-yl)-L-phenylalanine + + + + + + CROSSLNK 2-cysteinyl-L-phenylalanine (Cys-Phe) + + + + + + alpha-(L-cystein-S-yl)-L-phenylalanine + + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-phenylalanine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-phenylalanine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 12 H 12 N 2 O 2 S 1 + 248.3 + 248.06195 + C, F + natural + uniprot.ptm:PTM-0011 + (2S)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylpropanoic acid + (2S,5R)-2,5-diamino-3-thia-2-phenylmethylhexanedioic acid + 2-(L-cystein-S-yl)-D-phenylalanine + CROSSLNK 2-cysteinyl-D-phenylalanine (Cys-Phe) + alpha-(L-cystein-S-yl)-D-phenylalanine + PSI-MOD + MOD:00346 + Cross-link 2. + 2-(S-L-cysteinyl)-D-phenylalanine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-phenylalanine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-phenylalanine. + PubMed:12696888 + PubMed:3936839 + RESID:AA0341 + + + + + (2S)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylpropanoic acid + + + + + + (2S,5R)-2,5-diamino-3-thia-2-phenylmethylhexanedioic acid + + + + + + 2-(L-cystein-S-yl)-D-phenylalanine + + + + + + CROSSLNK 2-cysteinyl-D-phenylalanine (Cys-Phe) + + + + + + alpha-(L-cystein-S-yl)-D-phenylalanine + + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-allo-threonine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 7 H 10 N 2 O 3 S 1 + 202.23 + 202.04121 + C, T + natural + uniprot.ptm:PTM-0010 + (2R,5S,6R)-2,5-diamino-5-carboxy-6-hydroxy-4-thiaheptanoic acid + (2S,3R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid + 2-(L-cystein-S-yl)-D-allo-threonine + CROSSLNK 2-cysteinyl-D-allo-threonine (Cys-Thr) + alpha-(L-cystein-S-yl)-D-allo-threonine + PSI-MOD + MOD:00347 + Cross-link 2. + 2-(S-L-cysteinyl)-D-allo-threonine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-allo-threonine. + PubMed:12696888 + PubMed:3936839 + RESID:AA0342 + + + + + (2R,5S,6R)-2,5-diamino-5-carboxy-6-hydroxy-4-thiaheptanoic acid + + + + + + (2S,3R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid + + + + + + 2-(L-cystein-S-yl)-D-allo-threonine + + + + + + CROSSLNK 2-cysteinyl-D-allo-threonine (Cys-Thr) + + + + + + alpha-(L-cystein-S-yl)-D-allo-threonine + + + + + + + + + + + A protein modification that effectively converts an L-alanine residue to N-carbamoyl-L-alanine. + 43.02 + C 1 H 1 N 1 O 1 + 43.005814 + C 4 H 7 N 2 O 2 + 115.11 + 115.05075 + A + natural + N-term + uniprot.ptm:PTM-0374 + (S)-2-(carbamoylamino)propanoic acid + 2-ureidopropanoic acid + MOD_RES N-carbamoylalanine + N-carbamoyl-L-alanine + N-carbamylalanine + N2CbmAla + PSI-MOD + MOD:00348 + N-carbamoyl-L-alanine + + + + + A protein modification that effectively converts an L-alanine residue to N-carbamoyl-L-alanine. + PubMed:12203680 + RESID:AA0343 + + + + + (S)-2-(carbamoylamino)propanoic acid + + + + + + 2-ureidopropanoic acid + + + + + + MOD_RES N-carbamoylalanine + + + + + + N-carbamoyl-L-alanine + + + + + + N-carbamylalanine + + + + + + N2CbmAla + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form 4-amino-3-isothiazolidinone-L-serine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 6 H 8 N 2 O 3 S 1 + 188.2 + 188.02556 + C, S + natural + uniprot.ptm:PTM-0037 + (2S)-2-[(4R)-4-amino-3-oxo-1,2-thiazolidin-2-yl]-3-hydroxypropanoic acid + 2-(4-amino-3-oxo-isothiazolidin-2-yl)-3-hydroxy-propanoic acid + 4-amino-3-isothiazolidinone-L-serine + CROSSLNK N,N-(cysteine-1,S-diyl)serine (Cys-Ser) + N,N-(L-cysteine-1,S-diyl)-L-serine + serine-cysteine sulfenyl amide cross-link + serine-cysteine sulphenyl amide cross-link + PSI-MOD + MOD:00349 + Cross-link 2. + 4-amino-3-isothiazolidinone-L-serine + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form 4-amino-3-isothiazolidinone-L-serine. + PubMed:12802338 + PubMed:12802339 + RESID:AA0344 + + + + + (2S)-2-[(4R)-4-amino-3-oxo-1,2-thiazolidin-2-yl]-3-hydroxypropanoic acid + + + + + + 2-(4-amino-3-oxo-isothiazolidin-2-yl)-3-hydroxy-propanoic acid + + + + + + 4-amino-3-isothiazolidinone-L-serine + + + + + + CROSSLNK N,N-(cysteine-1,S-diyl)serine (Cys-Ser) + + + + + + N,N-(L-cysteine-1,S-diyl)-L-serine + + + + + + serine-cysteine sulfenyl amide cross-link + + + + + + serine-cysteine sulphenyl amide cross-link + + + + + + + + + + + A protein modification that effectively attaches an L-threonine residue to murein peptidoglycan by a pentaglycine linker peptide. + T + natural + C-term + uniprot.ptm:PTM-0246 + (2R,6S)-2-(N-mureinyl-(R)-alanyl-(S)-isoglutamyl)amino-6-(threonyl-pentaglycyl)amino-pimeloyl-(S)-alanyl-(S)-alanine + L-threonyl-pentaglycyl-murein peptidoglycan + MOD_RES Pentaglycyl murein peptidoglycan amidated threonine + PSI-MOD + MOD:00350 + L-threonyl-pentaglycyl-murein peptidoglycan + + + + + A protein modification that effectively attaches an L-threonine residue to murein peptidoglycan by a pentaglycine linker peptide. + PubMed:10754567 + PubMed:1638631 + RESID:AA0345 + + + + + (2R,6S)-2-(N-mureinyl-(R)-alanyl-(S)-isoglutamyl)amino-6-(threonyl-pentaglycyl)amino-pimeloyl-(S)-alanyl-(S)-alanine + + + + + + L-threonyl-pentaglycyl-murein peptidoglycan + + + + + + MOD_RES Pentaglycyl murein peptidoglycan amidated threonine + + + + + + + + + + + A protein modification that effectively converts a glycine residue to N-glycyl-1-(phosphatidyl)ethanolamine. + 699.99 + C 39 H 74 N 1 O 7 P 1 + 699.52026 + C 41 H 78 N 2 O 9 P 1 + 774.05 + 773.5445 + G + natural + C-term + uniprot.ptm:PTM-0249 + (R)-1-hexadecanoyloxy-2-((Z)-9-octadecenoyloxy)-3-[2-(aminoacetylamino)ethyloxyphospho]propane + LIPID Phosphatidylethanolamine amidated glycine + N-glycyl-1-(phosphatidyl)ethanolamine + N-glycyl-1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine + PSI-MOD + MOD:00351 + N-glycyl-1-(phosphatidyl)ethanolamine + + + + + A protein modification that effectively converts a glycine residue to N-glycyl-1-(phosphatidyl)ethanolamine. + PubMed:11100732 + RESID:AA0346 + + + + + (R)-1-hexadecanoyloxy-2-((Z)-9-octadecenoyloxy)-3-[2-(aminoacetylamino)ethyloxyphospho]propane + + + + + + LIPID Phosphatidylethanolamine amidated glycine + + + + + + N-glycyl-1-(phosphatidyl)ethanolamine + + + + + + N-glycyl-1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine + + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-omega-hydroxyceramide ester. + 761.31 + C 50 H 96 N 0 O 4 + 760.73083 + C 55 H 104 N 2 O 6 + 889.44 + 888.7894 + Q + natural + uniprot.ptm:PTM-0236 + (S)-2-amino-5-[30-((2S,3R,4E)-1,3-dihydroxyicos-4-en-2-ylamino)-30-oxotriacontan-1-yloxy]-5-oxopentanoic acid + 2-[30-(isoglutamyloxy)triacontanoyl]icosasphingosine + L-glutamyl 5-omega-hydroxyceramide ester + LIPID Omega-hydroxyceramide glutamate ester + PSI-MOD + MOD:00352 + L-glutamyl 5-omega-hydroxyceramide ester + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-omega-hydroxyceramide ester. + PubMed:10411887 + PubMed:9651377 + RESID:AA0347 + + + + + (S)-2-amino-5-[30-((2S,3R,4E)-1,3-dihydroxyicos-4-en-2-ylamino)-30-oxotriacontan-1-yloxy]-5-oxopentanoic acid + + + + + + 2-[30-(isoglutamyloxy)triacontanoyl]icosasphingosine + + + + + + L-glutamyl 5-omega-hydroxyceramide ester + + + + + + LIPID Omega-hydroxyceramide glutamate ester + + + + + + + + + + + + + A protein modification that effectively cross-links an L-tryptophan residue with an L-tyrosine residue by a carbon-carbon bond, and cross-links the L-tyrosine residue to an L-methionine residue by a thioether bond to form S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium. + -3.02 + C 0 H -3 N 0 O 0 S 0 + -3.024024 + 1+ + C 25 H 25 N 4 O 4 S 1 + 477.56 + 477.1591 + M, W, Y + natural + uniprot.ptm:PTM-0328 + 5'-(6'-tryptophyl)-tyrosin-3'-yl-methionin-S-ium + S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium + PSI-MOD + MOD:00353 + Cross-link 3. + S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium + + + + + A protein modification that effectively cross-links an L-tryptophan residue with an L-tyrosine residue by a carbon-carbon bond, and cross-links the L-tyrosine residue to an L-methionine residue by a thioether bond to form S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium. + PubMed:12172540 + PubMed:16285713 + RESID:AA0348 + + + + + 5'-(6'-tryptophyl)-tyrosin-3'-yl-methionin-S-ium + + + + + + S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-(riboflavin phosphoryl)-L-threonine. + 438.33 + C 17 H 19 N 4 O 8 P 1 + 438.09406 + C 21 H 26 N 5 O 10 P 1 + 539.44 + 539.1417 + T + natural + Unimod:442 + uniprot.ptm:PTM-0126 + (2S,3R)-2-amino-3-(riboflavin 5'-hydrogen phosphonoxy)butanoic acid + MOD_RES FMN phosphoryl threonine + O-(riboflavin phosphoryl)-L-threonine + O3-threonyl FMN + O3-threonyl flavin mononucleotide + OFMNThr + PSI-MOD + FMN + O3-(riboflavin phosphoryl) + MOD:00354 + + O-(riboflavin phosphoryl)-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-(riboflavin phosphoryl)-L-threonine. + PubMed:10587447 + PubMed:11163785 + PubMed:11248234 + RESID:AA0349 + Unimod:442#T + + + + + (2S,3R)-2-amino-3-(riboflavin 5'-hydrogen phosphonoxy)butanoic acid + + + + + + MOD_RES FMN phosphoryl threonine + + + + + + O-(riboflavin phosphoryl)-L-threonine + + + + + + O3-threonyl FMN + + + + + + O3-threonyl flavin mononucleotide + + + + + + OFMNThr + + + + + + FMN + + + + + + O3-(riboflavin phosphoryl) + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-(riboflavin phosphoryl)-L-serine. + 438.33 + C 17 H 19 N 4 O 8 P 1 + 438.09406 + C 20 H 24 N 5 O 10 P 1 + 525.41 + 525.1261 + S + natural + Unimod:442 + uniprot.ptm:PTM-0125 + (R)-2-amino-3-(riboflavin 5'-hydrogen phosphonoxy)propanoic acid + MOD_RES FMN phosphoryl serine + O-(riboflavin phosphoryl)-L-serine + O3-seryl FMN + O3-seryl flavin mononucleotide + OFMNSer + PSI-MOD + FMN + O3-(riboflavin phosphoryl) + MOD:00355 + + O-(riboflavin phosphoryl)-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-(riboflavin phosphoryl)-L-serine. + RESID:AA0350 + Unimod:442#S + + + + + (R)-2-amino-3-(riboflavin 5'-hydrogen phosphonoxy)propanoic acid + + + + + + MOD_RES FMN phosphoryl serine + + + + + + O-(riboflavin phosphoryl)-L-serine + + + + + + O3-seryl FMN + + + + + + O3-seryl flavin mononucleotide + + + + + + OFMNSer + + + + + + FMN + + + + + + O3-(riboflavin phosphoryl) + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-(4a-FMN)-L-cysteine. + 456.35 + C 17 H 21 N 4 O 9 P 1 S 0 + 456.1046 + C 20 H 26 N 5 O 10 P 1 S 1 + 559.49 + 559.1138 + C + natural + Unimod:443 + uniprot.ptm:PTM-0270 + (R)-2-amino-3-(4a-riboflavin 5'-dihydrogen phosphate)sulfanylpropanoic acid + 4a-(S-cysteinyl)FMN + 4a-(S-cysteinyl)flavin mononucleotide + MOD_RES S-4a-FMN cysteine + S-(4a-FMN)-L-cysteine + S4aFMNCys + PSI-MOD + FMNC + S-(4a-FMN) + MOD:00356 + + S-(4alpha-FMN)-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-(4a-FMN)-L-cysteine. + PubMed:12668455 + PubMed:12846567 + PubMed:7692961 + RESID:AA0351 + Unimod:443#C + + + + + (R)-2-amino-3-(4a-riboflavin 5'-dihydrogen phosphate)sulfanylpropanoic acid + + + + + + 4a-(S-cysteinyl)FMN + + + + + + 4a-(S-cysteinyl)flavin mononucleotide + + + + + + MOD_RES S-4a-FMN cysteine + + + + + + S-(4a-FMN)-L-cysteine + + + + + + S4aFMNCys + + + + + + FMNC + + + + + + S-(4a-FMN) + + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FMN)-L-histidine. + 454.33 + C 17 H 19 N 4 O 9 P 1 + 454.08896 + C 23 H 26 N 7 O 10 P 1 + 591.47 + 591.1479 + H + natural + Unimod:409 + uniprot.ptm:PTM-0289 + (S)-2-amino-3-(1-[8alpha riboflavin 5'-dihydrogen phosphate]imidazol-4-yl)propanoic acid + 1'-(8alpha-FMN)-L-histidine + 8alpha-(N(epsilon)-histidyl)FMN + 8alpha-(N1'-histidyl)FMN + MOD_RES Tele-8alpha-FMN histidine + N(tau)-(8alpha-FMN)-histidine + Ntele8aFMNHis + tele-(8alpha-FMN)-histidine + PSI-MOD + FMNH + flavin mononucleotide + MOD:00357 + + 1'-(8alpha-FMN)-L-histidine + + + + + A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FMN)-L-histidine. + PubMed:11902668 + PubMed:8611516 + RESID:AA0352 + Unimod:409#H + + + + + (S)-2-amino-3-(1-[8alpha riboflavin 5'-dihydrogen phosphate]imidazol-4-yl)propanoic acid + + + + + + 1'-(8alpha-FMN)-L-histidine + + + + + + 8alpha-(N(epsilon)-histidyl)FMN + + + + + + 8alpha-(N1'-histidyl)FMN + + + + + + MOD_RES Tele-8alpha-FMN histidine + + + + + + N(tau)-(8alpha-FMN)-histidine + + + + + + Ntele8aFMNHis + + + + + + tele-(8alpha-FMN)-histidine + + + + + + FMNH + + + + + + flavin mononucleotide + + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FMN)-L-histidine. + 454.33 + C 17 H 19 N 4 O 9 P 1 + 454.08896 + C 23 H 26 N 7 O 10 P 1 + 591.47 + 591.1479 + H + hypothetical + Unimod:409 + (S)-2-amino-3-(3-[8alpha riboflavin 5'-dihydrogen phosphate]imidazol-4-yl)propanoic acid + 3'-(8alpha-FMN)-L-histidine + 8alpha-(N(delta)-histidyl)FMN + 8alpha-(N3'-histidyl)FMN + N(pi)-(8alpha-FMN)-histidine + Npros8aFMNHis + pros-(8alpha-FMN)-histidine + PSI-MOD + FMNH + flavin mononucleotide + MOD:00358 + + In a later publication, PubMed:19438211, the authors changed the enzyme activity, the connection from a histidine nitrogen to a cysteine sulfur, and the identity of the flavin from FMN to FAD. They now believe the modification is S-(8alpha-FAD)-L-cysteine, see MOD:00152. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. + 3'-(8alpha-FMN)-L-histidine + + + + + A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FMN)-L-histidine. + PubMed:12417325 + RESID:AA0353 + Unimod:409#H + + + + + (S)-2-amino-3-(3-[8alpha riboflavin 5'-dihydrogen phosphate]imidazol-4-yl)propanoic acid + + + + + + 3'-(8alpha-FMN)-L-histidine + + + + + + 8alpha-(N(delta)-histidyl)FMN + + + + + + 8alpha-(N3'-histidyl)FMN + + + + + + N(pi)-(8alpha-FMN)-histidine + + + + + + Npros8aFMNHis + + + + + + pros-(8alpha-FMN)-histidine + + + + + + FMNH + + + + + + flavin mononucleotide + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to N2-acetyl-L-arginine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 8 H 15 N 4 O 2 + 199.23 + 199.1195 + R + natural + N-term + uniprot.ptm:PTM-0180 + (S)-2-acetamido-5-carbamimidamidopentanoic acid + 2-acetamido-5-guanidinopentanoic acid + 2-acetylamino-5-guanidinopentanoic acid + AcArg + MOD_RES N2-acetylarginine + N(alpha)-acetylarginine + N2-acetyl-L-arginine + N2-acetylated L-arginine + acetylarginine + alpha-acetylamino-delta-guanidinovaleric acid + PSI-MOD + MOD:00359 + N2-acetyl-L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to N2-acetyl-L-arginine. + PubMed:12883043 + PubMed:1894641 + RESID:AA0354 + + + + + (S)-2-acetamido-5-carbamimidamidopentanoic acid + + + + + + 2-acetamido-5-guanidinopentanoic acid + + + + + + 2-acetylamino-5-guanidinopentanoic acid + + + + + + AcArg + + + + + + MOD_RES N2-acetylarginine + + + + + + N(alpha)-acetylarginine + + + + + + N2-acetyl-L-arginine + + + + + + N2-acetylated L-arginine + + + + + + acetylarginine + + + + + + alpha-acetylamino-delta-guanidinovaleric acid + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide. + 922.07 + C 19 Cu 1 H 24 Mo 1 N 8 O 15 P 2 S 3 + 922.83484 + C 22 Cu 1 H 29 Mo 1 N 9 O 16 P 2 S 4 + 1025.2 + 1025.844 + C + natural + Unimod:444 + L-cysteinyl copper sulfido molybdopterin cytosine dinucleotide + [8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with cytosine)methyl-6-oxo-3,4-dimercapto-pteridino[6,7-5,6]pyranoato-S3,S4]-cysteinyl-S-copper-mu-sulfido-molybdenum hydroxide oxide + cysteinyl copper mu-sulfido Mo-pterin cytosine dinucleotide + PSI-MOD + CuSMo + copper sulfido molybdopterin cytosine dinuncleotide + MOD:00360 + L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide. + PubMed:12475995 + RESID:AA0355 + Unimod:444#C + + + + + L-cysteinyl copper sulfido molybdopterin cytosine dinucleotide + + + + + + [8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with cytosine)methyl-6-oxo-3,4-dimercapto-pteridino[6,7-5,6]pyranoato-S3,S4]-cysteinyl-S-copper-mu-sulfido-molybdenum hydroxide oxide + + + + + + cysteinyl copper mu-sulfido Mo-pterin cytosine dinucleotide + + + + + + CuSMo + + + + + + copper sulfido molybdopterin cytosine dinuncleotide + + + + + + + + + + + A protein modification that effectively converts three L-cysteine residues, an S-adenosylmethionine and a four-iron four-sulfur cluster to tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide. + 747.03 + C 15 Fe 4 H 19 N 6 O 5 S 5 + 746.7424 + 1- + C 24 Fe 4 H 34 N 9 O 8 S 8 + 1056.45 + 1055.7699 + C, C, C + natural + METAL Iron-sulfur (4Fe-4S-S-AdoMet) + tetra-mu3-sulfido(S-adenosylmethion-N,O-diyliron)tris(S-cysteinyliron) + tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide + PSI-MOD + MOD:00361 + Cross-link 3. + tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide + + + + + A protein modification that effectively converts three L-cysteine residues, an S-adenosylmethionine and a four-iron four-sulfur cluster to tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide. + PubMed:11222759 + PubMed:14704425 + RESID:AA0356 + + + + + METAL Iron-sulfur (4Fe-4S-S-AdoMet) + + + + + + tetra-mu3-sulfido(S-adenosylmethion-N,O-diyliron)tris(S-cysteinyliron) + + + + + + tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide + + + + + + + + + + + + A protein modification that effectively converts three L-cysteine residues, an L-arginine residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-arginyl diiron disulfide. + 172.79 + C 0 Fe 2 H -3 N 0 O 0 S 2 + 172.79164 + 2- + C 15 Fe 2 H 24 N 7 O 4 S 5 + 638.39 + 637.9203 + C, C, C, R + natural + METAL Iron-sulfur (2Fe-2S) + di-mu-sulfido(N(eta1)-arginyl-S-cysteinyliron)(bis-S-cysteinyliron) + tris-L-cysteinyl L-arginyl diiron disulfide + PSI-MOD + MOD:00362 + Cross-link 4. + tris-L-cysteinyl L-arginyl diiron disulfide + + + + + A protein modification that effectively converts three L-cysteine residues, an L-arginine residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-arginyl diiron disulfide. + PubMed:14704425 + RESID:AA0357 + + + + + METAL Iron-sulfur (2Fe-2S) + + + + + + di-mu-sulfido(N(eta1)-arginyl-S-cysteinyliron)(bis-S-cysteinyliron) + + + + + + tris-L-cysteinyl L-arginyl diiron disulfide + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-selenocysteine residues to form L-cysteinyl-L-selenocystine. + -2.02 + C 0 H -2 N 0 O 0 S 0 Se 0 + -2.01565 + C 6 H 8 N 2 O 2 S 1 Se 1 + 251.17 + 251.94717 + C, U + natural + uniprot.ptm:PTM-0109 + (R,R)-2-amino-3-[3-(2-aminopropanoic acid)sulfanyl]selanylpropanoic acid + CROSSLNK Cysteinyl-selenocysteine (Cys-Sec) + CROSSLNK Cysteinyl-selenocysteine (Sec-Cys) + L-cysteinyl-L-selenocysteine + PSI-MOD + MOD:00363 + + Cross-link 2. + L-cysteinyl-L-selenocysteine (Cys-Sec) + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-selenocysteine residues to form L-cysteinyl-L-selenocystine. + PubMed:12911312 + RESID:AA0358#SEC + + + + + (R,R)-2-amino-3-[3-(2-aminopropanoic acid)sulfanyl]selanylpropanoic acid + + + + + + CROSSLNK Cysteinyl-selenocysteine (Cys-Sec) + + + + + + CROSSLNK Cysteinyl-selenocysteine (Sec-Cys) + + + + + + L-cysteinyl-L-selenocysteine + + + + + + + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 5-hydroxy-N6,N6,N6-trimethyl-L-lysine. + 59.09 + C 3 H 7 N 0 O 1 + 59.04914 + 1+ + C 9 H 19 N 2 O 2 + 187.26 + 187.1441 + K + natural + Unimod:445 + uniprot.ptm:PTM-0186 + (2R,5Xi)-5-amino-5-carboxy-2-hydroxy-N,N,N-trimethylpentan-1-aminium + (2Xi,5S)-5-amino-5-carboxy-2-hydroxy-N,N,N-trimethylpentanaminium + (2Xi,5S)-5-azanyl-5-carboxy-2-hydroxy-N,N,N-trimethylpentanazanium + 5-hydroxy-N(zeta)-trimethyllysine + 5-hydroxy-N6,N6,N6-trimethyl-L-lysine + 5-hydroxy-N6,N6,N6-trimethyllysin-N6-ium + 5-hydroxy-N6,N6,N6-trimethyllysine cation + 5-hydroxylated N6,N6,N6-trimethylated L-lysine + 5HyN6Me3Lys + MOD_RES N6,N6,N6-trimethyl-5-hydroxylysine + alpha-amino-epsilon-dimethylamino-delta-hydroxycaproic acid + delta-hydroxy-epsilon-N,N,N-trimethyllysine + lysine derivative Lys(z) + PSI-MOD + 5-hydroxy-N6,N6,N6-trimethyl + Hydroxytrimethyl + MOD:00364 + Incidental to RESID:AA0278; secondary to RESID:AA0028; secondary to RESID:AA0074. + 5-hydroxy-N6,N6,N6-trimethyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to 5-hydroxy-N6,N6,N6-trimethyl-L-lysine. + PubMed:11349130 + PubMed:14661085 + RESID:AA0359 + Unimod:445#K + + + + + (2R,5Xi)-5-amino-5-carboxy-2-hydroxy-N,N,N-trimethylpentan-1-aminium + + + + + + (2Xi,5S)-5-amino-5-carboxy-2-hydroxy-N,N,N-trimethylpentanaminium + + + + + + (2Xi,5S)-5-azanyl-5-carboxy-2-hydroxy-N,N,N-trimethylpentanazanium + + + + + + 5-hydroxy-N(zeta)-trimethyllysine + + + + + + 5-hydroxy-N6,N6,N6-trimethyl-L-lysine + + + + + + 5-hydroxy-N6,N6,N6-trimethyllysin-N6-ium + + + + + + 5-hydroxy-N6,N6,N6-trimethyllysine cation + + + + + + 5-hydroxylated N6,N6,N6-trimethylated L-lysine + + + + + + 5HyN6Me3Lys + + + + + + MOD_RES N6,N6,N6-trimethyl-5-hydroxylysine + + + + + + alpha-amino-epsilon-dimethylamino-delta-hydroxycaproic acid + + + + + + delta-hydroxy-epsilon-N,N,N-trimethyllysine + + + + + + lysine derivative Lys(z) + + + + + + 5-hydroxy-N6,N6,N6-trimethyl + + + + + + Hydroxytrimethyl + + + + + + + + + + + + + A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue by an isopeptide bond to form N-(L-isoglutamyl)-glycine. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 7 H 9 N 2 O 3 + 169.16 + 169.06131 + E, G + natural + N-term + uniprot.ptm:PTM-0157 + (S)-2-amino-5-(carboxymethyl)amino-5-oxopentanoic acid + 2-amino-N5-(carboxymethyl)-pentanediamic acid + CROSSLNK Isoglutamyl glycine isopeptide (Gly-Glu) + N-(L-isoglutamyl)-glycine + N-gamma-glutamylglycine + isoglutamyl glycine + PSI-MOD + MOD:00365 + Cross-link 2. + N-(L-isoglutamyl)-glycine + + + + + A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue by an isopeptide bond to form N-(L-isoglutamyl)-glycine. + PubMed:14531691 + RESID:AA0360 + + + + + (S)-2-amino-5-(carboxymethyl)amino-5-oxopentanoic acid + + + + + + 2-amino-N5-(carboxymethyl)-pentanediamic acid + + + + + + CROSSLNK Isoglutamyl glycine isopeptide (Gly-Glu) + + + + + + N-(L-isoglutamyl)-glycine + + + + + + N-gamma-glutamylglycine + + + + + + isoglutamyl glycine + + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-sulfo-L-serine. + 80.06 + C 0 H 0 N 0 O 3 S 1 + 79.95682 + C 3 H 5 N 1 O 5 S 1 + 167.13 + 166.98885 + S + natural + Unimod:40 + uniprot.ptm:PTM-0284 + (2S)-2-amino-3-(sulfooxy)propanoic acid + 2-amino-3-hydroxypropanoic acid 3-sulfate + MOD_RES Sulfoserine + O-sulfo-L-serine + O3-sulfonoserine + O3-sulfoserine + serine sulfate ester + PSI-MOD + O-Sulfonation + Sulfo + MOD:00366 + + O-sulfo-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-sulfo-L-serine. + PubMed:14752058 + RESID:AA0361 + Unimod:40#S + + + + + (2S)-2-amino-3-(sulfooxy)propanoic acid + + + + + + 2-amino-3-hydroxypropanoic acid 3-sulfate + + + + + + MOD_RES Sulfoserine + + + + + + O-sulfo-L-serine + + + + + + O3-sulfonoserine + + + + + + O3-sulfoserine + + + + + + serine sulfate ester + + + + + + O-Sulfonation + + + + + + Sulfo + + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-sulfo-L-threonine. + 80.06 + C 0 H 0 N 0 O 3 S 1 + 79.95682 + C 4 H 7 N 1 O 5 S 1 + 181.16 + 181.00449 + T + natural + Unimod:40 + uniprot.ptm:PTM-0285 + (2S,3R)-2-amino-3-(sulfooxy)butanoic acid + 2-amino-3-hydroxybutanoic acid 3-sulfate + MOD_RES Sulfothreonine + O-sulfo-L-threonine + O3-sulfonothreonine + O3-sulfothreonine + threonine sulfate ester + PSI-MOD + O-Sulfonation + Sulfo + MOD:00367 + + O-sulfo-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-sulfo-L-threonine. + PubMed:14752058 + RESID:AA0362 + Unimod:40#T + + + + + (2S,3R)-2-amino-3-(sulfooxy)butanoic acid + + + + + + 2-amino-3-hydroxybutanoic acid 3-sulfate + + + + + + MOD_RES Sulfothreonine + + + + + + O-sulfo-L-threonine + + + + + + O3-sulfonothreonine + + + + + + O3-sulfothreonine + + + + + + threonine sulfate ester + + + + + + O-Sulfonation + + + + + + Sulfo + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to N-carboxy-L-methionine. + 44.01 + C 1 H 0 N 0 O 2 S 0 + 43.98983 + C 6 H 10 N 1 O 3 S 1 + 176.21 + 176.03813 + M + hypothetical + N-term + Unimod:299 + (S)-2-carboxyamino-4-(methylsulfanyl)butanoic acid + 2-carbamic-4-(methylsulfanyl)butanoic acid + 2-carbamic-4-(methylthio)butanoic acid + N-carboxy-L-methionine + N-carboxymethionine + PSI-MOD + Carboxy + Carboxylation + MOD:00368 + At least three protein crystallographic structures have been reported with this modification. However, no chemical evidence for this modification is provided, there were no reports of this modification before these crystallographic reports, and there is no metabolic explanation for the conversion of a formyl group to a carboxy group. There is confusion in its description, and misnaming is common. This modification is probably a misidentification of N-(dihydroxymethyl)methionine, the hydrated form of N-formylmethionine. See MOD:01446 [JSG]. + N-carboxy-L-methionine + + + + + A protein modification that effectively converts an L-methionine residue to N-carboxy-L-methionine. + PubMed:10368287 + PubMed:11120890 + PubMed:12595263 + PubMed:8312270 + RESID:AA0363 + Unimod:299#M + + + + + (S)-2-carboxyamino-4-(methylsulfanyl)butanoic acid + + + + + + 2-carbamic-4-(methylsulfanyl)butanoic acid + + + + + + 2-carbamic-4-(methylthio)butanoic acid + + + + + + N-carboxy-L-methionine + + + + + + N-carboxymethionine + + + + + + Carboxy + + + + + + Carboxylation + + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-acetyl-L-serine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 5 H 7 N 1 O 3 + 129.12 + 129.04259 + S + natural + Unimod:1 + uniprot.ptm:PTM-0232 + (2S)-3-(acetyloxy)-2-aminopropanoic acid + MOD_RES O-acetylserine + O-acetyl-L-serine + O-acetylated L-serine + O-acetylserine + OAcSer + serine acetate ester + PSI-MOD + Acetyl + Acetylation + MOD:00369 + + incidental to RESID:AA0051 + O-acetyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-acetyl-L-serine. + ChEBI:17981 + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + PubMed:14730666 + PubMed:15350136 + PubMed:16731519 + PubMed:489587 + PubMed:7309355 + RESID:AA0364 + Unimod:1#S + + + + + (2S)-3-(acetyloxy)-2-aminopropanoic acid + + + + + + MOD_RES O-acetylserine + + + + + + O-acetyl-L-serine + + + + + + O-acetylated L-serine + + + + + + O-acetylserine + + + + + + OAcSer + + + + + + serine acetate ester + + + + + + Acetyl + + + + + + Acetylation + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to (E)-2,3-didehydrotyrosine. + -2.02 + C 0 H -2 N 0 O 0 + -2.01565 + C 9 H 7 N 1 O 2 + 161.16 + 161.04768 + Y + natural + uniprot.ptm:PTM-0001 + (2E)-2-amino-3-(4-hydroxyphenyl)prop-2-enoic acid + (E)-2,3-didehydrogenated tyrosine + (E)-2,3-didehydrotyrosine + E-dHTyr + MOD_RES (E)-2,3-didehydrotyrosine + amino-(para-hydroxybenzylidenyl)acetic acid + blue non-fluorescent pocilloporin chromophore + para-hydroxybenzylidene-imidazolidinone chromophore + trans-dehydrotyrosine + PSI-MOD + 2-amino-3-oxo-butanoic_acid + Didehydro + MOD:00370 + + incidental to RESID:AA0184; incidental to RESID:AA0187; incidental to RESID:AA0188; incidental to RESID:AA0189; incidental to RESID:AA0378; incidental to RESID:AA0379; incidental to RESID:AA0380; incidental to RESID:AA0381 + (E)-2,3-didehydrotyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to (E)-2,3-didehydrotyrosine. + PubMed:12623015 + RESID:AA0365 + + + + + (2E)-2-amino-3-(4-hydroxyphenyl)prop-2-enoic acid + + + + + + (E)-2,3-didehydrogenated tyrosine + + + + + + (E)-2,3-didehydrotyrosine + + + + + + E-dHTyr + + + + + + MOD_RES (E)-2,3-didehydrotyrosine + + + + + + amino-(para-hydroxybenzylidenyl)acetic acid + + + + + + blue non-fluorescent pocilloporin chromophore + + + + + + para-hydroxybenzylidene-imidazolidinone chromophore + + + + + + trans-dehydrotyrosine + + + + + + 2-amino-3-oxo-butanoic_acid + + + + + + Didehydro + + + + + + + + + + + + + + A protein modification that effectively converts two L-aspartic acid residues, three L-glutamic acid residues, an L-histidine residue, and a one-calcium, four-iron, four-oxygen cluster to bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide. + 317.78 + C 0 Ca 1 H -6 Mn 4 N 0 O 4 + 317.6475 + C 29 Ca 1 H 32 Mn 4 N 8 O 20 + 1072.44 + 1071.8881 + D, D, E, E, E, H + hypothetical + 4Mn-Ca-4O cluster + bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide + mu3-1:2:3kappaO-oxido-mu3-1:3:4kappaO-oxido-mu3-2:3:4kappaO-oxido-mu4-1:2:4:5kappaO-oxido-N1'-histidino-O5-glutamato 2-manganese-O5,O5-glutamato 3-manganese-O4-aspartato 4-manganese-O4-aspartato-O5-glutamato 5-manganese + photosystem II catalytic cluster + PSI-MOD + MOD:00371 + Cross-link 6. + bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide + + + + + A protein modification that effectively converts two L-aspartic acid residues, three L-glutamic acid residues, an L-histidine residue, and a one-calcium, four-iron, four-oxygen cluster to bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide. + PubMed:14764885 + RESID:AA0366 + + + + + 4Mn-Ca-4O cluster + + + + + + bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide + + + + + + mu3-1:2:3kappaO-oxido-mu3-1:3:4kappaO-oxido-mu3-2:3:4kappaO-oxido-mu4-1:2:4:5kappaO-oxido-N1'-histidino-O5-glutamato 2-manganese-O5,O5-glutamato 3-manganese-O4-aspartato 4-manganese-O4-aspartato-O5-glutamato 5-manganese + + + + + + photosystem II catalytic cluster + + + + + + + + + + + A protein modification that effectively cross-links two L-tyrosine residues with a carbon-carbon bond to form 3'-(3'-L-tyrosinyl)-L-tyrosine. + -2.02 + C 0 H -2 N 0 O 0 + -2.01565 + C 18 H 16 N 2 O 4 + 324.34 + 324.111 + Y, Y + natural + (2S,2'S)-3,3'-(6,6'-dihydroxybiphenyl-3,3'-diyl)bis(2-aminopropanoic acid) + 3'-(L-tyros-3'-yl)-L-tyrosine + 3,3'-BiTyr (Crosslink) + 6,6'-dihydroxy-(1,1'-biphenyl)-3,3'-bis(2-aminopropanoic acid) + alpha,alpha'-diamino-6,6'-dihydroxy-(1,1'-biphenyl)-3,3'-dipropanoic acid + bityrosine + o,o-dityrosine + PSI-MOD + MOD:00372 + Cross-link 2; From DeltaMass: Average Mass: -2. + 3'-(3'-L-tyrosinyl)-L-tyrosine + + + + + A protein modification that effectively cross-links two L-tyrosine residues with a carbon-carbon bond to form 3'-(3'-L-tyrosinyl)-L-tyrosine. + DeltaMass:0 + PubMed:14249161 + PubMed:637884 + PubMed:8702710 + PubMed:8937563 + RESID:AA0367 + + + + + (2S,2'S)-3,3'-(6,6'-dihydroxybiphenyl-3,3'-diyl)bis(2-aminopropanoic acid) + + + + + + 3'-(L-tyros-3'-yl)-L-tyrosine + + + + + + 3,3'-BiTyr (Crosslink) + + + + + + 6,6'-dihydroxy-(1,1'-biphenyl)-3,3'-bis(2-aminopropanoic acid) + + + + + + alpha,alpha'-diamino-6,6'-dihydroxy-(1,1'-biphenyl)-3,3'-dipropanoic acid + + + + + + bityrosine + + + + + + o,o-dityrosine + + + + + + + + + + + A protein modification that effectively cross-links L-tyrosine residues with an ether bond to form 3'-(O4'-L-tyrosinyl)-L-tyrosine. + -2.02 + C 0 H -2 N 0 O 0 + -2.01565 + C 18 H 16 N 2 O 4 + 324.34 + 324.111 + Y, Y + natural + uniprot.ptm:PTM-0155 + (2S)-2-amino-3-[3-(4-[(2S)-2-amino-2-carboxyethyl]phenoxy)-4-hydroxyphenyl]propanoic acid + 2-amino-3-[4-(5-[(2S)-2-amino-2-carboxyethyl]-2-hydroxyphenoxy)phenyl]propanoic acid + 3'-(L-tyros-O4'-yl)-L-tyrosine + CROSSLNK Isodityrosine (Tyr-Tyr) + IsodiTyr (Crosslink) + O-(5-(2-amino-2-carboxyethyl)-2-hydroxyphenyl)-L-tyrosine + isodityrosine + PSI-MOD + MOD:00373 + Cross-link 2; secondary to RESID:AA0146; From DeltaMass: Average Mass: -2. + 3'-(O4'-L-tyrosinyl)-L-tyrosine + + + + + A protein modification that effectively cross-links L-tyrosine residues with an ether bond to form 3'-(O4'-L-tyrosinyl)-L-tyrosine. + DeltaMass:0 + PubMed:12719529 + PubMed:7115340 + PubMed:8702710 + RESID:AA0368 + + + + + (2S)-2-amino-3-[3-(4-[(2S)-2-amino-2-carboxyethyl]phenoxy)-4-hydroxyphenyl]propanoic acid + + + + + + 2-amino-3-[4-(5-[(2S)-2-amino-2-carboxyethyl]-2-hydroxyphenoxy)phenyl]propanoic acid + + + + + + 3'-(L-tyros-O4'-yl)-L-tyrosine + + + + + + CROSSLNK Isodityrosine (Tyr-Tyr) + + + + + + IsodiTyr (Crosslink) + + + + + + O-(5-(2-amino-2-carboxyethyl)-2-hydroxyphenyl)-L-tyrosine + + + + + + isodityrosine + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to 3,4-dihydroxy-L-arginine. + 32.0 + C 0 H 0 N 0 O 2 + 31.989828 + C 6 H 12 N 4 O 3 + 188.19 + 188.09094 + R + natural + Unimod:425 + uniprot.ptm:PTM-0022 + (2S,3Xi,4Xi)-2-amino-5-carbamimidamido-3,4-dihydroxypentanoic acid + 2-amino-5-guanidino-3,4-dihydroxypentanoic acid + 3,4-dihydroxy-L-arginine + 3,4-dihydroxylated L-arginine + 34Hy2Arg + MOD_RES 3,4-dihydroxyarginine + beta,gamma-dihydroxyarginine + PSI-MOD + Dioxidation + dihydroxy + MOD:00374 + 3,4-dihydroxy-L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to 3,4-dihydroxy-L-arginine. + ChEBI:141829 + PubMed:10978343 + PubMed:12686488 + RESID:AA0369 + Unimod:425#R + + + + + (2S,3Xi,4Xi)-2-amino-5-carbamimidamido-3,4-dihydroxypentanoic acid + + + + + + 2-amino-5-guanidino-3,4-dihydroxypentanoic acid + + + + + + 3,4-dihydroxy-L-arginine + + + + + + 3,4-dihydroxylated L-arginine + + + + + + 34Hy2Arg + + + + + + MOD_RES 3,4-dihydroxyarginine + + + + + + beta,gamma-dihydroxyarginine + + + + + + Dioxidation + + + + + + dihydroxy + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 4,5-dihydroxy-L-lysine. + 32.0 + C 0 H 0 N 0 O 2 + 31.989828 + C 6 H 12 N 2 O 3 + 160.17 + 160.0848 + K + natural + Unimod:425 + uniprot.ptm:PTM-0036 + (2S,4Xi,5Xi)-2,6-diamino-4,5-dihydroxyhexanoic acid + 4,5-dihydroxy-L-lysine + 4,5-dihydroxylated L-lysine + 45Hy2Lys + MOD_RES 4,5-dihydroxylysine + alpha,epsilon-diamino-delta,gamma-dihydroxycaproic acid + delta,gamma-dihydroxylysine + PSI-MOD + Dioxidation + dihydroxy + MOD:00375 + 4,5-dihydroxy-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to 4,5-dihydroxy-L-lysine. + PubMed:10978343 + PubMed:12686488 + RESID:AA0370 + Unimod:425#K + + + + + (2S,4Xi,5Xi)-2,6-diamino-4,5-dihydroxyhexanoic acid + + + + + + 4,5-dihydroxy-L-lysine + + + + + + 4,5-dihydroxylated L-lysine + + + + + + 45Hy2Lys + + + + + + MOD_RES 4,5-dihydroxylysine + + + + + + alpha,epsilon-diamino-delta,gamma-dihydroxycaproic acid + + + + + + delta,gamma-dihydroxylysine + + + + + + Dioxidation + + + + + + dihydroxy + + + + + + + + + + + A protein modification that effectively crosslinks an L-histidine residue and 5'-phosphoadenosine through a phosphoramide ester bond to form 1'-(phospho-5'-adenosine)-L-histidine. + 329.21 + C 10 H 12 N 5 O 6 P 1 + 329.05252 + C 16 H 19 N 8 O 7 P 1 + 466.35 + 466.11142 + H + natural + Unimod:405 + (2S)-2-amino-3-[1-(5'-adenosine phosphono)imidazol-4-yl]propanoic acid + 1'-(phospho-5'-adenosine)-L-histidine + ACT_SITE Tele-AMP-histidine intermediate + L-histidine 5'-adenosine phosphoramidester + L-histidine monoanhydride with 5'-adenylic acid + N(tau)-5'-adenylic-L-histidine + N1'-adenylylated histidine + tele-5'-adenylic-L-histidine + PSI-MOD + AMP binding site + Phosphoadenosine + MOD:00376 + + 1'-(phospho-5'-adenosine)-L-histidine + + + + + A protein modification that effectively crosslinks an L-histidine residue and 5'-phosphoadenosine through a phosphoramide ester bond to form 1'-(phospho-5'-adenosine)-L-histidine. + PubMed:15182206 + PubMed:9323207 + RESID:AA0371 + Unimod:405#H + + + + + (2S)-2-amino-3-[1-(5'-adenosine phosphono)imidazol-4-yl]propanoic acid + + + + + + 1'-(phospho-5'-adenosine)-L-histidine + + + + + + ACT_SITE Tele-AMP-histidine intermediate + + + + + + L-histidine 5'-adenosine phosphoramidester + + + + + + L-histidine monoanhydride with 5'-adenylic acid + + + + + + N(tau)-5'-adenylic-L-histidine + + + + + + N1'-adenylylated histidine + + + + + + tele-5'-adenylic-L-histidine + + + + + + AMP binding site + + + + + + Phosphoadenosine + + + + + + + + + + + A protein modification that effectively crosslinks an L-histidine residue and 5'-phosphouridine through a phosphoramide ester bond to form 1'-(phospho-5'-uridine)-L-histidine. + 306.17 + C 9 H 11 N 2 O 8 P 1 + 306.0253 + C 15 H 18 N 5 O 9 P 1 + 443.31 + 443.08423 + H + natural + Unimod:417 + uniprot.ptm:PTM-0500 + (S)-2-amino-3-[1-(5'-uridine phosphono)imidazol-4-yl]propanoic acid + 1'-(phospho-5'-uridine)-L-histidine + ACT_SITE Tele-UMP-histidine intermediate + L-histidine 5'-uridine phosphoramidester + L-histidine monoanhydride with 5'-uridylic acid + MOD_RES O-UMP-histidine + N(tau)-5'-uridylic-L-histidine + N1'-uridylylated histidine + tele-5'-uridylic-L-histidine + PSI-MOD + PhosphoUridine + uridine phosphodiester + MOD:00377 + + 1'-(phospho-5'-uridine)-L-histidine + + + + + A protein modification that effectively crosslinks an L-histidine residue and 5'-phosphouridine through a phosphoramide ester bond to form 1'-(phospho-5'-uridine)-L-histidine. + PubMed:11467524 + PubMed:321007 + PubMed:380639 + PubMed:8794735 + RESID:AA0372 + Unimod:417#H + + + + + (S)-2-amino-3-[1-(5'-uridine phosphono)imidazol-4-yl]propanoic acid + + + + + + 1'-(phospho-5'-uridine)-L-histidine + + + + + + ACT_SITE Tele-UMP-histidine intermediate + + + + + + L-histidine 5'-uridine phosphoramidester + + + + + + L-histidine monoanhydride with 5'-uridylic acid + + + + + + MOD_RES O-UMP-histidine + + + + + + N(tau)-5'-uridylic-L-histidine + + + + + + N1'-uridylylated histidine + + + + + + tele-5'-uridylic-L-histidine + + + + + + PhosphoUridine + + + + + + uridine phosphodiester + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl semialdehyde. + -16.0 + C 0 H 0 N 0 O -1 + -15.994915 + C 4 H 5 N 1 O 2 + 99.09 + 99.03203 + D + natural + Unimod:447 + uniprot.ptm:PTM-0064 + (S)-2-amino-4-oxobutanoic acid + L-aminosuccinaldehydic acid + L-aminosuccinic acid semialdehyde + L-aspartate-beta-semialdehyde + L-aspartic beta-semialdehyde + L-aspartyl aldehyde + L-beta-formylalanine + MOD_RES Aspartyl aldehyde + aspartyl 4-semialdehyde + aspartyl aldehyde + PSI-MOD + Deoxy + reduction + MOD:00378 + + L-aspartyl semialdehyde + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl semialdehyde. + PubMed:1093385 + PubMed:14235557 + PubMed:15237995 + RESID:AA0373 + Unimod:447#D + + + + + (S)-2-amino-4-oxobutanoic acid + + + + + + L-aminosuccinaldehydic acid + + + + + + L-aminosuccinic acid semialdehyde + + + + + + L-aspartate-beta-semialdehyde + + + + + + L-aspartic beta-semialdehyde + + + + + + L-aspartyl aldehyde + + + + + + L-beta-formylalanine + + + + + + MOD_RES Aspartyl aldehyde + + + + + + aspartyl 4-semialdehyde + + + + + + aspartyl aldehyde + + + + + + Deoxy + + + + + + reduction + + + + + + + + + + A protein modification that effectively converts an L-serine residue to L-serine microcin E492 siderophore ester. + 831.69 + C 36 H 37 N 3 O 20 + 831.197 + C 39 H 43 N 4 O 23 + 935.78 + 935.2318 + S + natural + C-term + Unimod:448 + uniprot.ptm:PTM-0276 + L-serine microcin E492 siderophore ester + MOD_RES Serine microcin E492 siderophore ester + N-[5-(6-O-seryl-beta-glucosyl)-2,3-dihydroxybenzoyl]-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)seryl]seryl]serine + PSI-MOD + Microcin + microcin E492 siderophore ester from serine + MOD:00379 + Unimod origin corrected [JSG]. + L-serine microcin E492 siderophore ester + + + + + A protein modification that effectively converts an L-serine residue to L-serine microcin E492 siderophore ester. + PubMed:15102848 + RESID:AA0374 + Unimod:448#C-term + + + + + L-serine microcin E492 siderophore ester + + + + + + MOD_RES Serine microcin E492 siderophore ester + + + + + + N-[5-(6-O-seryl-beta-glucosyl)-2,3-dihydroxybenzoyl]-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)seryl]seryl]serine + + + + + + Microcin + + + + + + microcin E492 siderophore ester from serine + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide). + 1572.02 + C 40 H 47 Mo 1 N 20 O 26 P 4 S 4 + 1572.9857 + C 44 H 52 Mo 1 N 21 O 29 P 4 S 4 + 1687.1 + 1688.0127 + D + natural + Unimod:424 + 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide + L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide) + bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-aspartyl-molybdenum + nitrate reductase A aspartyl Mo-bisMGD cofactor + phosphoric acid 4-(2-amino-4-oxo-3,4,5,6,-tetrahydro-pteridin-6-yl)-2-hydroxy-3,4-dimercapto-but-3-en-yl ester guanylate ester + PSI-MOD + MolybdopterinGD + molybdenum bis(molybdopterin guanine dinucleotide) + MOD:00380 + L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide) + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide). + PubMed:12910261 + PubMed:14725769 + RESID:AA0375 + Unimod:424#D + + + + + 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide + + + + + + L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide) + + + + + + bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-aspartyl-molybdenum + + + + + + nitrate reductase A aspartyl Mo-bisMGD cofactor + + + + + + phosphoric acid 4-(2-amino-4-oxo-3,4,5,6,-tetrahydro-pteridin-6-yl)-2-hydroxy-3,4-dimercapto-but-3-en-yl ester guanylate ester + + + + + + MolybdopterinGD + + + + + + molybdenum bis(molybdopterin guanine dinucleotide) + + + + + + + + + + + + A protein modification that effectively converts an L-selenocysteine residue to L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide). + 1691.97 + C 40 H 47 N 20 O 26 P 4 S 5 Se 0 W 1 + 1691.0034 + C 43 H 52 N 21 O 27 P 4 S 5 Se 1 W 1 + 1842.02 + 1841.957 + U + natural + PSI-MOD + MOD:00381 + L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide) (Sec) + + + + + A protein modification that effectively converts an L-selenocysteine residue to L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide). + PubMed:11372198 + PubMed:12220497 + RESID:AA0376#SEC + + + + + + + + + + A protein modification that effectively crosslinks an L-methionyl-L-tyrosine dipeptide to form 3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one. + -20.03 + C 0 H -4 N 0 O -1 S 0 + -20.026215 + C 14 H 15 N 2 O 2 S 1 + 275.35 + 275.08542 + M, Y + hypothetical + N-term + 3-(2-methylsulfanyl)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one + 3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-amino-3,6-didehydropyrazin-2-ol + 3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one + GFP-like chromoprotein asFP595 chromophore + L-methionyl-L-tyrosyl-2-keto-5-iminopiperazine + PSI-MOD + MOD:00382 + carboxamidine; cross-link 1. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. + 3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one + + + + + A protein modification that effectively crosslinks an L-methionyl-L-tyrosine dipeptide to form 3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one. + PubMed:10852900 + PubMed:11259412 + PubMed:15491166 + RESID:AA0377 + + + + + 3-(2-methylsulfanyl)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one + + + + + + 3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-amino-3,6-didehydropyrazin-2-ol + + + + + + 3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one + + + + + + GFP-like chromoprotein asFP595 chromophore + + + + + + L-methionyl-L-tyrosyl-2-keto-5-iminopiperazine + + + + + + + + + + + + A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue to form 2-imino-glutamic acid 5-imidazolinone glycine. + -20.03 + C 0 H -4 N 0 O -1 + -20.026215 + C 7 H 6 N 2 O 3 + 166.14 + 166.03784 + E, G + hypothetical + uniprot.ptm:PTM-0014 + 2,N-didehydroglutamyl-5-imidazolinone glycine + 2-(3-carboxy-1-iminopropyl)-1-carboxymethyl-1-imidazolin-5-one + 2-imino-glutamic acid 5-imidazolinone glycine + 2-imino-glutamyl-5-imidazolinone glycine + 4-[1-(carboxymethyl)-5-oxo-4,5-dihydro-1H-imidazol-2-yl]-4-iminobutanoic acid + CROSSLNK 2-iminomethyl-5-imidazolinone (Glu-Gly) + [2-(3-carboxy-1-iminopropyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid + para-hydroxybenzylidene-imidazolidinone chromophore + PSI-MOD + MOD:00383 + Cross-link 2; carboxamidine; cross-link 1; incidental to RESID:AA0183; incidental to RESID:AA0365. + 2-imino-glutamic acid 5-imidazolinone glycine + + + + + A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue to form 2-imino-glutamic acid 5-imidazolinone glycine. + PubMed:11682051 + RESID:AA0378 + + + + + 2,N-didehydroglutamyl-5-imidazolinone glycine + + + + + + 2-(3-carboxy-1-iminopropyl)-1-carboxymethyl-1-imidazolin-5-one + + + + + + 2-imino-glutamic acid 5-imidazolinone glycine + + + + + + 2-imino-glutamyl-5-imidazolinone glycine + + + + + + 4-[1-(carboxymethyl)-5-oxo-4,5-dihydro-1H-imidazol-2-yl]-4-iminobutanoic acid + + + + + + CROSSLNK 2-iminomethyl-5-imidazolinone (Glu-Gly) + + + + + + [2-(3-carboxy-1-iminopropyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid + + + + + + para-hydroxybenzylidene-imidazolidinone chromophore + + + + + + + + + + + + A protein modification that effectively crosslinks an L-methionine residue and a glycine residue to form 2-imino-methionine 5-imidazolinone glycine. + -20.03 + C 0 H -4 N 0 O -1 S 0 + -20.026215 + C 7 H 8 N 2 O 1 S 1 + 168.21 + 168.03574 + G, M + natural + uniprot.ptm:PTM-0015 + (2-[1-imino-3-(methylsulfanyl)propyl]-5-oxo-4,5-dihydro-imidazol-1-yl)acetic acid + (2-[3-(methylsulfanyl)propanimidoyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid + 2,N-didehydromethionyl-5-imidazolinone glycine + 2-[1-imino-3-(methylsulfanyl)propyl]-1-carboxymethyl-1-imidazolin-5-one + 2-imino-methionine 5-imidazolinone glycine + 2-imino-methionyl-5-imidazolinone glycine + CROSSLNK 2-iminomethyl-5-imidazolinone (Met-Gly) + GFP-like chromoprotein asFP595 chromophore + para-hydroxybenzylidene-imidazolidinone chromophore + red fluorescent protein eqFP611 chromophore + PSI-MOD + MOD:00384 + Cross-link 2; carboxamidine; cross-link 1; incidental to RESID:AA0183; incidental to RESID:AA0365. + 2-imino-methionine 5-imidazolinone glycine + + + + + A protein modification that effectively crosslinks an L-methionine residue and a glycine residue to form 2-imino-methionine 5-imidazolinone glycine. + PubMed:10852900 + PubMed:12185250 + PubMed:12909624 + PubMed:15542608 + RESID:AA0379 + + + + + (2-[1-imino-3-(methylsulfanyl)propyl]-5-oxo-4,5-dihydro-imidazol-1-yl)acetic acid + + + + + + (2-[3-(methylsulfanyl)propanimidoyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid + + + + + + 2,N-didehydromethionyl-5-imidazolinone glycine + + + + + + 2-[1-imino-3-(methylsulfanyl)propyl]-1-carboxymethyl-1-imidazolin-5-one + + + + + + 2-imino-methionine 5-imidazolinone glycine + + + + + + 2-imino-methionyl-5-imidazolinone glycine + + + + + + CROSSLNK 2-iminomethyl-5-imidazolinone (Met-Gly) + + + + + + GFP-like chromoprotein asFP595 chromophore + + + + + + para-hydroxybenzylidene-imidazolidinone chromophore + + + + + + red fluorescent protein eqFP611 chromophore + + + + + + + + + + + + + A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue to form L-asparagine 5-imidazolinone glycine. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 6 H 7 N 3 O 2 + 153.14 + 153.05383 + G, N + hypothetical + uniprot.ptm:PTM-0046 + (2-[(1S)-1,3-diamino-3-oxopropyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid + 2-[(S)-1,3-diamino-3-oxopropyl]-1-carboxymethyl-1-imidazolin-5-one + CROSSLNK 5-imidazolinone (Asn-Gly) + L-asparagine 5-imidazolinone glycine + Zoanthus sp. fluorescent protein FP506 chromophore + [2-(1,3-diamino-3-oxopropyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid + asparaginyl-5-imidazolinone glycine + para-hydroxybenzylidene-imidazolidinone chromophore + PSI-MOD + MOD:00385 + Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365. + L-asparagine 5-imidazolinone glycine + + + + + A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue to form L-asparagine 5-imidazolinone glycine. + PubMed:10504696 + RESID:AA0380 + + + + + (2-[(1S)-1,3-diamino-3-oxopropyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid + + + + + + 2-[(S)-1,3-diamino-3-oxopropyl]-1-carboxymethyl-1-imidazolin-5-one + + + + + + CROSSLNK 5-imidazolinone (Asn-Gly) + + + + + + L-asparagine 5-imidazolinone glycine + + + + + + Zoanthus sp. fluorescent protein FP506 chromophore + + + + + + [2-(1,3-diamino-3-oxopropyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid + + + + + + asparaginyl-5-imidazolinone glycine + + + + + + para-hydroxybenzylidene-imidazolidinone chromophore + + + + + + + + + + + + + A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form L-lysine 5-imidazolinone glycine. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 8 H 13 N 3 O 1 + 167.21 + 167.10587 + G, K + hypothetical + uniprot.ptm:PTM-0048 + (2-[(1S)-1,5-diaminopentyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid + 2-[(S)-1,5-diaminopentanyl]-1-carboxymethyl-1-imidazolin-5-one + Anemonia majano fluorescent protein FP486 chromophore + CROSSLNK 5-imidazolinone (Lys-Gly) + L-lysine 5-imidazolinone glycine + [2-(1,5-diaminopentanyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid + lysyl-5-imidazolinone glycine + para-hydroxybenzylidene-imidazolidinone chromophore + PSI-MOD + MOD:00386 + Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365. + L-lysine 5-imidazolinone glycine + + + + + A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form L-lysine 5-imidazolinone glycine. + PubMed:10504696 + RESID:AA0381 + + + + + (2-[(1S)-1,5-diaminopentyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid + + + + + + 2-[(S)-1,5-diaminopentanyl]-1-carboxymethyl-1-imidazolin-5-one + + + + + + Anemonia majano fluorescent protein FP486 chromophore + + + + + + CROSSLNK 5-imidazolinone (Lys-Gly) + + + + + + L-lysine 5-imidazolinone glycine + + + + + + [2-(1,5-diaminopentanyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid + + + + + + lysyl-5-imidazolinone glycine + + + + + + para-hydroxybenzylidene-imidazolidinone chromophore + + + + + + + + + + + + A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form 2-tetrahydropyridinyl-5-imidazolinone glycine. + -37.06 + C 0 H -7 N -1 O -1 + -37.052765 + C 8 H 9 N 2 O 1 + 149.17 + 149.07149 + G, K + natural + N-term + uniprot.ptm:PTM-0018 + 2-(3,4,5,6-tetrahydropyridin-2-yl)-1-carboxymethyl-1-imidazolin-5-one + 2-(tetrahydropyrid-2-yl)-5-imidazolinone glycine + 2-tetrahydropyridinyl-5-imidazolinone glycine + CROSSLNK 2-tetrahydro-2-pyridyl-5-imidazolinone (Lys-Gly) + Zoanthus sp. fluorescent protein zFP538 chromophore + [5-oxo-2-(3,4,5,6-tetrahydropyridin-2-yl)-4,5-dihydro-1H-imidazol-1-yl]acetic acid + para-hydroxybenzylidene-imidazolidinone chromophore + PSI-MOD + MOD:00387 + Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365. + 2-tetrahydropyridinyl-5-imidazolinone glycine + + + + + A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form 2-tetrahydropyridinyl-5-imidazolinone glycine. + PubMed:10504696 + PubMed:15628861 + RESID:AA0382 + + + + + 2-(3,4,5,6-tetrahydropyridin-2-yl)-1-carboxymethyl-1-imidazolin-5-one + + + + + + 2-(tetrahydropyrid-2-yl)-5-imidazolinone glycine + + + + + + 2-tetrahydropyridinyl-5-imidazolinone glycine + + + + + + CROSSLNK 2-tetrahydro-2-pyridyl-5-imidazolinone (Lys-Gly) + + + + + + Zoanthus sp. fluorescent protein zFP538 chromophore + + + + + + [5-oxo-2-(3,4,5,6-tetrahydropyridin-2-yl)-4,5-dihydro-1H-imidazol-1-yl]acetic acid + + + + + + [5-oxo-2-(3,4,5,6-tetrahydropyridin-2-yl)-4,5-dihydro-1H-imidazol-1-yl]acetic acid + + + + + + para-hydroxybenzylidene-imidazolidinone chromophore + + + + + + + + + + + A protein modification that effectively attaches an L-alanine residue to murein peptidoglycan by a pentaglycine linker peptide. + A + hypothetical + C-term + uniprot.ptm:PTM-0245 + (2R,6S)-2-(N-mureinyl-(R)-alanyl-(S)-isoglutamyl)amino-6-(alanyl-pentaglycyl)amino-pimeloyl-(S)-alanyl-(S)-alanine + L-alanyl-pentaglycyl-murein peptidoglycan + MOD_RES Pentaglycyl murein peptidoglycan amidated alanine + PSI-MOD + MOD:00388 + L-alanyl-pentaglycyl-murein peptidoglycan + + + + + A protein modification that effectively attaches an L-alanine residue to murein peptidoglycan by a pentaglycine linker peptide. + PubMed:8163519 + RESID:AA0383 + + + + + (2R,6S)-2-(N-mureinyl-(R)-alanyl-(S)-isoglutamyl)amino-6-(alanyl-pentaglycyl)amino-pimeloyl-(S)-alanyl-(S)-alanine + + + + + + L-alanyl-pentaglycyl-murein peptidoglycan + + + + + + MOD_RES Pentaglycyl murein peptidoglycan amidated alanine + + + + + + + + + + + + A protein modification that effectively converts an L-proline residue to N-formyl-L-proline. + 28.01 + C 1 H 0 N 0 O 1 + 27.994915 + C 6 H 8 N 1 O 2 + 126.14 + 126.055504 + P + hypothetical + N-term + Unimod:122 + (2S)-1-formylpyrrolidine-2-carboxylic acid + 1-formyl-2-pyrrolidinecarboxylic acid + 1-formylproline + N-formyl-L-proline + N-formylated L-proline + NFoPro + PSI-MOD + MOD:00389 + CAUTION - observations of this modification can be attributed to unintended artifactual production, or to spurious peptide MS identification. This modification is probably not a natural post-translational modification [JSG]. + N-formyl-L-proline + + + + + A protein modification that effectively converts an L-proline residue to N-formyl-L-proline. + PubMed:12051774 + PubMed:5464655 + RESID:AA0384 + Unimod:122#N-term + + + + + (2S)-1-formylpyrrolidine-2-carboxylic acid + + + + + + 1-formyl-2-pyrrolidinecarboxylic acid + + + + + + 1-formylproline + + + + + + N-formyl-L-proline + + + + + + N-formylated L-proline + + + + + + NFoPro + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-decanoyl-L-serine. + 154.25 + C 10 H 18 N 0 O 1 + 154.13576 + C 13 H 23 N 1 O 3 + 241.33 + 241.1678 + S + natural + Unimod:449 + uniprot.ptm:PTM-0234 + (2S)-2-amino-3-(decanoyloxy)propanoic acid + L-serine decanoate ester + LIPID O-decanoyl serine + O-decanoyl-L-serine + O-decanoylated L-serine + O3-decanoyl-L-serine + ODecSer + PSI-MOD + Decanoyl + lipid + MOD:00390 + O-decanoyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-decanoyl-L-serine. + PubMed:12630926 + RESID:AA0385 + Unimod:449#S + + + + + (2S)-2-amino-3-(decanoyloxy)propanoic acid + + + + + + L-serine decanoate ester + + + + + + LIPID O-decanoyl serine + + + + + + O-decanoyl-L-serine + + + + + + O-decanoylated L-serine + + + + + + O3-decanoyl-L-serine + + + + + + ODecSer + + + + + + Decanoyl + + + + + + lipid + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-octanoyl-L-threonine. + 126.2 + C 8 H 14 N 0 O 1 + 126.10446 + C 12 H 21 N 1 O 3 + 227.3 + 227.15215 + T + natural + Unimod:426 + uniprot.ptm:PTM-0240 + (2S)-2-amino-3-(octanoyloxy)butanoic acid + L-threonine octanoate ester + LIPID O-octanoyl threonine + O-octanoyl-L-threonine + O-octanoylated L-threonine + O3-octanoyl-L-threonine + OOctThr + PSI-MOD + Octanoyl + octanoyl + MOD:00391 + + O-octanoyl-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-octanoyl-L-threonine. + PubMed:11546772 + PubMed:12716131 + RESID:AA0386 + Unimod:426#T + + + + + (2S)-2-amino-3-(octanoyloxy)butanoic acid + + + + + + L-threonine octanoate ester + + + + + + LIPID O-octanoyl threonine + + + + + + O-octanoyl-L-threonine + + + + + + O-octanoylated L-threonine + + + + + + O3-octanoyl-L-threonine + + + + + + OOctThr + + + + + + Octanoyl + + + + + + octanoyl + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-decanoyl-L-threonine. + 154.25 + C 10 H 18 N 0 O 1 + 154.13576 + C 14 H 25 N 1 O 3 + 255.36 + 255.18344 + T + natural + Unimod:449 + uniprot.ptm:PTM-0235 + (2S)-2-amino-3-(decanoyloxy)propanoic acid + L-threonine decanoate ester + LIPID O-decanoyl threonine + O-decanoyl-L-threonine + O-decanoylated L-threonine + O3-decanoyl-L-threonine + ODecThr + PSI-MOD + Decanoyl + lipid + MOD:00392 + O-decanoyl-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-decanoyl-L-threonine. + PubMed:11546772 + RESID:AA0387 + Unimod:449#T + + + + + (2S)-2-amino-3-(decanoyloxy)propanoic acid + + + + + + L-threonine decanoate ester + + + + + + LIPID O-decanoyl threonine + + + + + + O-decanoyl-L-threonine + + + + + + O-decanoylated L-threonine + + + + + + O3-decanoyl-L-threonine + + + + + + ODecThr + + + + + + Decanoyl + + + + + + lipid + + + + + + + + + + A protein modification that effectively replaces a hydroxyl group hydrogen with a methyl group to produce either an ether from an alcohol or an ester from an acid. + OMeRes + PSI-MOD + MOD:00393 + + O-methylated residue + + + + + A protein modification that effectively replaces a hydroxyl group hydrogen with a methyl group to produce either an ether from an alcohol or an ester from an acid. + PubMed:18688235 + + + + + OMeRes + + + + + + + + + + A protein modification that effectively replaces one hydrogen atom with one acetyl group. + 42.04 + C 2 H 2 O 1 + 42.010567 + X + artifact + Unimod:1 + Ac1Res + Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac) + PSI-MOD + Acetyl + Acetylation + MOD:00394 + + Amino hydrogens are replaced to produce amides; hydroxyl hydrogens are replaced to produce esters; and hydrosulfanyl (thiol) hydrogens are replaced to produce sulfanyl esters (thiol esters). From DeltaMass: Average Mass: 42 + monoacetylated residue + + + + + A protein modification that effectively replaces one hydrogen atom with one acetyl group. + DeltaMass:0 + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + PubMed:14730666 + PubMed:15350136 + Unimod:1 + + + + + Ac1Res + + + + + + Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac) + + + + + + Acetyl + + + + + + Acetylation + + + + + + + + + + + A protein modification that crosslinks two residues by formation of a thioester bond between a cysteine thiol and either an alpha-carbonyl, as in S-(L-methionyl-L-cysteine), or a sidechain carbonyl, as in S-(L-isoglutamyl)-L-cysteine. + PSI-MOD + MOD:00395 + + thioester crosslinked residues + + + + + A protein modification that crosslinks two residues by formation of a thioester bond between a cysteine thiol and either an alpha-carbonyl, as in S-(L-methionyl-L-cysteine), or a sidechain carbonyl, as in S-(L-isoglutamyl)-L-cysteine. + PubMed:18688235 + + + + + + + + + A protein modification that effectively replaces a residue hydrogen atom on an oxygen with a carbohydrate-like group through a glycosidic bond. + OGlycoRes + PSI-MOD + MOD:00396 + + O-glycosylated residue + + + + + A protein modification that effectively replaces a residue hydrogen atom on an oxygen with a carbohydrate-like group through a glycosidic bond. + PubMed:18688235 + + + + + OGlycoRes + + + + + + + + + + A protein modification that is produced by reaction with iodoacetamide, usually replacement of a reactive hydrogen with a methylcarboxamido group. + 57.05 + C 2 H 3 N 1 O 1 + 57.021465 + X + artifact + Unimod:4 + PSI-MOD + Carbamidomethyl + Iodoacetamide derivative + MOD:00397 + + iodoacetamide derivatized residue + + + + + A protein modification that is produced by reaction with iodoacetamide, usually replacement of a reactive hydrogen with a methylcarboxamido group. + PubMed:11327326 + PubMed:11510821 + PubMed:12422359 + Unimod:4 + + + + + Carbamidomethyl + + + + + + Iodoacetamide derivative + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a carbamoyl (carboxamido) group. Replacement of an amino hydrogen produces a ureido group. + 43.02 + C 1 H 1 N 1 O 1 + 43.005814 + X + Unimod:5 + Carbamylation + PSI-MOD + Carbamyl + Carbamylation + MOD:00398 + + This modification can be produced by hydrogen cyanate, either used as a reagent or as released by urea degradation in solution [JSG]. + carbamoylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with a carbamoyl (carboxamido) group. Replacement of an amino hydrogen produces a ureido group. + DeltaMass:56 + PubMed:10978403 + PubMed:12203680 + Unimod:5 + + + + + Carbamylation + + + + + + Carbamyl + + + + + + Carbamylation + + + + + + + + + + A protein modification that is produced by reaction with iodoacetic acid, usually replacement of a reactive hydrogen with a methylcarboxy group. + 58.04 + C 2 H 2 O 2 + 58.005478 + X + artifact + Unimod:6 + Carboxymethyl (on Cysteine) + PSI-MOD + Carboxymethyl + Iodoacetic acid derivative + MOD:00399 + + From DeltaMass: Average Mass: 58 Abbreviation:CmC Average Mass Change:58 Notes:Cysteine reacts with iodoacetic acid to produce carboxymethyl cysteine. + iodoacetic acid derivatized residue + + + + + A protein modification that is produced by reaction with iodoacetic acid, usually replacement of a reactive hydrogen with a methylcarboxy group. + DeltaMass:64 + Unimod:6 + + + + + Carboxymethyl (on Cysteine) + + + + + + Carboxymethyl + + + + + + Iodoacetic acid derivative + + + + + + + + + + A protein modification that effectively replaces a carboxamido group with a carboxyl group, with both a gain of oxygen and loss of a nitrogen and a hydrogen. + 0.98 + H -1 N -1 O 1 + 0.984016 + X + Unimod:7 + Deamidation of Asparagine and Glutamine to Aspartate and Glutamate + dNRes + deamidationkq + PSI-MOD + Deamidated + Deamidation + MOD:00400 + + From DeltaMass: References:Vish Katta. + deamidated residue + + + + + A protein modification that effectively replaces a carboxamido group with a carboxyl group, with both a gain of oxygen and loss of a nitrogen and a hydrogen. + DeltaMass:32 + OMSSA:4 + Unimod:7 + + + + + Deamidation of Asparagine and Glutamine to Aspartate and Glutamate + + + + + + dNRes + + + + + + deamidationkq + + + + + + Deamidated + + + + + + Deamidation + + + + + + + + + + + A protein modification that is produced by formation of an adduct of a cysteine residue with the Gygi isotope-coded affinity tag d0 reagent. + 486.63 + C 22 H 38 N 4 O 6 S 1 + 486.25122 + C 25 H 43 N 5 O 7 S 2 + 589.77 + 589.2604 + C + artifact + Unimod:8 + PSI-MOD + Gygi ICAT(TM) d0 + ICAT-G + MOD:00401 + Gygi ICAT(TM) d0 modified cysteine + + + + + A protein modification that is produced by formation of an adduct of a cysteine residue with the Gygi isotope-coded affinity tag d0 reagent. + PubMed:10504701 + Unimod:8#C + + + + + Gygi ICAT(TM) d0 + + + + + + ICAT-G + + + + + + + + + + + A protein modification that is produced by formation of an adduct of a cysteine residue with the Gygi isotope-coded affinity tag d8 reagent. + 494.3 + C 22 (1)H 30 (2)H 8 N 4 O 6 S 1 + 494.30142 + C 25 (1)H 35 (2)H 8 N 5 O 7 S 2 + 597.31 + 597.3106 + C + artifact + Unimod:9 + PSI-MOD + Gygi ICAT(TM) d8 + ICAT-G:2H(8) + MOD:00402 + Gygi ICAT(TM) d8 modified cysteine + + + + + A protein modification that is produced by formation of an adduct of a cysteine residue with the Gygi isotope-coded affinity tag d8 reagent. + PubMed:10504701 + Unimod:9#C + + + + + Gygi ICAT(TM) d8 + + + + + + ICAT-G:2H(8) + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to homoserine. + -30.09 + C -1 H -2 O 1 S -1 + -29.992805 + C 4 H 7 N 1 O 2 + 101.1 + 101.047676 + M + artifact + C-term + Unimod:10 + Homoserine formed from Met by CNBr treatment + ctermpephsem + PSI-MOD + Homoserine + Met->Hse + MOD:00403 + + Usually formed from methionine by reaction with cyanogen bromide, CNBr, which cleaves the peptide at the methionine carboxyl group and the following residue amino group. + homoserine + + + + + A protein modification that effectively converts an L-methionine residue to homoserine. + DeltaMass:113 + OMSSA:56 + Unimod:10#M + + + + + Homoserine formed from Met by CNBr treatment + + + + + + ctermpephsem + + + + + + Homoserine + + + + + + Met->Hse + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to homoserine lactone. + -48.1 + C -1 H -4 S -1 + -48.003372 + C 4 H 5 N 1 O 1 + 83.09 + 83.03712 + M + artifact + C-term + Unimod:11 + ctermpephselactm + PSI-MOD + Homoserine lactone + Met->Hsl + MOD:00404 + + Usually formed from methionine by reaction with cyanogen bromide, CNBr, which cleaves the peptide at the methionine carboxyl group. Under acid conditions the homoserine dehydrates to form the cyclic lactone. + homoserine lactone + + + + + A protein modification that effectively converts an L-methionine residue to homoserine lactone. + DeltaMass:90 + OMSSA:57 + Unimod:11#M + + + + + ctermpephselactm + + + + + + Homoserine lactone + + + + + + Met->Hsl + + + + + + + + + + + A protein modification that is produced by formation of an adduct of a cysteine residue with the Applied Biosystems original isotope-coded affinity tag d8 reagent. + 450.28 + C 20 (1)H 26 (2)H 8 N 4 O 5 S 1 + 450.2752 + C 23 (1)H 31 (2)H 8 N 5 O 6 S 2 + 553.28 + 553.28436 + C + artifact + Unimod:12 + PSI-MOD + Applied Biosystems original ICAT(TM) d8 + ICAT-D:2H(8) + MOD:00405 + + Applied Biosystems original ICAT(TM) d8 modified cysteine + + + + + A protein modification that is produced by formation of an adduct of a cysteine residue with the Applied Biosystems original isotope-coded affinity tag d8 reagent. + Unimod:12#C + + + + + Applied Biosystems original ICAT(TM) d8 + + + + + + ICAT-D:2H(8) + + + + + + + + + + + A protein modification that is produced by formation of an adduct of a cysteine residue with the Applied Biosystems original isotope-coded affinity tag d0 reagent. + 442.22 + C 20 (1)H 34 N 4 O 5 S 1 + 442.225 + C 23 (1)H 39 N 5 O 6 S 2 + 545.23 + 545.2342 + C + artifact + Unimod:13 + PSI-MOD + Applied Biosystems original ICAT(TM) d0 + ICAT-D + MOD:00406 + + Applied Biosystems original ICAT(TM) d0 modified cysteine + + + + + A protein modification that is produced by formation of an adduct of a cysteine residue with the Applied Biosystems original isotope-coded affinity tag d0 reagent. + Unimod:13#C + + + + + Applied Biosystems original ICAT(TM) d0 + + + + + + ICAT-D + + + + + + + + + A protein modification that effectively replaces a carboxyl group with a carboxy methyl ester group. OBSOLETE because Unimod:14 merged with entry 34, remap to MOD:00599. + MOD:00599 + 14.03 + C 1 H 2 + 14.01565 + X + ResOMe + PSI-MOD + MOD:00407 + residue methyl ester + true + + + + + A protein modification that effectively replaces a carboxyl group with a carboxy methyl ester group. OBSOLETE because Unimod:14 merged with entry 34, remap to MOD:00599. + PubMed:18688235 + + + + + ResOMe + + + + + + + + + + + A protein modification that effectively replaces a residue amino or imino hydrogen with an acetyl group. + 42.04 + C 2 H 2 O 1 + 42.010567 + X + N-Acetyl + N-Acetylation + NAcRes + PSI-MOD + MOD:00408 + + mono N-acetylated residue + + + + + A protein modification that effectively replaces a residue amino or imino hydrogen with an acetyl group. + PubMed:18688235 + + + + + N-Acetyl + + + + + + N-Acetylation + + + + + + NAcRes + + + + + + + + + + + A protein modification that effectively replaces a residue amino group with a formamido group. + 28.01 + C 1 O 1 + 27.994915 + X + NFoRes + ntermformyl + ntermpepformyl + PSI-MOD + Formyl + MOD:00409 + + N-formylated residue + + + + + A protein modification that effectively replaces a residue amino group with a formamido group. + OMSSA:44 + OMSSA:82 + + + + + NFoRes + + + + + + ntermformyl + + + + + + ntermpepformyl + + + + + + Formyl + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-(N-isopropylcarboxamidomethyl)-L-cysteine. + 99.13 + C 5 H 9 N 1 O 1 S 0 + 99.06841 + C 8 H 14 N 2 O 2 S 1 + 202.27 + 202.0776 + C + artifact + Unimod:17 + nipcam + PSI-MOD + N-isopropylcarboxamidomethyl + NIPCAM + MOD:00410 + S-(N-isopropylcarboxamidomethyl)-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-(N-isopropylcarboxamidomethyl)-L-cysteine. + OMSSA:84 + PubMed:11465505 + PubMed:8465942 + Unimod:17#C + + + + + nipcam + + + + + + N-isopropylcarboxamidomethyl + + + + + + NIPCAM + + + + + + + + + modification from Unimod Isotopic label. OBSOLETE because Unimod:18 is now merged with entry 258 remap to MOD:00581 'single 018 label' + MOD:00581 + 2.0 + (16)O -1 (18)O 1 + 2.004246 + X + artifact + PSI-MOD + MOD:00411 + A modification from Unimod:18 + O18 label + true + + + + + modification from Unimod Isotopic label. OBSOLETE because Unimod:18 is now merged with entry 258 remap to MOD:00581 'single 018 label' + PubMed:18688235 + + + + + + + + modification from Unimod artifact. OBSOLETE because Unimod entry 19 is now merged with Unimod 35 remap to MOD:00425 'monohydroxylated residue'. + MOD:00425 + 16.0 + O 1 + 15.994915 + X + PSI-MOD + MOD:00412 + oxidation + true + + + + + modification from Unimod artifact. OBSOLETE because Unimod entry 19 is now merged with Unimod 35 remap to MOD:00425 'monohydroxylated residue'. + PubMed:18688235 + + + + + + + + + + A protein modification that is produced by reaction of a cysteine residue with biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine. + 414.52 + C 18 H 30 N 4 O 5 S 1 + 414.1937 + C 21 H 35 N 5 O 6 S 2 + 517.66 + 517.2029 + C + artifact + Unimod:20 + PSI-MOD + Biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine + PEO-Iodoacetyl-LC-Biotin + MOD:00413 + biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine derivatized cysteine + + + + + A protein modification that is produced by reaction of a cysteine residue with biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine. + Unimod:20#C + + + + + Biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine + + + + + + PEO-Iodoacetyl-LC-Biotin + + + + + + + + + + + A protein modification that effectively replaces one hydrogen atom of an L-arginine residue with one methyl group. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 7 H 14 N 4 O 1 + 170.22 + 170.11676 + R + Unimod:34 + Me1Arg + N-methyl Arginyl + methylr + PSI-MOD + Methyl + MOD:00414 + + From DeltaMass: formula incorrect, N and O reversed + monomethylated L-arginine + + + + + A protein modification that effectively replaces one hydrogen atom of an L-arginine residue with one methyl group. + DeltaMass:215 + OMSSA:77 + Unimod:34#R + + + + + Me1Arg + + + + + + N-methyl Arginyl + + + + + + methylr + + + + + + Methyl + + + + + + + + + modification from Unimod - OBSOLETE because Unimod entry 22 is now merged with entry 21 remap to MOD:00696 'phosphorylated residue'. + MOD:00696 + 79.98 + H 1 O 3 P 1 + 79.96633 + X + artifact + PSI-MOD + MOD:00415 + phosphorylation without neutral loss + true + + + + + modification from Unimod - OBSOLETE because Unimod entry 22 is now merged with entry 21 remap to MOD:00696 'phosphorylated residue'. + PubMed:18688235 + + + + + + + + + + A change resulting in an alteration of the measured molecular mass of a peptide or protein hydroxyl amino acid phosphorylated promptly followed by secondary loss of a neutral trihydrogen phosphate molecular fragment. + -18.02 + H -2 O -1 + -18.010565 + X + artifact + Unimod:23 + PSI-MOD + Dehydrated + Dehydration + MOD:00416 + + O4-phosphotyrosine does not lose phosphate by this mechanism. Unimod does not provide a citation for this particular modification [JSG]. + phosphorylation of an hydroxyl amino acid with prompt loss of phosphate + + + + + A change resulting in an alteration of the measured molecular mass of a peptide or protein hydroxyl amino acid phosphorylated promptly followed by secondary loss of a neutral trihydrogen phosphate molecular fragment. + Unimod:23 + + + + + Dehydrated + + + + + + Dehydration + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-carboxamidoethyl-L-cysteine. + 71.08 + C 3 H 5 N 1 O 1 S 0 + 71.03712 + C 6 H 10 N 2 O 2 S 1 + 174.22 + 174.0463 + C + artifact + Unimod:24 + PAM-Cys + Propionamide or Acrylamide adduct + S-(3-amino-3-oxopropyl)cysteine + S-carbamoylethyl-L-cysteine + S-propanamide-L-cysteine + propionamidec + PSI-MOD + Acrylamide adduct + Propionamide + MOD:00417 + From DeltaMass: References: Anal. Biochem. Vol 216 No. 1 p131 (citation not found) Notes: Residual acrylamide in SDS gels can label free cysteines to produce propionamido-Cys (also known as PAM-Cys) + S-carboxamidoethyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-carboxamidoethyl-L-cysteine. + DeltaMass:72 + OMSSA:5 + PubMed:1481983 + Unimod:24#C + + + + + PAM-Cys + + + + + + Propionamide or Acrylamide adduct + + + + + + S-(3-amino-3-oxopropyl)cysteine + + + + + + S-carbamoylethyl-L-cysteine + + + + + + S-propanamide-L-cysteine + + + + + + propionamidec + + + + + + Acrylamide adduct + + + + + + Propionamide + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an (pyridin-3-yl)acetyl group. + 119.12 + C 7 H 5 N 1 O 1 + 119.03712 + X + artifact + Unimod:25 + PSI-MOD + Pyridylacetyl + pyridylacetyl + MOD:00418 + Produced by reaction with N-[(pyrid-3-yl)acetyl]oxy-succinimide [JSG]. + pyridylacetylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an (pyridin-3-yl)acetyl group. + PubMed:9276974 + Unimod:25 + + + + + Pyridylacetyl + + + + + + pyridylacetyl + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid. + 40.02 + C 2 H 0 N 0 O 1 S 0 + 39.994915 + C 5 H 6 N 1 O 2 S 1 + 144.17 + 144.01192 + C + artifact + N-term + Unimod:26 + (R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid + 5-oxothiomorpholine-3-carboxylic acid + Otc + S-carbamoylmethylcysteine cyclization (N-terminus) + PSI-MOD + Pyro-carbamidomethyl + S-carbamoylmethylcysteine cyclization (N-terminus) + MOD:00419 + From DeltaMass: A secondary modification affecting peptides with S-carbamoylmethyl-L-cysteine (CamC) at the N-terminus. These exist in enzymatic digests of proteins that have been S-alkylated with iodoacetamide. Cyclization of N-terminal CamC gives a residue of (R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid. Peptides in which this has occurred become more hydrophobic, and lose 17 Da from the N-terminal residue. + (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid + + + + + A protein modification that effectively converts an L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid. + DeltaMass:336 + PubMed:12643538 + Unimod:26#C + + + + + (R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid + + + + + + 5-oxothiomorpholine-3-carboxylic acid + + + + + + Otc + + + + + + S-carbamoylmethylcysteine cyclization (N-terminus) + + + + + + Pyro-carbamidomethyl + + + + + + S-carbamoylmethylcysteine cyclization (N-terminus) + + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to 2-pyrrolidone-5-carboxylic acid. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 5 H 6 N 1 O 2 + 112.11 + 112.039856 + E + artifact + N-term + Unimod:27 + uniprot.ptm:PTM-0262 + (2S)-5-oxo-2-pyrrolidinecarboxylic acid + 2-oxopyrrolidine-5-carboxylic acid + 2-pyrrolidone-5-carboxylic acid + 5-oxoproline + 5-oxopyrrolidine-2-carboxylic acid + 5-pyrrolidone-2-carboxylic acid + MOD_RES Pyrrolidone carboxylic acid (Glu) + PCA + PyrGlu(Glu) + Pyroglutamic Acid formed from Glutamic Acid + ntermpeppyroe + pyroglutamic acid + PSI-MOD + Glu->pyro-Glu + Pyro-glu from E + MOD:00420 + From DeltaMass: References: The conversion of glutamic acid to pyroglutamic was reported for the beta-amyloid protein. Miller et al. Arch. Biochem. Biophy. (1993) 301, 41-52 [DeltaMass]. The modification in amyloid protein is probably an artifact of treatment with strong acid under anhydrous conditions. Peptides with N-terminal glutamic acid isolated from single cells of Aplysia neurons show partial conversion to pyroglutamic acid, possibly dependent on a temperature sensitive factor [JSG]. + 2-pyrrolidone-5-carboxylic acid (Glu) + + + + + A protein modification that effectively converts an L-glutamic acid residue to 2-pyrrolidone-5-carboxylic acid. + DeltaMass:16 + OMSSA:109 + PubMed:10214721 + PubMed:1836357 + PubMed:3473473 + PubMed:8382902 + RESID:AA0031#GLU + Unimod:27#E + + + + + (2S)-5-oxo-2-pyrrolidinecarboxylic acid + + + + + + 2-oxopyrrolidine-5-carboxylic acid + + + + + + 2-pyrrolidone-5-carboxylic acid + + + + + + 5-oxoproline + + + + + + 5-oxopyrrolidine-2-carboxylic acid + + + + + + 5-pyrrolidone-2-carboxylic acid + + + + + + MOD_RES Pyrrolidone carboxylic acid (Glu) + + + + + + PCA + + + + + + PyrGlu(Glu) + + + + + + Pyroglutamic Acid formed from Glutamic Acid + + + + + + ntermpeppyroe + + + + + + pyroglutamic acid + + + + + + Glu->pyro-Glu + + + + + + Pyro-glu from E + + + + + + + + + + A protein modification that effectively replaces a residue hydrogen atom on a carbon with a carbohydrate-like group through a glycosidic bond. + CGlycoRes + PSI-MOD + MOD:00421 + + C-glycosylated residue + + + + + A protein modification that effectively replaces a residue hydrogen atom on a carbon with a carbohydrate-like group through a glycosidic bond. + PubMed:18688235 + + + + + CGlycoRes + + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a morpholine-2-acetyl group. + 127.14 + C 6 H 9 N 1 O 2 + 127.06333 + X + artifact + N-term + Unimod:29 + N-succinimidylmorpholine-2-acetate alpha-amino derivative + PSI-MOD + N-Succinimidyl-2-morpholine acetate + SMA + MOD:00422 + The Unimod name "N-Succinimidyl-3-morpholine acetate" appears to have been a typographical error [JSG]. + alpha-amino morpholine-2-acetylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a morpholine-2-acetyl group. + PubMed:10446193 + Unimod:29#N-term + + + + + N-succinimidylmorpholine-2-acetate alpha-amino derivative + + + + + + N-Succinimidyl-2-morpholine acetate + + + + + + SMA + + + + + + + + + + A protein modification that effectively substitutes one sodium atom for one hydrogen atom. + 21.98 + H -1 Na 1 + 21.981943 + X + Unimod:30 + Na1Res + Sodium + PSI-MOD + Cation:Na + Sodium adduct + MOD:00423 + + monosodium salt + + + + + A protein modification that effectively substitutes one sodium atom for one hydrogen atom. + DeltaMass:0 + Unimod:30 + + + + + Na1Res + + + + + + Sodium + + + + + + Cation:Na + + + + + + Sodium adduct + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-pyridylethyl-L-cysteine. + 105.14 + C 7 H 7 N 1 + 105.057846 + C 10 H 12 N 2 O 1 S 1 + 208.28 + 208.06703 + C + artifact + Unimod:31 + PECys + Pyridylethyl Cystenyl + S-pyridinylethyl-L-cysteine + spyridylethylc + vinylpyridine derivatized cysteine residue + PSI-MOD + Pyridylethyl + S-pyridylethylation + MOD:00424 + From DeltaMass: Formula:C10H12O2N1S1 (formula incorrect, N and O reversed) Monoisotopic Mass Change:208.067 Average Mass Change:208.286 (mass incorrect, aggregate not delta) References:PE Sciex + S-pyridylethyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-pyridylethyl-L-cysteine. + DeltaMass:253 + OMSSA:112 + PubMed:11760118 + PubMed:626389 + PubMed:8297018 + PubMed:8783016 + Unimod:31#C + + + + + PECys + + + + + + Pyridylethyl Cystenyl + + + + + + S-pyridinylethyl-L-cysteine + + + + + + spyridylethylc + + + + + + vinylpyridine derivatized cysteine residue + + + + + + Pyridylethyl + + + + + + S-pyridylethylation + + + + + + + + + + A protein modification that effectively replaces one hydrogen atom with a hydroxyl group. + 16.0 + O 1 + 15.994915 + X + Unimod:35 + Hy1Res + PSI-MOD + Oxidation + Oxidation or Hydroxylation + MOD:00425 + + monohydroxylated residue + + + + + A protein modification that effectively replaces one hydrogen atom with a hydroxyl group. + Unimod:35 + + + + + Hy1Res + + + + + + Oxidation + + + + + + Oxidation or Hydroxylation + + + + + + + + + + A protein modification that effectively replaces a residue hydrogen atom on a sulfur with a carbohydrate-like group through a glycosidic bond. + SGlycoRes + PSI-MOD + MOD:00426 + S-glycosylated residue + + + + + A protein modification that effectively replaces a residue hydrogen atom on a sulfur with a carbohydrate-like group through a glycosidic bond. + PubMed:18688235 + + + + + SGlycoRes + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a methyl group. + MeRes + Methylation (N terminus, N epsilon of Lysine, O of Serine, Threonine or C terminus, N of Asparagine) + PSI-MOD + MOD:00427 + + From DeltaMass: Average Mass: 14 Average Mass Change:14 References:Methylation of Asparagine (found in phycobiliproteins) Klotz and Glazer (1987) J. Biol. Chem. 262; 17350-17355 + methylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with a methyl group. + DeltaMass:36 + + + + + MeRes + + + + + + Methylation (N terminus, N epsilon of Lysine, O of Serine, Threonine or C terminus, N of Asparagine) + + + + + + + + + + A protein modification that effectively replaces two hydrogen atoms with two hydroxyl groups. + 32.0 + C 0 H 0 N 0 O 2 + 31.989828 + X + Unimod:425 + Hy2Res + PSI-MOD + Dioxidation + dihydroxy + MOD:00428 + + dihydroxylated residue + + + + + A protein modification that effectively replaces two hydrogen atoms with two hydroxyl groups. + PubMed:12686488 + Unimod:425 + + + + + Hy2Res + + + + + + Dioxidation + + + + + + dihydroxy + + + + + + + + + + A protein modification that effectively replaces two hydrogen atoms with two methyl groups. + 28.05 + C 2 H 4 + 28.0313 + X + Unimod:36 + Me2Res + N,N dimethylation (of Arginine or Lysine) + PSI-MOD + Dimethyl + di-Methylation + MOD:00429 + + For amino-terminal proline residues, dimethylation can effectively only be accomplished with a protonated imino group. This process accounts only for dimethylation and not protonation. The alternative Me2+Res process accounts for both protonation and dimethylation [JSG]. + dimethylated residue + + + + + A protein modification that effectively replaces two hydrogen atoms with two methyl groups. + DeltaMass:0 + PubMed:12964758 + PubMed:14570711 + Unimod:36 + + + + + Me2Res + + + + + + N,N dimethylation (of Arginine or Lysine) + + + + + + Dimethyl + + + + + + di-Methylation + + + + + + + + + + A protein modification that effectively replaces three hydrogen atoms with three methyl groups. + 42.08 + C 3 H 6 + 42.04695 + X + Unimod:37 + Me3Res + PSI-MOD + Trimethyl + tri-Methylation + MOD:00430 + + For amino acids residues, amine trimethylation can effectively only be accomplished with an aminium, protonated primary amino, group. This process accounts only for trimethylation and not protonation. The alternative Me3+Res process accounts for both protonation and trimethylation. + trimethylated residue + + + + + A protein modification that effectively replaces three hydrogen atoms with three methyl groups. + PubMed:12590383 + PubMed:3145979 + PubMed:4304194 + PubMed:6778808 + PubMed:7093227 + PubMed:8453381 + Unimod:37 + + + + + Me3Res + + + + + + Trimethyl + + + + + + tri-Methylation + + + + + + + + + + Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral molecular fragment. + NLModRes + PSI-MOD + MOD:00431 + + modified residue with a secondary neutral loss + + + + + Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral molecular fragment. + PubMed:18688235 + + + + + NLModRes + + + + + + + + + + Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral trihydrogen phosphate molecular fragment. + dPhosModRes + PSI-MOD + MOD:00432 + + modified residue with neutral loss of phosphate + + + + + Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral trihydrogen phosphate molecular fragment. + PubMed:18688235 + + + + + dPhosModRes + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an glucose group through a glycosidic bond. + 162.14 + C 6 H 10 N 0 O 5 + 162.05283 + X + GlcRes + PSI-MOD + MOD:00433 + + monoglucosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an glucose group through a glycosidic bond. + PubMed:18688235 + + + + + GlcRes + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexose sugar group through a glycosidic bond. + X + natural + Unimod:41 + Hex + Hexoses (Fru, Gal, Glc, Man) + O-Glycosyl- + PSI-MOD + Hex + Hexose + MOD:00434 + + From DeltaMass: Average Mass: 162 Formula:C6 H10 05 Monoisotopic Mass Change:162.053 Average Mass Change:162.143 References:PE Sciex. + hexosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexose sugar group through a glycosidic bond. + DeltaMass:203 + PubMed:15279557 + Unimod:41 + + + + + Hex + + + + + + Hexoses (Fru, Gal, Glc, Man) + + + + + + O-Glycosyl- + + + + + + Hex + + + + + + Hexose + + + + + + + + + + + + + + + + Covalent modification of a peptide or protein amino acid phosphorylated serine with a secondary loss of a neutral trihydrogen phosphate molecular fragment. + -97.99 + C 0 H -3 N 0 O -4 P -1 + -97.9769 + C 3 H 3 N 1 O 1 + 69.06 + 69.02146 + MOD:00046 + artifact + dPhosOPhosSer + PSI-MOD + MOD:00435 + + O-phospho-L-serine with neutral loss of phosphate + + + + + Covalent modification of a peptide or protein amino acid phosphorylated serine with a secondary loss of a neutral trihydrogen phosphate molecular fragment. + PubMed:18688235 + + + + + dPhosOPhosSer + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylhexosamine group through a glycosidic bond. + 203.19 + C 8 H 13 N 1 O 5 + 203.07938 + X + GNO:G29068FM + HexNAc + PSI-MOD + HexNAc + N-Acetylhexosamine + MOD:00436 + + N-acetylhexosaminylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylhexosamine group through a glycosidic bond. + PubMed:18688235 + + + + + HexNAc + + + + + + HexNAc + + + + + + N-Acetylhexosamine + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a farnesyl group. + 204.36 + C 15 H 24 + 204.1878 + X + natural + Unimod:44 + FarnRes + Farnesylation + PSI-MOD + Farnesyl + Farnesylation + MOD:00437 + + From DeltaMass: Average Mass: 204 + farnesylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with a farnesyl group. + DeltaMass:0 + PubMed:15609361 + Unimod:44 + + + + + FarnRes + + + + + + Farnesylation + + + + + + Farnesyl + + + + + + Farnesylation + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a myristoyl group. + 210.36 + C 14 H 26 O 1 + 210.19836 + X + natural + Unimod:45 + C14:0 aliphatic acylated residue + MyrRes + Myristoylation + PSI-MOD + Myristoyl + Myristoylation + MOD:00438 + + From DeltaMass: Average Mass: 210 + myristoylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with a myristoyl group. + DeltaMass:0 + Unimod:45 + + + + + C14:0 aliphatic acylated residue + + + + + + MyrRes + + + + + + Myristoylation + + + + + + Myristoyl + + + + + + Myristoylation + + + + + + + + + + + + + + + + + Covalent modification of a peptide or protein amino acid phosphorylated threonine with a secondary loss of a neutral trihydrogen phosphate molecular fragment. + -97.99 + C 0 H -3 N 0 O -4 P -1 + -97.9769 + C 4 H 5 N 1 O 1 + 83.09 + 83.03712 + MOD:00047 + artifact + dPhosOPhosThr + PSI-MOD + MOD:00439 + + O-phospho-L-threonine with neutral loss of phosphate + + + + + Covalent modification of a peptide or protein amino acid phosphorylated threonine with a secondary loss of a neutral trihydrogen phosphate molecular fragment. + PubMed:18688235 + + + + + dPhosOPhosThr + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a palmitoyl group. + 238.41 + C 16 H 30 O 1 + 238.22966 + X + natural + Hexadecanoylated residue + Palmitoylation + PamRes + PSI-MOD + Palmitoyl + Palmitoylation + MOD:00440 + + From DeltaMass: Average Mass: 238 + palmitoylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with a palmitoyl group. + DeltaMass:0 + + + + + Hexadecanoylated residue + + + + + + Palmitoylation + + + + + + PamRes + + + + + + Palmitoyl + + + + + + Palmitoylation + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a geranylgeranyl group. + 272.48 + C 20 H 32 + 272.2504 + X + natural + Unimod:48 + Geranylgeranylation + GergerRes + PSI-MOD + Geranyl-geranyl + GeranylGeranyl + MOD:00441 + + From DeltaMass: Average Mass: 272 + geranylgeranylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with a geranylgeranyl group. + DeltaMass:0 + PubMed:15609361 + Unimod:48 + + + + + Geranylgeranylation + + + + + + GergerRes + + + + + + Geranyl-geranyl + + + + + + GeranylGeranyl + + + + + + + + + + + Covalent modification of a peptide or protein L-arginine residue to protonated omega-N,omega-N'-dimethylated L-arginine with secondary loss of an N,N'-carbodiimide molecular fragment. + 42.04 + C 1 H 2 N 2 O 0 + 42.021797 + C 7 H 14 N 2 O 1 + 142.2 + 142.11061 + R + artifact + dCDI-NNMe2+Arg + PSI-MOD + MOD:00442 + protonated omega-N,omega-N'-dimethylated L-arginine with secondary neutral loss of N,N'-carbodiimide + + + + + Covalent modification of a peptide or protein L-arginine residue to protonated omega-N,omega-N'-dimethylated L-arginine with secondary loss of an N,N'-carbodiimide molecular fragment. + PubMed:15835918 + PubMed:18688235 + + + + + dCDI-NNMe2+Arg + + + + + + + + + + + Covalent modification of a peptide or protein L-arginine residue to protonated omega-N,omega-N-dimethlyated L-arginine with secondary neutral loss of an N,N-dimethylamine molecular fragment. + 59.09 + C 2 H 7 N 2 + 59.060925 + C 6 H 10 N 3 O 1 + 140.17 + 140.08238 + R + artifact + dDMA-NoMe2+Arg + PSI-MOD + MOD:00443 + protonated omega-N,omega-N-dimethlyated L-arginine with secondary neutral loss of N,N-dimethylamine + + + + + Covalent modification of a peptide or protein L-arginine residue to protonated omega-N,omega-N-dimethlyated L-arginine with secondary neutral loss of an N,N-dimethylamine molecular fragment. + PubMed:15835918 + PubMed:18688235 + + + + + dDMA-NoMe2+Arg + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine. + 789.32 + C 51 H 96 O 5 + 788.72577 + C 54 H 101 N 1 O 6 S 1 + 892.46 + 891.735 + C + natural + N-term + Unimod:51 + ntermpeptripalmitatec + PSI-MOD + N-acyl diglyceride cysteine + Tripalmitate + MOD:00444 + N-palmitoyl-S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine. + OMSSA:118 + PubMed:10356335 + Unimod:51 + + + + + ntermpeptripalmitatec + + + + + + N-acyl diglyceride cysteine + + + + + + Tripalmitate + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to L-homoarginine, such as reaction with O-methylisourea. + 42.04 + C 1 H 2 N 2 + 42.021797 + C 7 H 14 N 4 O 1 + 170.22 + 170.11676 + K + artifact + Unimod:52 + guanidinationk + PSI-MOD + Guanidination + Guanidinyl + MOD:00445 + + L-homoarginine + + + + + A protein modification that effectively converts an L-lysine residue to L-homoarginine, such as reaction with O-methylisourea. + OMSSA:53 + PubMed:11078590 + PubMed:11085420 + PubMed:11821862 + Unimod:52 + + + + + guanidinationk + + + + + + Guanidination + + + + + + Guanidinyl + + + + + + + + + + A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal. + 156.22 + C 9 H 16 O 2 + 156.11504 + X + artifact + Unimod:53 + PSI-MOD + 4-hydroxynonenal (HNE) + HNE + MOD:00446 + 4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG]. + 4-hydroxynonenal adduct + + + + + A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal. + PubMed:11327326 + PubMed:15133838 + Unimod:53 + + + + + 4-hydroxynonenal (HNE) + + + + + + HNE + + + + + + + + + + A protein modification that effectively results from forming an adduct with a glucuronic acid either through a carboxyl group amide or ester bond, or through C1-glycosylation. + 176.12 + C 6 H 8 O 6 + 176.03209 + X + Unimod:54 + N-Glucuronyl (N terminus) + PSI-MOD + Glucuronyl + N-glucuronylation + MOD:00447 + + N-glucuronylated residue + + + + + A protein modification that effectively results from forming an adduct with a glucuronic acid either through a carboxyl group amide or ester bond, or through C1-glycosylation. + DeltaMass:0 + PubMed:7398618 + Unimod:54#N-term + + + + + N-Glucuronyl (N terminus) + + + + + + Glucuronyl + + + + + + N-glucuronylation + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an N-acetylaminoglucose group through a glycosidic bond. + 203.19 + C 8 H 13 N 1 O 5 + 203.07938 + X + GlcNAcRes + PSI-MOD + HexNAc + MOD:00448 + + mono-N-acetylaminoglucosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an N-acetylaminoglucose group through a glycosidic bond. + PubMed:18688235 + + + + + GlcNAcRes + + + + + + HexNAc + + + + + + + + + + modification from Unimod Isotopic label + 45.03 + C 2 (1)H -1 (2)H 3 O 1 + 45.029396 + X + artifact + N-term + Unimod:56 + PSI-MOD + Acetate labeling reagent (N-term & K) (heavy form, +3amu) + Acetyl:2H(3) + MOD:00449 + acetate labeling reagent (N-term) (heavy form, +3amu) + + + + + modification from Unimod Isotopic label + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + Unimod:56 + + + + + Acetate labeling reagent (N-term & K) (heavy form, +3amu) + + + + + + Acetyl:2H(3) + + + + + + + + + OBSOLETE because this isotopic label from Unimod entry 57 is deprecated + 42.01 + C 2 (1)H 2 O 1 + 42.010567 + K + artifact + PSI-MOD + MOD:00450 + acetate labeling reagent light form (K) + true + + + + + OBSOLETE because this isotopic label from Unimod entry 57 is deprecated + PubMed:11857757 + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a propanoyl group. + 56.06 + C 3 H 4 O 1 + 56.026215 + X + artifact + N-term + Unimod:58 + PSI-MOD + Propionate labeling reagent light form (N-term & K) + Propionyl + MOD:00451 + alpha-amino propanoylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a propanoyl group. + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + Unimod:58#N-term + + + + + Propionate labeling reagent light form (N-term & K) + + + + + + Propionyl + + + + + + + + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 3x(13)C-labeled propanoyl group. + 59.04 + (13)C 3 H 4 O 1 + 59.036278 + (12)C 6 (13)C 3 H 16 N 2 O 2 + 187.13 + 187.13124 + X + artifact + N-term + Unimod:59 + PSI-MOD + Propionate labeling reagent heavy form (+3amu), N-term & K + Propionyl:13C(3) + MOD:00452 + alpha-amino 3x(13)C-labeled propanoylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 3x(13)C-labeled propanoyl group. + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + Unimod:59#N-term + + + + + Propionate labeling reagent heavy form (+3amu), N-term & K + + + + + + Propionyl:13C(3) + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent light form group. + 127.19 + C 7 H 13 N 1 O 1 + 127.09972 + X + artifact + Unimod:60 + PSI-MOD + GIST-Quat + Quaternary amine labeling reagent light form (N-term & K) + MOD:00453 + quaternary amine labeling reagent light form (N-term & K) + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent light form group. + PubMed:11857757 + Unimod:60 + + + + + GIST-Quat + + + + + + Quaternary amine labeling reagent light form (N-term & K) + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+3amu) form group. + 130.12 + C 7 (1)H 10 (2)H 3 N 1 O 1 + 130.11855 + C 13 (1)H 22 (2)H 3 N 3 O 2 + 258.21 + 258.2135 + X + artifact + Unimod:61 + PSI-MOD + GIST-Quat:2H(3) + Quaternary amine labeling reagent heavy (+3amu) form, N-term & K + MOD:00454 + quaternary amine labeling reagent heavy form (+3amu) (N-term & K) + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+3amu) form group. + PubMed:11857757 + Unimod:61 + + + + + GIST-Quat:2H(3) + + + + + + Quaternary amine labeling reagent heavy (+3amu) form, N-term & K + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+6amu) form group. + 133.14 + C 7 H 7 (2)H 6 N 1 O 1 + 133.13737 + X + artifact + Unimod:62 + PSI-MOD + GIST-Quat:2H(6) + Quaternary amine labeling reagent heavy form (+6amu), N-term & K + MOD:00455 + quaternary amine labeling reagent heavy form (+6amu) (N-term & K) + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+6amu) form group. + PubMed:11857757 + Unimod:62 + + + + + GIST-Quat:2H(6) + + + + + + Quaternary amine labeling reagent heavy form (+6amu), N-term & K + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+9amu) form group. + 136.16 + C 7 (1)H 4 (2)H 9 N 1 O 1 + 136.1562 + C 13 (1)H 16 (2)H 9 N 3 O 2 + 264.25 + 264.25116 + X + artifact + Unimod:63 + PSI-MOD + GIST-Quat:2H(9) + Quaternary amine labeling reagent heavy form (+9amu), N-term & K + MOD:00456 + quaternary amine labeling reagent heavy form (+9amu) (N-term & K) + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+9amu) form group. + PubMed:11857757 + Unimod:63 + + + + + GIST-Quat:2H(9) + + + + + + Quaternary amine labeling reagent heavy form (+9amu), N-term & K + + + + + + + + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a light succinyl group. + 100.03 + (12)C 4 (1)H 4 O 3 + 100.016045 + X + natural + N-term + Unimod:64 + PSI-MOD + Succinic anhydride labeling reagent light form (N-term) + Succinyl + MOD:00457 + 4x(12)C, 4x(1)H labeled alpha-amino succinylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a light succinyl group. + PubMed:11857757 + PubMed:12175151 + Unimod:64#N-term + + + + + Succinic anhydride labeling reagent light form (N-term) + + + + + + Succinyl + + + + + + + + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 4x(2)H labeled succinyl group. + 104.04 + C 4 (2)H 4 O 3 + 104.04115 + X + artifact + N-term + Unimod:65 + PSI-MOD + Succinic anhydride labeling reagent, heavy form (+4amu, 4H2), N-term + Succinyl:2H(4) + MOD:00458 + 4x(2)H labeled alpha-amino succinylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 4x(2)H labeled succinyl group. + PubMed:11857757 + PubMed:12175151 + Unimod:65#N-term + + + + + Succinic anhydride labeling reagent, heavy form (+4amu, 4H2), N-term + + + + + + Succinyl:2H(4) + + + + + + + + + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 4x(13)C labeled succinyl group. + 104.03 + (13)C 4 H 4 O 3 + 104.029465 + X + Unimod:66 + PSI-MOD + Succinic anhydride labeling reagent, heavy form (+4amu, 4C13), N-term & K + Succinyl:13C(4) + MOD:00459 + 4x(13)C labeled alpha-amino succinylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 4x(13)C labeled succinyl group. + PubMed:11857757 + PubMed:12175151 + Unimod:66#N-term + + + + + Succinic anhydride labeling reagent, heavy form (+4amu, 4C13), N-term & K + + + + + + Succinyl:13C(4) + + + + + + + + + + A protein modification that effectively trioxygenates an L-cysteine residue to L-cysteine sulfonic acid. + 48.0 + C 0 H 0 N 0 O 3 S 0 + 47.984745 + C 3 H 5 N 1 O 4 S 1 + 151.14 + 150.99393 + C + artifact + Unimod:345 + uniprot.ptm:PTM-0634 + (2R)-2-amino-3-sulfopropanoic acid + 2-amino-2-carboxyethanesulfonic acid + 2-azanyl-3-sulfopropanoic acid + 3-sulfoalanine + Cya + CysO3H + Cysteic acid, oxidation of cysteine + L-cysteine sulfonic acid + MOD_RES Cysteine sulfonic acid (-SO3H) + cysteic acid + cysteicacidc + cysteine sulphonic acid + PSI-MOD + Trioxidation + cysteine oxidation to cysteic acid + MOD:00460 + + From DeltaMass: Notes:Treatment of cysteine by strongly oxidising reagents such as performic acid results in the complete oxidation of the sulphur atom. Such treatment is often carried out prior to amino acid analysis as the resulting cysteic acid is then resistant to acid degradation during the hydrolysis procedure. + L-cysteic acid (L-cysteine sulfonic acid) + + + + + A protein modification that effectively trioxygenates an L-cysteine residue to L-cysteine sulfonic acid. + ChEBI:17285 + DeltaMass:334 + OMSSA:34 + PubMed:14678012 + PubMed:18306178 + PubMed:19522542 + PubMed:9252331 + RESID:AA0556 + Unimod:345#C + + + + + (2R)-2-amino-3-sulfopropanoic acid + + + + + + 2-amino-2-carboxyethanesulfonic acid + + + + + + 2-azanyl-3-sulfopropanoic acid + + + + + + 3-sulfoalanine + + + + + + Cya + + + + + + CysO3H + + + + + + Cysteic acid, oxidation of cysteine + + + + + + L-cysteine sulfonic acid + + + + + + MOD_RES Cysteine sulfonic acid (-SO3H) + + + + + + cysteic acid + + + + + + cysteicacidc + + + + + + cysteine sulphonic acid + + + + + + Trioxidation + + + + + + cysteine oxidation to cysteic acid + + + + + + + + + + A protein modification that effectively substitutes a nitrite (NO2) group for a hydrogen atom. + 45.0 + H -1 N 1 O 2 + 44.985077 + X + Unimod:354 + Nitro (NO2) + PSI-MOD + Nitro + Oxidation to nitro + MOD:00461 + + Note, this is often misrepresented as the introduction of a nitrate (NO3) group [JSG]. + nitrated residue + + + + + A protein modification that effectively substitutes a nitrite (NO2) group for a hydrogen atom. + DeltaMass:0 + PubMed:8839040 + PubMed:9252331 + Unimod:354 + + + + + Nitro (NO2) + + + + + + Nitro + + + + + + Oxidation to nitro + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to L-kynurenine. + 3.99 + C -1 O 1 + 3.994915 + C 10 H 10 N 2 O 2 + 190.2 + 190.07423 + W + artifact + Unimod:351 + (2S)-2-amino-4-(2-aminophenyl)-4-oxo-butanoic acid + kynureninw + PSI-MOD + Trp->Kynurenin + tryptophan oxidation to kynurenin + MOD:00462 + + L-kynurenine + + + + + A protein modification that effectively converts an L-tryptophan residue to L-kynurenine. + DeltaMass:357 + OMSSA:66 + PubMed:11029593 + PubMed:9252331 + Unimod:351#W + + + + + (2S)-2-amino-4-(2-aminophenyl)-4-oxo-butanoic acid + + + + + + kynureninw + + + + + + Trp->Kynurenin + + + + + + tryptophan oxidation to kynurenin + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to 3'-hydroxy-L-kynurenine. + 19.99 + C -1 O 2 + 19.989828 + C 10 H 10 N 2 O 3 + 206.2 + 206.06914 + W + artifact + Unimod:350 + hydroxykynureninw + PSI-MOD + Trp->Hydroxykynurenin + tryptophan oxidation to hydroxykynurenin + MOD:00463 + + 3'-hydroxy-L-kynurenine + + + + + A protein modification that effectively converts an L-tryptophan residue to 3'-hydroxy-L-kynurenine. + OMSSA:58 + PubMed:9252331 + Unimod:350#W + + + + + hydroxykynureninw + + + + + + Trp->Hydroxykynurenin + + + + + + tryptophan oxidation to hydroxykynurenin + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to N'-formyl-L-kynurenine. + 32.0 + O 2 + 31.989828 + C 11 H 10 N 2 O 3 + 218.21 + 218.06914 + W + artifact + Unimod:425 + Double oxidation of Trp + formylkynureninw + PSI-MOD + Dioxidation + dihydroxy + tryptophan oxidation to formylkynurenin + MOD:00464 + + From DeltaMass: References:Willy V. Bienvenut, Catherine Déon, Carla Pasquarello, Jennifer M. Campbell, Jean-Charles Sanchez, Marvin L. Vestal, Denis F. Hochstrasser Matrix-assisted laser desorption/ionization-tandemmass spectrometry with high resolution andsensitivity for identification and characterizationof proteins. Proteomics 2002, 2, 868-876 Notes: A double oxidation of tryptophan for which the N-formylkynurenine (+32) structure can be proposed. Many minor peaks accompanying the main peak might also be attributed to other oxidation products of the tryptophan such as kynurenine (+4), an unknown by-product found in all oxidized tryptophan patterns (+13), hydroxytryptophan (+16), 3-hydroxykynurenine (+20) and hydroxy-N-formylkynurenine (+48). See proposed structures at http://www.abrf.org/images/misc/dmass32.jpg. + N'-formyl-L-kynurenine + + + + + A protein modification that effectively converts an L-tryptophan residue to N'-formyl-L-kynurenine. + DeltaMass:356 + OMSSA:45 + PubMed:12124932 + PubMed:12686488 + PubMed:9252331 + Unimod:425#W + + + + + Double oxidation of Trp + + + + + + formylkynureninw + + + + + + Dioxidation + + + + + + dihydroxy + + + + + + tryptophan oxidation to formylkynurenin + + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to a dihydroxyphenylalanine. + 32.0 + O 2 + 31.989828 + C 9 H 9 N 1 O 3 + 179.17 + 179.05824 + F + artifact + Unimod:425 + dihydroxyf + PSI-MOD + Dioxidation + dihydroxy + MOD:00465 + + Dihydroxyphenyalanines with a 4'-hydroxyl orginate naturally by a monohydroxylation of tyrosine, and not by dihydroxylation of phenylalanine [JSG]. + dihydroxyphenylalanine (Phe) + + + + + A protein modification that effectively converts an L-phenylalanine residue to a dihydroxyphenylalanine. + OMSSA:39 + PubMed:1610822 + PubMed:1903612 + PubMed:3734192 + PubMed:9252331 + RESID:AA0146#var + Unimod:425#F + + + + + dihydroxyf + + + + + + Dioxidation + + + + + + dihydroxy + + + + + + + + + + + A protein modification that effectively converts a residue to a glycosylsphingolipidinositolethanolamidated. + GSIRes + PSI-MOD + MOD:00466 + glycosylsphingolipidinositolated residue + + + + + A protein modification that effectively converts a residue to a glycosylsphingolipidinositolethanolamidated. + PubMed:12626404 + PubMed:18688235 + PubMed:8404891 + + + + + GSIRes + + + + + + + + + + A protein modification that effectively substitutes an iminobiotinyl group for a hydrogen atom. + 225.31 + C 10 H 15 N 3 O 1 S 1 + 225.09358 + X + artifact + Unimod:89 + PSI-MOD + Iminobiotin + Iminobiotinylation + MOD:00467 + iminobiotinyl modified residue + + + + + A protein modification that effectively substitutes an iminobiotinyl group for a hydrogen atom. + PubMed:9750125 + Unimod:89 + + + + + Iminobiotin + + + + + + Iminobiotinylation + + + + + + + + + + modification from Unimod Isotopic label + 338.47 + C 16 H 26 N 4 O 2 S 1 + 338.17764 + X + artifact + Unimod:90 + PSI-MOD + ESP + ESP-Tag light d0 + MOD:00468 + ESP-Tag light d0 + + + + + modification from Unimod Isotopic label + Unimod:90 + + + + + ESP + + + + + + ESP-Tag light d0 + + + + + + + + + + modification from Unimod Isotopic label + 348.24 + C 16 (1)H 16 (2)H 10 N 4 O 2 S 1 + 348.24042 + X + artifact + Unimod:91 + PSI-MOD + ESP-Tag heavy d10 + ESP:2H(10) + MOD:00469 + ESP-Tag heavy d10 + + + + + modification from Unimod Isotopic label + Unimod:91 + + + + + ESP-Tag heavy d10 + + + + + + ESP:2H(10) + + + + + + + + + + modification from Unimod Chemical derivative + 339.45 + C 16 H 25 N 3 O 3 S 1 + 339.16165 + X + artifact + Unimod:92 + PSI-MOD + NHS-LC-Biotin + MOD:00470 + NHS-LC-Biotin + + + + + modification from Unimod Chemical derivative + Unimod:92 + + + + + NHS-LC-Biotin + + + + + + NHS-LC-Biotin + + + + + + + + + + modification from Unimod Chemical derivative + 601.8 + C 25 H 39 N 5 O 6 S 3 + 601.20624 + X + artifact + Unimod:93 + PSI-MOD + EDT-maleimide-PEO-biotin + MOD:00471 + EDT-maleimide-PEO-biotin + + + + + modification from Unimod Chemical derivative + Unimod:93 + + + + + EDT-maleimide-PEO-biotin + + + + + + EDT-maleimide-PEO-biotin + + + + + + + + + + modification from Unimod Isotopic label + 68.04 + C 3 (1)H 4 N 2 + 68.037445 + C 9 H 16 N 4 O 1 + 196.13 + 196.13242 + K + artifact + Unimod:94 + PSI-MOD + IMID + IMID d0 + MOD:00472 + IMID d0 + + + + + modification from Unimod Isotopic label + PubMed:11746907 + URL:http://dx.doi.org/10.1002/rcm.517 + Unimod:94 + + + + + IMID + + + + + + IMID d0 + + + + + + + + + + modification from Unimod Isotopic label + 72.06 + C 3 (2)H 4 N 2 + 72.06255 + C 9 (1)H 12 (2)H 4 N 4 O 1 + 200.16 + 200.15752 + K + artifact + Unimod:95 + PSI-MOD + IMID d4 + IMID:2H(4) + MOD:00473 + IMID d4 + + + + + modification from Unimod Isotopic label + PubMed:11746907 + URL:http://dx.doi.org/10.1002/rcm.517 + Unimod:95 + + + + + IMID d4 + + + + + + IMID:2H(4) + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-(1,1,2-(2)H3)-propanamide-L-cysteine. + 74.06 + C 3 (1)H 2 (2)H 3 N 1 O 1 + 74.05595 + C 6 (1)H 7 (2)H 3 N 2 O 2 S 1 + 177.07 + 177.06512 + C + artifact + Unimod:97 + S-([1,1,2-(2)H3]-3-amino-3-oxopropyl)cysteine + S-([1,1,2-(2)H3]-carbamoylethyl)-L-cysteine + S-([1,1,2-(2)H3]-propanamide)-L-cysteine + PSI-MOD + Acrylamide d3 + Propionamide:2H(3) + MOD:00474 + S-([1,1,2-(2)H3]-carboxamidoethyl)-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-(1,1,2-(2)H3)-propanamide-L-cysteine. + Unimod:97#C + + + + + S-([1,1,2-(2)H3]-3-amino-3-oxopropyl)cysteine + + + + + + S-([1,1,2-(2)H3]-carbamoylethyl)-L-cysteine + + + + + + S-([1,1,2-(2)H3]-propanamide)-L-cysteine + + + + + + Acrylamide d3 + + + + + + Propionamide:2H(3) + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to 2-amino-L-tyrosine. + 15.02 + H 1 N 1 + 15.010899 + C 9 H 10 N 2 O 2 + 178.19 + 178.07423 + Y + artifact + Unimod:342 + PSI-MOD + Amino + Tyrosine oxidation to 2-aminotyrosine + MOD:00475 + 2-amino-L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to 2-amino-L-tyrosine. + PubMed:8839040 + PubMed:9252331 + Unimod:342#Y + + + + + Amino + + + + + + Tyrosine oxidation to 2-aminotyrosine + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an galactose group through a glycosidic bond. + 162.14 + C 6 H 10 O 5 + 162.05283 + X + natural + GalRes + PSI-MOD + MOD:00476 + + monogalactosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an galactose group through a glycosidic bond. + PubMed:18688235 + + + + + GalRes + + + + + + + + + + + A protein modification that effectively converts, by oxidative decarboxylation, an L-proline residue to 2-pyrrolidone with breakage of the peptide chain. + -13.02 + C -1 H -1 N 0 O 0 + -13.007825 + C 4 H 6 N 1 O 1 + 84.1 + 84.04494 + P + artifact + Unimod:360 + PSI-MOD + Pro->Pyrrolidinone + Proline oxidation to pyrrolidinone + MOD:00477 + The oxidative decarboxylation of a proline residue results in breaking of the peptide chain, leaving a peptidyl-2-pyrrolidone at the C-terminus. The difference formula, derived from the result in the original citation, has been corrected from the Unimod entry. + 2-pyrrolidone + + + + + A protein modification that effectively converts, by oxidative decarboxylation, an L-proline residue to 2-pyrrolidone with breakage of the peptide chain. + PubMed:2161657 + PubMed:9252331 + Unimod:360#P + + + + + Pro->Pyrrolidinone + + + + + + Proline oxidation to pyrrolidinone + + + + + + + + + + + + A protein modification that effectively converts an L-proline residue to L-glutamyl semialdehyde. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 5 H 7 N 1 O 2 + 113.12 + 113.047676 + P + artifact + Unimod:35 + Oxidation of proline to gamma-glutamyl semialdehyde + gamma-glutamyl semialdehyde + glutamyl 5-semialdehyde + glutamyl aldehyde + PSI-MOD + Oxidation + Oxidation or Hydroxylation + MOD:00478 + glutamyl semialdehyde (Pro) + + + + + A protein modification that effectively converts an L-proline residue to L-glutamyl semialdehyde. + DeltaMass:354 + PubMed:11120890 + PubMed:2563380 + PubMed:9252331 + Unimod:35#P + + + + + Oxidation of proline to gamma-glutamyl semialdehyde + + + + + + gamma-glutamyl semialdehyde + + + + + + glutamyl 5-semialdehyde + + + + + + glutamyl aldehyde + + + + + + Oxidation + + + + + + Oxidation or Hydroxylation + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to L-glutamyl semialdehyde. + -43.07 + C -1 H -5 N -3 O 1 + -43.053432 + C 5 H 7 N 1 O 2 + 113.12 + 113.047676 + R + artifact + Unimod:344 + Oxidation of arginine (to glutamic acid) + PSI-MOD + Arg->GluSA + Arginine oxidation to glutamic semialdehyde + MOD:00479 + From DeltaMass: Average Mass: -27 Monoisotopic Mass Change:-27.06 Average Mass Change:-27.07 References:Amici A, Levine, RL, Tsai, L, and Stadtman, ER: Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. Journal of Biological Chemistry 264: 3341-3346 1989.Requena JR, Chao CC, Levine RL, and Stadtman ER: Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. Proceedings of the National Academy of Sciences USA 98: 69-74 2001. + glutamyl semialdehyde (Arg) + + + + + A protein modification that effectively converts an L-arginine residue to L-glutamyl semialdehyde. + DeltaMass:351 + PubMed:11120890 + PubMed:1680314 + PubMed:9252331 + Unimod:344#R + + + + + Oxidation of arginine (to glutamic acid) + + + + + + Arg->GluSA + + + + + + Arginine oxidation to glutamic semialdehyde + + + + + + + + + + modification from Unimod Isotopic label + 227.26 + C 10 H 17 N 3 O 3 + 227.12698 + C 13 H 22 N 4 O 4 S 1 + 330.4 + 330.13617 + C + artifact + Unimod:105 + icatlight + PSI-MOD + Applied Biosystems cleavable ICAT(TM) light + ICAT-C + MOD:00480 + + Applied Biosystems cleavable ICAT(TM) light + + + + + modification from Unimod Isotopic label + OMSSA:129 + URL:http://www.appliedbiosystems.com/products/productdetail.cfm?prod_id=153 + Unimod:105#C + + + + + icatlight + + + + + + Applied Biosystems cleavable ICAT(TM) light + + + + + + ICAT-C + + + + + + + + + + modification from Unimod Isotopic label + 236.16 + (12)C 1 (13)C 9 H 17 N 3 O 3 + 236.15718 + (12)C 4 (13)C 9 H 22 N 4 O 4 S 1 + 339.17 + 339.16638 + C + artifact + Unimod:106 + icatheavy + PSI-MOD + Applied Biosystems cleavable ICAT(TM) heavy + ICAT-C:13C(9) + MOD:00481 + + Applied Biosystems cleavable ICAT(TM) heavy + + + + + modification from Unimod Isotopic label + OMSSA:130 + URL:http://www.appliedbiosystems.com/products/productdetail.cfm?prod_id=153 + Unimod:106#C + + + + + icatheavy + + + + + + Applied Biosystems cleavable ICAT(TM) heavy + + + + + + ICAT-C:13C(9) + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to N-formyl-L-methionine (not known as a natural, post-translational modification process). + 28.01 + C 1 H 0 N 0 O 1 S 0 + 27.994915 + C 6 H 10 N 1 O 2 S 1 + 160.21 + 160.04323 + M + artifact + N-term + Unimod:122 + uniprot.ptm:PTM-0212 + (2S)-2-formylamino-4-(methylsulfanyl)butanoic acid + 2-formamido-4-(methylsulfanyl)butanoic acid + 2-formylamino-4-(methylthio)butanoic acid + 2-formylazanyl-4-(methylsulfanyl)butanoic acid + MOD_RES N-formylmethionine + N-formyl-L-methionine + N-formylated L-methionine + NFoMet + PSI-MOD + MOD:00482 + This entry is for the artifactual formation of N-formyl-L-methionine from methionine. For encoded N-formyl-L-methionine, use MOD:00030 [JSG]. + N-formyl-L-methionine (Met) + + + + + A protein modification that effectively converts an L-methionine residue to N-formyl-L-methionine (not known as a natural, post-translational modification process). + PubMed:11152118 + PubMed:2165784 + PubMed:3042771 + RESID:AA0021#MET + Unimod:122#M + + + + + (2S)-2-formylamino-4-(methylsulfanyl)butanoic acid + + + + + + 2-formamido-4-(methylsulfanyl)butanoic acid + + + + + + 2-formylamino-4-(methylthio)butanoic acid + + + + + + 2-formylazanyl-4-(methylsulfanyl)butanoic acid + + + + + + MOD_RES N-formylmethionine + + + + + + N-formyl-L-methionine + + + + + + N-formylated L-methionine + + + + + + NFoMet + + + + + + + + + + + A protein modification that is produced by reaction with N-ethylmaleimide. + 125.13 + C 6 H 7 N 1 O 2 + 125.047676 + C 9 H 12 N 2 O 3 S 1 + 228.27 + 228.05687 + C + artifact + Unimod:108 + nemc + PSI-MOD + N-ethylmaleimide on cysteines + Nethylmaleimide + MOD:00483 + N-ethylmaleimide derivatized cysteine + + + + + A protein modification that is produced by reaction with N-ethylmaleimide. + OMSSA:83 + PubMed:11813307 + PubMed:12777388 + Unimod:108#C + + + + + nemc + + + + + + N-ethylmaleimide on cysteines + + + + + + Nethylmaleimide + + + + + + + + + + + modification from Unimod Chemical derivative + 354.47 + C 16 H 26 N 4 O 3 S 1 + 354.17258 + C 22 H 38 N 6 O 4 S 1 + 482.64 + 482.26752 + K + artifact + Unimod:112 + PSI-MOD + OxLysBiotinRed + Oxidized lysine biotinylated with biotin-LC-hydrazide, reduced + MOD:00484 + oxidized lysine biotinylated with biotin-LC-hydrazide, reduced + + + + + modification from Unimod Chemical derivative + Unimod:112#K + + + + + OxLysBiotinRed + + + + + + Oxidized lysine biotinylated with biotin-LC-hydrazide, reduced + + + + + + + + + + + modification from Unimod Chemical derivative + 352.45 + C 16 H 24 N 4 O 3 S 1 + 352.15692 + C 22 H 36 N 6 O 4 S 1 + 480.63 + 480.25186 + K + artifact + Unimod:113 + PSI-MOD + OxLysBiotin + Oxidized lysine biotinylated with biotin-LC-hydrazide + MOD:00485 + oxidized lysine biotinylated with biotin-LC-hydrazide + + + + + modification from Unimod Chemical derivative + Unimod:113#K + + + + + OxLysBiotin + + + + + + Oxidized lysine biotinylated with biotin-LC-hydrazide + + + + + + + + + + + modification from Unimod Chemical derivative + 371.5 + C 16 H 29 N 5 O 3 S 1 + 371.1991 + C 21 H 36 N 6 O 4 S 1 + 468.62 + 468.25186 + P + artifact + Unimod:114 + PSI-MOD + OxProBiotinRed + Oxidized proline biotinylated with biotin-LC-hydrazide, reduced + MOD:00486 + oxidized proline biotinylated with biotin-LC-hydrazide, reduced + + + + + modification from Unimod Chemical derivative + Unimod:114#C + + + + + OxProBiotinRed + + + + + + Oxidized proline biotinylated with biotin-LC-hydrazide, reduced + + + + + + + + + + + modification from Unimod Chemical derivative + 369.48 + C 16 H 27 N 5 O 3 S 1 + 369.18347 + C 21 H 34 N 6 O 4 S 1 + 466.6 + 466.23624 + P + artifact + Unimod:115 + PSI-MOD + OxProBiotin + Oxidized Proline biotinylated with biotin-LC-hydrazide + MOD:00487 + oxidized proline biotinylated with biotin-LC-hydrazide + + + + + modification from Unimod Chemical derivative + Unimod:115#C + + + + + OxProBiotin + + + + + + Oxidized Proline biotinylated with biotin-LC-hydrazide + + + + + + + + + + + modification from Unimod Chemical derivative + 310.41 + C 15 H 22 N 2 O 3 S 1 + 310.1351 + C 21 H 34 N 6 O 4 S 1 + 466.6 + 466.23624 + R + artifact + PSI-MOD + OxArgBiotin + Oxidized arginine biotinylated with biotin-LC-hydrazide + MOD:00488 + oxidized arginine biotinylated with biotin-LC-hydrazide + + + + + modification from Unimod Chemical derivative + Unimod:116#C + + + + + OxArgBiotin + + + + + + Oxidized arginine biotinylated with biotin-LC-hydrazide + + + + + + + + + + + modification from Unimod Chemical derivative + 312.43 + C 15 H 24 N 2 O 3 S 1 + 312.15076 + C 21 H 36 N 6 O 4 S 1 + 468.62 + 468.25186 + R + artifact + Unimod:117 + PSI-MOD + OxArgBiotinRed + Oxidized arginine biotinylated with biotin-LC-hydrazide, reduced + MOD:00489 + oxidized arginine biotinylated with biotin-LC-hydrazide, reduced + + + + + modification from Unimod Chemical derivative + Unimod:117#C + + + + + OxArgBiotinRed + + + + + + Oxidized arginine biotinylated with biotin-LC-hydrazide, reduced + + + + + + + + + + modification from Unimod Chemical derivative + 490.7 + C 20 H 34 N 4 O 4 S 3 + 490.17422 + X + Unimod:118 + PSI-MOD + EDT-iodo-PEO-biotin + EDT-iodoacetyl-PEO-biotin + MOD:00490 + EDT-iodo-PEO-biotin + + + + + modification from Unimod Chemical derivative + Unimod:118 + + + + + EDT-iodo-PEO-biotin + + + + + + EDT-iodoacetyl-PEO-biotin + + + + + + + + + + + + modification from Unimod Chemical derivative + 316.38 + C 22 H 21 P 1 + 316.1381 + C 25 H 26 N 1 O 1 P 1 S 1 + 419.52 + 419.14728 + C + artifact + Unimod:119 + PSI-MOD + IBTP + Thio Ether Formation - BTP Adduct + MOD:00491 + thio ether formation - BTP Adduct + + + + + modification from Unimod Chemical derivative + PubMed:11861642 + Unimod:119#C + + + + + IBTP + + + + + + Thio Ether Formation - BTP Adduct + + + + + + + + + + + + + + + + + + A protein modification that crosslinks the N6-amino of a peptidyl lysine with the carboxyl of glycylglycine, the two glycine residues left after tryptic digestion of ubiquitin. + 114.1 + C 4 H 6 N 2 O 2 + 114.04293 + C 10 H 18 N 4 O 3 + 242.28 + 242.1379 + K + artifact + Unimod:121 + N6-(glycylglycyl)lysine + N6-glycylglycyl-L-lysine + glyglyk + PSI-MOD + GlyGly + ubiquitinylation residue + MOD:00492 + ubiquitination signature dipeptidyl lysine + + + + + A protein modification that crosslinks the N6-amino of a peptidyl lysine with the carboxyl of glycylglycine, the two glycine residues left after tryptic digestion of ubiquitin. + OMSSA:52 + PubMed:11125103 + PubMed:12612601 + PubMed:12872131 + RESID:AA0125#var + Unimod:121#K + + + + + N6-(glycylglycyl)lysine + + + + + + N6-glycylglycyl-L-lysine + + + + + + glyglyk + + + + + + GlyGly + + + + + + ubiquitinylation residue + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a formyl group. + 28.01 + C 1 O 1 + 27.994915 + X + Unimod:122 + FoRes + Formylation (CHO) + PSI-MOD + Formyl + Formylation + MOD:00493 + + From DeltaMass: Average Mass: 28 + formylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with a formyl group. + DeltaMass:0 + PubMed:15799070 + Unimod:122 + + + + + FoRes + + + + + + Formylation (CHO) + + + + + + Formyl + + + + + + Formylation + + + + + + + + + + + modification from Unimod Isotopic label + 345.78 + C 15 Cl 1 H 20 N 1 O 6 S 0 + 345.0979 + C 18 Cl 1 H 25 N 2 O 7 S 1 + 448.91 + 448.1071 + C + artifact + Unimod:123 + PSI-MOD + ICAT-H + N-iodoacetyl, p-chlorobenzyl-12C6-glucamine + MOD:00494 + N-iodoacetyl, p-chlorobenzyl-12C6-glucamine + + + + + modification from Unimod Isotopic label + PubMed:12185208 + Unimod:123#C + + + + + ICAT-H + + + + + + N-iodoacetyl, p-chlorobenzyl-12C6-glucamine + + + + + + + + + + + modification from Unimod Isotopic label + 351.12 + (12)C 9 (13)C 6 Cl 1 H 20 N 1 O 6 S 0 + 351.11804 + (12)C 12 (13)C 6 Cl 1 H 25 N 2 O 7 S 1 + 454.13 + 454.12723 + C + artifact + Unimod:124 + PSI-MOD + ICAT-H:13C(6) + N-iodoacetyl, p-chlorobenzyl-13C6-glucamine + MOD:00495 + N-iodoacetyl, p-chlorobenzyl-13C6-glucamine + + + + + modification from Unimod Isotopic label + PubMed:12185208 + Unimod:124#C + + + + + ICAT-H:13C(6) + + + + + + N-iodoacetyl, p-chlorobenzyl-13C6-glucamine + + + + + + + + + OBSOLETE because Unimod entry 125 is merged with entry 199, remap to id: MOD:00552 + MOD:00552 + 32.06 + C 2 (2)H 4 + 32.056408 + K + artifact + Unimod:125 + PSI-MOD + MOD:00496 + reductive amination-D + true + + + + + OBSOLETE because Unimod entry 125 is merged with entry 199, remap to id: MOD:00552 + Unimod:125 + + + + + + + + + + modification from Unimod [(35)S]dithiobis(succinimidyl propionate) crosslinking + 88.12 + C 3 H 4 O 1 S 1 + 87.99828 + C 9 H 16 N 2 O 2 S 1 + 216.3 + 216.09325 + K + artifact + Unimod:126 + PSI-MOD + 3,3-Dithio-bis-(sulfosuccinimidyl)propionate + 3-sulfanylpropanoyl + Thioacyl + MOD:00497 + The name "thioacylation of primary amines" in Unimod was a misdescription [JSG]. + 3-sulfanylpropanoyl (N-term and Lys) + + + + + modification from Unimod [(35)S]dithiobis(succinimidyl propionate) crosslinking + PubMed:957432 + Unimod:126 + + + + + 3,3-Dithio-bis-(sulfosuccinimidyl)propionate + + + + + + 3-sulfanylpropanoyl + + + + + + Thioacyl + + + + + + + + + + A protein modification that effectively substitutes a hydrogen of a residue with a fluorine atom. + X + artifact + FRes + Fluorophenylalanyl + PSI-MOD + Fluoro + fluorophenylalanine replacement of phenylalanine + MOD:00498 + fluorinated residue + + + + + A protein modification that effectively substitutes a hydrogen of a residue with a fluorine atom. + PubMed:18688235 + + + + + FRes + + + + + + Fluorophenylalanyl + + + + + + Fluoro + + + + + + fluorophenylalanine replacement of phenylalanine + + + + + + + + + + + modification from Unimod Chemical derivative + 388.35 + C 22 H 14 N 1 O 6 + 388.08212 + C 25 H 19 N 2 O 7 S 1 + 491.49 + 491.0913 + C + artifact + Unimod:128 + PSI-MOD + 5-Iodoacetamidofluorescein (Molecular Probe, Eugene, OR) + Fluorescein + MOD:00499 + 5-iodoacetamidofluorescein + + + + + modification from Unimod Chemical derivative + PubMed:3311742 + PubMed:3578767 + Unimod:128#C + + + + + 5-Iodoacetamidofluorescein (Molecular Probe, Eugene, OR) + + + + + + Fluorescein + + + + + + + + + + A protein modification that effectively substitutes one hydrogen atom of a residue with one iodine atom. + 125.9 + H -1 I 1 + 125.896645 + X + Unimod:129 + I1Res + Iodination (of Histidine[C4] or Tyrosine[C3]) + PSI-MOD + Iodination + Iodo + MOD:00500 + + From DeltaMass: Average Mass: 126 + monoiodinated residue + + + + + A protein modification that effectively substitutes one hydrogen atom of a residue with one iodine atom. + DeltaMass:0 + PubMed:15627961 + PubMed:2026710 + Unimod:129 + + + + + I1Res + + + + + + Iodination (of Histidine[C4] or Tyrosine[C3]) + + + + + + Iodination + + + + + + Iodo + + + + + + + + + + A protein modification that effectively substitutes two hydrogen atoms of a residue with two iodine atoms. + 251.79 + H -2 I 2 + 251.79329 + X + Unimod:130 + I2Res + PSI-MOD + Diiodo + di-Iodination + MOD:00501 + + From DeltaMass: Average Mass: 252 + diiodinated residue + + + + + A protein modification that effectively substitutes two hydrogen atoms of a residue with two iodine atoms. + Unimod:130 + + + + + I2Res + + + + + + Diiodo + + + + + + di-Iodination + + + + + + + + + + A protein modification that effectively substitutes three hydrogen atoms of a residue with three iodine atoms. + 377.69 + H -3 I 3 + 377.68994 + X + artifact + Unimod:131 + I3Res + triiodinationy + PSI-MOD + Triiodo + tri-Iodination + MOD:00502 + + From Unimod. In PubMed:2026710, mono- and diiodination of tyrosine are discussed, but triiodination of tyrosine is not mentioned. In PubMed:15627961, triiodothyronine (see MOD:00186) is discussed, but triiodotyrosine is not mentioned. This modification probably does not exist, and may be a confusion of "tyrosine" for "thyronine", a common error [JSG]. + triiodinated residue + + + + + A protein modification that effectively substitutes three hydrogen atoms of a residue with three iodine atoms. + OMSSA:116 + PubMed:15627961 + PubMed:2026710 + Unimod:131 + + + + + I3Res + + + + + + triiodinationy + + + + + + Triiodo + + + + + + tri-Iodination + + + + + + + + + + + A protein modification that effectively converts a glycine residue to N-(cis-delta 5)-tetradecaenoylglycine. + 208.35 + C 14 H 24 N 0 O 1 + 208.18271 + C 16 H 27 N 1 O 2 + 265.4 + 265.2042 + G + natural + N-term + Unimod:134 + N-(C14:1 aliphatic acyl)glycine + myristoleylation (one double bond) + ntermpepmyristoyeylationg + PSI-MOD + (cis-delta 5)-tetradecaenoyl + Myristoleyl + MOD:00503 + N-(cis-delta 5)-tetradecaenoylglycine + + + + + A protein modification that effectively converts a glycine residue to N-(cis-delta 5)-tetradecaenoylglycine. + OMSSA:78 + PubMed:11955007 + PubMed:11955008 + PubMed:1326520 + PubMed:1386601 + PubMed:6436247 + PubMed:7543369 + RESID:AA0059#var + Unimod:134#G + + + + + N-(C14:1 aliphatic acyl)glycine + + + + + + myristoleylation (one double bond) + + + + + + ntermpepmyristoyeylationg + + + + + + (cis-delta 5)-tetradecaenoyl + + + + + + Myristoleyl + + + + + + + + + + + A protein modification that effectively converts a glycine residue to N-(cis,cis-delta 5,delta 8)-tetradecadienoylglycine. + 206.33 + C 14 H 22 O 1 + 206.16707 + C 16 H 25 N 1 O 2 + 263.38 + 263.18854 + G + natural + N-term + Unimod:135 + N-(C14:2 aliphatic acyl)glycine + myristoylation-4H (two double bonds) + ntermpepmyristoyl4hg + PSI-MOD + (cis,cis-delta 5, delta 8)-tetradecadienoyl + Myristoyl+Delta:H(-4) + MOD:00504 + N-(cis,cis-delta 5,delta 8)-tetradecadienoylglycine + + + + + A protein modification that effectively converts a glycine residue to N-(cis,cis-delta 5,delta 8)-tetradecadienoylglycine. + OMSSA:79 + PubMed:11955007 + PubMed:11955008 + PubMed:1326520 + PubMed:1386601 + PubMed:6436247 + PubMed:7543369 + RESID:AA0059#var + Unimod:135#G + + + + + N-(C14:2 aliphatic acyl)glycine + + + + + + myristoylation-4H (two double bonds) + + + + + + ntermpepmyristoyl4hg + + + + + + (cis,cis-delta 5, delta 8)-tetradecadienoyl + + + + + + Myristoyl+Delta:H(-4) + + + + + + + + + + modification from Unimod Isotopic label + 104.11 + C 7 H 4 O 1 + 104.026215 + X + artifact + Unimod:136 + Benzoyl (Bz) + PSI-MOD + Benzoyl + labeling reagent light form (N-term & K) + MOD:00505 + From DeltaMass: Average Mass: 104 + benzoyl labeling reagent light form (N-term and K) + + + + + modification from Unimod Isotopic label + DeltaMass:0 + PubMed:15456300 + Unimod:136 + + + + + Benzoyl (Bz) + + + + + + Benzoyl + + + + + + labeling reagent light form (N-term & K) + + + + + + + + + + + modification from Unimod N-linked glycosylation, Hex(5) HexNAc(2) + 1217.09 + C 46 H 76 N 2 O 35 + 1216.4229 + C 50 H 82 N 4 O 37 + 1331.2 + 1330.4658 + N + natural + GNO:G02815KT + Unimod:137 + PSI-MOD + Hex(5)HexNAc(2) + N-linked glycan core + MOD:00506 + N-linked glycan core N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation, Hex(5) HexNAc(2) + PubMed:111247 + PubMed:1694179 + PubMed:5490222 + RESID:AA0151#var + Unimod:137#N + + + + + Hex(5)HexNAc(2) + + + + + + N-linked glycan core + + + + + + + + + OBSOLETE because redundant, replaced by MOD:01653. Remap to MOD:01653. + MOD:01653 + 233.29 + C 12 H 11 N 1 O 2 S 1 + 233.05106 + X + artifact + Unimod:139 + Dansyl (Dns) + PSI-MOD + 5-dimethylaminonaphthalene-1-sulfonyl + Dansyl + MOD:00507 + From DeltaMass: Average Mass: 233 + 5-dimethylaminonaphthalene-1-sulfonyl + true + + + + + OBSOLETE because redundant, replaced by MOD:01653. Remap to MOD:01653. + DeltaMass:0 + Unimod:139 + + + + + Dansyl (Dns) + + + + + + 5-dimethylaminonaphthalene-1-sulfonyl + + + + + + Dansyl + + + + + + + + + OBSOLETE because this is an ion type and is not a biological or chemical modification to a polypeptide, can be handled by PSI-MS CV term, MS:1001229 + X + artifact + C-term + Unimod:140 + PSI-MOD + ISD a-series (C-Term) + a-type-ion + MOD:00508 + Virtual Modification for MS/MS of a-type ions, by decarboxylation of C-terminus as reaction inside the mass spectrometer. + ISD a-series (C-Term) + true + + + + + OBSOLETE because this is an ion type and is not a biological or chemical modification to a polypeptide, can be handled by PSI-MS CV term, MS:1001229 + PubMed:14588022 + Unimod:140 + + + + + ISD a-series (C-Term) + + + + + + a-type-ion + + + + + + + + + + modification from Unimod Chemical derivative + 41.05 + C 2 H 3 N 1 + 41.02655 + X + artifact + Unimod:141 + PSI-MOD + Amidine + amidination of lysines or N-terminal amines with methyl acetimidate + MOD:00509 + amidination of lysines or N-terminal amines with methyl acetimidate + + + + + modification from Unimod Chemical derivative + PubMed:12643539 + PubMed:6273432 + Unimod:141 + + + + + Amidine + + + + + + amidination of lysines or N-terminal amines with methyl acetimidate + + + + + + + + + + + modification from Unimod N-linked glycosylation, dHex HexNAc + 349.34 + C 14 H 23 N 1 O 9 + 349.13727 + C 18 H 29 N 3 O 11 + 463.44 + 463.1802 + N + natural + GNO:G00194GV + Unimod:142 + dHexHexNAcN + PSI-MOD + HexNAc(1)dHex(1) + HexNAc1dHex1 + MOD:00510 + HexNAc1dHex1 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation, dHex HexNAc + OMSSA:183 + PubMed:111247 + PubMed:1694179 + PubMed:5490222 + RESID:AA0151#var + Unimod:142 + + + + + dHexHexNAcN + + + + + + HexNAc(1)dHex(1) + + + + + + HexNAc1dHex1 + + + + + + + + + + + modification from Unimod N-linked glycosylation, HexNAc(2) + 406.39 + C 16 H 26 N 2 O 10 + 406.15875 + C 20 H 32 N 4 O 12 + 520.49 + 520.20166 + N + natural + GNO:G27391WQ + Unimod:143 + PSI-MOD + HexNAc(2) + HexNAc2 + MOD:00511 + HexNAc2 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation, HexNAc(2) + PubMed:111247 + PubMed:1694179 + PubMed:5490222 + RESID:AA0151#var + Unimod:143 + + + + + HexNAc(2) + + + + + + HexNAc2 + + + + + + + + + + + modification from Unimod N-linked glycosylation, Hex3 + 486.42 + C 18 H 30 O 15 + 486.15848 + C 22 H 36 N 2 O 17 + 600.53 + 600.2014 + N + natural + GNO:G39365VM + Unimod:144 + PSI-MOD + Hex(3) + Hex3 + MOD:00512 + Hex3 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation, Hex3 + PubMed:111247 + PubMed:1694179 + PubMed:5490222 + RESID:AA0151#var + Unimod:144 + + + + + Hex(3) + + + + + + Hex3 + + + + + + + + + + + modification from Unimod N-linked glycosylation, dHex(2) HexNAc + 495.48 + C 20 H 33 N 1 O 13 + 495.1952 + C 24 H 39 N 3 O 15 + 609.58 + 609.2381 + N + natural + GNO:G74392IM + Unimod:145 + PSI-MOD + HexNAc(1)dHex(2) + HexNAc1dHex2 + MOD:00513 + HexNAc1dHex2 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation, dHex(2) HexNAc + PubMed:111247 + PubMed:1694179 + PubMed:5490222 + RESID:AA0151#var + Unimod:145 + + + + + HexNAc(1)dHex(2) + + + + + + HexNAc1dHex2 + + + + + + + + + + + modification from Unimod N-linked glycosylation, dHex Hex HexNAc + 511.48 + C 20 H 33 N 1 O 14 + 511.1901 + C 24 H 39 N 3 O 16 + 625.58 + 625.23303 + N + natural + GNO:G54129SE + Unimod:146 + PSI-MOD + Hex(1)HexNAc(1)dHex(1) + Hex1HexNAc1dHex1 + MOD:00514 + Hex1HexNAc1dHex1 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation, dHex Hex HexNAc + PubMed:111247 + PubMed:1694179 + PubMed:5490222 + RESID:AA0151#var + Unimod:146 + + + + + Hex(1)HexNAc(1)dHex(1) + + + + + + Hex1HexNAc1dHex1 + + + + + + + + + + + modification from Unimod N-linked glycosylation, dHex HexNAc(2) + 552.53 + C 22 H 36 N 2 O 14 + 552.2167 + C 26 H 42 N 4 O 16 + 666.63 + 666.2596 + N + natural + GNO:G06042JP + Unimod:147 + PSI-MOD + HexNAc(2)dHex(1) + HexNAc2dHex1 + MOD:00515 + HexNAc2dHex1 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation, dHex HexNAc(2) + PubMed:111247 + PubMed:1694179 + PubMed:5490222 + RESID:AA0151#var + Unimod:147 + + + + + HexNAc(2)dHex(1) + + + + + + HexNAc2dHex1 + + + + + + + + + + + modification from Unimod N-linked glycosylation + 568.53 + C 22 H 36 N 2 O 15 + 568.21155 + C 26 H 42 N 4 O 17 + 682.63 + 682.2545 + N + natural + GNO:G58001LT + Unimod:148 + PSI-MOD + Hex(1)HexNAc(2) + Hex1HexNAc2 + MOD:00516 + Hex1HexNAc2 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation + RESID:AA0151#var + Unimod:148 + + + + + Hex(1)HexNAc(2) + + + + + + Hex1HexNAc2 + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond. + 657.6 + C 25 H 41 N 2 O 18 + 657.2354 + X + natural + GNO:G17015OC + NeuAc-Hex-HexNAc + PSI-MOD + Hex(1)HexNAc(1)NeuAc(1) + Hex1HexNAc1NeuAc1 + MOD:00517 + From DeltaMass: Average Mass: 657 + Hex1HexNAc1NeuAc1 glycosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond. + DeltaMass:0 + Unimod:149 + + + + + NeuAc-Hex-HexNAc + + + + + + Hex(1)HexNAc(1)NeuAc(1) + + + + + + Hex1HexNAc1NeuAc1 + + + + + + + + + + + modification from Unimod N-linked glycosylation + 698.67 + C 28 H 46 N 2 O 18 + 698.27454 + C 32 H 52 N 4 O 20 + 812.78 + 812.3175 + N + natural + GNO:G90423UY + Unimod:150 + PSI-MOD + HexNAc(2)dHex(2) + HexNAc2dHex2 + MOD:00518 + HexNAc2dHex2 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation + RESID:AA0151#var + Unimod:150 + + + + + HexNAc(2)dHex(2) + + + + + + HexNAc2dHex2 + + + + + + + + + + + modification from Unimod N-linked glycosylation + 700.64 + C 27 H 44 N 2 O 19 + 700.25385 + C 31 H 50 N 4 O 21 + 814.75 + 814.29675 + N + natural + GNO:G54968WM + Unimod:151 + PSI-MOD + Hex(1)HexNAc(2)Pent(1) + Hex1HexNAc2Pent1 + MOD:00519 + Hex1HexNAc2Pent1 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation + RESID:AA0151#var + Unimod:151 + + + + + Hex(1)HexNAc(2)Pent(1) + + + + + + Hex1HexNAc2Pent1 + + + + + + + + + + + modification from Unimod N-linked glycosylation + 714.67 + C 28 H 46 N 2 O 19 + 714.2695 + C 32 H 52 N 4 O 21 + 828.77 + 828.3124 + N + natural + GNO:G94583DZ + Unimod:152 + PSI-MOD + Hex(1)HexNAc(2)dHex(1) + Hex1HexNAc2dHex1 + MOD:00520 + Hex1HexNAc2dHex1 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation + RESID:AA0151#var + Unimod:152 + + + + + Hex(1)HexNAc(2)dHex(1) + + + + + + Hex1HexNAc2dHex1 + + + + + + + + + + + modification from Unimod N-linked glycosylation + 730.67 + C 28 H 46 N 2 O 20 + 730.2644 + C 32 H 52 N 4 O 22 + 844.77 + 844.3073 + N + natural + GNO:G53434XO + Unimod:153 + PSI-MOD + Hex(2)HexNAc(2) + Hex2HexNAc2 + MOD:00521 + Hex2HexNAc2 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation + RESID:AA0151#var + Unimod:153 + + + + + Hex(2)HexNAc(2) + + + + + + Hex2HexNAc2 + + + + + + + + + + + modification from Unimod N-linked glycosylation + 821.73 + C 31 H 51 N 1 O 24 + 821.2801 + C 35 H 57 N 3 O 26 + 935.84 + 935.32306 + N + natural + GNO:G64686LL + Unimod:154 + PSI-MOD + Hex(3)HexNAc(1)Pent(1) + Hex3HexNAc1Pent1 + MOD:00522 + Hex3HexNAc1Pent1 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation + RESID:AA0151#var + Unimod:154 + + + + + Hex(3)HexNAc(1)Pent(1) + + + + + + Hex3HexNAc1Pent1 + + + + + + + + + + + modification from Unimod N-linked glycosylation + 846.79 + C 33 H 54 N 2 O 23 + 846.3117 + C 35 H 57 N 3 O 26 + 960.89 + 960.3547 + N + natural + GNO:G84825UQ + Unimod:155 + PSI-MOD + Hex(1)HexNAc(2)dHex(1)Pent(1) + Hex1HexNAc2dHex1Pent1 + MOD:00523 + Hex1HexNAc2dHex1Pent1 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation + RESID:AA0151#var + Unimod:155 + + + + + Hex(1)HexNAc(2)dHex(1)Pent(1) + + + + + + Hex1HexNAc2dHex1Pent1 + + + + + + + + + + + modification from Unimod N-linked glycosylation + 860.81 + C 34 H 56 N 2 O 23 + 860.3274 + C 38 H 62 N 4 O 25 + 974.92 + 974.3703 + N + natural + GNO:G05460KC + Unimod:156 + PSI-MOD + Hex(1)HexNAc(2)dHex(2) + Hex1HexNAc2dHex2 + MOD:00524 + Hex1HexNAc2dHex2 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation + RESID:AA0151#var + Unimod:156 + + + + + Hex(1)HexNAc(2)dHex(2) + + + + + + Hex1HexNAc2dHex2 + + + + + + + + + + + modification from Unimod N-linked glycosylation + 862.79 + C 33 H 54 N 2 O 24 + 862.30664 + C 37 H 60 N 4 O 26 + 976.89 + 976.34955 + N + natural + GNO:G18999EB + Unimod:157 + PSI-MOD + Hex(2)HexNAc(2)Pent(1) + Hex2HexNAc2Pent1 + MOD:00525 + Hex2HexNAc2Pent1 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation + RESID:AA0151#var + Unimod:157 + + + + + Hex(2)HexNAc(2)Pent(1) + + + + + + Hex2HexNAc2Pent1 + + + + + + + + + + + modification from Unimod N-linked glycosylation + 876.81 + C 34 H 56 N 2 O 24 + 876.3223 + C 38 H 62 N 4 O 26 + 990.92 + 990.36523 + N + natural + GNO:G93579XB + Unimod:158 + PSI-MOD + Hex(2)HexNAc(2)dHex(1) + Hex2HexNAc2dHex1 + MOD:00526 + Hex2HexNAc2dHex1 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation + RESID:AA0151#var + Unimod:158 + + + + + Hex(2)HexNAc(2)dHex(1) + + + + + + Hex2HexNAc2dHex1 + + + + + + + + + + + modification from Unimod N-linked glycosylation + 892.81 + C 34 H 56 N 2 O 25 + 892.3172 + C 38 H 62 N 4 O 27 + 1006.92 + 1006.36017 + N + natural + GNO:G28681TP + Unimod:159 + (Hex)3-HexNAc-HexNAc + PSI-MOD + Hex(3)HexNAc(2) + Hex3HexNAc2 + MOD:00527 + From DeltaMass: Average Mass: 893 + Hex3HexNAc2 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation + DeltaMass:0 + RESID:AA0151#var + Unimod:159 + + + + + (Hex)3-HexNAc-HexNAc + + + + + + Hex(3)HexNAc(2) + + + + + + Hex3HexNAc2 + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond. + 947.85 + C 36 H 57 N 3 O 26 + 947.32306 + X + natural + GNO:G23729WG + Unimod:160 + PSI-MOD + Hex(1)HexNAc(1)NeuAc(2) + Hex1HexNAc1NeuAc2 + MOD:00528 + Hex1HexNAc1NeuAc2 glycosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond. + Unimod:160 + + + + + Hex(1)HexNAc(1)NeuAc(2) + + + + + + Hex1HexNAc1NeuAc2 + + + + + + + + + + + modification from Unimod N-linked glycosylation + 972.79 + C 34 H 57 N 2 O 28 P 1 + 972.28357 + C 38 H 63 N 4 O 30 P 1 + 1086.89 + 1086.3264 + N + natural + GNO:G88520YF + Unimod:161 + PSI-MOD + Hex(3)HexNAc(2)P(1) + Hex3HexNAc2P1 + MOD:00529 + Hex3HexNAc2P1 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation + RESID:AA0151#var + Unimod:161 + + + + + Hex(3)HexNAc(2)P(1) + + + + + + Hex3HexNAc2P1 + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to L-selenomethionine. + 46.91 + C 0 H 0 N 0 S -1 Se 1 + 47.94445 + C 5 H 9 N 1 O 1 Se 1 + 178.1 + 178.98494 + M + artifact + Unimod:162 + Se(S)Met + semetm + PSI-MOD + Delta:S(-1)Se(1) + Selenium replaces sulphur + MOD:00530 + L-selenomethionine + + + + + A protein modification that effectively converts an L-methionine residue to L-selenomethionine. + OMSSA:113 + PubMed:12148805 + Unimod:162#M + + + + + Se(S)Met + + + + + + semetm + + + + + + Delta:S(-1)Se(1) + + + + + + Selenium replaces sulphur + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to L-aspartic acid with one (18)O as the result of having been deglycosylated in (18)O water. + 2.99 + H -1 N -1 (18)O 1 + 2.988262 + C 4 H 5 N 1 (16)O 2 (18)O 1 + 117.03 + 117.03119 + N + artifact + Unimod:170 + PSI-MOD + Delta:H(1)O(-1)18O(1) + glycosylated asparagine 18O labeling + MOD:00531 + + (18)O labeled deglycosylated asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to L-aspartic acid with one (18)O as the result of having been deglycosylated in (18)O water. + PubMed:14435542 + Unimod:170 + + + + + Delta:H(1)O(-1)18O(1) + + + + + + glycosylated asparagine 18O labeling + + + + + + + + + + modification from Unimod Chemical derivative + 159.01 + (13)C 6 H 3 N 1 O 2 S 1 + 159.00858 + (12)C 11 (13)C 6 H 13 N 3 O 3 S 1 + 345.09 + 345.0879 + W + artifact + Unimod:171 + PSI-MOD + NBS:13C(6) + Shimadzu NBS-13C + MOD:00532 + Shimadzu 13CNBS + + + + + modification from Unimod Chemical derivative + PubMed:12845591 + Unimod:171 + + + + + NBS:13C(6) + + + + + + Shimadzu NBS-13C + + + + + + + + + + modification from Unimod Chemical derivative + 152.99 + (12)C 6 H 3 N 1 O 2 S 1 + 152.98845 + (12)C 17 H 13 N 3 O 3 S 1 + 339.07 + 339.06775 + W + artifact + Unimod:172 + PSI-MOD + NBS + Shimadzu NBS-12C + MOD:00533 + Shimadzu 12CNBS + + + + + modification from Unimod Chemical derivative + PubMed:12845591 + Unimod:172 + + + + + NBS + + + + + + Shimadzu NBS-12C + + + + + + + + + + modification from Unimod Post-translational + 218.34 + C 15 H 22 O 1 + 218.16707 + X + artifact + Unimod:176 + PSI-MOD + BHT + Michael addition of BHT quinone methide to Cysteine and Lysine + MOD:00534 + Butylated Hydroxytoluene adduct. + Michael addition of BHT quinone methide to cysteine and lysine + + + + + modification from Unimod Post-translational + PubMed:9448752 + Unimod:176 + + + + + BHT + + + + + + Michael addition of BHT quinone methide to Cysteine and Lysine + + + + + + + + + + modification from Unimod Chemical derivative + 87.18 + C 4 H 9 N 1 O -1 S 1 + 87.05066 + X + artifact + Unimod:178 + PSI-MOD + DAET + phosphorylation to amine thiol + MOD:00535 + DAET = 2-(dimethylamino)ethanethiol. The phosphorylation to amine is the beta elimination of phosphate and Michael addition of 2-(dimethylamino)ethanethiol to the site. + phosphorylation to amine thiol + + + + + modification from Unimod Chemical derivative + PubMed:12216740 + Unimod:178 + + + + + DAET + + + + + + phosphorylation to amine thiol + + + + + + + + + OBSOLETE because Unimod 179 merged with Unimod 447 remap to ??? a protein modification that replaces an L-serine residue with an L-alanine residue + -16.0 + O -1 + -15.994915 + S + artifact + Unimod:179 + Ser_Ala + PSI-MOD + MOD:00536 + L-serine to L-alanine replacement + true + + + + + OBSOLETE because Unimod 179 merged with Unimod 447 remap to ??? a protein modification that replaces an L-serine residue with an L-alanine residue + Unimod:179 + + + + + Ser_Ala + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to L-alanine. + -30.03 + C -1 H -2 O -1 + -30.010565 + C 3 H 5 N 1 O 1 + 71.08 + 71.03712 + T + Unimod:659 + Thr(Ala) + PSI-MOD + Thr->Ala + Thr->Ala substitution + MOD:00537 + This could represent either an engineered replacement or a chemical modification. + L-alanine residue (Thr) + + + + + A protein modification that effectively converts an L-threonine residue to L-alanine. + Unimod:659 + + + + + Thr(Ala) + + + + + + Thr->Ala + + + + + + Thr->Ala substitution + + + + + + + + + + Modified amino acid residues groups into isobaric sets at particular mass resolution cut-offs. + PSI-MOD + MOD:00538 + + protein modification categorized by isobaric sets + + + + + Modified amino acid residues groups into isobaric sets at particular mass resolution cut-offs. + PubMed:18688235 + + + + + + + + OBSOLETE because Unimod 179 merged wth Unimod 447 remap to ??? modification from Unimod O-linked glycosylation + -17.01 + H -1 O -1 + -17.00274 + T + artifact + Unimod:182 + PSI-MOD + MOD:00539 + threonine reduced to aminobutynate + true + + + + + OBSOLETE because Unimod 179 merged wth Unimod 447 remap to ??? modification from Unimod O-linked glycosylation + Unimod:182 + + + + + + + + + A protein modification that effectively converts a residue containing common isotopes to a 9x(13)C labeled residue. + 9.03 + (12)C -9 (13)C 9 + 9.030194 + X + artifact + Unimod:184 + PSI-MOD + 13C(9) Silac label + Label:13C(9) + MOD:00540 + 9x(13)C labeled residue + + + + + A protein modification that effectively converts a residue containing common isotopes to a 9x(13)C labeled residue. + PubMed:12716131 + Unimod:184 + + + + + 13C(9) Silac label + + + + + + Label:13C(9) + + + + + + + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to 9x(13)C labeled L-phosphotyrosine. + 89.0 + (12)C -9 (13)C 9 H 1 O 3 P 1 + 88.99652 + (13)C 9 H 10 N 1 O 5 P 1 + 252.06 + 252.05986 + Y + artifact + Unimod:185 + PSI-MOD + C13 label (Phosphotyrosine) + Label:13C(9)+Phospho + MOD:00541 + 9x(13)C labeled L-phosphotyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to 9x(13)C labeled L-phosphotyrosine. + PubMed:12716131 + Unimod:185 + + + + + C13 label (Phosphotyrosine) + + + + + + Label:13C(9)+Phospho + + + + + + + + + + + modification from Unimod Chemical derivative + 132.12 + C 8 H 4 O 2 + 132.02113 + C 14 H 16 N 4 O 3 + 288.31 + 288.12225 + R + artifact + Unimod:186 + PSI-MOD + HPG + Hydroxyphenylglyoxal arginine + MOD:00542 + hydroxyphenylglyoxal arginine + + + + + modification from Unimod Chemical derivative + PubMed:11698400 + PubMed:11914093 + Unimod:186 + + + + + HPG + + + + + + Hydroxyphenylglyoxal arginine + + + + + + + + + + + modification from Unimod Chemical derivative + 282.25 + C 16 H 10 O 5 + 282.05283 + C 22 H 22 N 4 O 6 + 438.44 + 438.15393 + R + artifact + Unimod:187 + PSI-MOD + 2HPG + bis(hydroxphenylglyoxal) arginine + MOD:00543 + OH-PGO and PGO react with arginine at a stoichiometry of 2:1 [Unimod]. + bis(hydroxyphenylglyoxal) arginine + + + + + modification from Unimod Chemical derivative + PubMed:11698400 + Unimod:187 + + + + + 2HPG + + + + + + bis(hydroxphenylglyoxal) arginine + + + + + + + + + + A protein modification that effectively converts a residue containing common isotopes to a 6x(13)C labeled residue. + 6.02 + (12)C -6 (13)C 6 + 6.020129 + X + artifact + Unimod:188 + PSI-MOD + 13C(6) Silac label + Label:13C(6) + MOD:00544 + + 6x(13)C labeled residue + + + + + A protein modification that effectively converts a residue containing common isotopes to a 6x(13)C labeled residue. + PubMed:12716131 + Unimod:188 + + + + + 13C(6) Silac label + + + + + + Label:13C(6) + + + + + + + + + OBSOLETE because redundant with MOD:00927. Remap to MOD:00927. + MOD:00927 + X + artifact + N-term + PSI-MOD + MOD:00545 + deuterated dimethyl labeling (D) + true + + + + + OBSOLETE because redundant with MOD:00927. Remap to MOD:00927. + PubMed:14670044 + + + + + + + + + A protein modification that effectively substitutes two (18)O atom for the two (16)O atoms of an alpha-carboxyl (1-carboxyl) group. + 4.01 + (16)O -2 (18)O 2 + 4.008493 + X + artifact + C-term + Unimod:193 + ctermpepdio18 + PSI-MOD + Label:18O(2) + O18 label at both C-terminal oxygens + MOD:00546 + + (18)O label at both C-terminal oxygens + + + + + A protein modification that effectively substitutes two (18)O atom for the two (16)O atoms of an alpha-carboxyl (1-carboxyl) group. + OMSSA:88 + PubMed:11467524 + Unimod:193 + + + + + ctermpepdio18 + + + + + + Label:18O(2) + + + + + + O18 label at both C-terminal oxygens + + + + + + + + + + modification from Unimod Chemical derivative used for amino acid analysis + 170.17 + C 10 H 6 N 2 O 1 + 170.04802 + X + artifact + Unimod:194 + PSI-MOD + 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate + AccQTag + MOD:00547 + 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate + + + + + modification from Unimod Chemical derivative used for amino acid analysis + PubMed:14997490 + Unimod:194 + + + + + 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate + + + + + + AccQTag + + + + + + + + + + modification from Unimod Chemical derivative + 171.26 + C 9 H 19 N 2 O 1 + 171.14973 + C 12 H 24 N 3 O 2 S 1 + 274.4 + 274.15894 + C + artifact + Unimod:195 + PSI-MOD + APTA-d0 + QAT + MOD:00548 + Derivatization of cysteine with 3-acrylamidopropyl)trimethylammonium chloride [JSG]. + APTA + + + + + modification from Unimod Chemical derivative + PubMed:15283597 + Unimod:195 + + + + + APTA-d0 + + + + + + QAT + + + + + + + + + + modification from Unimod Isotopic label + 174.17 + C 9 (1)H 16 (2)H 3 N 2 O 1 + 174.16856 + C 12 (1)H 21 (2)H 3 N 3 O 2 S 1 + 277.18 + 277.17776 + C + artifact + Unimod:196 + PSI-MOD + (3-acrylamidopropyl)trimethylammonium + APTA d3 + QAT:2H(3) + MOD:00549 + Derivatization of cysteine with 3-acrylamidopropyl)trimethylammonium chloride (difference formula correct) [JSG]. + APTA d3 + + + + + modification from Unimod Isotopic label + PubMed:15283597 + Unimod:196 + + + + + (3-acrylamidopropyl)trimethylammonium + + + + + + APTA d3 + + + + + + QAT:2H(3) + + + + + + + + + + modification from Unimod Chemical derivative + 184.28 + C 10 H 20 N 2 O 1 + 184.15756 + C 13 H 25 N 3 O 2 S 1 + 287.42 + 287.16675 + C + artifact + Unimod:197 + PSI-MOD + EAPTA d0 + EQAT + MOD:00550 + EAPTA d0 + + + + + modification from Unimod Chemical derivative + Unimod:197 + + + + + EAPTA d0 + + + + + + EQAT + + + + + + + + + + modification from Unimod Isotopic label + 189.19 + C 10 (1)H 15 (2)H 5 N 2 O 1 + 189.18895 + C 13 (1)H 20 (2)H 5 N 3 O 2 S 1 + 292.2 + 292.19812 + C + artifact + Unimod:198 + PSI-MOD + EAPTA d5 + EQAT:2H(5) + MOD:00551 + EAPTA d5 + + + + + modification from Unimod Isotopic label + Unimod:198 + + + + + EAPTA d5 + + + + + + EQAT:2H(5) + + + + + + + + + + A protein modification that effectively converts a residue containing common isotopes to a 4x(2)H labeled dimethylated residue. + 32.06 + C 2 (2)H 4 + 32.056408 + X + artifact + Unimod:199 + PSI-MOD + DiMethyl-CHD2 + Dimethyl:2H(4) + MOD:00552 + + Supposed to be alpha-amino and Lys-N6 derivatized by C(2)H2O and reduction. + 4x(2)H labeled dimethylated residue + + + + + A protein modification that effectively converts a residue containing common isotopes to a 4x(2)H labeled dimethylated residue. + PubMed:14670044 + Unimod:199 + + + + + DiMethyl-CHD2 + + + + + + Dimethyl:2H(4) + + + + + + + + + + A protein modification that effectively substitutes a (2-sulfanylethyl)sulfanyl (or thioethylthiol) group for a hydroxy group. + 76.18 + C 2 H 4 O -1 S 2 + 75.98053 + X + artifact + Unimod:200 + 1,2-ethanedithiol (EDT) + PSI-MOD + EDT + Ethanedithiol + MOD:00553 + From DeltaMass: Average Mass: 93; supposed to be derivatization of serine and threonine. + 1,2-ethanedithiol modified residue + + + + + A protein modification that effectively substitutes a (2-sulfanylethyl)sulfanyl (or thioethylthiol) group for a hydroxy group. + DeltaMass:0 + PubMed:11507762 + Unimod:200 + + + + + 1,2-ethanedithiol (EDT) + + + + + + EDT + + + + + + Ethanedithiol + + + + + + + + + OBSOLETE because Unimod entry 202 was merged with entry 195, remap to MOD:00548. modification from Unimod Chemical derivative + MOD:00548 + 170.26 + C 9 H 18 N 2 O 1 + 170.1419 + C + artifact + Unimod:202 + PSI-MOD + MOD:00554 + APTA-d0 with no neutral loss + true + + + + + OBSOLETE because Unimod entry 202 was merged with entry 195, remap to MOD:00548. modification from Unimod Chemical derivative + Unimod:202 + + + + + + + + OBSOLETE because Unimod entry 202 was merged with entry 195, remap to MOD:00548. modification from Unimod Chemical derivative + MOD:00548 + 170.26 + C 9 H 18 N 2 O 1 + 170.1419 + C + artifact + Unimod:203 + PSI-MOD + MOD:00555 + APTA-d0 with quaternary amine loss + true + + + + + OBSOLETE because Unimod entry 202 was merged with entry 195, remap to MOD:00548. modification from Unimod Chemical derivative + Unimod:203 + + + + + + + + OBSOLETE because this modification not supported by any literature that I can find[PMT] + 94.11 + C 6 H 6 O 1 + 94.04186 + C 12 H 18 N 2 O 2 + 222.29 + 222.13683 + K + artifact + Unimod:205 + PSI-MOD + Acrolein addition +94 + Delta:H(6)C(6)O(1) + MOD:00556 + acrolein addition +94 + true + + + + + OBSOLETE because this modification not supported by any literature that I can find[PMT] + Unimod:205 + + + + + Acrolein addition +94 + + + + + + Delta:H(6)C(6)O(1) + + + + + + + + + OBSOLETE because this modification not supported by the papers listed or any other that I can find[PMT] + 56.06 + C 3 H 4 O 1 + 56.026215 + X + artifact + Unimod:206 + PSI-MOD + Acrolein addition +56 + Delta:H(4)C(3)O(1) + MOD:00557 + acrolein addition +56 + true + + + + + OBSOLETE because this modification not supported by the papers listed or any other that I can find[PMT] + PubMed:10825247 + PubMed:15541752 + Unimod:206 + + + + + Acrolein addition +56 + + + + + + Delta:H(4)C(3)O(1) + + + + + + + + + OBSOLETE because this modification not supported by any literature that I can find[PMT] + 38.05 + C 3 H 2 + 38.01565 + C 9 H 14 N 2 O 1 + 166.22 + 166.11061 + K + artifact + Unimod:207 + PSI-MOD + Acrolein addition +38 + Delta:H(2)C(3) + MOD:00558 + acrolein addition +38 + true + + + + + OBSOLETE because this modification not supported by any literature that I can find[PMT] + Unimod:207 + + + + + Acrolein addition +38 + + + + + + Delta:H(2)C(3) + + + + + + + + + OBSOLETE because this modification not supported by any literature that I can find[PMT] + 76.1 + C 6 H 4 + 76.0313 + C 12 H 16 N 2 O 1 + 204.27 + 204.12627 + K + artifact + Unimod:208 + PSI-MOD + Acrolein addition +76 + Delta:H(4)C(6) + MOD:00559 + acrolein addition +76 + true + + + + + OBSOLETE because this modification not supported by any literature that I can find[PMT] + Unimod:208 + + + + + Acrolein addition +76 + + + + + + Delta:H(4)C(6) + + + + + + + + + OBSOLETE because this modification not supported by any literature that I can find[PMT] + 112.13 + C 6 H 8 O 2 + 112.05243 + C 12 H 20 N 2 O 3 + 240.3 + 240.1474 + K + artifact + Unimod:209 + PSI-MOD + Acrolein addition +112 + Delta:H(8)C(6)O(2) + MOD:00560 + acrolein addition +112 + true + + + + + OBSOLETE because this modification not supported by any literature that I can find[PMT] + Unimod:209 + + + + + Acrolein addition +112 + + + + + + Delta:H(8)C(6)O(2) + + + + + + + + + + modification from Unimod Isotopic label + 85.11 + C 4 H 7 N 1 O 1 + 85.052765 + X + artifact + Unimod:211 + PSI-MOD + N-ethyl iodoacetamide-d0 + NEIAA + MOD:00561 + N-ethyl iodoacetamide- + + + + + modification from Unimod Isotopic label + PubMed:12766232 + Unimod:211 + + + + + N-ethyl iodoacetamide-d0 + + + + + + NEIAA + + + + + + + + + + modification from Unimod Isotopic label + 90.08 + C 4 (1)H 2 (2)H 5 N 1 O 1 + 90.084145 + X + artifact + Unimod:212 + PSI-MOD + N-ethyl iodoacetamide-d5 + NEIAA:2H(5) + MOD:00562 + N-ethyl iodoacetamide-d5 + + + + + modification from Unimod Isotopic label + PubMed:12766232 + Unimod:212 + + + + + N-ethyl iodoacetamide-d5 + + + + + + NEIAA:2H(5) + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an N-acetylaminogalactose group through a glycosidic bond. + 203.19 + C 8 H 13 N 1 O 5 + 203.07938 + X + GalNAcRes + PSI-MOD + HexNAc + MOD:00563 + + mono-N-acetylaminogalactosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an N-acetylaminogalactose group through a glycosidic bond. + PubMed:18688235 + + + + + GalNAcRes + + + + + + HexNAc + + + + + + + + + Modification from Unimod Isotopic label. The Unimod term was extracted when it had not been approved. OBSOLETE because redundant to MOD:01505. Remap to MOD:01505, or one of the child terms MOD:01493 or MOD:01497. + MOD:01505 + X + artifact + Unimod:214 + PSI-MOD + Representative mass and accurate mass for 116 & 117 + iTRAQ4plex + MOD:00564 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + true + + + + + Modification from Unimod Isotopic label. The Unimod term was extracted when it had not been approved. OBSOLETE because redundant to MOD:01505. Remap to MOD:01505, or one of the child terms MOD:01493 or MOD:01497. + URL:http://docs.appliedbiosystems.com/pebiodocs/04351918.pdf + Unimod:214 + + + + + Representative mass and accurate mass for 116 & 117 + + + + + + iTRAQ4plex + + + + + + + + + + modification from Unimod N-linked glycosylation + 0.98 + H -1 N -1 O 1 + 0.984016 + C 4 H 5 N 1 O 3 + 115.09 + 115.02694 + N + artifact + Unimod:7 + PSI-MOD + Deamidated + Deamidation + MOD:00565 + Conversion of glycosylated asparagine residues upon deglycosylation with PGNase F in H2O. CAUTION - the difference formula appears to be based on a partial structure [JSG]. + deglycosylated asparagine + + + + + modification from Unimod N-linked glycosylation + Unimod:7#N + + + + + Deamidated + + + + + + Deamidation + + + + + + + + + + + modification from Unimod Chemical derivative + 297.15 + Br 1 C 12 H 13 N 2 O 2 + 296.01605 + Br 1 C 15 H 18 N 3 O 3 S 1 + 400.29 + 399.02524 + C + artifact + Unimod:243 + PSI-MOD + IGBP + Light IDBEST tag for quantitation + MOD:00566 + "IDBEST tag for quantitation, http://www.targetdiscovery.com/index.php?topic=prod.idbe" + label cysteine with IGBP reagent + + + + + modification from Unimod Chemical derivative + Unimod:243 + + + + + IGBP + + + + + + Light IDBEST tag for quantitation + + + + + + + + + OBSOLETE because Unimod entry 244 is redundant with Unimod 348. Remap to MOD:00775. + -23.04 + C -2 H -1 N -1 O 1 + -23.015984 + H + artifact + Unimod:244 + PSI-MOD + MOD:00567 + histidine oxidation to asparagine + true + + + + + OBSOLETE because Unimod entry 244 is redundant with Unimod 348. Remap to MOD:00775. + ChEBI:29956 + PubMed:15736973 + PubMed:5681232 + PubMed:6692818 + PubMed:9789001 + RESID:AA0003 + Unimod:244 + + + + + + + + OBSOLETE because Unimod entry 245 is redundant with Unimod 349. Remap to MOD:00776 + MOD:00776 + -22.05 + C -2 H -2 N -2 O 2 + -22.03197 + H + artifact + Unimod:245 + PSI-MOD + MOD:00568 + histidine oxidation to aspartic acid + true + + + + + OBSOLETE because Unimod entry 245 is redundant with Unimod 349. Remap to MOD:00776 + PubMed:1097438 + PubMed:339692 + PubMed:4399050 + PubMed:5764436 + PubMed:6692818 + PubMed:8089117 + PubMed:9521123 + PubMed:9582379 + Unimod:245 + + + + + + + + + Natural or modified residues that are isobaric at a resolution below 0.000001 Da. + PSI-MOD + MOD:00569 + + residues isobaric at a resolution below 0.000001 Da + + + + + Natural or modified residues that are isobaric at a resolution below 0.000001 Da. + PubMed:18688235 + + + + + + + + + + Natural or modified residues with a mass of 71.037114 Da. + PSI-MOD + MOD:00570 + residues isobaric at 71.037114 Da + + + + + Natural or modified residues with a mass of 71.037114 Da. + PubMed:18688235 + + + + + + + + + + + A modification that effectively oxygenates C5 of an L-proline residue to form a 2-pyrrolidone-5-carboxylic acid, pyroglutamic acid. + 13.98 + H -2 O 1 + 13.979265 + C 5 H 6 N 1 O 2 + 112.11 + 112.039856 + P + artifact + Unimod:359 + PyrGlu(Pro) + pyroglutamicp + PSI-MOD + Pro->pyro-Glu + Pyroglutamic + MOD:00571 + The review article PubMed:9252331 does not provide an original citation for this modification [JSG]. + 2-pyrrolidone-5-carboxylic acid (Pro) + + + + + A modification that effectively oxygenates C5 of an L-proline residue to form a 2-pyrrolidone-5-carboxylic acid, pyroglutamic acid. + OMSSA:111 + PubMed:9252331 + Unimod:359 + + + + + PyrGlu(Pro) + + + + + + pyroglutamicp + + + + + + Pro->pyro-Glu + + + + + + Pyroglutamic + + + + + + + + + + + modification from Unimod Chemical derivative + 199.27 + C 9 H 13 N 1 O 2 S 1 + 199.0667 + C 15 H 25 N 5 O 3 S 1 + 355.46 + 355.16782 + R + artifact + Unimod:343 + PSI-MOD + Argbiotinhydrazide + oxidized Arginine biotinylated with biotin hydrazide + MOD:00572 + oxidized arginine biotinylated with biotin hydrazide + + + + + modification from Unimod Chemical derivative + PubMed:15174056 + PubMed:15828771 + Unimod:343 + + + + + Argbiotinhydrazide + + + + + + oxidized Arginine biotinylated with biotin hydrazide + + + + + + + + + + + modification from Unimod Chemical derivative + 241.31 + C 10 H 15 N 3 O 2 S 1 + 241.0885 + C 16 H 27 N 5 O 3 S 1 + 369.48 + 369.18347 + K + artifact + Unimod:353 + PSI-MOD + Lysbiotinhydrazide + oxidized Lysine biotinylated with biotin hydrazide + MOD:00573 + "http://www.piercenet.com/Proteomics/browse.cfm?fldID=84EBE112-F871-4CA5-807F-47327153CFCB" + oxidized lysine biotinylated with biotin hydrazide + + + + + modification from Unimod Chemical derivative + PubMed:15174056 + Unimod:353 + + + + + Lysbiotinhydrazide + + + + + + oxidized Lysine biotinylated with biotin hydrazide + + + + + + + + + + + modification from Unimod Chemical derivative + 258.34 + C 10 H 18 N 4 O 2 S 1 + 258.11505 + C 15 H 25 N 5 O 3 S 1 + 355.46 + 355.16782 + P + artifact + Unimod:357 + PSI-MOD + oxidized proline biotinylated with biotin hydrazide + probiotinhydrazide + MOD:00574 + "http://www.piercenet.com/Proteomics/browse.cfm?fldID=84EBE112-F871-4CA5-807F-47327153CFCB" + oxidized proline biotinylated with biotin hydrazide + + + + + modification from Unimod Chemical derivative + PubMed:15174056 + Unimod:357 + + + + + oxidized proline biotinylated with biotin hydrazide + + + + + + probiotinhydrazide + + + + + + + + + + + modification from Unimod Chemical derivative + 240.32 + C 10 H 16 N 4 O 1 S 1 + 240.10448 + C 14 H 23 N 5 O 3 S 1 + 341.43 + 341.15216 + T + artifact + Unimod:361 + PSI-MOD + Thrbiotinhydrazide + oxidized Threonine biotinylated with biotin hydrazide + MOD:00575 + "http://www.piercenet.com/Proteomics/browse.cfm?fldID=84EBE112-F871-4CA5-807F-47327153CFCB" + oxidized threonine biotinylated with biotin hydrazide + + + + + modification from Unimod Chemical derivative + PubMed:15174056 + Unimod:361 + + + + + Thrbiotinhydrazide + + + + + + oxidized Threonine biotinylated with biotin hydrazide + + + + + + + + + + modification from Unimod Other + 70.09 + C 4 H 6 O 1 + 70.04186 + X + artifact + Unimod:253 + PSI-MOD + Crotonaldehyde + MOD:00576 + crotonylated residue + + + + + modification from Unimod Other + PubMed:11283024 + PubMed:25907603 + Unimod:253 + + + + + Crotonaldehyde + + + + + + Crotonaldehyde + + + + + + + + + + + modification occurs as a Schiff base in the presence of pentalysine + 26.04 + C 2 H 2 + 26.01565 + C 8 H 14 N 2 O 1 + 666.91 + 666.4905 + K, K, K, K, K + artifact + Unimod:254 + PSI-MOD + Acetaldehyde +26 + Delta:H(2)C(2) + MOD:00577 + acetaldehyde crosslinked penta-L-lysine + + + + + modification occurs as a Schiff base in the presence of pentalysine + PubMed:7744761 + Unimod:254 + + + + + Acetaldehyde +26 + + + + + + Delta:H(2)C(2) + + + + + + + + + OBSOLETE because this modification not supported by any literature that I can find [PMT] + 28.05 + C 2 H 4 + 28.0313 + C + X + artifact + Unimod:255 + PSI-MOD + Acetaldehyde +28 + Delta:H(4)C(2) + MOD:00578 + acetaldehyde +28 + true + + + + + OBSOLETE because this modification not supported by any literature that I can find [PMT] + Unimod:255 + + + + + Acetaldehyde +28 + + + + + + Delta:H(4)C(2) + + + + + + + + + OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other + 40.06 + C 3 H 4 + 40.0313 + X + artifact + Unimod:256 + PSI-MOD + Delta:H(4)C(3) + Propionaldehyde +40 + MOD:00579 + propionaldehyde +40 + true + + + + + OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other + Unimod:256 + + + + + Delta:H(4)C(3) + + + + + + Propionaldehyde +40 + + + + + + + + + OBSOLETE because entry removed from Unimod. Remap potentially to MOD:00579 propionaldehyde +40 + MOD:00579 + 42.08 + C 3 H 6 + 42.04695 + X + artifact + Unimod:257 + PSI-MOD + MOD:00580 + propionaldehyde +42 + true + + + + + OBSOLETE because entry removed from Unimod. Remap potentially to MOD:00579 propionaldehyde +40 + Unimod:257 + + + + + + + + + A protein modification that effectively substitutes one (18)O atom for one (16)O atom. + 2.0 + (16)O -1 (18)O 1 + 2.004246 + X + artifact + C-term + Unimod:258 + ctermpepo18 + PSI-MOD + Label:18O(1) + O18 Labeling + MOD:00581 + + (18)O monosubstituted residue + + + + + A protein modification that effectively substitutes one (18)O atom for one (16)O atom. + OMSSA:87 + PubMed:11467524 + Unimod:258 + + + + + ctermpepo18 + + + + + + Label:18O(1) + + + + + + O18 Labeling + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 6x(13)C,2x(15)N labeled L-lysine. + 8.01 + (12)C -6 (13)C 6 (14)N -2 (15)N 2 + 8.014199 + (13)C 6 H 12 (15)N 2 O 1 + 136.11 + 136.10916 + K + artifact + Unimod:259 + lys-13C615N2 + PSI-MOD + 13C(6) 15N(2) Silac label + Label:13C(6)15N(2) + MOD:00582 + 6x(13)C,2x(15)N labeled L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to 6x(13)C,2x(15)N labeled L-lysine. + OMSSA:181 + PubMed:12716131 + Unimod:259 + + + + + lys-13C615N2 + + + + + + 13C(6) 15N(2) Silac label + + + + + + Label:13C(6)15N(2) + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a thiophosphono group (H2PO2S, 'thiophosphate'). + 96.04 + H 1 O 2 P 1 S 1 + 95.94349 + X + artifact + Unimod:260 + PSI-MOD + Thiophospho + Thiophosphorylation + MOD:00583 + thiophosphorylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with a thiophosphono group (H2PO2S, 'thiophosphate'). + PubMed:12110917 + Unimod:260 + + + + + Thiophospho + + + + + + Thiophosphorylation + + + + + + + + + + A protein modification produced by formation of an adduct with 4-sulfophenyl isothiocyanate. + 215.24 + C 7 H 5 N 1 O 3 S 2 + 214.97108 + X + artifact + N-term + Unimod:261 + PSI-MOD + 4-sulfophenyl isothiocyanate + SPITC + MOD:00584 + 4-sulfophenyl isothiocyanate derivatized residue + + + + + A protein modification produced by formation of an adduct with 4-sulfophenyl isothiocyanate. + PubMed:14689565 + PubMed:14745769 + PubMed:16526082 + Unimod:261 + + + + + 4-sulfophenyl isothiocyanate + + + + + + SPITC + + + + + + + + + + A protein modification that effectively substitutes three (2)H deuterium atoms for three (1)H protium atoms. + 3.02 + (1)H -3 (2)H 3 + 3.01883 + X + artifact + Unimod:262 + D(H)3Res + PSI-MOD + Label:2H(3) + Trideuteration + MOD:00585 + deuterium trisubstituted residue + + + + + A protein modification that effectively substitutes three (2)H deuterium atoms for three (1)H protium atoms. + Unimod:262 + + + + + D(H)3Res + + + + + + Label:2H(3) + + + + + + Trideuteration + + + + + + + + + + modification from Unimod Chemical derivative + 121.2 + C 7 H 7 N 1 O -1 S 1 + 121.035 + X + artifact + Unimod:264 + PSI-MOD + PET + phosphorylation to pyridyl thiol + MOD:00586 + pyridyl thiol modified residue + + + + + modification from Unimod Chemical derivative + Unimod:264 + + + + + PET + + + + + + phosphorylation to pyridyl thiol + + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to 6x(13)C, 4x(15)N labeled L-arginine. + 10.01 + (12)C -6 (13)C 6 (14)N -4 (15)N 4 + 10.008269 + (13)C 6 H 12 (15)N 4 O 1 + 166.11 + 166.10938 + R + artifact + Unimod:267 + arg-13c6-15n4 + PSI-MOD + 13C(6) 15N(4) Silac label + Label:13C(6)15N(4) + MOD:00587 + + 6x(13)C,4x(15)N labeled L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to 6x(13)C, 4x(15)N labeled L-arginine. + OMSSA:137 + PubMed:12716131 + Unimod:267 + + + + + arg-13c6-15n4 + + + + + + 13C(6) 15N(4) Silac label + + + + + + Label:13C(6)15N(4) + + + + + + + + + + + A protein modification that effectively converts an L-valine residue to 5x(13)C,1x(15)N labeled L-valine. + 6.01 + (12)C -5 (13)C 5 (14)N -1 (15)N 1 + 6.013809 + (13)C 5 H 9 (15)N 1 O 1 + 105.08 + 105.08222 + V + artifact + Unimod:268 + PSI-MOD + 13C(5) 15N(1) Silac label + Label:13C(5)15N(1) + MOD:00588 + 5x(13)C,1x(15)N labeled L-valine + + + + + A protein modification that effectively converts an L-valine residue to 5x(13)C,1x(15)N labeled L-valine. + PubMed:12771378 + Unimod:268#V + + + + + 13C(5) 15N(1) Silac label + + + + + + Label:13C(5)15N(1) + + + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to (13)C,(15)N labeled L-phenylalanine. + 10.03 + (12)C -9 (13)C 9 (14)N -1 (15)N 1 + 10.027228 + (13)C 9 H 9 (15)N 1 O 1 + 157.1 + 157.09564 + F + artifact + Unimod:269 + PSI-MOD + 13C(9) 15N(1) Silac label + Label:13C(9)15N(1) + MOD:00589 + 9x(13)C,1x(15)N labeled L-phenylalanine + + + + + A protein modification that effectively converts an L-phenylalanine residue to (13)C,(15)N labeled L-phenylalanine. + PubMed:12771378 + Unimod:269 + + + + + 13C(9) 15N(1) Silac label + + + + + + Label:13C(9)15N(1) + + + + + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative + 362.38 + C 19 H 22 O 7 + 362.13657 + X + artifact + Unimod:270 + PSI-MOD + Cytopiloyne + nucleophilic addtion to cytopiloyne + MOD:00590 + nucleophilic addtion to cytopiloyne + true + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative + PubMed:15549660 + Unimod:270 + + + + + Cytopiloyne + + + + + + nucleophilic addtion to cytopiloyne + + + + + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative + 380.39 + C 19 H 24 O 8 + 380.14713 + X + artifact + Unimod:271 + PSI-MOD + Cytopiloyne+water + nucleophilic addition to cytopiloyne+H2O + MOD:00591 + nucleophilic addition to cytopiloyne+H2O + true + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative + PubMed:15549660 + Unimod:271 + + + + + Cytopiloyne+water + + + + + + nucleophilic addition to cytopiloyne+H2O + + + + + + + + + + modification from Unimod Chemical derivative + 136.12 + C 3 H 4 O 4 S 1 + 135.98303 + X + artifact + N-term + Unimod:272 + PSI-MOD + CAF + sulfonation of N-terminus + MOD:00592 + sulfonation of N-terminal + + + + + modification from Unimod Chemical derivative + PubMed:12705581 + PubMed:15732931 + PubMed:16046801 + Unimod:272 + + + + + CAF + + + + + + sulfonation of N-terminus + + + + + + + + + OBSOLETE because removed from Unimod. modification from Unimod Chemical derivative + 253.25 + C 12 H 15 N 1 O 5 + 253.09502 + C 18 H 27 N 3 O 6 + 381.43 + 381.18997 + K + artifact + Unimod:273 + PSI-MOD + Xlink:SSD + covalent modification of lysine by cross-linking reagent + MOD:00593 + J. Prot. Chem. 2, 263-277, 1983 + covalent modification of lysine by omega-maleimido alkanoyl N-hydroxysuccinimido esters + true + + + + + OBSOLETE because removed from Unimod. modification from Unimod Chemical derivative + Unimod:273 + + + + + Xlink:SSD + + + + + + covalent modification of lysine by cross-linking reagent + + + + + + + + + + + Natural or modified resiues with a mass of 113.047678 Da. + PSI-MOD + MOD:00594 + + residues isobaric at 113.047678 Da + + + + + Natural or modified resiues with a mass of 113.047678 Da. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an manose group through a glycosidic bond + 162.14 + C 6 H 10 O 5 + 162.05283 + X + natural + ManRes + PSI-MOD + MOD:00595 + + monomannosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an manose group through a glycosidic bond + PubMed:18688235 + + + + + ManRes + + + + + + + + + + A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS. + 183.23 + C 8 H 9 N 1 O 2 S 1 + 183.0354 + X + artifact + Unimod:276 + AEBSF + PSI-MOD + AEBS + Aminoethylbenzenesulfonylation + MOD:00596 + From DeltaMass: Average Mass: 183 Average Mass Change:183 References:We have found that AEBSF modifies many proteins by covalent attachment, preferentially on Tyr, and to a lesser extent on Lys, His, and the amino-terminus. These modifications were identified by electrospray MS of the proteins (adds 183 Da per AEBS-group) and by peptide mapping and MS/MS. All the proteins we examined were modified after 24 hrs. at 4 C with 1 mM AEBSF in TRIS, pH 8.0. The reaction is 10-20x slower at pH 7; however AEBSF is quite stable in aqueous solution and the extent of to which the protein is modified continues to increase for several days. We have seen the addition of 10 or more AEBS-groups to proteins after prolonged storage. We found no equivalent modification from PMSF, probably because it degrades so quickly. We no longer use AEBSF, and urge caution to those who do. To address the problem, Boehringer Mannheim (now Roche Molecular Biochemicals) introduced Pefabloc PLUS which includes an additional component to compete for these side reactions. In our limited experience with Pefabloc PLUS, it reduces the +183 modifications, but does not always eliminate them. As a result, we prefer PMSF, despite its own set of drawbacks. We have never found PMSF-induced modification of proteins (except trypsin), probably due to its short half-life in aqeous solution. + 4-(2-aminoethyl)benzenesulfonyl fluoride derivatized residue + + + + + A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS. + DeltaMass:235 + PubMed:8597590 + Unimod:276 + + + + + AEBSF + + + + + + AEBS + + + + + + Aminoethylbenzenesulfonylation + + + + + + + + + OBSOLETE because Unimod entry 277 redundant with Unimod 39. Remap to MOD:00110. + MOD:00110 + 46.09 + C 1 H 2 S 1 + 45.98772 + C + artifact + Unimod:277 + PSI-MOD + MOD:00597 + methyl methanethiosulfonate + true + + + + + OBSOLETE because Unimod entry 277 redundant with Unimod 39. Remap to MOD:00110. + Unimod:277 + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-(2-hydroxyethyl)cysteine + 44.05 + C 2 H 4 O 1 + 44.026215 + C 5 H 9 N 1 O 2 S 1 + 147.19 + 147.0354 + C + artifact + Unimod:278 + PSI-MOD + Ethanolation of Cys + Ethanolyl + MOD:00598 + + This modification of cysteine is produced by the reagent iodoethanol with triethylphosphine [JSG]. + S-(2-hydroxyethyl)cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-(2-hydroxyethyl)cysteine + PubMed:15351294 + Unimod:278 + + + + + Ethanolation of Cys + + + + + + Ethanolyl + + + + + + + + + + A protein modification that effectively replaces one hydrogen atom with one methyl group. + 14.03 + C 1 H 2 + 14.01565 + X + Unimod:34 + Me1Res + PSI-MOD + Methyl + Methylation + MOD:00599 + + monomethylated residue + + + + + A protein modification that effectively replaces one hydrogen atom with one methyl group. + PubMed:11875433 + Unimod:34 + + + + + Me1Res + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-ethyl ester. + 28.05 + C 2 H 4 + 28.0313 + C 7 H 11 N 1 O 3 + 157.17 + 157.0739 + E + artifact + Unimod:280 + Ethyl + PSI-MOD + Ethyl + Ethylation + MOD:00600 + From DeltaMass: Average Mass: 28 with no citation. The Unimod citation refers to the formation of glutamate ethyl ester and not to either lysine or N-terminal alkylation. For dimethylated residues, see MOD:00429 and its children [JSG]. + L-glutamic acid 5-ethyl ester + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-ethyl ester. + DeltaMass:0 + PubMed:9629898 + Unimod:280#E + + + + + Ethyl + + + + + + Ethyl + + + + + + Ethylation + + + + + + + + + + A protein modification that effectively produces an heterocyclic amino acid with a covalent bond between the side chain and either its alpha amino or 1-carboxyl group, possibly breaking the peptide chain. + CycRes + PSI-MOD + MOD:00601 + + cyclized residue + + + + + A protein modification that effectively produces an heterocyclic amino acid with a covalent bond between the side chain and either its alpha amino or 1-carboxyl group, possibly breaking the peptide chain. + PubMed:18688235 + + + + + CycRes + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue amino or imino group with an methyl group. + NMeRes + PSI-MOD + MOD:00602 + + N-methylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue amino or imino group with an methyl group. + PubMed:18688235 + + + + + NMeRes + + + + + + + + + OBSOLETE because Unimod entry 283 is redundant with Unimod 280. Remap to MOD:00600 + MOD:00600 + 28.05 + C 2 H 4 + 28.0313 + X + artifact + N-term + Unimod:283 + PSI-MOD + MOD:00603 + N-ethylation + true + + + + + OBSOLETE because Unimod entry 283 is redundant with Unimod 280. Remap to MOD:00600 + Unimod:283 + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 2x(2)H labeled monomethylated L-lysine. + 16.03 + C 1 (2)H 2 + 16.028204 + C 7 (1)H 12 (2)H 2 N 2 O 1 + 144.12 + 144.12317 + K + artifact + Unimod:284 + PSI-MOD + Deuterium Methylation of Lysine + Methyl:2H(2) + MOD:00604 + 2x(2)H monomethylated L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to 2x(2)H labeled monomethylated L-lysine. + PubMed:15525938 + Unimod:284 + + + + + Deuterium Methylation of Lysine + + + + + + Methyl:2H(2) + + + + + + + + + + modification from Unimod Chemical derivative, C-Terminal/Glutamate/Aspartate sulfonation + 155.0 + (12)C 6 H 5 N 1 O 2 S 1 + 155.0041 + X + artifact + C-term + Unimod:285 + PSI-MOD + Light Sulfanilic Acid (SA) C12 + SulfanilicAcid + MOD:00605 + Sulfanilic Acid (SA), light C12 + + + + + modification from Unimod Chemical derivative, C-Terminal/Glutamate/Aspartate sulfonation + Unimod:285 + + + + + Light Sulfanilic Acid (SA) C12 + + + + + + SulfanilicAcid + + + + + + + + + + modification from Unimod Chemical derivative + 161.02 + (13)C 6 H 5 N 1 O 2 S 1 + 161.02423 + X + artifact + C-term + Unimod:286 + PSI-MOD + Heavy Sulfanilic Acid (SA) C13 + SulfanilicAcid:13C(6) + MOD:00606 + Sulfanilic Acid (SA), heavy C13 + + + + + modification from Unimod Chemical derivative + PubMed:9254591 + Unimod:286 + + + + + Heavy Sulfanilic Acid (SA) C13 + + + + + + SulfanilicAcid:13C(6) + + + + + + + + + + modification from Unimod Chemical derivative + 30.99 + H -1 O 2 + 30.982004 + C 11 H 9 N 2 O 3 + 217.2 + 217.06131 + W + artifact + C-term + Unimod:288 + PSI-MOD + Trp->Oxolactone + Tryptophan oxidation to oxolactone + MOD:00607 + Unimod name, formula, and terminal specification corrected. Formula corresponded to uncleaved intermediate [JSG]. + dioxoindolealanine lactone + + + + + modification from Unimod Chemical derivative + PubMed:7949339 + Unimod:288 + + + + + Trp->Oxolactone + + + + + + Tryptophan oxidation to oxolactone + + + + + + + + + + modification from Unimod Chemical derivative + X + artifact + Unimod:289 + PSI-MOD + Biotin polyethyleneoxide amine + Biotin-PEO-Amine + MOD:00608 + biotin polyethyleneoxide amine + + + + + modification from Unimod Chemical derivative + Unimod:289 + + + + + Biotin polyethyleneoxide amine + + + + + + Biotin-PEO-Amine + + + + + + + + + + + modification from Unimod Chemical derivative + 428.61 + C 19 H 32 N 4 O 3 S 2 + 428.1916 + C 22 H 37 N 5 O 4 S 3 + 531.75 + 531.20074 + C + artifact + Unimod:290 + PSI-MOD + Biotin-HPDP + Pierce EZ-Link Biotin-HPDP + MOD:00609 + Pierce EZ-Link Biotin-HPDP modified L-cysteine + + + + + modification from Unimod Chemical derivative + Unimod:290 + + + + + Biotin-HPDP + + + + + + Pierce EZ-Link Biotin-HPDP + + + + + + + + + + + + modification from Unimod Chemical derivative + 200.59 + Hg 1 + 201.97064 + C 3 H 5 Hg 1 N 1 O 1 S 1 + 303.73 + 304.97983 + C + artifact + Unimod:291 + PSI-MOD + Delta:Hg(1) + Mercury Mercaptan + MOD:00610 + cysteinyl mercury + + + + + modification from Unimod Chemical derivative + PubMed:10695144 + Unimod:291 + + + + + Delta:Hg(1) + + + + + + Mercury Mercaptan + + + + + + + + + + A protein modification that is produced by reaction of iodouridine monophosphate with a residue. + 322.17 + C 9 H 11 N 2 O 9 P 1 + 322.0202 + X + artifact + Unimod:292 + PSI-MOD + Cross-link of (Iodo)-uracil MP with W,F,Y + IodoU-AMP + MOD:00611 + iodouridine monophosphate derivatized residue + + + + + A protein modification that is produced by reaction of iodouridine monophosphate with a residue. + PubMed:11112526 + PubMed:11567090 + PubMed:6540775 + Unimod:292 + + + + + Cross-link of (Iodo)-uracil MP with W,F,Y + + + + + + IodoU-AMP + + + + + + + + + + + A protein modification that is produced by derivatization of a residue with 3,3-dithiobis[sulfosuccinimidyl propanoate], DTSSP, or with Pierce EZ-Link Sulfo-NHS-SS-Biotin reagent, sulfosuccinimidyl 3-[(2-[biotinamido]ethyl)disulfanyl]propanoate, followed by reduction with dithiothreitol and then reaction with iodoacetamide. + 145.18 + C 5 H 7 N 1 O 2 S 1 + 145.01974 + X + artifact + Unimod:293 + PSI-MOD + 3-(carbamidomethylthio)propanoyl + CAMthiopropanoyl + MOD:00612 + 3-(carboxamidomethylthio)propanoylated residue + + + + + A protein modification that is produced by derivatization of a residue with 3,3-dithiobis[sulfosuccinimidyl propanoate], DTSSP, or with Pierce EZ-Link Sulfo-NHS-SS-Biotin reagent, sulfosuccinimidyl 3-[(2-[biotinamido]ethyl)disulfanyl]propanoate, followed by reduction with dithiothreitol and then reaction with iodoacetamide. + PubMed:15121203 + Unimod:293 + + + + + 3-(carbamidomethylthio)propanoyl + + + + + + CAMthiopropanoyl + + + + + + + + + + + modification from Unimod Chemical derivative + 326.42 + C 14 H 22 N 4 O 3 S 1 + 326.14127 + C 17 H 27 N 5 O 4 S 2 + 429.55 + 429.15045 + C + artifact + Unimod:294 + PSI-MOD + IED-Biotin + biotinoyl-iodoacetyl-ethylenediamine + MOD:00613 + biotinoyl-iodoacetyl-ethylenediamine + + + + + modification from Unimod Chemical derivative + PubMed:10906242 + Unimod:294 + + + + + IED-Biotin + + + + + + biotinoyl-iodoacetyl-ethylenediamine + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a fucose (6-deoxy-D-galactose) group through a glycosidic bond. + 146.14 + C 6 H 10 O 4 + 146.0579 + X + natural + GNO:G49112ZN + Unimod:295 + Fuc + PSI-MOD + Fucose + dHex + MOD:00614 + + fucosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a fucose (6-deoxy-D-galactose) group through a glycosidic bond. + PubMed:11344537 + PubMed:15189151 + Unimod:295 + + + + + Fuc + + + + + + Fucose + + + + + + dHex + + + + + + + + + OBSOLETE because entry Unimod:261 site N-term R was abandoned. Remap to MOD:00584 + MOD:00584 + 215.24 + C 7 H 5 N 1 O 3 S 2 + 214.97108 + R + artifact + N-term + Unimod:261 + PSI-MOD + MOD:00615 + 4-sulfophenyl isothiocyante modification to N-term R + true + + + + + OBSOLETE because entry Unimod:261 site N-term R was abandoned. Remap to MOD:00584 + PubMed:14689565 + Unimod:261 + + + + + + + + + Natural or modified residues that are isobaric at a resolution below 0.1 Da. + PSI-MOD + MOD:00616 + + residues isobaric at a resolution below 0.1 Da + + + + + Natural or modified residues that are isobaric at a resolution below 0.1 Da. + PubMed:18688235 + + + + + + + + + A protein modification that effectively converts a residue containing common isotopes to a 3x(2)H labeled residue methyl ester. + 17.03 + C 1 (1)H -1 (2)H 3 + 17.03448 + X + artifact + C-term + Unimod:298 + ctermpeptrideuteromethyl + PSI-MOD + Methyl:2H(3) + deuterated methyl ester + MOD:00617 + 3x(2)H residue methyl ester + + + + + A protein modification that effectively converts a residue containing common isotopes to a 3x(2)H labeled residue methyl ester. + OMSSA:21 + Unimod:298 + + + + + ctermpeptrideuteromethyl + + + + + + Methyl:2H(3) + + + + + + deuterated methyl ester + + + + + + + + + + + modification from Unimod Chemical derivative + 44.01 + C 1 O 2 + 43.98983 + C 12 H 10 N 2 O 3 + 230.22 + 230.06914 + W + artifact + Unimod:299 + PSI-MOD + Carboxy + Carboxylation + MOD:00618 + There is no literature citation for this Unimod entry [JSG]. + tryptophan carboxylation + + + + + modification from Unimod Chemical derivative + Unimod:299#W + + + + + Carboxy + + + + + + Carboxylation + + + + + + + + + OBSOLETE because entry 300 is redundant with Unimod 6 remap to MOD:01328 + MOD:01328 + 58.04 + C 2 H 2 O 2 + 58.005478 + W + artifact + Unimod:300 + PSI-MOD + MOD:00619 + hydroxylethanone + true + + + + + OBSOLETE because entry 300 is redundant with Unimod 6 remap to MOD:01328 + Unimod:300 + + + + + + + + + + modification from Unimod Chemical derivative + 190.2 + C 10 H 10 N 2 O 2 + 190.07423 + C 13 H 15 N 3 O 3 S 1 + 293.34 + 293.0834 + C + artifact + Unimod:301 + PSI-MOD + Bromobimane + Monobromobimane derivative + MOD:00620 + 1-(bromomethyl)-2,6,7-trimethylpyrazolo[1,2-a]pyrazole-3,5-dione, C 10 H 11 Br 1 N 2 O 2. + cysteine monobromobimane derivative + + + + + modification from Unimod Chemical derivative + PubMed:7856876 + Unimod:301 + + + + + Bromobimane + + + + + + Monobromobimane derivative + + + + + + + + + + modification from Unimod Chemical derivative + 170.17 + C 11 H 6 O 2 + 170.03677 + X + artifact + Unimod:302 + PSI-MOD + Menadione + Menadione quinone derivative + MOD:00621 + menadione quinone derivative + + + + + modification from Unimod Chemical derivative + PubMed:15939799 + Unimod:302 + + + + + Menadione + + + + + + Menadione quinone derivative + + + + + + + + + + + modification from Unimod Chemical derivative + 76.11 + C 2 H 4 O 1 S 1 + 75.99828 + C 5 H 9 N 1 O 2 S 2 + 179.25 + 179.00748 + C + artifact + Unimod:303 + Beta mercaptoethanol adduct + PSI-MOD + Cysteine mercaptoethanol + DeStreak + MOD:00622 + From DeltaMass: Average Mass: 76 Average Mass Change:76 PubMed:8019414. + cysteine mercaptoethanol + + + + + modification from Unimod Chemical derivative + DeltaMass:80 + PubMed:12442261 + Unimod:303 + + + + + Beta mercaptoethanol adduct + + + + + + Cysteine mercaptoethanol + + + + + + DeStreak + + + + + + + + + + + modification from Unimod N-linked glycosylation + 1443.33 + C 56 H 90 N 4 O 39 + 1442.5182 + C 60 H 96 N 6 O 41 + 1557.43 + 1556.5612 + N + natural + GNO:G25987BV + Unimod:305 + PSI-MOD + Fucosylated biantennary (-2 galactose) + dHex(1)Hex(3)HexNAc(4) + MOD:00623 + fucosylated biantennary (-2 galactose) N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation + Unimod:305 + + + + + Fucosylated biantennary (-2 galactose) + + + + + + dHex(1)Hex(3)HexNAc(4) + + + + + + + + + + Natural or modified residues with a mass of 113.0-113.1 Da. + PSI-MOD + MOD:00624 + + residues isobaric at 113.0-113.1 Da + + + + + Natural or modified residues with a mass of 113.0-113.1 Da. + PubMed:18688235 + + + + + + + + + modification from Unimod Chemical derivative + 111.1 + C 5 H 5 N 1 O 2 + 111.03203 + X + artifact + Unimod:314 + PSI-MOD + Nmethylmaleimide + MOD:00625 + N-methylmaleimide derivatized residue + + + + + modification from Unimod Chemical derivative + Unimod:314 + + + + + Nmethylmaleimide + + + + + + Nmethylmaleimide + + + + + + + + + + modification from Unimod Chemical derivative + 421.43 + C 21 H 15 N 3 O 5 S 1 + 421.07324 + X + artifact + Unimod:478 + PSI-MOD + FTC + fluorescein-5-thiosemicarbazide + MOD:00626 + fluorescein-5-thiosemicarbazide modified residue + + + + + modification from Unimod Chemical derivative + PubMed:2883911 + Unimod:478 + + + + + FTC + + + + + + fluorescein-5-thiosemicarbazide + + + + + + + + + + + modification from Unimod Chemical derivative + 78.11 + C 6 H 6 + 78.04695 + C 12 H 18 N 2 O 1 + 206.29 + 206.1419 + K + artifact + Unimod:316 + (2S)-2-amino-6-(2,5-dimethylpyrrolidin-1-yl)hexanoic acid + 6-(2,5-dimethylpyrrolidin-1-yl)norleucine + PSI-MOD + 2,5-dimethypyrrole + DimethylpyrroleAdduct + MOD:00627 + There is no citation for this Unimod entry. Add PubMed:7981420, correct spelling [JSG]. + 2,5-dimethylpyrrole lysine from 2,5-hexanedione adduct + + + + + modification from Unimod Chemical derivative + Unimod:316 + + + + + (2S)-2-amino-6-(2,5-dimethylpyrrolidin-1-yl)hexanoic acid + + + + + + 6-(2,5-dimethylpyrrolidin-1-yl)norleucine + + + + + + 2,5-dimethypyrrole + + + + + + DimethylpyrroleAdduct + + + + + + + + + + a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with two hexose sugar groups through glycosidic bonds + 324.28 + C 12 H 20 O 10 + 324.10565 + X + natural + GNO:G90627TW + PSI-MOD + MOD:00628 + Hex2 + + + + + a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with two hexose sugar groups through glycosidic bonds + PubMed:18688235 + + + + + + + + + + modification from Unimod Chemical derivative + 62.07 + C 5 H 2 + 62.01565 + C 11 H 14 N 2 O 1 + 190.25 + 190.11061 + K + artifact + Unimod:318 + PSI-MOD + Delta:H(2)C(5) + MDA adduct +62 + MOD:00629 + Usually major adduct formed from malondialdehyde (MDA) with the amino group of lysine residues [UniProt]. + MDA adduct +62 + + + + + modification from Unimod Chemical derivative + Unimod:318 + + + + + Delta:H(2)C(5) + + + + + + MDA adduct +62 + + + + + + + + + + modification from Unimod Chemical derivative + 54.05 + C 3 H 2 O 1 + 54.010567 + X + artifact + Unimod:319 + PSI-MOD + Delta:H(2)C(3)O(1) + MDA adduct +54 + MOD:00630 + This is not a legitimate ontological entry and will become obsolete when the children are reassigned [JSG] + C3-H2-O adduct (+54 amu) of malondialdehyde with lysine or methylglyoxal with arginine. + + + + + modification from Unimod Chemical derivative + PubMed:9328283 + Unimod:319 + + + + + Delta:H(2)C(3)O(1) + + + + + + MDA adduct +54 + + + + + + + + + + modification from Unimod Chemical derivative + 143.14 + C 6 H 9 N 1 O 3 + 143.05824 + X + artifact + Unimod:320 + PSI-MOD + Nethylmaleimide+water + Nethylmaleimidehydrolysis + MOD:00631 + N-ethylmaeimide adduct + H20 (a mixture of isobaric products) [JSG]. + hydrolyzed N-ethylmaleimide adduct + + + + + modification from Unimod Chemical derivative + Unimod:320 + + + + + Nethylmaleimide+water + + + + + + Nethylmaleimidehydrolysis + + + + + + + + + OBSOLETE because this chemical derivative modification from Unimod 321 is deprecated. + -17.01 + H -1 O -1 + -17.00274 + N + artifact + Unimod:321 + PSI-MOD + MOD:00632 + N-succinimide + true + + + + + OBSOLETE because this chemical derivative modification from Unimod 321 is deprecated. + Unimod:321 + + + + + + + + + + modification from Unimod Chemical derivative + 713.57 + C 31 H 30 I 1 N 4 O 6 S 1 + 713.0931 + C 34 H 35 I 1 N 5 O 7 S 2 + 816.71 + 816.10223 + C + artifact + Unimod:323 + bis-((N-iodoacetyl)piperazinyl)sulfonerhodamine + PSI-MOD + Xlink:B10621 + bis-N-I-sulfonerahodamine + MOD:00633 + Invitrogen B-10621, a red fluorescent cross-linking reagent (only link to Cys is indicated) [Unimod]. + bis-N-I-sulfonerahodamine + + + + + modification from Unimod Chemical derivative + Unimod:323 + + + + + bis-((N-iodoacetyl)piperazinyl)sulfonerhodamine + + + + + + Xlink:B10621 + + + + + + bis-N-I-sulfonerahodamine + + + + + + + + + + modification from Unimod Chemical derivative + 123.6 + C 3 Cl 1 H 6 N 1 S 1 + 122.99095 + X + artifact + Unimod:324 + PSI-MOD + DTBP + dimethyl 3,3'-dithiobispropionimidate + MOD:00634 + Pierce reagent, needs sites for N, Q, R, K, and N-term [JSG]. + dimethyl 3,3'-dithiobispropionimidate + + + + + modification from Unimod Chemical derivative + PubMed:770170 + Unimod:324 + + + + + DTBP + + + + + + dimethyl 3,3'-dithiobispropionimidate + + + + + + + + + + + + modification from Unimod Chemical derivative + 572.75 + C 27 H 49 N 4 O 5 P 1 S 1 + 572.3161 + C 30 H 54 N 5 O 7 P 1 S 1 + 659.82 + 659.34814 + S + artifact + Unimod:325 + PSI-MOD + 10-ethoxyphosphinyl-N-(biotinamidopentyl)decanamide + FP-Biotin + MOD:00635 + 10-fluoroethoxyphosphinyl-N-(biotinamidopentyl)decanamide + + + + + modification from Unimod Chemical derivative + PubMed:10611275 + Unimod:325 + + + + + 10-ethoxyphosphinyl-N-(biotinamidopentyl)decanamide + + + + + + FP-Biotin + + + + + + + + + + A protein modification that effectively converts an L-serine residue to S-ethylcysteine. + 44.11 + C 2 H 4 O -1 S 1 + 44.008457 + C 5 H 9 N 1 O 1 S 1 + 131.19 + 131.04048 + S + artifact + Unimod:327 + PSI-MOD + Delta:H(4)C(2)O(-1)S(1) + S-Ethylcystine from Serine + MOD:00636 + Modification from Unimod. Phosphoserine is converted to dehydroalanine then by Michael addition of ethanethiol to S-ethylcysteine. Needs parent and sibling for S-ethyl-cysteine. + S-ethylcysteine (Ser) + + + + + A protein modification that effectively converts an L-serine residue to S-ethylcysteine. + Unimod:327 + + + + + Delta:H(4)C(2)O(-1)S(1) + + + + + + S-Ethylcystine from Serine + + + + + + + + + + + + + + + + + + A protein modification that effectively replaces one hydrogen atom of an L-arginine residue with a (13)C,3x(2)H labeled methyl group to form a 1x(13)C,3x(2)H labeled monomethylated L-arginine. + 18.04 + (13)C 1 (1)H -1 (2)H 3 + 18.037834 + (12)C 6 (13)C 1 (1)H 11 (2)H 3 N 4 O 1 + 174.14 + 174.13895 + R + artifact + Unimod:329 + PSI-MOD + Methyl:2H(3)13C(1) + monomethylated arginine + MOD:00637 + 1x(13)C,3x(2)H labeled monomethylated L-arginine + + + + + A protein modification that effectively replaces one hydrogen atom of an L-arginine residue with a (13)C,3x(2)H labeled methyl group to form a 1x(13)C,3x(2)H labeled monomethylated L-arginine. + Unimod:329 + + + + + Methyl:2H(3)13C(1) + + + + + + monomethylated arginine + + + + + + + + + + + + + + + + + + A protein modification that effectively replaces two hydrogen atoms of an L-arginine residue with two (13)C,3x(2)H labeled methyl groups to form a 2x(13)C,6x(2)H labeled dimethylated L-arginine. + 36.08 + (13)C 2 (1)H -2 (2)H 6 + 36.07567 + (12)C 6 (13)C 2 (1)H 10 (2)H 6 N 4 O 1 + 192.18 + 192.17679 + R + artifact + Unimod:330 + PSI-MOD + Dimethyl:2H(6)13C(2) + dimethylated arginine + MOD:00638 + 2x(13)C,6x(2)H labeled dimethylated L-arginine + + + + + A protein modification that effectively replaces two hydrogen atoms of an L-arginine residue with two (13)C,3x(2)H labeled methyl groups to form a 2x(13)C,6x(2)H labeled dimethylated L-arginine. + PubMed:15782174 + Unimod:330 + + + + + Dimethyl:2H(6)13C(2) + + + + + + dimethylated arginine + + + + + + + + + + + modification from Unimod Chemical derivative + 525.66 + C 19 H 34 N 4 O 5 P 1 S 3 + 525.1429 + X + artifact + Unimod:332 + PSI-MOD + Thiophos-S-S-biotin + thiophosphate labeled with biotin-HPDP + MOD:00639 + thiophosphate labeled with biotin-HPDP + + + + + modification from Unimod Chemical derivative + Unimod:332 + + + + + Thiophos-S-S-biotin + + + + + + thiophosphate labeled with biotin-HPDP + + + + + + + + + + + + modification from Unimod Chemical derivative + 467.54 + C 19 F 1 H 35 N 3 O 5 P 1 S 1 + 467.2019 + C 22 F 1 H 40 N 4 O 7 P 1 S 1 + 554.62 + 554.23395 + S + artifact + Unimod:333 + PSI-MOD + 6-N-biotinylaminohexyl isopropyl phosphate + Can-FP-biotin + MOD:00640 + 6-N-biotinylaminohexyl isopropyl phosphorofluoridate + + + + + modification from Unimod Chemical derivative + Unimod:333 + + + + + 6-N-biotinylaminohexyl isopropyl phosphate + + + + + + Can-FP-biotin + + + + + + + + + OBSOLETE because Unimod entry 334 is merged with Unimod 293. Remap to MOD:00612 + MOD:00612 + 146.18 + C 5 H 8 N 1 O 2 S 1 + 146.02757 + K + artifact + Unimod:334 + PSI-MOD + MOD:00641 + CAMthiopropanoyl of Lys + true + + + + + OBSOLETE because Unimod entry 334 is merged with Unimod 293. Remap to MOD:00612 + Unimod:334 + + + + + + + + + + + + + + + + A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4. + 158.24 + C 9 H 18 O 2 + 158.13068 + X + artifact + Unimod:335 + PSI-MOD + HNE+Delta:H(2) + reduced 4-Hydroxynonenal + MOD:00642 + 4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG]. + reduced 4-hydroxynonenal adduct + + + + + A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4. + PubMed:11910026 + PubMed:15133838 + Unimod:335 + + + + + HNE+Delta:H(2) + + + + + + reduced 4-Hydroxynonenal + + + + + + + + + + modification from Unimod Artifact + 13.04 + C 1 H 3 N 1 O -1 + 13.031634 + X + artifact + Unimod:337 + PSI-MOD + Methylamine + Michael addition with methylamine + MOD:00643 + methylamine Michael addition derivatized residue + + + + + modification from Unimod Artifact + PubMed:11968134 + Unimod:337 + + + + + Methylamine + + + + + + Michael addition with methylamine + + + + + + + + + + + A protein modification that effectively replaces a residue hydroxyl group with an acetoxy group. + 42.04 + C 2 H 2 O 1 + 42.010567 + X + natural + OAcRes + PSI-MOD + MOD:00644 + + mono O-acetylated residue + + + + + A protein modification that effectively replaces a residue hydroxyl group with an acetoxy group. + PubMed:18688235 + + + + + OAcRes + + + + + + + + + + + A protein modification that effectively replaces a residue sulfanyl group with an acetylsulfanyl group. + 42.04 + C 2 H 2 O 1 S 0 + 42.010567 + X + natural + SAcRes + PSI-MOD + MOD:00645 + + mono S-acetylated residue + + + + + A protein modification that effectively replaces a residue sulfanyl group with an acetylsulfanyl group. + PubMed:18688235 + + + + + SAcRes + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to either N-acetyl-L-cysteine or S-acetyl-L-cysteine. + 42.04 + C 2 H 2 N 0 O 1 S 0 + 42.010567 + C 5 H 7 N 1 O 2 S 1 + 145.18 + 145.01974 + C + natural + AcCys + PSI-MOD + MOD:00646 + + monoacetylated L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to either N-acetyl-L-cysteine or S-acetyl-L-cysteine. + PubMed:18688235 + + + + + AcCys + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to either N-acetyl-L-serine, O-acetyl-L-serine, or N,O-diacetyl-L-serine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + S + natural + AcSer + PSI-MOD + MOD:00647 + + monoacetylated L-serine + + + + + A protein modification that effectively converts an L-serine residue to either N-acetyl-L-serine, O-acetyl-L-serine, or N,O-diacetyl-L-serine. + PubMed:18688235 + + + + + AcSer + + + + + + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to N,O-diacetyl-L-serine. + 84.07 + C 4 H 4 N 0 O 2 + 84.021126 + C 7 H 10 N 1 O 4 + 172.16 + 172.06099 + S + artifact + N-term + (S)-2-acetamido-3-acetyloxypropanoic acid + N,O-diacetyl-L-serine + N,O-diacetylserine + NOAc2Ser + PSI-MOD + MOD:00648 + In one paper, the samples were prepared using glacial acetic acid, and were probably artifactual [JSG]. + N,O-diacetylated L-serine + + + + + A protein modification that effectively converts an L-serine residue to N,O-diacetyl-L-serine. + PubMed:16731519 + PubMed:489587 + PubMed:7309355 + RESID:AA0051#var + RESID:AA0364#var + + + + + (S)-2-acetamido-3-acetyloxypropanoic acid + + + + + + N,O-diacetyl-L-serine + + + + + + N,O-diacetylserine + + + + + + NOAc2Ser + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an acyl group. + AcylRes + PSI-MOD + MOD:00649 + + acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an acyl group. + PubMed:18688235 + + + + + AcylRes + + + + + + + + + + + A protein modification that effectively replaces a residue amino group with a myristoylamino group. + 210.36 + C 14 H 26 O 1 + 210.19836 + X + natural + NMyrRes + PSI-MOD + MOD:00650 + + N-myristoylated residue + + + + + A protein modification that effectively replaces a residue amino group with a myristoylamino group. + PubMed:18688235 + + + + + NMyrRes + + + + + + + + + + + A protein modification that effectively replaces a residue amino group with a palmitoylamino group. + 238.41 + C 16 H 30 O 1 + 238.22966 + X + natural + N-hexadecanoylated residue + NPamRes + PSI-MOD + MOD:00651 + + N-palmitoylated residue + + + + + A protein modification that effectively replaces a residue amino group with a palmitoylamino group. + PubMed:18688235 + + + + + N-hexadecanoylated residue + + + + + + NPamRes + + + + + + + + + + + A protein modification that effectively replaces a residue hydroxyl group with a palmitoyloxy group. + 238.41 + C 16 H 30 O 1 + 238.22966 + X + natural + O-hexadecanoylated residue + OPamRes + PSI-MOD + MOD:00652 + + O-palmitoylated residue + + + + + A protein modification that effectively replaces a residue hydroxyl group with a palmitoyloxy group. + PubMed:18688235 + + + + + O-hexadecanoylated residue + + + + + + OPamRes + + + + + + + + + + + A protein modification that effectively replaces a residue sulfanyl group with an palmitoylsulfanyl group. + 238.41 + C 16 H 30 O 1 S 0 + 238.22966 + X + natural + S-hexadecanoylated residue + SPamRes + PSI-MOD + MOD:00653 + + S-palmitoylated residue + + + + + A protein modification that effectively replaces a residue sulfanyl group with an palmitoylsulfanyl group. + PubMed:18688235 + + + + + S-hexadecanoylated residue + + + + + + SPamRes + + + + + + + + + + a protein modification that effectively replaces a sulfanyl group with a methylsulfanyl group + SMeRes + PSI-MOD + MOD:00654 + + S-methylated residue + + + + + a protein modification that effectively replaces a sulfanyl group with a methylsulfanyl group + PubMed:18688235 + + + + + SMeRes + + + + + + + + + + + A protein modification that effectively replaces a residue sulfanyl group with an myristoylsulfanyl group. + 210.36 + C 14 H 26 O 1 S 0 + 210.19836 + X + natural + SMyrRes + PSI-MOD + MOD:00655 + S-myristoylated residue + + + + + A protein modification that effectively replaces a residue sulfanyl group with an myristoylsulfanyl group. + PubMed:18688235 + + + + + SMyrRes + + + + + + + + + + A protein modification that effectively replaces a residue hydrocarbyl hydrogen with an methyl group. + CMeRes + PSI-MOD + MOD:00656 + C-methylated residue + + + + + A protein modification that effectively replaces a residue hydrocarbyl hydrogen with an methyl group. + PubMed:18688235 + + + + + CMeRes + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-glutamine residue to L-glutamate 5-methyl ester. + 15.01 + C 1 H 1 N -1 O 1 + 14.999666 + C 6 H 9 N 1 O 3 + 143.14 + 143.05824 + Q + natural + Unimod:528 + uniprot.ptm:PTM-0127 + (2S)-2-amino-5-methoxy-5-oxopentanoic acid + (5)-methyl L-hydrogen glutamate + 2-aminopentanedioic acid 5-methyl ester + 5-methyl L-2-aminoglutarate + 5-methyl L-glutamate + L-glutamic acid 5-methyl ester + MOD_RES Glutamate methyl ester (Gln) + O5MeGlu(Gln) + deamidated 5-methyl esterified glutamine + glutamic acid 5-methyl ester + glutamic acid gamma-methyl ester + PSI-MOD + Deamidation followed by a methylation + Methyl+Deamidated + MOD:00657 + + This is known to be a natural modification of glutamine in prokaryotes. + L-glutamic acid 5-methyl ester (Gln) + + + + + A protein modification that effectively converts an L-glutamine residue to L-glutamate 5-methyl ester. + PubMed:16888 + PubMed:6300110 + RESID:AA0072#GLN + Unimod:528 + + + + + (2S)-2-amino-5-methoxy-5-oxopentanoic acid + + + + + + (5)-methyl L-hydrogen glutamate + + + + + + 2-aminopentanedioic acid 5-methyl ester + + + + + + 5-methyl L-2-aminoglutarate + + + + + + 5-methyl L-glutamate + + + + + + L-glutamic acid 5-methyl ester + + + + + + MOD_RES Glutamate methyl ester (Gln) + + + + + + O5MeGlu(Gln) + + + + + + deamidated 5-methyl esterified glutamine + + + + + + glutamic acid 5-methyl ester + + + + + + glutamic acid gamma-methyl ester + + + + + + Deamidation followed by a methylation + + + + + + Methyl+Deamidated + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to a methylated arginine, either 5-methylargine, N5-methylarginine, or an omega-N-methylated L-arginine. + R + uniprot.ptm:PTM-0238 + MeArg + PSI-MOD + MOD:00658 + + methylated arginine + + + + + A protein modification that effectively converts an L-arginine residue to a methylated arginine, either 5-methylargine, N5-methylarginine, or an omega-N-methylated L-arginine. + PubMed:18688235 + + + + + MeArg + + + + + + + + + + + A protein modification that effectively converts an L-glutamine residue to a methylated glutamine, either 2-methylated glutamine, N5-methylated glutamine, or methyl esterified deamidated glutamine. + Q + natural + MeGln + PSI-MOD + MOD:00659 + + methylated glutamine + + + + + A protein modification that effectively converts an L-glutamine residue to a methylated glutamine, either 2-methylated glutamine, N5-methylated glutamine, or methyl esterified deamidated glutamine. + PubMed:18688235 + + + + + MeGln + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to a methylated cysteine, either S-methylcysteine, or cysteine methyl ester. + C + natural + MeCys + PSI-MOD + MOD:00660 + + methylated cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to a methylated cysteine, either S-methylcysteine, or cysteine methyl ester. + PubMed:18688235 + + + + + MeCys + + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to a methylated histidine, such as pros-methylhistidine, or tele-methylhistidine. + H + natural + MeHis + PSI-MOD + MOD:00661 + + methylated histidine + + + + + A protein modification that effectively converts an L-histidine residue to a methylated histidine, such as pros-methylhistidine, or tele-methylhistidine. + PubMed:18688235 + + + + + MeHis + + + + + + + + + + + A protein modification that effectively converts an L-leucine residue to a methylated leucine, either N-methylleucine, or leucine methyl ester. + L + natural + MeLeu + PSI-MOD + MOD:00662 + + methylated leucine + + + + + A protein modification that effectively converts an L-leucine residue to a methylated leucine, either N-methylleucine, or leucine methyl ester. + PubMed:18688235 + + + + + MeLeu + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to a methylated lysine. + K + natural + uniprot.ptm:PTM-0193 + MeLys + PSI-MOD + MOD:00663 + + methylated lysine + + + + + A protein modification that effectively converts an L-lysine residue to a methylated lysine. + PubMed:18688235 + + + + + MeLys + + + + + + + + + + A protein modification that effectively replaces a residue L-enantiomer (stereoisomer) with a D-enantiomer or with a different diastereomeric isomer. + D-Res + PSI-MOD + MOD:00664 + stereoisomerized residue + + + + + A protein modification that effectively replaces a residue L-enantiomer (stereoisomer) with a D-enantiomer or with a different diastereomeric isomer. + PubMed:18688235 + + + + + D-Res + + + + + + + + + + + A protein modification that effectively converts an L-alanine residue to a methylated alanine, such as N-methylalanine, N,N-dimethylalanine, or N,N,N-trimethylalanine. + A + natural + MeAla + PSI-MOD + MOD:00665 + + methylated alanine + + + + + A protein modification that effectively converts an L-alanine residue to a methylated alanine, such as N-methylalanine, N,N-dimethylalanine, or N,N,N-trimethylalanine. + PubMed:18688235 + + + + + MeAla + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an octanoyl group. + 126.2 + C 8 H 14 N 0 O 1 + 126.10446 + X + natural + OctRes + PSI-MOD + MOD:00666 + + octanoylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an octanoyl group. + PubMed:18688235 + + + + + OctRes + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a decanoyl group. + 154.25 + C 10 H 18 N 0 O 1 + 154.13576 + X + natural + DecRes + PSI-MOD + MOD:00667 + decanoylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with a decanoyl group. + PubMed:18688235 + + + + + DecRes + + + + + + + + + + + A protein modification that effectively replaces a residue hydroxyl group with a decanoyloxy group. + 154.25 + C 10 H 18 N 0 O 1 + 154.13576 + X + natural + Unimod:449 + ODecRes + PSI-MOD + Decanoyl + lipid + MOD:00668 + O-decanoylated residue + + + + + A protein modification that effectively replaces a residue hydroxyl group with a decanoyloxy group. + Unimod:449 + + + + + ODecRes + + + + + + Decanoyl + + + + + + lipid + + + + + + + + + + + A protein modification that effectively replaces a residue hydroxyl group with a octanoyloxy group. + 126.2 + C 8 H 14 N 0 O 1 + 126.10446 + X + natural + Unimod:426 + OOctRes + PSI-MOD + Octanoyl + octanoyl + MOD:00669 + + O-octanoylated residue + + + + + A protein modification that effectively replaces a residue hydroxyl group with a octanoyloxy group. + Unimod:426 + + + + + OOctRes + + + + + + Octanoyl + + + + + + octanoyl + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acyl group. + NAcylRes + PSI-MOD + MOD:00670 + + N-acylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acyl group. + PubMed:18688235 + + + + + NAcylRes + + + + + + + + + + A protein modification that effectively replaces a residue hydroxyl group with a acyloxy group. + OAcylRes + PSI-MOD + MOD:00671 + + O-acylated residue + + + + + A protein modification that effectively replaces a residue hydroxyl group with a acyloxy group. + PubMed:18688235 + + + + + OAcylRes + + + + + + + + + + A protein modification that effectively replaces a residue sulfanyl group with an acylsulfanyl group. + SAcylRes + PSI-MOD + MOD:00672 + + S-acylated residue + + + + + A protein modification that effectively replaces a residue sulfanyl group with an acylsulfanyl group. + PubMed:18688235 + + + + + SAcylRes + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to a methylated asparagine, such as N4-methyl-L-asparagine, or N4,N4-dimethyl-L-asparagine. + N + natural + MeAsn + PSI-MOD + MOD:00673 + + methylated asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to a methylated asparagine, such as N4-methyl-L-asparagine, or N4,N4-dimethyl-L-asparagine. + PubMed:18688235 + + + + + MeAsn + + + + + + + + + + A protein modification that effectively replaces a carboxyl group with a carboxamido group. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + X + PSI-MOD + MOD:00674 + + amidated residue + + + + + A protein modification that effectively replaces a carboxyl group with a carboxamido group. + PubMed:18688235 + + + + + + + + + A protein modification that effectively either removes neutral hydrogen atoms (proton and electron), or adds oxygen atoms to a residue with or without the removal of hydrogen atoms. + X + OxRes + PSI-MOD + MOD:00675 + + oxidized residue + + + + + A protein modification that effectively either removes neutral hydrogen atoms (proton and electron), or adds oxygen atoms to a residue with or without the removal of hydrogen atoms. + PubMed:18688235 + + + + + OxRes + + + + + + + + + + A protein modification that effectively adds oxygen atoms to a residue with or without the removal of hydrogen atoms. + X + OxyRes + PSI-MOD + MOD:00676 + + oxygenated residue + + + + + A protein modification that effectively adds oxygen atoms to a residue with or without the removal of hydrogen atoms. + PubMed:18688235 + + + + + OxyRes + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an hydroxyl group. + X + HyRes + Hydroxylation (of delta C of Lysine, beta C of Tryptophan, C3 or C4 of Proline, beta C of Aspartate) + PSI-MOD + MOD:00677 + + From DeltaMass: Average Mass: 16 + hydroxylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an hydroxyl group. + DeltaMass:0 + + + + + HyRes + + + + + + Hydroxylation (of delta C of Lysine, beta C of Tryptophan, C3 or C4 of Proline, beta C of Aspartate) + + + + + + + + + + + A protein modification that effectively converts an L-proline residue to an hydroxylated L-proline. + P + HyPro + PSI-MOD + MOD:00678 + + hydroxylated proline + + + + + A protein modification that effectively converts an L-proline residue to an hydroxylated L-proline. + PubMed:18688235 + + + + + HyPro + + + + + + + + + + A protein modification that effectively adds oxygen atoms to a carbon atom of a residue and removes hydrogen atoms. + COxyRes + PSI-MOD + MOD:00679 + + carbon oxygenated residue + + + + + A protein modification that effectively adds oxygen atoms to a carbon atom of a residue and removes hydrogen atoms. + PubMed:18688235 + + + + + COxyRes + + + + + + + + + + A protein modification that effectively adds oxygen atoms to a sulfur atom of a residue without removing hydrogen atoms. + SOxyRes + PSI-MOD + MOD:00680 + + sulfur oxygenated residue + + + + + A protein modification that effectively adds oxygen atoms to a sulfur atom of a residue without removing hydrogen atoms. + PubMed:18688235 + + + + + SOxyRes + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to a hydroxylated L-lysine. + K + HyLys + PSI-MOD + MOD:00681 + + hydroxylated lysine + + + + + A protein modification that effectively converts an L-lysine residue to a hydroxylated L-lysine. + PubMed:18688235 + + + + + HyLys + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to a hydroxylated L-arginine. + R + uniprot.ptm:PTM-0498 + HyArg + PSI-MOD + MOD:00682 + hydroxylated arginine + + + + + A protein modification that effectively converts an L-arginine residue to a hydroxylated L-arginine. + PubMed:18688235 + + + + + HyArg + + + + + + + + + + A protein modification that effectively removes neutral hydrogen atoms (proton and electron) from a residue. + X + dHRes + PSI-MOD + MOD:00683 + + dehydrogenated residue + + + + + A protein modification that effectively removes neutral hydrogen atoms (proton and electron) from a residue. + PubMed:18688235 + + + + + dHRes + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to L-aspartic acid. + 0.98 + C 0 H -1 N -1 O 1 + 0.984016 + C 4 H 5 N 1 O 3 + 115.09 + 115.02694 + N + natural + Unimod:7 + uniprot.ptm:PTM-0116 + (2S)-2-aminobutanedioic acid + 2-azanylbutanedioic acid + L-aspartic acid + MOD_RES Deamidated asparagine + aminosuccinic acid + dNAsn + PSI-MOD + MOD:00684 + + incidental to RESID:AA0059 + deamidated L-asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to L-aspartic acid. + PubMed:1097438 + PubMed:339692 + PubMed:4399050 + PubMed:5764436 + PubMed:6692818 + PubMed:8089117 + PubMed:9521123 + PubMed:9582379 + RESID:AA0004#ASN + Unimod:7#N + + + + + (2S)-2-aminobutanedioic acid + + + + + + 2-azanylbutanedioic acid + + + + + + L-aspartic acid + + + + + + MOD_RES Deamidated asparagine + + + + + + aminosuccinic acid + + + + + + dNAsn + + + + + + + + + + + A protein modification that effectively converts an L-glutamine residue to L-glutamic acid. + 0.98 + C 0 H -1 N -1 O 1 + 0.984016 + C 5 H 7 N 1 O 3 + 129.12 + 129.04259 + Q + natural + Unimod:7 + uniprot.ptm:PTM-0117 + (2S)-2-aminopentanedioic acid + 1-aminopropane-1,3-dicarboxylic acid + 2-aminoglutaric acid + 2-azanylpentanedioic acid + L-glutamic acid + MOD_RES Deamidated glutamine + alpha-aminoglutaric acid + dNGln + glutaminic acid + PSI-MOD + MOD:00685 + + deamidated L-glutamine + + + + + A protein modification that effectively converts an L-glutamine residue to L-glutamic acid. + PubMed:1881881 + PubMed:4565668 + PubMed:4922541 + PubMed:6692818 + PubMed:9192900 + PubMed:957425 + RESID:AA0006#GLN + Unimod:7#Q + + + + + (2S)-2-aminopentanedioic acid + + + + + + 1-aminopropane-1,3-dicarboxylic acid + + + + + + 2-aminoglutaric acid + + + + + + 2-azanylpentanedioic acid + + + + + + L-glutamic acid + + + + + + MOD_RES Deamidated glutamine + + + + + + alpha-aminoglutaric acid + + + + + + dNGln + + + + + + glutaminic acid + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to L-selenocysteine (not known as a natural, post-translational modification process). + 46.91 + C 0 H 0 N 0 O 0 S -1 Se 1 + 47.94445 + C 3 H 5 N 1 O 1 Se 1 + 150.05 + 150.95363 + C + artifact + Unimod:162 + (2R)-2-amino-3-selanylpropanoic acid + 2-azanyl-3-selanylpropanoic acid + 3-selenylalanine + L-selenocysteine + NON_STD Selenocysteine + SeCys + Sec(Cys) + selenium cysteine + PSI-MOD + MOD:00686 + This entry is for the artifactual formation of L-selenocysteine from cysteine. For encoded L-selenocysteine, use MOD:00031 [JSG]. + L-selenocysteine (Cys) + + + + + A protein modification that effectively converts an L-cysteine residue to L-selenocysteine (not known as a natural, post-translational modification process). + PubMed:10523135 + PubMed:2037562 + PubMed:2963330 + PubMed:6217842 + PubMed:6714945 + RESID:AA0022#CYS + Unimod:162#C + + + + + (2R)-2-amino-3-selanylpropanoic acid + + + + + + 2-azanyl-3-selanylpropanoic acid + + + + + + 3-selenylalanine + + + + + + L-selenocysteine + + + + + + NON_STD Selenocysteine + + + + + + SeCys + + + + + + Sec(Cys) + + + + + + selenium cysteine + + + + + + + + + + + A protein modification that crosslinks two residues by formation of a thioether bond between a cysteine thiol and either an alkyl C as in lanthionine, or an aryl C as 2'-(S-cysteinyl)-L-histidine. + PSI-MOD + MOD:00687 + thioether crosslinked residues + + + + + A protein modification that crosslinks two residues by formation of a thioether bond between a cysteine thiol and either an alkyl C as in lanthionine, or an aryl C as 2'-(S-cysteinyl)-L-histidine. + PubMed:18688235 + + + + + + + + + A protein modification that crosslinks two residues with an amide bond where either the donor amino or carboxyl is not an alpha group. + PSI-MOD + MOD:00688 + + isopeptide crosslinked residues + + + + + A protein modification that crosslinks two residues with an amide bond where either the donor amino or carboxyl is not an alpha group. + PubMed:18688235 + + + + + + + + + A protein modification that crosslinks two cysteine residues by formation of a disulfide bond. + PSI-MOD + MOD:00689 + + disulfide crosslinked residues + + + + + A protein modification that crosslinks two cysteine residues by formation of a disulfide bond. + PubMed:18688235 + + + + + + + + + A protein modification that crosslinks two residues by formation of an oxazole or thiazole ring. + PSI-MOD + MOD:00690 + oxazole/thiazole ring crosslinked residues + + + + + A protein modification that crosslinks two residues by formation of an oxazole or thiazole ring. + PubMed:18688235 + + + + + + + + + A protein modification that crosslinks two residues by formation of an 5-imidazolinone ring. + PSI-MOD + MOD:00691 + 5-imidazolinone ring crosslinked residues + + + + + A protein modification that crosslinks two residues by formation of an 5-imidazolinone ring. + PubMed:18688235 + + + + + + + + + A protein crosslink modification that is not chemically categorized. + PSI-MOD + MOD:00692 + + uncategorized crosslinked residues + + + + + A protein crosslink modification that is not chemically categorized. + PubMed:18688235 + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an carbohydrate-like group through a glycosidic bond. + natural + GlycoRes + PSI-MOD + MOD:00693 + + glycosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an carbohydrate-like group through a glycosidic bond. + PubMed:18688235 + + + + + GlycoRes + + + + + + + + + + A protein modification that effectively substitutes a halogen atom for a hydrogen atom. + HalRes + halogenated residue + PSI-MOD + MOD:00694 + + halogen containing residue + + + + + A protein modification that effectively substitutes a halogen atom for a hydrogen atom. + PubMed:18688235 + + + + + HalRes + + + + + + halogenated residue + + + + + + + + + + A protein modification that effectively substitutes a sulfonyl group for the hydrogen atom of a hydroxyl or sulfanyl group. + 80.06 + O 3 S 1 + 79.95682 + X + natural + Unimod:40 + SulfRes + Sulphonation (SO3H) (of PMC group) + PSI-MOD + O-Sulfonation + Sulfo + MOD:00695 + + From DeltaMass: Average Mass: 80. + sulfated residue + + + + + A protein modification that effectively substitutes a sulfonyl group for the hydrogen atom of a hydroxyl or sulfanyl group. + DeltaMass:0 + PubMed:14752058 + Unimod:40 + + + + + SulfRes + + + + + + Sulphonation (SO3H) (of PMC group) + + + + + + O-Sulfonation + + + + + + Sulfo + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a phosphono group (H2PO3 or 'phosphate'). + 79.98 + H 1 O 3 P 1 + 79.96633 + X + Unimod:21 + PhosRes + Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) + PSI-MOD + Phospho + Phosphorylation + MOD:00696 + + From DeltaMass: Average Mass: 80. + phosphorylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with a phosphono group (H2PO3 or 'phosphate'). + DeltaMass:0 + Unimod:21 + + + + + PhosRes + + + + + + Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) + + + + + + Phospho + + + + + + Phosphorylation + + + + + + + + + + A protein modification that effectively results from forming an adduct with a compound containing a flavin group. + X + natural + FlavRes + PSI-MOD + FAD + Flavin adenine dinucleotide + MOD:00697 + + flavin modified residue + + + + + FlavRes + + + + + + FAD + + + + + + Flavin adenine dinucleotide + + + + + + + + + + A protein modification that effectively substitutes a metal atom or a metal cluster for hydrogen atoms, or coordinates a metal ion. + MetalRes + PSI-MOD + MOD:00698 + + metal or metal cluster containing modified residue + + + + + A protein modification that effectively substitutes a metal atom or a metal cluster for hydrogen atoms, or coordinates a metal ion. + PubMed:18688235 + + + + + MetalRes + + + + + + + + + + A protein modification that effectively results from forming an adduct with a compound containing a porphyrin group. + PorphRes + PSI-MOD + MOD:00699 + + porphyrin modified residue + + + + + A protein modification that effectively results from forming an adduct with a compound containing a porphyrin group. + PubMed:18688235 + + + + + PorphRes + + + + + + + + + + A protein modification that effectively results from forming an adduct with a compound containing a tetrapyrrole group. + TetrapyrRes + PSI-MOD + MOD:00700 + tetrapyrrole modified residue + + + + + A protein modification that effectively results from forming an adduct with a compound containing a tetrapyrrole group. + PubMed:18688235 + + + + + TetrapyrRes + + + + + + + + + + A protein modification that effectively results from forming an adduct with a compound containing a nucleotide or a polynucleotide through formation of either a phosphodiester bond, a phosphoramide ester bond, or a glycosidic bond. + NucRes + PSI-MOD + MOD:00701 + + nucleotide or nucleic acid modified residue + + + + + A protein modification that effectively results from forming an adduct with a compound containing a nucleotide or a polynucleotide through formation of either a phosphodiester bond, a phosphoramide ester bond, or a glycosidic bond. + PubMed:18688235 + + + + + NucRes + + + + + + + + + + A protein modification that effectively substitutes atoms of particular common isotopes with atoms or groups containing isotopes that are not the most common. + IsoTagRes + SILAC + PSI-MOD + MOD:00702 + + In SILAC (stable isotope labelling of amino acids in cell culture), the label may be introduced either through labeling of an incorporated residue or labeling of the substrates in a metabolic modification. For isotope labeling introduced through a modification reagent see MOD:01426. + isotope labeled residue + + + + + A protein modification that effectively substitutes atoms of particular common isotopes with atoms or groups containing isotopes that are not the most common. + PubMed:18688235 + + + + + IsoTagRes + + + + + + SILAC + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20) group. + IpRes + PSI-MOD + MOD:00703 + + isoprenylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20) group. + PubMed:18688235 + + + + + IpRes + + + + + + + + + + A protein modification that effectively forms a double bond by removing a molecule of water from a residue. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + X + natural + Unimod:23 + PSI-MOD + Dehydrated + Dehydration + MOD:00704 + + dehydrated residue + + + + + A protein modification that effectively forms a double bond by removing a molecule of water from a residue. + DeltaMass:0 + Unimod:23 + + + + + Dehydrated + + + + + + Dehydration + + + + + + + + + + A protein modification that effectively converts an L-valine residue to D-valine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 5 H 9 N 1 O 1 + 99.13 + 99.06841 + V + natural + uniprot.ptm:PTM-0124 + (R)-2-amino-3-methylbutanoic acid + D-Val + D-valine + MOD_RES D-valine + alpha-amino-beta-methylbutyric acid + alpha-aminoisovaleric acid + PSI-MOD + MOD:00705 + D-valine + + + + + A protein modification that effectively converts an L-valine residue to D-valine. + ChEBI:30016 + PubMed:15853325 + RESID:AA0200 + + + + + (R)-2-amino-3-methylbutanoic acid + + + + + + D-Val + + + + + + D-valine + + + + + + MOD_RES D-valine + + + + + + alpha-amino-beta-methylbutyric acid + + + + + + alpha-aminoisovaleric acid + + + + + + + + + + + A protein modification that effectively converts L-tyrosine to 2,3-didehydrotyrosine. + -2.02 + C 0 H -2 N 0 O 0 + -2.01565 + C 9 H 7 N 1 O 2 + 161.16 + 161.04768 + Y + natural + Unimod:401 + uniprot.ptm:PTM-0008 + MOD_RES 2,3-didehydrotyrosine + dHTyr + PSI-MOD + MOD:00706 + + dehydrogenated tyrosine + + + + + A protein modification that effectively converts L-tyrosine to 2,3-didehydrotyrosine. + Unimod:401#Y + + + + + MOD_RES 2,3-didehydrotyrosine + + + + + + dHTyr + + + + + + + + + + + a protein modification that effectively converts an L-tyrosine residue to a multihydroxylated L-phenylalanine + Y + natural + HyTyr + PSI-MOD + MOD:00707 + + hydroxylated tyrosine + + + + + a protein modification that effectively converts an L-tyrosine residue to a multihydroxylated L-phenylalanine + PubMed:18688235 + + + + + HyTyr + + + + + + + + + + + A protein modification that effectively adds oxygen atoms to a sulfur atom of L-cysteine residue without removing hydrogen atoms. + C + artifact + SOxyCys + PSI-MOD + MOD:00708 + + sulfur oxygenated L-cysteine + + + + + A protein modification that effectively adds oxygen atoms to a sulfur atom of L-cysteine residue without removing hydrogen atoms. + PubMed:18688235 + + + + + SOxyCys + + + + + + + + + + + A protein modification that effectively adds oxygen atoms to a sulfur atom of L-methionine residue without removing hydrogen atoms. + M + artifact + SOxyMet + PSI-MOD + MOD:00709 + + sulfur oxygenated L-methionine + + + + + A protein modification that effectively adds oxygen atoms to a sulfur atom of L-methionine residue without removing hydrogen atoms. + PubMed:18688235 + + + + + SOxyMet + + + + + + + + + + A protein modification that effectively adds a proton and replaces two hydrogen atoms with two methyl groups. + Me2+Res + PSI-MOD + MOD:00710 + + For N-terminal proline residues, dimethylation can effectively only be accomplished with a protonated imino group. This process accounts for both protonation and dimethylation. The alternative Me2Res process accounts only for dimethylation and not protonation. + protonated-dimethylated residue + + + + + A protein modification that effectively adds a proton and replaces two hydrogen atoms with two methyl groups. + PubMed:18688235 + + + + + Me2+Res + + + + + + + + + + A protein modification that effectively replaces three hydrogen atoms with three methyl groups, after a proton has been added to form an aminium group. + 43.09 + C 3 H 7 N 0 O 0 S 0 + 43.054226 + 1+ + X + natural + Me3+Res + PSI-MOD + MOD:00711 + + For amino acids residues, amine trimethylation can effectively only be accomplished with a protonated primary amino group. This process accounts for both protonation and trimethylation. The alternative Me3Res process accounts only for trimethylation and not protonation. + trimethylated protonated-residue + + + + + A protein modification that effectively replaces three hydrogen atoms with three methyl groups, after a proton has been added to form an aminium group. + PubMed:18688235 + + + + + Me3+Res + + + + + + + + + + + A protein modification that effectively converts an L-proline residue to a methylated proline, such as N,N-dimethylproline. + P + natural + MePro + PSI-MOD + MOD:00712 + + methylated proline + + + + + A protein modification that effectively converts an L-proline residue to a methylated proline, such as N,N-dimethylproline. + PubMed:18688235 + + + + + MePro + + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to a methylated glutamic acid, such as L-glutamate 5-methyl ester. + X + natural + MeGlu + PSI-MOD + MOD:00713 + + methylated glutamic acid + + + + + A protein modification that effectively converts an L-glutamic acid residue to a methylated glutamic acid, such as L-glutamate 5-methyl ester. + PubMed:18688235 + + + + + MeGlu + + + + + + + + + + + A protein modification that effectively converts a glycine residue to a methylated glycine, such as N-methylglycine. + G + natural + MeGly + PSI-MOD + MOD:00714 + methylated glycine + + + + + A protein modification that effectively converts a glycine residue to a methylated glycine, such as N-methylglycine. + PubMed:18688235 + + + + + MeGly + + + + + + + + + + + A protein modification that effectively converts an L-isoleucine residue to a methylated isoleucine residue, such as N-methyl-L-isoleucine. + I + natural + MeIle + PSI-MOD + MOD:00715 + methylated isoleucine + + + + + A protein modification that effectively converts an L-isoleucine residue to a methylated isoleucine residue, such as N-methyl-L-isoleucine. + PubMed:18688235 + + + + + MeIle + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to a methylated methionine, such as N-methyl-L-methionine. + M + natural + N-term + MeMet + PSI-MOD + MOD:00716 + + methylated methionine + + + + + A protein modification that effectively converts an L-methionine residue to a methylated methionine, such as N-methyl-L-methionine. + PubMed:18688235 + + + + + MeMet + + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to a methylated phenylalanine, such as N-methyl-L-phenylalanine. + F + natural + MePhe + PSI-MOD + MOD:00717 + + methylated phenylalanine + + + + + A protein modification that effectively converts an L-phenylalanine residue to a methylated phenylalanine, such as N-methyl-L-phenylalanine. + PubMed:18688235 + + + + + MePhe + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to a methylated tyrosine, such as N-methyl-L-tyrosine. + Y + natural + N-term + MeTyr + PSI-MOD + MOD:00718 + methylated tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to a methylated tyrosine, such as N-methyl-L-tyrosine. + PubMed:18688235 + + + + + MeTyr + + + + + + + + + + + A protein modification that oxygenates an L-methionine residue to one of the diastereomeric L-methionine sulfoxide residues. + 16.0 + C 0 H 0 N 0 O 1 S 0 + 15.994915 + C 5 H 9 N 1 O 2 S 1 + 147.19 + 147.0354 + M + artifact + Unimod:35 + uniprot.ptm:PTM-0469 + (2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid + L-methionine (R)-S-oxide + L-methionine (R)-sulfoxide + L-methionine S-oxide + L-methionine sulfoxide + MOD_RES Methionine sulfoxide + MetO + Methionyl Sulfoxide + oxym + PSI-MOD + Oxidation + MOD:00719 + + From DeltaMass: Average Mass: 147 Formula:C5H9O1N2S Monoisotopic Mass Change:147.035 Average Mass Change:147.195 (formula incorrect, N and O reversed) References:PE Sciex. + L-methionine sulfoxide + + + + + A protein modification that oxygenates an L-methionine residue to one of the diastereomeric L-methionine sulfoxide residues. + DeltaMass:177 + OMSSA:1 + PubMed:21406390 + PubMed:22116028 + RESID:AA0581 + Unimod:35#M + + + + + (2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid + + + + + + L-methionine (R)-S-oxide + + + + + + L-methionine (R)-sulfoxide + + + + + + L-methionine S-oxide + + + + + + L-methionine sulfoxide + + + + + + MOD_RES Methionine sulfoxide + + + + + + MetO + + + + + + Methionyl Sulfoxide + + + + + + oxym + + + + + + Oxidation + + + + + + + + + + A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide R-diastereomer. + 16.0 + C 0 H 0 N 0 O 1 S 0 + 15.994915 + C 5 H 9 N 1 O 2 S 1 + 147.19 + 147.0354 + M + natural + uniprot.ptm:PTM-0480 + (2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid + L-methionine (R)-S-oxide + L-methionine (R)-sulfoxide + MOD_RES Methionine (R)-sulfoxide + R-MetO + PSI-MOD + MOD:00720 + L-methionine (R)-sulfoxide + + + + + A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide R-diastereomer. + ChEBI:45764 + PubMed:21406390 + PubMed:22116028 + PubMed:23911929 + RESID:AA0581 + + + + + (2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid + + + + + + L-methionine (R)-S-oxide + + + + + + L-methionine (R)-sulfoxide + + + + + + MOD_RES Methionine (R)-sulfoxide + + + + + + R-MetO + + + + + + + + + + A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide S-diastereomer. + 16.0 + C 0 H 0 N 0 O 1 S 0 + 15.994915 + C 5 H 9 N 1 O 2 S 1 + 147.19 + 147.0354 + M + artifact + uniprot.ptm:PTM-0481 + MOD_RES Methionine (S)-sulfoxide + S-MetO + PSI-MOD + MOD:00721 + L-methionine (S)-sulfoxide + + + + + A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide S-diastereomer. + PubMed:18688235 + + + + + MOD_RES Methionine (S)-sulfoxide + + + + + + S-MetO + + + + + + + + + + + A protein modification that effectively replaces one hydrogen atom of an L-glutamine residue with one methyl group. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 6 H 10 N 2 O 2 + 142.16 + 142.07423 + Q + natural + Unimod:34 + Me1Gln + methylq + PSI-MOD + MOD:00722 + + monomethylated L-glutamine + + + + + A protein modification that effectively replaces one hydrogen atom of an L-glutamine residue with one methyl group. + OMSSA:14 + Unimod:34#Q + + + + + Me1Gln + + + + + + methylq + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to either N2-acetyl-L-lysine, or N6-acetyl-L-lysine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 8 H 15 N 2 O 2 + 171.22 + 171.11336 + K + natural + NAcLys + PSI-MOD + MOD:00723 + + N-acetylated L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to either N2-acetyl-L-lysine, or N6-acetyl-L-lysine. + PubMed:18688235 + + + + + NAcLys + + + + + + + + + + + + A protein modification that effectively replaces one hydrogen atom on a nitrogen of an L-histidine residue with one methyl group. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 7 H 9 N 3 O 1 + 151.17 + 151.07455 + H + natural + Unimod:34 + NMeHis + methylh + PSI-MOD + Methyl + MOD:00724 + + N-methylated L-histidine + + + + + A protein modification that effectively replaces one hydrogen atom on a nitrogen of an L-histidine residue with one methyl group. + OMSSA:74 + Unimod:34#H + + + + + NMeHis + + + + + + methylh + + + + + + Methyl + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group linked through a glycosidic bond. + PSI-MOD + MOD:00725 + complex glycosylation + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group linked through a glycosidic bond. + PubMed:18688235 + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a glucose group through a glycosidic bond. + MOD:00433 + X + natural + Glc + PSI-MOD + MOD:00726 + glucosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a glucose group through a glycosidic bond. + PubMed:18688235 + + + + + Glc + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a mannose group through a glycosidic bond, + X + natural + Man + PSI-MOD + MOD:00727 + mannosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a mannose group through a glycosidic bond, + PubMed:18688235 + + + + + Man + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a galactose group through a glycosidic bond. + X + natural + Gal + PSI-MOD + MOD:00728 + galactosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a galactose group through a glycosidic bond. + PubMed:18688235 + + + + + Gal + + + + + + + + + + a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a pentose sugar group through a glycosidic bond + 132.12 + C 5 H 8 O 4 + 132.04225 + X + natural + Pent + Pentoses (Ara, Rib, Xyl) + Pentosyl + PSI-MOD + MOD:00729 + for Pentoses DeltaMass gives mass 132, for Pentosyl DeltaMass gives formula C 6 H 10 N4 with mass 146 + pentosylated residue + + + + + a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a pentose sugar group through a glycosidic bond + DeltaMass:172 + + + + + Pent + + + + + + Pentoses (Ara, Rib, Xyl) + + + + + + Pentosyl + + + + + + + + + + a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a arabinose sugar group through a glycosidic bond + 132.12 + C 5 H 8 O 4 + 132.04225 + X + natural + Ara + PSI-MOD + MOD:00730 + arabinosylated residue + + + + + a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a arabinose sugar group through a glycosidic bond + PubMed:18688235 + + + + + Ara + + + + + + + + + + a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a ribose sugar group through a glycosidic bond + 132.12 + C 5 H 8 O 4 + 132.04225 + X + natural + Rib + PSI-MOD + MOD:00731 + ribosylated residue + + + + + a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a ribose sugar group through a glycosidic bond + PubMed:18688235 + + + + + Rib + + + + + + + + + + a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a xylose sugar group through a glycosidic bond + 132.12 + C 5 H 8 O 4 + 132.04225 + X + natural + Xyl + PSI-MOD + MOD:00732 + xylosylated residue + + + + + a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a xylose sugar group through a glycosidic bond + PubMed:18688235 + + + + + Xyl + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylglucosamine group through a glycosidic bond. + 203.19 + C 8 H 13 N 1 O 5 + 203.07938 + X + GlcNAc + PSI-MOD + MOD:00733 + N-acetylaminoglucosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylglucosamine group through a glycosidic bond. + PubMed:18688235 + + + + + GlcNAc + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylgalactosamine group through a glycosidic bond. + 203.19 + C 8 H 13 N 1 O 5 + 203.07938 + X + GalNAc + N-acetylhexosamines (GalNAc, GlcNAc) + PSI-MOD + MOD:00734 + From DeltaMass: Average Mass: 203 Formula:C8H13O5N1 Monoisotopic Mass Change:203.079 Average Mass Change:203.196 References:PE Sciex + N-acetylaminogalactosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylgalactosamine group through a glycosidic bond. + DeltaMass:247 + + + + + GalNAc + + + + + + N-acetylhexosamines (GalNAc, GlcNAc) + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexosuronic acid group through a glycosidic bond. + 176.12 + C 6 H 8 O 6 + 176.03209 + X + natural + HexA + PSI-MOD + MOD:00735 + hexosuronylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexosuronic acid group through a glycosidic bond. + PubMed:18688235 + + + + + HexA + + + + + + + + + + a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a deoxyhexose group through a glycosidic bond + 146.14 + C 6 H 10 O 4 + 146.0579 + X + natural + GNO:G02438LG + Deoxyhexoses (Fuc, Rha) + dHex + PSI-MOD + MOD:00736 + + From DeltaMass: Average Mass: 146 + deoxyhexosylated residue + + + + + a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a deoxyhexose group through a glycosidic bond + DeltaMass:0 + + + + + Deoxyhexoses (Fuc, Rha) + + + + + + dHex + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylneuraminic acid (sialic acid) group through a glycosidic bond. + 291.26 + C 11 H 17 N 1 O 8 + 291.09543 + X + natural + GNO:G76685HR + N-acetylneuraminic acid (Sialic acid, NeuAc, NANA, SA) + NeuNAc + PSI-MOD + MOD:00737 + From DeltaMass: Average Mass: 291 + N-acetylneuraminylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylneuraminic acid (sialic acid) group through a glycosidic bond. + DeltaMass:0 + + + + + N-acetylneuraminic acid (Sialic acid, NeuAc, NANA, SA) + + + + + + NeuNAc + + + + + + + + + + A protein modification that effectively substitutes an iron atom or a cluster containing iron for hydrogen atoms, or that coordinates an iron ion. + FeRes + PSI-MOD + MOD:00738 + iron containing modified residue + + + + + A protein modification that effectively substitutes an iron atom or a cluster containing iron for hydrogen atoms, or that coordinates an iron ion. + PubMed:18688235 + + + + + FeRes + + + + + + + + + + + A protein modification that effectively substitutes a cluster of iron and sulfur atoms for hydrogen atoms. + FeSRes + PSI-MOD + MOD:00739 + iron-sulfur cluster containing modification + + + + + A protein modification that effectively substitutes a cluster of iron and sulfur atoms for hydrogen atoms. + PubMed:18688235 + + + + + FeSRes + + + + + + + + + + A protein modification that effectively substitutes a manganese atom or a cluster containing manganese for hydrogen atoms, or that coordinates a manganese ion. + MnRes + PSI-MOD + MOD:00740 + manganese containing modified residue + + + + + A protein modification that effectively substitutes a manganese atom or a cluster containing manganese for hydrogen atoms, or that coordinates a manganese ion. + PubMed:18688235 + + + + + MnRes + + + + + + + + + + A protein modification that effectively substitutes a nickel atom or a cluster containing nickel for hydrogen atoms, or that coordinates a nickel ion. + NiRes + PSI-MOD + MOD:00741 + nickel containing modified residue + + + + + A protein modification that effectively substitutes a nickel atom or a cluster containing nickel for hydrogen atoms, or that coordinates a nickel ion. + PubMed:18688235 + + + + + NiRes + + + + + + + + + + A protein modification that effectively substitutes a copper atom or a cluster containing copper for hydrogen atoms, or that coordinates a copper ion. + CuRes + PSI-MOD + MOD:00742 + copper containing modified residue + + + + + A protein modification that effectively substitutes a copper atom or a cluster containing copper for hydrogen atoms, or that coordinates a copper ion. + PubMed:18688235 + + + + + CuRes + + + + + + + + + + A protein modification that effectively substitutes a molybdenum atom or a cluster containing molybdenum for hydrogen atoms, or that coordinates a molybdenum ion. + MoRes + PSI-MOD + MOD:00743 + + molybdenum containing modified residue + + + + + A protein modification that effectively substitutes a molybdenum atom or a cluster containing molybdenum for hydrogen atoms, or that coordinates a molybdenum ion. + PubMed:18688235 + + + + + MoRes + + + + + + + + + + + A protein modification containing a molybdenum atom in a pterin ring system. + MoPterRes + PSI-MOD + MOD:00744 + + molybdenum pterin containing modification + + + + + A protein modification containing a molybdenum atom in a pterin ring system. + PubMed:18688235 + + + + + MoPterRes + + + + + + + + + + A protein modification that effectively substitutes a selenium atom or a cluster containing selenium for hydrogen atoms. + SeRes + PSI-MOD + MOD:00745 + + selenium containing residue + + + + + A protein modification that effectively substitutes a selenium atom or a cluster containing selenium for hydrogen atoms. + PubMed:18688235 + + + + + SeRes + + + + + + + + + + A protein modification that effectively substitutes a tungsten atom or a cluster containing tungsten for hydrogen atoms, or that coordinates a tungsten ion. + WRes + PSI-MOD + MOD:00746 + tungsten containing modified residue + + + + + A protein modification that effectively substitutes a tungsten atom or a cluster containing tungsten for hydrogen atoms, or that coordinates a tungsten ion. + PubMed:18688235 + + + + + WRes + + + + + + + + + + A protein modification that effectively substitutes a sodium atom for a hydrogen atom. + NaRes + PSI-MOD + MOD:00747 + + sodium containing modified residue + + + + + A protein modification that effectively substitutes a sodium atom for a hydrogen atom. + PubMed:18688235 + + + + + NaRes + + + + + + + + + + A protein modification that effectively results from forming an adduct with a compound containing a pterin group. + PterRes + PSI-MOD + MOD:00748 + + pterin modified residue + + + + + A protein modification that effectively results from forming an adduct with a compound containing a pterin group. + PubMed:18688235 + + + + + PterRes + + + + + + + + + + A protein modification that effectively substitutes a sulfur atom for an oxygen atom. + S(O)Res + PSI-MOD + MOD:00749 + + sulfur substitution for oxygen + + + + + A protein modification that effectively substitutes a sulfur atom for an oxygen atom. + PubMed:18688235 + + + + + S(O)Res + + + + + + + + + + A protein modification that effectively crosslinks an amino acid residue and the 3'- or 5'-end of DNA through a phosphodiester bond. + DNARes + PSI-MOD + MOD:00750 + deoxyribonucleic acid linked residue + + + + + A protein modification that effectively crosslinks an amino acid residue and the 3'- or 5'-end of DNA through a phosphodiester bond. + PubMed:18688235 + + + + + DNARes + + + + + + + + + + a protein modification + RNARes + PSI-MOD + MOD:00751 + ribonucleic acid linked residue + + + + + a protein modification + PubMed:18688235 + + + + + RNARes + + + + + + + + + + A protein modification that effectively results from forming an adduct with one ADP-ribose through formation of a glycosidic bond. + 541.3 + C 15 H 21 N 5 O 13 P 2 + 541.0611 + X + natural + ADP-rybosylation (from NAD) + ADPRib1Res + PSI-MOD + MOD:00752 + + From DeltaMass: Average Mass: 541. + monoadenosine diphosphoribosyl (ADP-ribosyl) modified residue + + + + + A protein modification that effectively results from forming an adduct with one ADP-ribose through formation of a glycosidic bond. + DeltaMass:0 + + + + + ADP-rybosylation (from NAD) + + + + + + ADPRib1Res + + + + + + + + + + A protein modification that effectively substitutes a chlorine atom for a hydrogen atom. + X + ClRes + PSI-MOD + MOD:00753 + chlorinated residue + + + + + A protein modification that effectively substitutes a chlorine atom for a hydrogen atom. + PubMed:18688235 + + + + + ClRes + + + + + + + + + + A protein modification that effectively substitutes a bromine atom for a hydrogen atom. + X + BrRes + PSI-MOD + MOD:00754 + brominated residue + + + + + A protein modification that effectively substitutes a bromine atom for a hydrogen atom. + PubMed:18688235 + + + + + BrRes + + + + + + + + + + A protein modification that effectively substitutes an iodine atom of a residue for a hydrogen atom. + X + IRes + PSI-MOD + MOD:00755 + + iodinated residue + + + + + A protein modification that effectively substitutes an iodine atom of a residue for a hydrogen atom. + PubMed:18688235 + + + + + IRes + + + + + + + + + + + A protein modification that effectively converts an L-valine residue to 4-hydroxy-D-valine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 5 H 9 N 1 O 2 + 115.13 + 115.06333 + V + natural + uniprot.ptm:PTM-0111 + (2R,3Xi)-2-amino-4-hydroxy-3-methylbutanoic acid + 4-hydroxy-D-valine + D-4HyVal + D-gamma-hydroxyvaline + MOD_RES D-4-hydroxyvaline + PSI-MOD + MOD:00756 + 4-hydroxy-D-valine + + + + + A protein modification that effectively converts an L-valine residue to 4-hydroxy-D-valine. + PubMed:15853325 + RESID:AA0388 + + + + + (2R,3Xi)-2-amino-4-hydroxy-3-methylbutanoic acid + + + + + + 4-hydroxy-D-valine + + + + + + D-4HyVal + + + + + + D-gamma-hydroxyvaline + + + + + + MOD_RES D-4-hydroxyvaline + + + + + + + + + + A protein modification that effectively converts an L-proline residue to O4-galactosyl-L-hydroxyproline. + 178.14 + C 6 H 10 N 0 O 6 + 178.04774 + C 11 H 17 N 1 O 7 + 275.26 + 275.1005 + P + natural + uniprot.ptm:PTM-0558 + (2S,4R)-4-(beta-D-galactopyranosyloxy)pyrrolidine-2-carboxylic acid + 4-(beta-D-galactopyranosyloxy)proline + 4-(galactosyloxy)proline + CARBOHYD O-linked (Gal) hydroxyproline + O4-galactosyl-L-hydroxyproline + O4-glycosyl-hydroxyproline + beta-galactopyranosyl-4-hydroxyproline + PSI-MOD + MOD:00757 + secondary to RESID:AA0030 + O4-galactosyl-L-hydroxyproline + + + + + A protein modification that effectively converts an L-proline residue to O4-galactosyl-L-hydroxyproline. + RESID:AA0389 + + + + + (2S,4R)-4-(beta-D-galactopyranosyloxy)pyrrolidine-2-carboxylic acid + + + + + + 4-(beta-D-galactopyranosyloxy)proline + + + + + + 4-(galactosyloxy)proline + + + + + + CARBOHYD O-linked (Gal) hydroxyproline + + + + + + O4-galactosyl-L-hydroxyproline + + + + + + O4-glycosyl-hydroxyproline + + + + + + beta-galactopyranosyl-4-hydroxyproline + + + + + + + + + + A protein modification that effectively converts an L-proline residue to O4-(N-acetylamino)glucosyl-L-hydroxyproline. + 219.19 + C 8 H 13 N 1 O 6 + 219.07428 + C 13 H 20 N 2 O 7 + 316.31 + 316.12704 + P + natural + uniprot.ptm:PTM-0578 + (2S,4R)-4-[2-acetamido-2-deoxy-alpha-D-glucopyranosyloxy]pyrrolidine-2-carboxylic acid + 4-(N-acetylglucosaminyloxy)proline + 4-[(2-N-acetylamino)-alpha-D-glucopyranosyl]oxyproline + CARBOHYD O-linked (GlcNAc) hydroxyproline + O4-(N-acetylamino)glucosyl-L-hydroxyproline + O4-glycosyl-hydroxyproline + O4GlcNAcHyPro + alpha-2-(N-acetylamino)glucopyranosyl-4-hydroxyproline + PSI-MOD + HexNAc + MOD:00758 + secondary to RESID:AA0030 + O4-(N-acetylamino)glucosyl-L-hydroxyproline + + + + + A protein modification that effectively converts an L-proline residue to O4-(N-acetylamino)glucosyl-L-hydroxyproline. + PubMed:15238247 + PubMed:9660787 + RESID:AA0390 + + + + + (2S,4R)-4-[2-acetamido-2-deoxy-alpha-D-glucopyranosyloxy]pyrrolidine-2-carboxylic acid + + + + + + 4-(N-acetylglucosaminyloxy)proline + + + + + + 4-[(2-N-acetylamino)-alpha-D-glucopyranosyl]oxyproline + + + + + + CARBOHYD O-linked (GlcNAc) hydroxyproline + + + + + + O4-(N-acetylamino)glucosyl-L-hydroxyproline + + + + + + O4-glycosyl-hydroxyproline + + + + + + O4GlcNAcHyPro + + + + + + alpha-2-(N-acetylamino)glucopyranosyl-4-hydroxyproline + + + + + + HexNAc + + + + + + + + + + + modification from Unimod N-linked glycosylation + 1607.48 + C 62 H 102 N 4 O 44 + 1606.5867 + C 66 H 108 N 6 O 46 + 1721.59 + 1720.6296 + N + natural + GNO:G59937CP + Unimod:307 + PSI-MOD + Fucosylated biantennary (-1 galactose) + dHex(1)Hex(4)HexNAc(4) + MOD:00759 + fucosylated biantennary (-1 galactose) N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation + Unimod:307 + + + + + Fucosylated biantennary (-1 galactose) + + + + + + dHex(1)Hex(4)HexNAc(4) + + + + + + + + + + + modification from Unimod N-linked glycosylation - missing ref + 1623.48 + C 62 H 102 N 4 O 45 + 1622.5817 + C 66 H 108 N 6 O 47 + 1737.59 + 1736.6245 + N + natural + GNO:G10486CT + Unimod:311 + PSI-MOD + Biantennary + Hex(5)HexNAc(4) + MOD:00760 + biantennary N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation - missing ref + Unimod:311 + + + + + Biantennary + + + + + + Hex(5)HexNAc(4) + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with one hexose sugar group through a glycosidic bond. + 162.14 + C 6 H 10 O 5 + 162.05283 + X + natural + GNO:G81399MY + Hex1 + PSI-MOD + MOD:00761 + monohexosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with one hexose sugar group through a glycosidic bond. + PubMed:18688235 + + + + + Hex1 + + + + + + + + + + + modification from Unimod N-linked glycosylation - missing ref + 1299.2 + C 50 H 82 N 4 O 35 + 1298.476 + C 54 H 88 N 6 O 37 + 1413.3 + 1412.5189 + N + natural + GNO:G35029YA + Unimod:309 + PSI-MOD + Biantennary (-2 galactose) + Hex(3)HexNAc(4) + MOD:00762 + biantennary (-2 galactose) N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation - missing ref + Unimod:309 + + + + + Biantennary (-2 galactose) + + + + + + Hex(3)HexNAc(4) + + + + + + + + + + + modification from Unimod N-linked glycosylation - missing ref + 1461.34 + C 56 H 92 N 4 O 40 + 1460.5288 + C 60 H 98 N 6 O 42 + 1575.44 + 1574.5717 + N + natural + GNO:G72787SB + Unimod:310 + PSI-MOD + Biantennary (-1 galactose) + Hex(4)HexNAc(4) + MOD:00763 + biantennary (-1 galactose) N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation - missing ref + Unimod:310 + + + + + Biantennary (-1 galactose) + + + + + + Hex(4)HexNAc(4) + + + + + + + + + + A protein modification that effectively results from forming an adduct with a carbohydrate-like group either through enzymatic formation of a glycosidic bond, or through non-enzymatic glycation formation of a Schiff-base or an Amadori ketosamine residue adduct. + PSI-MOD + MOD:00764 + + glycoconjugated residue + + + + + A protein modification that effectively results from forming an adduct with a carbohydrate-like group either through enzymatic formation of a glycosidic bond, or through non-enzymatic glycation formation of a Schiff-base or an Amadori ketosamine residue adduct. + PubMed:18688235 + PubMed:3743566 + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-(L-cysteinyl)-L-cysteine, forming a disulfide bond with free cysteine. + 119.14 + C 3 H 5 N 1 O 2 S 1 + 119.0041 + C 6 H 10 N 2 O 3 S 2 + 222.28 + 222.01329 + C + natural + Unimod:312 + uniprot.ptm:PTM-0415 + (2R,2'R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid) + 3,3'-disulfane-1,2-diylbis(2-azanylpropanoic acid) + 3,3'-dithiobis(2-aminopropanoic acid) + 3,3'-dithiobisalanine + 3,3'-dithiodialanine + Cysteinylation + L-cystine + MOD_RES S-cysteinyl cysteine + S-cystenyl cystenyl + SCysCys + beta,beta'-diamino-beta,beta'-dicarboxydiethyldisulfide + beta,beta'-dithiodialanine + bis(alpha-aminopropionic acid)-beta-disulfide + bis(beta-amino-beta-carboxyethyl)disulfide + dicysteine + PSI-MOD + 2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid + MOD:00765 + + This entry is for formation of a disulfide bond between a peptide cysteine and a free cysteine. For the cystine cross-link, see MOD:00234. From DeltaMass: (name misspelled and formula incorrect, N and O reversed) Formula: C6H10O2N3S2 Monoisotopic Mass Change: 222.013 Average Mass Change: 222.283 + cysteinylation (disulfide with free L-cysteine) + + + + + A protein modification that effectively converts an L-cysteine residue to S-(L-cysteinyl)-L-cysteine, forming a disulfide bond with free cysteine. + DeltaMass:260 + PubMed:1988019 + PubMed:2001356 + PubMed:2076469 + PubMed:3083866 + PubMed:366603 + PubMed:7918467 + PubMed:8344916 + RESID:AA0025#CYS1 + Unimod:312 + + + + + (2R,2'R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid) + + + + + + 3,3'-disulfane-1,2-diylbis(2-azanylpropanoic acid) + + + + + + 3,3'-dithiobis(2-aminopropanoic acid) + + + + + + 3,3'-dithiobisalanine + + + + + + 3,3'-dithiodialanine + + + + + + Cysteinylation + + + + + + L-cystine + + + + + + MOD_RES S-cysteinyl cysteine + + + + + + S-cystenyl cystenyl + + + + + + SCysCys + + + + + + beta,beta'-diamino-beta,beta'-dicarboxydiethyldisulfide + + + + + + beta,beta'-dithiodialanine + + + + + + bis(alpha-aminopropionic acid)-beta-disulfide + + + + + + bis(beta-amino-beta-carboxyethyl)disulfide + + + + + + dicysteine + + + + + + 2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid + + + + + + + + + modification from Unimod Post-translational - C-terminal loss of lysine OBSOLETE because the idenical to MOD:01642. Remap to MOD:01642 + MOD:01642 + -128.18 + C -6 H -12 N -2 O -1 + -128.09496 + X + C-term + Unimod:313 + PSI-MOD + Loss of C-terminal K from Heavy Chain of MAb + Lys-loss + MOD:00766 + C terminal -K from HC of MAb + true + + + + + modification from Unimod Post-translational - C-terminal loss of lysine OBSOLETE because the idenical to MOD:01642. Remap to MOD:01642 + PubMed:16078144 + Unimod:313 + + + + + Loss of C-terminal K from Heavy Chain of MAb + + + + + + Lys-loss + + + + + + + + + + A modification produced in a non-enzymatic reaction between a carbohydrate carbonyl group (C1 of aldohexose or C2 of fructose) and a protein amino group to form a Schiff-base or an Amadori ketosamine residue adduct. + artifact + PSI-MOD + MOD:00767 + glycated residue + + + + + A modification produced in a non-enzymatic reaction between a carbohydrate carbonyl group (C1 of aldohexose or C2 of fructose) and a protein amino group to form a Schiff-base or an Amadori ketosamine residue adduct. + PubMed:18688235 + + + + + + + + + Oxidation of methionine to methionine sulfone with neutral loss of CH3SO2H. + -80.1 + C -1 H -4 N 0 O -2 S -1 + -79.9932 + C 4 H 5 N 1 O 1 S 0 + 83.09 + 83.03712 + M + artifact + PSI-MOD + MOD:00768 + Originally created from Unimod:508 that was later deleted. + methionine oxidation with neutral loss of 80 Da + + + + + Oxidation of methionine to methionine sulfone with neutral loss of CH3SO2H. + PubMed:18688235 + PubMed:9004526 + + + + + + + + + Natural or modified residues with a mass of 71.0-71.1 Da. + PSI-MOD + MOD:00769 + + residues isobaric at 71.0-71.1 Da + + + + + Natural or modified residues with a mass of 71.0-71.1 Da. + PubMed:18688235 + + + + + + + + + Natural or modified residues that are isobaric at a resolution below 0.01 Da. + PSI-MOD + MOD:00770 + + residues isobaric at a resolution below 0.01 Da + + + + + Natural or modified residues that are isobaric at a resolution below 0.01 Da. + PubMed:18688235 + + + + + + + + + Natural or modified residues with a mass of 166.98-167.00 Da. + PSI-MOD + MOD:00771 + + residues isobaric at 166.98-167.00 Da + + + + + Natural or modified residues with a mass of 166.98-167.00 Da. + PubMed:18688235 + + + + + + + + + A protein modification that effectively substitutes a vanadium atom or a cluster containing vanadium for hydrogen atoms, or that coordinates a vanadium ion. + VRes + PSI-MOD + MOD:00772 + vanadium containing modified residue + + + + + A protein modification that effectively substitutes a vanadium atom or a cluster containing vanadium for hydrogen atoms, or that coordinates a vanadium ion. + PubMed:18688235 + + + + + VRes + + + + + + + + + + Natural or modified residues with a mass of 181.00-181.02 Da. + PSI-MOD + MOD:00773 + + residues isobaric at 181.00-181.02 Da + + + + + Natural or modified residues with a mass of 181.00-181.02 Da. + PubMed:18688235 + + + + + + + + + Natural or modified residues with a mass of 243.02-243.03 Da. + PSI-MOD + MOD:00774 + + residues isobaric at 243.02-243.03 Da + + + + + Natural or modified residues with a mass of 243.02-243.03 Da. + PubMed:18688235 + + + + + + + + + + An artifactual protein modification that converts an L-histidine residue to L-asparagine by oxidative degradation. + -23.04 + C -2 H -1 N -1 O 1 + -23.015984 + C 4 H 6 N 2 O 2 + 114.1 + 114.04293 + H + artifact + Unimod:348 + his2asnh + PSI-MOD + His->Asn + histidine oxidation to aspargine + MOD:00775 + L-asparagine (His) + + + + + An artifactual protein modification that converts an L-histidine residue to L-asparagine by oxidative degradation. + OMSSA:54 + PubMed:9252331 + Unimod:348 + + + + + his2asnh + + + + + + His->Asn + + + + + + histidine oxidation to aspargine + + + + + + + + + + + An artifactual protein modification that converts an L-histidine residue to L-aspartic acid by oxidative degradation. + -22.05 + C -2 H -2 N -2 O 2 + -22.03197 + C 4 H 5 N 1 O 3 + 115.09 + 115.02694 + H + artifact + Unimod:349 + his2asph + PSI-MOD + His->Asp + histidine oxidation to aspartic acid + MOD:00776 + From OMSSA: desc="oxidation of H to D" monomass= -23.015984 (this is the same mass difference as OMSSA:54, his2asnh) [JSG]. + L-aspartic acid (His) + + + + + An artifactual protein modification that converts an L-histidine residue to L-aspartic acid by oxidative degradation. + OMSSA:55 + PubMed:9252331 + Unimod:349 + + + + + his2asph + + + + + + His->Asp + + + + + + histidine oxidation to aspartic acid + + + + + + + + + + + Natural or modified residues with a mass of 182.96-182.98 Da. + PSI-MOD + MOD:00777 + residues isobaric at 182.96-182.98 Da + + + + + Natural or modified residues with a mass of 182.96-182.98 Da. + PubMed:18688235 + + + + + + + + + Natural or modified residues with a mass of 182.9-183.0 Da. + PSI-MOD + MOD:00778 + + residues isobaric at 182.9-183.0 Da + + + + + Natural or modified residues with a mass of 182.9-183.0 Da. + PubMed:18688235 + + + + + + + + OBSOLETE because redundant with MOD:00130. Remap to MOD:00130. + MOD:00130 + -1.03 + H -3 N -1 O 1 + -1.031634 + K + natural + Unimod:352 + Oxidation of lysine (to aminoadipic semialdehyde) + PSI-MOD + MOD:00779 + From DeltaMass: Average Mass: -1 Average Mass Change:-1 References:Amici A, Levine, RL, Tsai, L, and Stadtman, ER: Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. Journal of Biological Chemistry 264: 3341-3346 1989.Requena JR, Chao CC, Levine RL, and Stadtman ER: Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. Proceedings of the National Academy of Sciences USA 98: 69-74 2001. + lysine oxidation to aminoadipic semialdehyde + true + + + + + OBSOLETE because redundant with MOD:00130. Remap to MOD:00130. + DeltaMass:352 + PubMed:11332453 + PubMed:358196 + PubMed:5337886 + PubMed:5529814 + Unimod:352 + + + + + Oxidation of lysine (to aminoadipic semialdehyde) + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to N-acetyl-L-asparagine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 6 H 8 N 2 O 3 + 156.14 + 156.0535 + N + artifact + N-term + AcAsn + PSI-MOD + MOD:00780 + This modification has not been observed to occur naturally. + N-acetyl-L-asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to N-acetyl-L-asparagine. + PubMed:18688235 + + + + + AcAsn + + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to N2-acetyl-L-histidine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 8 H 9 N 3 O 2 + 179.18 + 179.06947 + H + artifact + N-term + AcHis + PSI-MOD + MOD:00781 + This modification has not been observed to occur naturally. + N2-acetyl-L-histidine + + + + + A protein modification that effectively converts an L-histidine residue to N2-acetyl-L-histidine. + PubMed:18688235 + + + + + AcHis + + + + + + + + + + + A protein modification that effectively converts an L-leucine residue to N-acetyl-L-leucine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 8 H 14 N 1 O 2 + 156.2 + 156.10245 + L + artifact + N-term + AcLeu + PSI-MOD + MOD:00782 + This modification has not been observed to occur naturally. + N-acetyl-L-leucine + + + + + A protein modification that effectively converts an L-leucine residue to N-acetyl-L-leucine. + PubMed:18688235 + + + + + AcLeu + + + + + + + + + + + A protein modification that effectively replaces two hydrogen atoms of an L-arginine residue with two methyl groups. + 28.05 + C 2 H 4 N 0 O 0 + 28.0313 + C 8 H 16 N 4 O 1 + 184.24 + 184.13242 + R + natural + Unimod:36 + uniprot.ptm:PTM-0341 + NNMe2Arg + dimethylr + PSI-MOD + Dimethyl + MOD:00783 + + dimethylated L-arginine + + + + + A protein modification that effectively replaces two hydrogen atoms of an L-arginine residue with two methyl groups. + OMSSA:37 + Unimod:36#R + + + + + NNMe2Arg + + + + + + dimethylr + + + + + + Dimethyl + + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to N-acetyl-L-phenylalanine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 11 H 11 N 1 O 2 + 189.21 + 189.07898 + F + artifact + N-term + AcPhe + PSI-MOD + MOD:00784 + This modification has not been observed to occur naturally. + N-acetyl-L-phenylalanine + + + + + A protein modification that effectively converts an L-phenylalanine residue to N-acetyl-L-phenylalanine. + PubMed:18688235 + + + + + AcPhe + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to N2-acetyl-L-tryptophan. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 13 H 12 N 2 O 2 + 228.25 + 228.08987 + W + artifact + N-term + AcTrp + PSI-MOD + MOD:00785 + This modification has not been observed to occur naturally. + N2-acetyl-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to N2-acetyl-L-tryptophan. + PubMed:18688235 + + + + + AcTrp + + + + + + + + + + A protein modification that effectively substitutes one or more (2)H deuterium atoms for (1)H protium atoms. + D(H)Res + PSI-MOD + MOD:00786 + + deuterium substituted residue + + + + + A protein modification that effectively substitutes one or more (2)H deuterium atoms for (1)H protium atoms. + PubMed:18688235 + + + + + D(H)Res + + + + + + + + + + + + modification from Unimod - label for the active site serine of the serine esterase/protease family also shown to label tyrosine in serum albumin + 164.14 + C 6 H 13 O 3 P 1 + 164.06023 + C 9 H 18 N 1 O 5 P 1 + 251.22 + 251.09225 + S + artifact + Unimod:362 + PSI-MOD + Diisopropylphosphate + O-Diisopropylphosphorylation + MOD:00787 + diisopropylphosphoserine + + + + + modification from Unimod - label for the active site serine of the serine esterase/protease family also shown to label tyrosine in serum albumin + Unimod:362 + + + + + Diisopropylphosphate + + + + + + O-Diisopropylphosphorylation + + + + + + + + + + + + modification from Unimod + 122.06 + C 3 H 7 O 3 P 1 + 122.01328 + C 12 H 16 N 1 O 5 P 1 + 285.24 + 285.0766 + Y + artifact + Unimod:363 + PSI-MOD + Isopropylphospho + O-Isopropylphosphorylation + MOD:00788 + isopropylphosphotyrosine + + + + + modification from Unimod + Unimod:363 + + + + + Isopropylphospho + + + + + + O-Isopropylphosphorylation + + + + + + + + + + modification from Unimod - isotopic label ICPL method - The paper describes an H/D labeling strategy whereas the commercial product follows a C/13C labeling strategy. The digest is typically applied AFTER ICPL_light/heavy labeling, only Protein N-term labeling and Lys-specific labeling is applied. + 111.04 + (13)C 6 H 3 N 1 O 1 + 111.041595 + X + artifact + Unimod:364 + PSI-MOD + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form + ICPL:13C(6) + MOD:00789 + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form + + + + + modification from Unimod - isotopic label ICPL method - The paper describes an H/D labeling strategy whereas the commercial product follows a C/13C labeling strategy. The digest is typically applied AFTER ICPL_light/heavy labeling, only Protein N-term labeling and Lys-specific labeling is applied. + PubMed:15602776 + URL:http://www.serva.de/products/sheets/39230-E.pdf + Unimod:364 + + + + + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form + + + + + + ICPL:13C(6) + + + + + + + + + + modification from Unimod - isotopic label ICPL method - The paper describes an H/D labeling strategy whereas the commercial product follows a C/13C labeling strategy. The digest is typically applied AFTER ICPL_light/heavy labeling, only Protein N-term labeling and Lys-specific labeling is applied. + 105.02 + (12)C 6 H 3 N 1 O 1 + 105.02146 + X + artifact + Unimod:365 + PSI-MOD + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form + ICPL + MOD:00790 + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form + + + + + modification from Unimod - isotopic label ICPL method - The paper describes an H/D labeling strategy whereas the commercial product follows a C/13C labeling strategy. The digest is typically applied AFTER ICPL_light/heavy labeling, only Protein N-term labeling and Lys-specific labeling is applied. + PubMed:15602776 + URL:http://www.serva.de/products/sheets/39230-E.pdf + Unimod:365 + + + + + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form + + + + + + ICPL + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-glutamine residue to L-glutamic acid with one (18)O. + 2.99 + H -1 N -1 (18)O 1 + 2.988262 + C 5 H 7 N 1 (16)O 2 (18)O 1 + 131.05 + 131.04684 + Q + artifact + Unimod:366 + PSI-MOD + Deamidated:18O(1) + Deamidation in presence of O18 + MOD:00791 + + 1x(18)O labeled deamidated L-glutamine + + + + + A protein modification that effectively converts an L-glutamine residue to L-glutamic acid with one (18)O. + PubMed:8382902 + Unimod:366#Q + + + + + Deamidated:18O(1) + + + + + + Deamidation in presence of O18 + + + + + + + + + + A protein modification that effectively substitutes one (2)H deuterium atom for one (1)H protium atom. + D(H)1Res + PSI-MOD + MOD:00792 + + deuterium monosubstituted residue + + + + + A protein modification that effectively substitutes one (2)H deuterium atom for one (1)H protium atom. + PubMed:18688235 + + + + + D(H)1Res + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to dehydroalanine. + -34.08 + C 0 H -2 N 0 O 0 S -1 + -33.98772 + C 3 H 3 N 1 O 1 + 69.06 + 69.02146 + C + natural + Unimod:368 + uniprot.ptm:PTM-0468 + 2,3-didehydroalanine + 2-aminoacrylic acid + 2-aminopropenoic acid + 4-methylidene-imidazole-5-one (MIO) active site + Dehydroalanine (from Cysteine) + Dha + MOD_RES 2,3-didehydroalanine (Cys) + anhydroserine + dHAla(Cys) + dehydroalanine + PSI-MOD + Cys->Dha + Dehydroalanine (from Cysteine) + MOD:00793 + + From DeltaMass: In an attempt to clarfiy the difference between the modification of cysteine to lanthionine and cysteine to dehydroalanine, the following contributions from the ABRF email forum are presented:Structurally speaking lanthionine is like cystine but lacks one S atom. I imagine one can think of it as a condensation of cysteine and dehydroalanine but I do not know how it is made biologically. Dehydroalanine could be derived from either serine or cysteine. If I recall Biochem 101 correctly lanthionine was first found in wool.-Lowell Ericsson (ERICSSONLH@U.WASHINGTON.EDU)As far as I know, the structure of lanthionine is two Ala's joined by a single sulphur with the loss of two hydrogens from the methyl group of the Ala.Stephen Bayne (sbay@novo.dk)Regarding the structure of lanthionine and dehydroalanine: dehydroalanine is formed by the loss of one sulfur atom and two hydrogen atoms from ONE cysteine residue. lanthionine is formed from TWO cysteines, is a thioether, and contains one sulfur atom less than the amino acid cystine. Dan McCormick (MCCORMICK@rcf.mayo.edu) [DeltaMass]. Most bacterially produced lanthionine crosslinks are made by dehydration of L-serine to dehydroalanine, and then reaction with L-cysteine so as to produce chiral inversion at the alpha-carbon of the original L-serine; the lanthionine is a meso-diastereomer with L-configuration of the original cysteine alpha-carbon and D-configuration of the original L-serine alpha-carbon. In cypemycin dehydroalanine has been shown to be produced by loss of hydrogen sulfide from cysteine. Beta-elimination of hydrogen sulfide does occur during treatment with performic acid [JSG]. + dehydroalanine (Cys) + + + + + A protein modification that effectively converts an L-cysteine residue to dehydroalanine. + ChEBI:17123 + DeltaMass:8 + PubMed:10220322 + PubMed:11212008 + PubMed:1547888 + PubMed:15799070 + PubMed:1815586 + PubMed:20805503 + PubMed:2914619 + PubMed:7947813 + PubMed:8239649 + RESID:AA0181#CYS + Unimod:368 + + + + + 2,3-didehydroalanine + + + + + + 2-aminoacrylic acid + + + + + + 2-aminopropenoic acid + + + + + + 4-methylidene-imidazole-5-one (MIO) active site + + + + + + Dehydroalanine (from Cysteine) + + + + + + Dha + + + + + + MOD_RES 2,3-didehydroalanine (Cys) + + + + + + anhydroserine + + + + + + dHAla(Cys) + + + + + + dehydroalanine + + + + + + Cys->Dha + + + + + + Dehydroalanine (from Cysteine) + + + + + + + + + OBSOLETE because redundant and identical to MOD:00477. Remap to MOD:00477. + MOD:00477 + -28.01 + C -1 O -1 + -27.994915 + C 4 H 7 N 1 O 0 + 69.11 + 69.057846 + P + artifact + Unimod:369 + PSI-MOD + Pro->Pyrrolidone + Pyrrolidone from Proline + MOD:00794 + This Unimod entry appears to have come from the same description in PubMed:9252331 as Unimod:360. This entry was not annotated as being approved. Neither difference formula corresponds to the result described in the original citation PubMed:2161657. + pyrrolidone from proline + true + + + + + OBSOLETE because redundant and identical to MOD:00477. Remap to MOD:00477. + PubMed:9252331 + Unimod:369 + + + + + Pro->Pyrrolidone + + + + + + Pyrrolidone from Proline + + + + + + + + + + modification from Unimod + 86.09 + C 4 H 6 O 2 + 86.03678 + C 7 H 11 N 1 O 3 S 1 + 189.23 + 189.04596 + C + artifact + Unimod:371 + PSI-MOD + HMVK + Michael addition of hydroxymethylvinyl ketone to cysteine + MOD:00795 + Michael addition of hydroxymethylvinyl ketone to cysteine + + + + + modification from Unimod + PubMed:11743741 + Unimod:371 + + + + + HMVK + + + + + + Michael addition of hydroxymethylvinyl ketone to cysteine + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to L-ornithine. + -42.04 + C -1 H -2 N -2 + -42.021797 + C 5 H 10 N 2 O 1 + 114.15 + 114.079315 + R + artifact + Unimod:372 + Ornithine (from Arginine) + Ornithyl + arg2orn + PSI-MOD + Arg->Orn + Ornithine from Arginine + MOD:00796 + + L-ornithine (Arg) + + + + + A protein modification that effectively converts an L-arginine residue to L-ornithine. + DeltaMass:129 + OMSSA:163 + PubMed:15489230 + Unimod:372 + + + + + Ornithine (from Arginine) + + + + + + Ornithyl + + + + + + arg2orn + + + + + + Arg->Orn + + + + + + Ornithine from Arginine + + + + + + + + + + + a protein modification that effectively converts an L-cysteine residue to the PEP adduct, 2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal + 168.04 + C 3 H 5 N 0 O 6 P 1 S 0 + 167.98238 + C 6 H 10 N 1 O 7 P 1 S 1 + 271.18 + 270.99155 + C + natural + uniprot.ptm:PTM-0424 + (2R)-2-amino-3-[1-carboxy-1-(phosphonooxy)ethyl]sulfanylpropanoic acid + 2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal + 2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-2-(phosphonooxy)propanoic acid + 2-([(2R)-2-azanyl-2-carboxyethyl]sulfanyl)-2-(phosphonooxy)propanoic acid + MOD_RES 2-(S-cysteinyl)pyruvic acid O-phosphothioketal + S-[1-carboxy-1-(phosphonooxy)ethyl]cysteine + SPEPCys + cysteinyl pyruvate O-phosphothioketal + phosphoenolpyruvate cysteine adduct + phospholactoyl cysteine adduct + PSI-MOD + MOD:00797 + 2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal + + + + + a protein modification that effectively converts an L-cysteine residue to the PEP adduct, 2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal + ChEBI:149496 + PubMed:4696757 + PubMed:7999765 + PubMed:8664284 + RESID:AA0391 + + + + + (2R)-2-amino-3-[1-carboxy-1-(phosphonooxy)ethyl]sulfanylpropanoic acid + + + + + + 2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal + + + + + + 2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-2-(phosphonooxy)propanoic acid + + + + + + 2-([(2R)-2-azanyl-2-carboxyethyl]sulfanyl)-2-(phosphonooxy)propanoic acid + + + + + + MOD_RES 2-(S-cysteinyl)pyruvic acid O-phosphothioketal + + + + + + S-[1-carboxy-1-(phosphonooxy)ethyl]cysteine + + + + + + SPEPCys + + + + + + cysteinyl pyruvate O-phosphothioketal + + + + + + phosphoenolpyruvate cysteine adduct + + + + + + phospholactoyl cysteine adduct + + + + + + + + + + A protein modification that can be regarded as effectively either one half of a cystine cross-link, or a cysteine residue with one hydrogen atom or proton removed. + -1.01 + C 0 H -1 N 0 O 0 S 0 + -1.007825 + C 3 H 4 N 1 O 1 S 1 + 102.13 + 102.00136 + C + Unimod:374 + PSI-MOD + Dehydro + Half of a disulfide bridge + MOD:00798 + half cystine + + + + + A protein modification that can be regarded as effectively either one half of a cystine cross-link, or a cysteine residue with one hydrogen atom or proton removed. + PubMed:1988019 + PubMed:2001356 + PubMed:2076469 + PubMed:3083866 + PubMed:366603 + PubMed:7918467 + PubMed:8344916 + Unimod:374 + + + + + Dehydro + + + + + + Half of a disulfide bridge + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-galactosyl-L-cysteine. + 162.14 + C 6 H 10 N 0 O 5 S 0 + 162.05283 + C 9 H 15 N 1 O 6 S 1 + 265.28 + 265.062 + C + artifact + uniprot.ptm:PTM-0624 + (2R)-2-amino-3-(D-galactopyranosylsulfanyl)propanoic acid + CARBOHYD S-linked (Gal) cysteine + S-(beta-D-galactopyranosyl)cysteine + S-galactosyl-L-cysteine + S-glycosyl-cysteine + SGalCys + PSI-MOD + MOD:00799 + The reported peptide has not been isolated or characterized in subsequent work, and the peptide sequence has not been found in the human proteome. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. + S-galactosyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-galactosyl-L-cysteine. + PubMed:11945907 + RESID:AA0392 + + + + + (2R)-2-amino-3-(D-galactopyranosylsulfanyl)propanoic acid + + + + + + CARBOHYD S-linked (Gal) cysteine + + + + + + S-(beta-D-galactopyranosyl)cysteine + + + + + + S-galactosyl-L-cysteine + + + + + + S-glycosyl-cysteine + + + + + + SGalCys + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and a one-vanadium seven-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide. + 932.51 + C 7 Fe 7 H 6 N 0 O 7 S 9 V 1 + 932.24854 + C 16 Fe 7 H 18 N 4 O 9 S 10 V 1 + 1172.8 + 1172.3167 + C, H + hypothetical + CysHis-[V7Fe9S] + L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide carbide + nitrogenase iron-vanadium cofactor + PSI-MOD + MOD:00800 + Cross-link 2; incidental to RESID:AA0300. + L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide + + + + + A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and a one-vanadium seven-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide. + PubMed:2345152 + RESID:AA0393 + + + + + CysHis-[V7Fe9S] + + + + + + L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide carbide + + + + + + nitrogenase iron-vanadium cofactor + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and an eight-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl octairon nonasulfide. + 937.42 + C 7 Fe 8 H 6 N 0 O 7 S 9 + 937.2406 + 2- + C 16 Fe 8 H 18 N 4 O 9 S 10 + 1177.7 + 1177.3087 + C, H + hypothetical + CysHis-[8Fe9S] + L-cysteinyl-L-histidino-homocitryl octairon nonasulfide carbide + nitrogenase iron-iron cofactor + PSI-MOD + MOD:00801 + Cross-link 2; incidental to RESID:AA0300. + L-cysteinyl-L-histidino-homocitryl octairon nonasulfide + + + + + A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and an eight-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl octairon nonasulfide. + PubMed:8392330 + RESID:AA0394 + + + + + CysHis-[8Fe9S] + + + + + + L-cysteinyl-L-histidino-homocitryl octairon nonasulfide carbide + + + + + + nitrogenase iron-iron cofactor + + + + + + + + + + + a protein modification that effectively converts an L-histidine residue to L-histidino vanadium tetraoxide + 116.95 + C 0 H 2 N 0 O 4 V 1 + 116.93927 + C 6 H 9 N 3 O 5 V 1 + 254.1 + 253.99818 + H + natural + (4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (dihydroxy)dioxovanadium + 1'-vanadato-L-histidine + L-histidino vanadium tetraoxide + N(tau)-vanadatohistidine + NtauH2VO4His + bromoperoxidase vanadium cofactor + chloroperoxidase vanadium cofactor + dihydrogen (4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (tetraoxido)vanadate + haloperoxidase vanadium cofactor + histidine-1-vanadate + histidine-N(epsilon)-vanadate + histidine-N1'-vanadate + tele-vanadatohistidine + PSI-MOD + MOD:00802 + L-histidino vanadium tetraoxide + + + + + a protein modification that effectively converts an L-histidine residue to L-histidino vanadium tetraoxide + PubMed:10543953 + PubMed:16494433 + PubMed:8552646 + RESID:AA0395 + + + + + (4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (dihydroxy)dioxovanadium + + + + + + 1'-vanadato-L-histidine + + + + + + L-histidino vanadium tetraoxide + + + + + + N(tau)-vanadatohistidine + + + + + + NtauH2VO4His + + + + + + bromoperoxidase vanadium cofactor + + + + + + chloroperoxidase vanadium cofactor + + + + + + dihydrogen (4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (tetraoxido)vanadate + + + + + + haloperoxidase vanadium cofactor + + + + + + histidine-1-vanadate + + + + + + histidine-N(epsilon)-vanadate + + + + + + histidine-N1'-vanadate + + + + + + tele-vanadatohistidine + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 3-(S-L-cysteinyl)-L-tyrosine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 12 H 12 N 2 O 3 S 1 + 264.3 + 264.05685 + C, Y + natural + uniprot.ptm:PTM-0020 + (2S,3R)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-(4-hydroxyphenyl)propanoic acid + 2-amino-3-(2-amino-2-carboxyethylthio)-3-(4-hydroxyphenyl)propanoic acid + 3-(L-cystein-S-yl)-L-tyrosine + CROSSLNK 3-(S-cysteinyl)-tyrosine (Cys-Tyr) + S-(tyros-3'-yl)cysteine + XLNKSCys3Tyr + PSI-MOD + MOD:00803 + Cross-link 2. + 3-(S-L-cysteinyl)-L-tyrosine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 3-(S-L-cysteinyl)-L-tyrosine. + PubMed:15342250 + RESID:AA0396 + + + + + (2S,3R)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-(4-hydroxyphenyl)propanoic acid + + + + + + 2-amino-3-(2-amino-2-carboxyethylthio)-3-(4-hydroxyphenyl)propanoic acid + + + + + + 3-(L-cystein-S-yl)-L-tyrosine + + + + + + CROSSLNK 3-(S-cysteinyl)-tyrosine (Cys-Tyr) + + + + + + S-(tyros-3'-yl)cysteine + + + + + + XLNKSCys3Tyr + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O3-beta-glucosylated L-serine. + 162.14 + C 6 H 10 N 0 O 5 + 162.05283 + C 9 H 15 N 1 O 7 + 249.22 + 249.08485 + S + natural + uniprot.ptm:PTM-0573 + (2S)-2-amino-3-(beta-D-glucopyranosyloxy)propanoic acid + CARBOHYD O-linked (Glc) serine + CARBOHYD O-linked (Hex) + O-glucosyl-L-serine + O-glycosylserine + O3-glucosylserine + OGlcSer + PSI-MOD + MOD:00804 + + O-glucosyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O3-beta-glucosylated L-serine. + PubMed:10734111 + PubMed:2105311 + PubMed:2511201 + RESID:AA0397 + + + + + (2S)-2-amino-3-(beta-D-glucopyranosyloxy)propanoic acid + + + + + + CARBOHYD O-linked (Glc) serine + + + + + + CARBOHYD O-linked (Hex) + + + + + + O-glucosyl-L-serine + + + + + + O-glycosylserine + + + + + + O3-glucosylserine + + + + + + OGlcSer + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O3-(N-acetylaminoglucosyl)-L-serine. + 203.19 + C 8 H 13 N 1 O 5 + 203.07938 + C 11 H 18 N 2 O 7 + 290.27 + 290.1114 + S + natural + uniprot.ptm:PTM-0580 + (2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)propanoic acid + CARBOHYD O-linked (GlcNAc) serine + CARBOHYD O-linked (HexNAc) + O-(2-acetylamino-2-deoxy-beta-D-glucopyranosyl)-L-serine + O-(N-acetylamino)glucosyl-L-serine + O-(N-acetylglucosaminyl)serine + O-glycosylserine + O-seryl-beta-N-acetylglucosaminide + O3-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-serine + O3-(N-acetylglucosaminyl)serine + OGlcNAcSer + PSI-MOD + HexNAc + MOD:00805 + + O-(N-acetylamino)glucosyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O3-(N-acetylaminoglucosyl)-L-serine. + PubMed:3086323 + PubMed:8404891 + RESID:AA0398 + + + + + (2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)propanoic acid + + + + + + CARBOHYD O-linked (GlcNAc) serine + + + + + + CARBOHYD O-linked (HexNAc) + + + + + + O-(2-acetylamino-2-deoxy-beta-D-glucopyranosyl)-L-serine + + + + + + O-(N-acetylamino)glucosyl-L-serine + + + + + + O-(N-acetylglucosaminyl)serine + + + + + + O-glycosylserine + + + + + + O-seryl-beta-N-acetylglucosaminide + + + + + + O3-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-serine + + + + + + O3-(N-acetylglucosaminyl)serine + + + + + + OGlcNAcSer + + + + + + HexNAc + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminoglucosyl)-L-threonine. + 203.19 + C 8 H 13 N 1 O 5 + 203.07938 + C 12 H 20 N 2 O 7 + 304.3 + 304.12704 + T + natural + uniprot.ptm:PTM-0582 + (2S,3R)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)butanoic acid + CARBOHYD O-linked (GlcNAc) threonine + CARBOHYD O-linked (HexNAc) + O-(2-acetylamino-2-deoxy-beta-D-glucopyranosyl)-L-threonine + O-(N-acetylamino)glucosyl-L-threonine + O-(N-acetylglucosaminyl)-L-threonine + O-glycosylthreonine + O-threonyl-beta-N-acetylglucosaminide + O3-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-threonine + O3-(N-acetylglucosaminyl)threonine + OGlcNAcThr + PSI-MOD + HexNAc + MOD:00806 + + O-(N-acetylamino)glucosyl-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminoglucosyl)-L-threonine. + PubMed:3086323 + PubMed:8404891 + RESID:AA0399 + + + + + (2S,3R)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)butanoic acid + + + + + + CARBOHYD O-linked (GlcNAc) threonine + + + + + + CARBOHYD O-linked (HexNAc) + + + + + + O-(2-acetylamino-2-deoxy-beta-D-glucopyranosyl)-L-threonine + + + + + + O-(N-acetylamino)glucosyl-L-threonine + + + + + + O-(N-acetylglucosaminyl)-L-threonine + + + + + + O-glycosylthreonine + + + + + + O-threonyl-beta-N-acetylglucosaminide + + + + + + O3-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-threonine + + + + + + O3-(N-acetylglucosaminyl)threonine + + + + + + OGlcNAcThr + + + + + + HexNAc + + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to pyruvic acid. + -17.03 + C 0 H -3 N -1 O 0 + -17.026548 + C 3 H 3 O 2 + 71.06 + 71.013306 + S + natural + N-term + Unimod:385 + uniprot.ptm:PTM-0266 + 2-oxopropanoic acid + MOD_RES Pyruvic acid (Ser) + Pyruvate + Pyruvoyl- (Serine) + pyruvic acid + PSI-MOD + MOD:00807 + + DeltaMass gives mass 70 and difference mass -16 with no formula + pyruvic acid (Ser) + + + + + A protein modification that effectively converts an L-serine residue to pyruvic acid. + DeltaMass:23 + PubMed:10085076 + PubMed:3042771 + PubMed:8464063 + RESID:AA0127#SER + Unimod:385#S + + + + + 2-oxopropanoic acid + + + + + + MOD_RES Pyruvic acid (Ser) + + + + + + Pyruvate + + + + + + Pyruvoyl- (Serine) + + + + + + pyruvic acid + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O3-galactosylserine. + 162.14 + C 6 H 10 N 0 O 5 + 162.05283 + C 9 H 15 N 1 O 7 + 249.22 + 249.08485 + S + natural + uniprot.ptm:PTM-0560 + (2S)-2-amino-3-(alpha-D-galactopyranosyloxy)propanoic acid + CARBOHYD O-linked (Gal) serine + CARBOHYD O-linked (Hex) + O-galactosyl-L-serine + O-glycosylserine + O3-galactosylserine + OGalSer + PSI-MOD + MOD:00808 + O-galactosyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O3-galactosylserine. + PubMed:666730 + RESID:AA0400 + + + + + (2S)-2-amino-3-(alpha-D-galactopyranosyloxy)propanoic acid + + + + + + CARBOHYD O-linked (Gal) serine + + + + + + CARBOHYD O-linked (Hex) + + + + + + O-galactosyl-L-serine + + + + + + O-glycosylserine + + + + + + O3-galactosylserine + + + + + + OGalSer + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O3-galactosylthreonine. + 162.14 + C 6 H 10 N 0 O 5 + 162.05283 + C 10 H 17 N 1 O 7 + 263.25 + 263.1005 + T + natural + uniprot.ptm:PTM-0562 + (2S,3R)-2-amino-3-(alpha-D-galactopyranosyloxy)butanoic acid + CARBOHYD O-linked (Gal) threonine + CARBOHYD O-linked (Hex) + O-galactosyl-L-threonine + O-glycosylthreonine + O3-galactosylthreonine + OGalThr + PSI-MOD + MOD:00809 + O-galactosyl-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O3-galactosylthreonine. + PubMed:2673008 + RESID:AA0401 + + + + + (2S,3R)-2-amino-3-(alpha-D-galactopyranosyloxy)butanoic acid + + + + + + CARBOHYD O-linked (Gal) threonine + + + + + + CARBOHYD O-linked (Hex) + + + + + + O-galactosyl-L-threonine + + + + + + O-glycosylthreonine + + + + + + O3-galactosylthreonine + + + + + + OGalThr + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O3-mannosylserine. + 162.14 + C 6 H 10 N 0 O 5 + 162.05283 + C 9 H 15 N 1 O 7 + 249.22 + 249.08485 + S + natural + uniprot.ptm:PTM-0588 + (2S)-2-amino-3-(alpha-D-mannopyranosyloxy)propanoic acid + CARBOHYD O-linked (Hex) + CARBOHYD O-linked (Man) serine + O-glycosylserine + O-mannopyranosylserine + O-mannosyl-L-serine + O3-mannosylserine + OManSer + PSI-MOD + MOD:00810 + O-mannosyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O3-mannosylserine. + PubMed:391559 + RESID:AA0402 + + + + + (2S)-2-amino-3-(alpha-D-mannopyranosyloxy)propanoic acid + + + + + + CARBOHYD O-linked (Hex) + + + + + + CARBOHYD O-linked (Man) serine + + + + + + O-glycosylserine + + + + + + O-mannopyranosylserine + + + + + + O-mannosyl-L-serine + + + + + + O3-mannosylserine + + + + + + OManSer + + + + + + + + + + + a protein modification that effectively forms a O3-mannosylthreonine + 162.14 + C 6 H 10 N 0 O 5 + 162.05283 + C 10 H 17 N 1 O 7 + 263.25 + 263.1005 + T + natural + uniprot.ptm:PTM-0591 + (2S,3R)-2-amino-3-(alpha-D-mannopyranosyloxy)butanoic acid + CARBOHYD O-linked (Hex) + CARBOHYD O-linked (Man) threonine + O-glycosylthreonine + O-mannosyl-L-threonine + O3-mannosylthreonine + OManThr + PSI-MOD + MOD:00811 + O-mannosyl-L-threonine + + + + + a protein modification that effectively forms a O3-mannosylthreonine + PubMed:391559 + RESID:AA0403 + + + + + (2S,3R)-2-amino-3-(alpha-D-mannopyranosyloxy)butanoic acid + + + + + + CARBOHYD O-linked (Hex) + + + + + + CARBOHYD O-linked (Man) threonine + + + + + + O-glycosylthreonine + + + + + + O-mannosyl-L-threonine + + + + + + O3-mannosylthreonine + + + + + + OManThr + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to an O-fucosylserine. + 146.14 + C 6 H 10 N 0 O 4 + 146.0579 + C 9 H 15 N 1 O 6 + 233.22 + 233.08994 + S + natural + Unimod:295 + uniprot.ptm:PTM-0550 + (2S)-2-amino-3-(6-deoxy-alpha-D-galactopyranosyloxy)propanoic acid + CARBOHYD O-linked (Fuc) + CARBOHYD O-linked (Fuc) serine + CARBOHYD O-linked (dHex) + O-fucosyl-L-serine + O-glycosylserine + O3-fucosylserine + OFucSer + PSI-MOD + Fucose + dHex + MOD:00812 + + O-fucosyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to an O-fucosylserine. + PubMed:10734111 + PubMed:11067851 + PubMed:11344537 + PubMed:12096136 + PubMed:1517205 + PubMed:15189151 + PubMed:1904059 + PubMed:3311742 + PubMed:3578767 + RESID:AA0404 + Unimod:295#S + + + + + (2S)-2-amino-3-(6-deoxy-alpha-D-galactopyranosyloxy)propanoic acid + + + + + + CARBOHYD O-linked (Fuc) + + + + + + CARBOHYD O-linked (Fuc) serine + + + + + + CARBOHYD O-linked (dHex) + + + + + + O-fucosyl-L-serine + + + + + + O-glycosylserine + + + + + + O3-fucosylserine + + + + + + OFucSer + + + + + + Fucose + + + + + + dHex + + + + + + + + + + + A protein modification that effectively converts an threonine residue to an O-fucosylthreonine. + 146.14 + C 6 H 10 N 0 O 4 + 146.0579 + C 10 H 17 N 1 O 6 + 247.25 + 247.10559 + T + natural + Unimod:295 + uniprot.ptm:PTM-0552 + (2S,3R)-2-amino-3-(6-deoxy-alpha-D-galactopyranosyloxy)butanoic acid + CARBOHYD O-linked (Fuc) threonine + CARBOHYD O-linked (dHex) + O-fucosyl-L-threonine + O-glycosylthreonine + O3-fucosylthreonine + OFucThr + PSI-MOD + Fucose + dHex + MOD:00813 + + O-fucosyl-L-threonine + + + + + A protein modification that effectively converts an threonine residue to an O-fucosylthreonine. + PubMed:11344537 + PubMed:11857757 + PubMed:15189151 + PubMed:1740125 + PubMed:1900431 + RESID:AA0405 + Unimod:295#T + + + + + (2S,3R)-2-amino-3-(6-deoxy-alpha-D-galactopyranosyloxy)butanoic acid + + + + + + CARBOHYD O-linked (Fuc) threonine + + + + + + CARBOHYD O-linked (dHex) + + + + + + O-fucosyl-L-threonine + + + + + + O-glycosylthreonine + + + + + + O3-fucosylthreonine + + + + + + OFucThr + + + + + + Fucose + + + + + + dHex + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O3-xylosylserine. + 132.12 + C 5 H 8 N 0 O 4 + 132.04225 + C 8 H 13 N 1 O 6 + 219.19 + 219.07428 + S + artifact + uniprot.ptm:PTM-0598 + (2S)-2-amino-3-(alpha-D-xylopyranosyloxy)propanoic acid + CARBOHYD O-linked (Xyl) serine + O-(beta-D-xylopyranosyl)-L-serine + O-glycosylserine + O-xylosyl-L-serine + O3-xylosylserine + OXylSer + PSI-MOD + MOD:00814 + One glycosylated serine with weak electron density was modeled as O3-alpha-xylosylserine, while O3-alpha-mannosyl serine and threonine were modeled at ten other positions. The authors do not discuss this exception or provide chemical evidence for it. Since an O3-xylosyl serine modification has not been reported in any other fungal proteins, the modification is probably also an O3-alpha-mannosyl serine, see MOD:00810 [JSG]. + O-xylosyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O3-xylosylserine. + PubMed:8747463 + RESID:AA0406 + + + + + (2S)-2-amino-3-(alpha-D-xylopyranosyloxy)propanoic acid + + + + + + CARBOHYD O-linked (Xyl) serine + + + + + + O-(beta-D-xylopyranosyl)-L-serine + + + + + + O-glycosylserine + + + + + + O-xylosyl-L-serine + + + + + + O3-xylosylserine + + + + + + OXylSer + + + + + + + + + OBSOLETE because redundant with MOD:00151. Remap to MOD:00151. + MOD:00151 + 520.27 + C 10 H 11 Mo 1 N 5 O 8 P 1 S 2 + 521.8841 + C + natural + PSI-MOD + MOD:00815 + molybdopterin + true + + + + + OBSOLETE because redundant with MOD:00151. Remap to MOD:00151. + PubMed:14527393 + PubMed:7878465 + PubMed:9428520 + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-stearoyl-L-cysteine. + 266.47 + C 18 H 34 N 0 O 1 S 0 + 266.26096 + C 21 H 39 N 1 O 2 S 1 + 369.61 + 369.27014 + C + natural + uniprot.ptm:PTM-0283 + (R)-2-amino-3-(octadecanoylsulfanyl)propanoic acid + 2-amino-3-(octadecanoylthio)propanoic acid + LIPID S-stearoyl cysteine + S-stearoyl-L-cysteine + SSteCys + Stearoylation + cysteine octadecanoate thioester + cysteine stearate thioester + PSI-MOD + MOD:00816 + + From DeltaMass: Average Mass: 266 + S-stearoyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-stearoyl-L-cysteine. + DeltaMass:0 + PubMed:2371783 + PubMed:3143715 + PubMed:8761467 + RESID:AA0407 + + + + + (R)-2-amino-3-(octadecanoylsulfanyl)propanoic acid + + + + + + 2-amino-3-(octadecanoylthio)propanoic acid + + + + + + LIPID S-stearoyl cysteine + + + + + + S-stearoyl-L-cysteine + + + + + + SSteCys + + + + + + Stearoylation + + + + + + cysteine octadecanoate thioester + + + + + + cysteine stearate thioester + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to 3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan. + 136.24 + C 10 H 16 N 0 O 0 + 136.1252 + C 21 H 26 N 2 O 1 + 322.45 + 322.2045 + W + natural + uniprot.ptm:PTM-0026 + (2S,3R)-3-geranyl-2,3-dihydro-2,N(alpha)-cyclo-L-tryptophan + (2S,3aR,8aS)-3a-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid + 3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan + 3'Ger2'N2cycTrp + LIPID 3'-geranyl-2',N2-cyclotryptophan + PSI-MOD + MOD:00817 + 3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to 3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan. + ChEBI:35304 + PubMed:16407988 + PubMed:8168130 + RESID:AA0408 + + + + + (2S,3R)-3-geranyl-2,3-dihydro-2,N(alpha)-cyclo-L-tryptophan + + + + + + (2S,3aR,8aS)-3a-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid + + + + + + 3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan + + + + + + 3'Ger2'N2cycTrp + + + + + + LIPID 3'-geranyl-2',N2-cyclotryptophan + + + + + + + + + + + + A protein modification that effectively converts a residue to a glycosylphosphatidylinositolethanolamidated. + 123.05 + C 2 H 6 N 1 O 3 P 1 + 123.00853 + X + natural + C-term + Unimod:394 + uniprot.ptm:PTM-0139 + GPIRes + LIPID GPI-anchor amidated carboxyl end + PSI-MOD + GPIanchor + glycosylphosphatidylinositol + MOD:00818 + glycosylphosphatidylinositolated residue + + + + + A protein modification that effectively converts a residue to a glycosylphosphatidylinositolethanolamidated. + PubMed:12643538 + Unimod:394#C-term + + + + + GPIRes + + + + + + LIPID GPI-anchor amidated carboxyl end + + + + + + GPIanchor + + + + + + glycosylphosphatidylinositol + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-2-aminobutanoic acid. + -44.01 + C -1 H 0 N 0 O -2 + -43.98983 + C 4 H 7 N 1 O 1 + 85.11 + 85.052765 + E + natural + (S)-2-aminobutanoic acid + Abu + L-2-amino-n-butyric acid + L-2-aminobutanoic acid + L-2-aminobutyric acid + L-alpha-amino-n-butyric acid + L-alpha-aminobutyric acid + L-butyrine + alpha-amino-n-butyric acid + alpha-aminobutyric acid + butyrine + dCbxGlu + PSI-MOD + MOD:00819 + L-2-aminobutanoic acid (Glu) + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-2-aminobutanoic acid. + ChEBI:35619 + DeltaMass:0 + PubMed:11740505 + RESID:AA0409 + + + + + (S)-2-aminobutanoic acid + + + + + + Abu + + + + + + Abu + + + + + + L-2-amino-n-butyric acid + + + + + + L-2-aminobutanoic acid + + + + + + L-2-aminobutyric acid + + + + + + L-alpha-amino-n-butyric acid + + + + + + L-alpha-aminobutyric acid + + + + + + L-butyrine + + + + + + alpha-amino-n-butyric acid + + + + + + alpha-aminobutyric acid + + + + + + butyrine + + + + + + dCbxGlu + + + + + + + + + + + + A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue to form 2-imino-alanine 5-imidazolinone glycine. + -64.04 + C -1 H -4 N 0 O -3 + -64.016045 + C 5 H 4 N 2 O 1 + 108.1 + 108.032364 + D, G + natural + (2-ethanimidoyl-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid + 2,N-didehydroalanyl-5-imidazolinone glycine + 2-(1-iminoethyl)-1-carboxymethyl-1-imidazolin-5-one + 2-imino-alanine 5-imidazolinone glycine + 2-imino-alanyl-5-imidazolinone glycine + [2-(1-iminoethyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid + alanyl-5-imidazolinone glycine + para-hydroxybenzylidene-imidazolidinone chromophore + red fluorescent protein zRFP574 chromophore + PSI-MOD + MOD:00820 + Cross-link 2; carboxamidine. + 2-imino-alanine 5-imidazolinone glycine + + + + + A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue to form 2-imino-alanine 5-imidazolinone glycine. + PubMed:16627946 + RESID:AA0410 + + + + + (2-ethanimidoyl-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid + + + + + + 2,N-didehydroalanyl-5-imidazolinone glycine + + + + + + 2-(1-iminoethyl)-1-carboxymethyl-1-imidazolin-5-one + + + + + + 2-imino-alanine 5-imidazolinone glycine + + + + + + 2-imino-alanyl-5-imidazolinone glycine + + + + + + [2-(1-iminoethyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid + + + + + + alanyl-5-imidazolinone glycine + + + + + + para-hydroxybenzylidene-imidazolidinone chromophore + + + + + + red fluorescent protein zRFP574 chromophore + + + + + + + + + + + + A protein modification that effectively crosslinks an L-alanine residue and an L-cysteine residue by a thioester bond to form S-(L-alanyl)-L-cysteine. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 6 H 9 N 2 O 2 S 1 + 173.21 + 173.03847 + A, C + hypothetical + C-term + (2R)-2-amino-3-([(2S)-2-aminopropanoyl]sulfanyl)propanoic acid + CROSSLNK Alanyl cysteine thioester (Cys-Ala) + S-(2-aminopropanoyl)cysteine + S-(L-alanyl)-L-cysteine + XLNK1AlaSCys + alanine cysteine thioester + PSI-MOD + MOD:00821 + Cross-link 2. + S-(L-alanyl)-L-cysteine + + + + + A protein modification that effectively crosslinks an L-alanine residue and an L-cysteine residue by a thioester bond to form S-(L-alanyl)-L-cysteine. + PubMed:11807079 + RESID:AA0411 + + + + + (2R)-2-amino-3-([(2S)-2-aminopropanoyl]sulfanyl)propanoic acid + + + + + + CROSSLNK Alanyl cysteine thioester (Cys-Ala) + + + + + + S-(2-aminopropanoyl)cysteine + + + + + + S-(L-alanyl)-L-cysteine + + + + + + XLNK1AlaSCys + + + + + + alanine cysteine thioester + + + + + + + + + + + + A protein modification that effectively crosslinks an L-leucine residue and an L-cysteine residue by a thioester bond to form S-(L-leucyl)-L-cysteine. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 9 H 15 N 2 O 2 S 1 + 215.29 + 215.08542 + C, L + natural + C-term + (2R)-2-amino-3-([(2S)-2-amino-4-methylpentanoyl]sulfanyl)propanoic acid + CROSSLNK Leucyl cysteine thioester (Cys-Leu) + S-(2-amino-4-methylpentanoyl)cysteine + S-(L-leucyl)-L-cysteine + XLNK1LeuSCys + leucine cysteine thioester + PSI-MOD + MOD:00822 + Cross-link 2. + S-(L-leucyl)-L-cysteine + + + + + A protein modification that effectively crosslinks an L-leucine residue and an L-cysteine residue by a thioester bond to form S-(L-leucyl)-L-cysteine. + PubMed:12591958 + RESID:AA0412 + + + + + (2R)-2-amino-3-([(2S)-2-amino-4-methylpentanoyl]sulfanyl)propanoic acid + + + + + + CROSSLNK Leucyl cysteine thioester (Cys-Leu) + + + + + + S-(2-amino-4-methylpentanoyl)cysteine + + + + + + S-(L-leucyl)-L-cysteine + + + + + + XLNK1LeuSCys + + + + + + leucine cysteine thioester + + + + + + + + + + + + A protein modification that effectively crosslinks an L-methionine residue and an L-cysteine residue by a thioester bond to form S-(L-methionyl)-L-cysteine. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 8 H 13 N 2 O 2 S 2 + 233.32 + 233.04184 + C, M + natural + C-term + (2R)-2-amino-3-([(2S)-2-amino-4-(methylsulfanyl)butanoyl]sulfanyl)propanoic acid + CROSSLNK Methionyl cysteine thioester (Cys-Met) + S-(2-amino-4-methylthiobutanoyl)cysteine + S-(L-methionyl)-L-cysteine + XLNK1MetSCys + methionine cysteine thioester + PSI-MOD + MOD:00823 + Cross-link 2. + S-(L-methionyl)-L-cysteine + + + + + A protein modification that effectively crosslinks an L-methionine residue and an L-cysteine residue by a thioester bond to form S-(L-methionyl)-L-cysteine. + PubMed:12146974 + RESID:AA0413 + + + + + (2R)-2-amino-3-([(2S)-2-amino-4-(methylsulfanyl)butanoyl]sulfanyl)propanoic acid + + + + + + CROSSLNK Methionyl cysteine thioester (Cys-Met) + + + + + + S-(2-amino-4-methylthiobutanoyl)cysteine + + + + + + S-(L-methionyl)-L-cysteine + + + + + + XLNK1MetSCys + + + + + + methionine cysteine thioester + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to dehydroalanine. + -94.11 + C -6 H -6 N 0 O -1 + -94.04186 + C 3 H 3 N 1 O 1 + 69.06 + 69.02146 + Y + natural + Unimod:400 + uniprot.ptm:PTM-0647 + 2,3-didehydroalanine + 2-aminoacrylic acid + 2-aminopropenoic acid + 4-methylidene-imidazole-5-one (MIO) active site + Dha + anhydroserine + dHAla(Tyr) + dehydroalanine + PSI-MOD + MOD:00824 + incidental to RESID:AA0178 + dehydroalanine (Tyr) + + + + + A protein modification that effectively converts an L-tyrosine residue to dehydroalanine. + PubMed:10220322 + PubMed:1547888 + PubMed:1815586 + PubMed:2914619 + PubMed:6838602 + PubMed:7947813 + PubMed:8239649 + RESID:AA0181#TYR + Unimod:400 + + + + + 2,3-didehydroalanine + + + + + + 2-aminoacrylic acid + + + + + + 2-aminopropenoic acid + + + + + + 4-methylidene-imidazole-5-one (MIO) active site + + + + + + Dha + + + + + + anhydroserine + + + + + + dHAla(Tyr) + + + + + + dehydroalanine + + + + + + + + + + + + A protein modification that effectively crosslinks an L-phenylalanine residue and an L-cysteine residue by a thioester bond to form S-(L-phenylalaninyl)-L-cysteine. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 12 H 13 N 2 O 2 S 1 + 249.31 + 249.06978 + C, F + natural + C-term + (2R)-2-amino-3-([(2S)-2-amino-3-phenylpropanoyl]sulfanyl)propanoic acid + CROSSLNK Phenylalanyl cysteine thioester (Cys-Phe) + S-(2-amino-3-phenylpropanoyl)cysteine + S-(L-phenylalanyl)-L-cysteine + XLNK1PheSCys + phenylalanine cysteine thioester + PSI-MOD + MOD:00825 + Cross-link 2. + S-(L-phenylalanyl)-L-cysteine + + + + + A protein modification that effectively crosslinks an L-phenylalanine residue and an L-cysteine residue by a thioester bond to form S-(L-phenylalaninyl)-L-cysteine. + PubMed:12591958 + RESID:AA0414 + + + + + (2R)-2-amino-3-([(2S)-2-amino-3-phenylpropanoyl]sulfanyl)propanoic acid + + + + + + CROSSLNK Phenylalanyl cysteine thioester (Cys-Phe) + + + + + + S-(2-amino-3-phenylpropanoyl)cysteine + + + + + + S-(L-phenylalanyl)-L-cysteine + + + + + + XLNK1PheSCys + + + + + + phenylalanine cysteine thioester + + + + + + + + + + + + A protein modification that effectively crosslinks an L-threonine residue and an L-cysteine residue by a thioester bond to form S-(L-threonyl)-L-cysteine. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 7 H 11 N 2 O 3 S 1 + 203.24 + 203.04904 + C, T + natural + C-term + (2R)-2-amino-3-([(2S,3R)-2-amino-3-hydroxybutanoyl]sulfanyl)propanoic acid + CROSSLNK Threonyl cysteine thioester (Cys-Thr) + S-(2-amino-3-hydroxybutanoyl)cysteine + S-(L-threonyl)-L-cysteine + XLNK1ThrSCys + threonine cysteine thioester + PSI-MOD + MOD:00826 + Cross-link 2. + S-(L-threonyl)-L-cysteine + + + + + A protein modification that effectively crosslinks an L-threonine residue and an L-cysteine residue by a thioester bond to form S-(L-threonyl)-L-cysteine. + PubMed:15268951 + RESID:AA0415 + + + + + (2R)-2-amino-3-([(2S,3R)-2-amino-3-hydroxybutanoyl]sulfanyl)propanoic acid + + + + + + CROSSLNK Threonyl cysteine thioester (Cys-Thr) + + + + + + S-(2-amino-3-hydroxybutanoyl)cysteine + + + + + + S-(L-threonyl)-L-cysteine + + + + + + XLNK1ThrSCys + + + + + + threonine cysteine thioester + + + + + + + + + + + + A protein modification that effectively crosslinks an L-tyrosine residue and an L-cysteine residue by a thioester bond to form S-(L-tyrosyl)-L-cysteine. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 12 H 13 N 2 O 3 S 1 + 265.31 + 265.0647 + C, Y + natural + C-term + (2R)-2-amino-3-([(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]sulfanyl)propanoic acid + CROSSLNK Tyrosyl cysteine thioester (Cys-Tyr) + S-(L-tyrosyl)-L-cysteine + S-[2-amino-3-(4-hydoxyphenyl)propanoyl]cysteine + XLNK1TyrSCys + tyrosine cysteine thioester + PSI-MOD + MOD:00827 + Cross-link 2. + S-(L-tyrosyl)-L-cysteine + + + + + A protein modification that effectively crosslinks an L-tyrosine residue and an L-cysteine residue by a thioester bond to form S-(L-tyrosyl)-L-cysteine. + PubMed:11807079 + RESID:AA0416 + + + + + (2R)-2-amino-3-([(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]sulfanyl)propanoic acid + + + + + + CROSSLNK Tyrosyl cysteine thioester (Cys-Tyr) + + + + + + S-(L-tyrosyl)-L-cysteine + + + + + + S-[2-amino-3-(4-hydoxyphenyl)propanoyl]cysteine + + + + + + XLNK1TyrSCys + + + + + + tyrosine cysteine thioester + + + + + + + + + + + + A protein modification that effectively crosslinks an L-tryptophan residue and an L-cysteine residue by a thioester bond to form S-(L-tryptophanyl)-L-cysteine. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 14 H 14 N 3 O 2 S 1 + 288.35 + 288.08066 + C, W + natural + C-term + (2R)-2-amino-3-([(2S)-2-amino-3-(1H-indol-3-yl)propanoyl]sulfanyl)propanoic acid + CROSSLNK Tryptophanyl cysteine thioester (Cys-Trp) + S-(L-tryptophanyl)-L-cysteine + S-[2-amino-3-(1H-indol-3-yl)propanoyl]cysteine + XLNK1TrpSCys + tryptophan cysteine thioester + PSI-MOD + MOD:00828 + Cross-link 2. + S-(L-tryptophanyl)-L-cysteine + + + + + A protein modification that effectively crosslinks an L-tryptophan residue and an L-cysteine residue by a thioester bond to form S-(L-tryptophanyl)-L-cysteine. + PubMed:16030216 + RESID:AA0417 + + + + + (2R)-2-amino-3-([(2S)-2-amino-3-(1H-indol-3-yl)propanoyl]sulfanyl)propanoic acid + + + + + + CROSSLNK Tryptophanyl cysteine thioester (Cys-Trp) + + + + + + S-(L-tryptophanyl)-L-cysteine + + + + + + S-[2-amino-3-(1H-indol-3-yl)propanoyl]cysteine + + + + + + XLNK1TrpSCys + + + + + + tryptophan cysteine thioester + + + + + + + + + + + + + A protein modification that effectively crosslinks an L-phenylalanine residue and an L-serine residue by an ester bond to form S-(L-phenylalaninyl)-L-serine. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 12 H 13 N 2 O 3 + 233.25 + 233.09262 + F, S + natural + C-term + (2S)-2-amino-3-([(2S)-2-amino-3-phenylpropanoyl]oxy)propanoic acid + CROSSLNK Phenylalanyl serine ester (Ser-Phe) + O-(2-amino-3-phenylpropanoyl)serine + O-(L-phenylalanyl)-L-serine + XLNK1PheOSer + phenylalanine serine ester + PSI-MOD + MOD:00829 + Cross-link 2. + O-(L-phenylalanyl)-L-serine + + + + + A protein modification that effectively crosslinks an L-phenylalanine residue and an L-serine residue by an ester bond to form S-(L-phenylalaninyl)-L-serine. + PubMed:12591958 + RESID:AA0418 + + + + + (2S)-2-amino-3-([(2S)-2-amino-3-phenylpropanoyl]oxy)propanoic acid + + + + + + CROSSLNK Phenylalanyl serine ester (Ser-Phe) + + + + + + O-(2-amino-3-phenylpropanoyl)serine + + + + + + O-(L-phenylalanyl)-L-serine + + + + + + XLNK1PheOSer + + + + + + phenylalanine serine ester + + + + + + + + + + + + A protein modification that effectively converts an L-proline residue to an N-methyl-L-proline. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 6 H 10 N 1 O 1 + 112.15 + 112.07624 + P + natural + N-term + uniprot.ptm:PTM-0219 + (S)-1-methylpyrrolidine-2-carboxylic acid + 1-methylpyrrolidine-2-carboxylic acid + MOD_RES N-methylproline + N-methyl-L-proline + N-methylated L-proline + NMePro + hygric acid + PSI-MOD + MOD:00830 + + Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG]. + N-methyl-L-proline + + + + + A protein modification that effectively converts an L-proline residue to an N-methyl-L-proline. + PubMed:3127388 + RESID:AA0419 + + + + + (S)-1-methylpyrrolidine-2-carboxylic acid + + + + + + 1-methylpyrrolidine-2-carboxylic acid + + + + + + MOD_RES N-methylproline + + + + + + N-methyl-L-proline + + + + + + N-methylated L-proline + + + + + + NMePro + + + + + + hygric acid + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to N4-(N-acetylaminoglucosyl)-L-asparagine. + 203.19 + C 8 H 13 N 1 O 5 + 203.07938 + C 12 H 19 N 3 O 7 + 317.3 + 317.1223 + N + natural + uniprot.ptm:PTM-0527 + CARBOHYD N-linked (GlcNAc) asparagine + N4GlcNAcAsn + PSI-MOD + HexNAc + MOD:00831 + + N4-(N-acetylamino)glucosyl-L-asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to N4-(N-acetylaminoglucosyl)-L-asparagine. + PubMed:111247 + PubMed:1694179 + PubMed:5490222 + RESID:AA0151#var + + + + + CARBOHYD N-linked (GlcNAc) asparagine + + + + + + N4GlcNAcAsn + + + + + + HexNAc + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminogalactosyl)-L-asparagine. + 203.19 + C 8 H 13 N 1 O 5 + 203.07938 + C 12 H 19 N 3 O 7 + 317.3 + 317.1223 + N + natural + uniprot.ptm:PTM-0512 + (2S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)amino-4-oxobutanoic acid + CARBOHYD N-linked (GalNAc) asparagine + N4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)-L-asparagine + N4-(2-acetylamino-2-deoxy-beta-D-galactopyranosyl)-L-asparagine + N4-(N-acetylamino)galactosyl-L-asparagine + N4-(N-acetylgalactosaminyl)asparagine + N4-asparagine-beta-N-acetylgalactosaminide + N4-glycosyl-L-asparagine + N4-glycosylasparagine + N4GalNAcAsn + PSI-MOD + HexNAc + MOD:00832 + N4-(N-acetylamino)galactosyl-L-asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminogalactosyl)-L-asparagine. + PubMed:8262914 + RESID:AA0420 + + + + + (2S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)amino-4-oxobutanoic acid + + + + + + CARBOHYD N-linked (GalNAc) asparagine + + + + + + N4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)-L-asparagine + + + + + + N4-(2-acetylamino-2-deoxy-beta-D-galactopyranosyl)-L-asparagine + + + + + + N4-(N-acetylamino)galactosyl-L-asparagine + + + + + + N4-(N-acetylgalactosaminyl)asparagine + + + + + + N4-asparagine-beta-N-acetylgalactosaminide + + + + + + N4-glycosyl-L-asparagine + + + + + + N4-glycosylasparagine + + + + + + N4GalNAcAsn + + + + + + HexNAc + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to N4-glucosyl-asparagine. + 162.14 + C 6 H 10 N 0 O 5 + 162.05283 + C 10 H 16 N 2 O 7 + 276.25 + 276.09576 + N + natural + uniprot.ptm:PTM-0517 + (2S)-2-amino-4-(D-glucopyranosyl)amino-4-oxobutanoic acid + CARBOHYD N-linked (Glc) + CARBOHYD N-linked (Glc) asparagine + N4-(D-glucopyranosyl)-L-asparagine + N4-asparagine-glucoside + N4-glucosyl-L-asparagine + N4-glucosylasparagine + N4-glycosyl-L-asparagine + N4-glycosylasparagine + N4GlcAsn + PSI-MOD + MOD:00833 + N4-glucosyl-L-asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to N4-glucosyl-asparagine. + PubMed:1569073 + PubMed:3410849 + RESID:AA0421 + + + + + (2S)-2-amino-4-(D-glucopyranosyl)amino-4-oxobutanoic acid + + + + + + CARBOHYD N-linked (Glc) + + + + + + CARBOHYD N-linked (Glc) asparagine + + + + + + N4-(D-glucopyranosyl)-L-asparagine + + + + + + N4-asparagine-glucoside + + + + + + N4-glucosyl-L-asparagine + + + + + + N4-glucosylasparagine + + + + + + N4-glycosyl-L-asparagine + + + + + + N4-glycosylasparagine + + + + + + N4GlcAsn + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O3-(N-acetamino)fucosylserine. + 187.19 + C 8 H 13 N 1 O 4 + 187.08446 + C 11 H 18 N 2 O 6 + 274.27 + 274.1165 + S + natural + uniprot.ptm:PTM-0553 + (2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-fucopyranosyloxy)propanoic acid + CARBOHYD O-linked (FucNAc) serine + O-(2-acetylamino-2-deoxy-beta-D-fucopyranosyl)-L-serine + O-(N-acetylamino)fucosyl-L-serine + O-(N-acetylfucosaminyl)serine + O-seryl-beta-N-acetylfucosaminide + O3-(2-acetamido-2-deoxy-beta-D-fucopyranosyl)-L-serine + O3-(N-acetylfucosaminyl)serine + OFucNAcSer + PSI-MOD + MOD:00834 + + O-(N-acetylamino)fucosyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O3-(N-acetamino)fucosylserine. + PubMed:11342554 + PubMed:12010970 + RESID:AA0422 + + + + + (2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-fucopyranosyloxy)propanoic acid + + + + + + CARBOHYD O-linked (FucNAc) serine + + + + + + O-(2-acetylamino-2-deoxy-beta-D-fucopyranosyl)-L-serine + + + + + + O-(N-acetylamino)fucosyl-L-serine + + + + + + O-(N-acetylfucosaminyl)serine + + + + + + O-seryl-beta-N-acetylfucosaminide + + + + + + O3-(2-acetamido-2-deoxy-beta-D-fucopyranosyl)-L-serine + + + + + + O3-(N-acetylfucosaminyl)serine + + + + + + OFucNAcSer + + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to L-oxoalanine. + -2.02 + C 0 H -2 N 0 O 0 + -2.01565 + C 3 H 3 N 1 O 2 + 85.06 + 85.01638 + S + natural + Unimod:401 + (S)-2-amino-3-oxopropanoic acid + 2-amino-3-oxopropionic acid + L-3-oxoalanine + L-amino-malonic acid semialdehyde + L-aminomalonaldehydic acid + MOD_RES 3-oxoalanine (Ser) + formylglycine (from serine) + PSI-MOD + C(alpha)-formylglycine + Didehydro + L-serinesemialdehyde + dehydrogenated serine residue + formylglycine + oxoalanine + MOD:00835 + + L-3-oxoalanine (Ser) + + + + + A protein modification that effectively converts an L-serine residue to L-oxoalanine. + DeltaMass:349 + PubMed:14563551 + PubMed:7628016 + PubMed:8681943 + PubMed:9276974 + PubMed:9478923 + RESID:AA0185#SER + Unimod:401#S + + + + + (S)-2-amino-3-oxopropanoic acid + + + + + + 2-amino-3-oxopropionic acid + + + + + + L-3-oxoalanine + + + + + + L-amino-malonic acid semialdehyde + + + + + + L-aminomalonaldehydic acid + + + + + + MOD_RES 3-oxoalanine (Ser) + + + + + + formylglycine (from serine) + + + + + + C(alpha)-formylglycine + + + + + + Didehydro + + + + + + L-serinesemialdehyde + + + + + + dehydrogenated serine residue + + + + + + formylglycine + + + + + + oxoalanine + + + + + + + + + + A protein modification that effectively substitutes two (2)H deuterium atoms for two (1)H protium atoms. + D(H)2Res + PSI-MOD + MOD:00836 + + deuterium disubstituted residue + + + + + A protein modification that effectively substitutes two (2)H deuterium atoms for two (1)H protium atoms. + PubMed:18688235 + + + + + D(H)2Res + + + + + + + + + + A protein modification that effectively substitutes four (2)H deuterium atoms for four (1)H protium atoms. + D(H)4Res + PSI-MOD + MOD:00837 + deuterium tetrasubstituted residue + + + + + A protein modification that effectively substitutes four (2)H deuterium atoms for four (1)H protium atoms. + PubMed:18688235 + + + + + D(H)4Res + + + + + + + + + + + A protein modification that effectively substitutes three (1)H protium atoms with three (2)H deuterium atoms to produce 3x(2)H labeled L-leucine. + 3.02 + (1)H -3 (2)H 3 + 3.01883 + C 6 (1)H 8 (2)H 3 N 1 O 1 + 116.1 + 116.1029 + L + artifact + Unimod:262 + D(H)3Leu + PSI-MOD + Label:2H(3) + Trideuteration + MOD:00838 + 3x(2)H labeled L-leucine + + + + + A protein modification that effectively substitutes three (1)H protium atoms with three (2)H deuterium atoms to produce 3x(2)H labeled L-leucine. + Unimod:262#L + + + + + D(H)3Leu + + + + + + Label:2H(3) + + + + + + Trideuteration + + + + + + + + + + A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing deuteriumm, (2)H. + PSI-MOD + MOD:00839 + + (2)H deuterium labeled residue + + + + + A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing deuteriumm, (2)H. + PubMed:18688235 + + + + + + + + + A protein modification produced by formation of an adduct with an isocyanate compound. + PSI-MOD + MOD:00840 + + isocyanate reagent derivatized residue + + + + + A protein modification produced by formation of an adduct with an isocyanate compound. + PubMed:18688235 + + + + + + + + + A protein modification produced by formation of an adduct with an isothiocyanate compound. + PSI-MOD + MOD:00841 + + isothiocyanate reagent derivatized residue + + + + + A protein modification produced by formation of an adduct with an isothiocyanate compound. + PubMed:18688235 + + + + + + + + + A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (13)C. + PSI-MOD + MOD:00842 + + (13)C labeled residue + + + + + A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (13)C. + PubMed:18688235 + + + + + + + + + A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (15)N. + PSI-MOD + MOD:00843 + + (15)N labeled residue + + + + + A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (15)N. + PubMed:18688235 + + + + + + + + + A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (18)O. + PSI-MOD + MOD:00844 + + (18)O labeled residue + + + + + A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (18)O. + PubMed:18688235 + + + + + + + + + A protein modification that effectively substitutes one or more (18)O atoms for (16)O atoms. + PSI-MOD + MOD:00845 + + (18)O substituted residue + + + + + A protein modification that effectively substitutes one or more (18)O atoms for (16)O atoms. + PubMed:18688235 + + + + + + + + + stub + PSI-MOD + MOD:00846 + levuglandinyl (prostaglandin H2) adduct + + + + + stub + PubMed:18688235 + + + + + + + + + A protein modification that effectively substitutes two (18)O atom for two (16)O atoms. + PSI-MOD + MOD:00847 + + (18)O disubstituted residue + + + + + A protein modification that effectively substitutes two (18)O atom for two (16)O atoms. + PubMed:18688235 + + + + + + + + + A protein modification that is produced by formation of an adduct with a particular compound used as a reagent. + PSI-MOD + MOD:00848 + + reagent derivatized residue + + + + + A protein modification that is produced by formation of an adduct with a particular compound used as a reagent. + PubMed:18688235 + + + + + + + + + A protein modification that effectively substitutes a potassium atom for a hydrogen atom. + KRes + PSI-MOD + MOD:00849 + + potassium containing modified residue + + + + + A protein modification that effectively substitutes a potassium atom for a hydrogen atom. + PubMed:18688235 + + + + + KRes + + + + + + + + + + A protein modification that inserts or replaces a residue with an unnatural residue that is not considered to be derived from a natural residue by some chemical process. + PSI-MOD + MOD:00850 + + unnatural residue + + + + + A protein modification that inserts or replaces a residue with an unnatural residue that is not considered to be derived from a natural residue by some chemical process. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with (18)O. + X + artifact + PSI-MOD + MOD:00851 + + (18)O labeled deamidated residue + + + + + A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with (18)O. + PubMed:18688235 + + + + + + + + + A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with one (18)O. + 2.99 + H -1 N -1 (18)O 1 + 2.988262 + X + artifact + Unimod:366 + PSI-MOD + MOD:00852 + + 1x(18)O labeled deamidated residue + + + + + A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with one (18)O. + PubMed:8382902 + Unimod:366 + + + + + + + + + A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with two (18)O. + 4.99 + H -1 N -1 (16)O -1 (18)O 2 + 4.992508 + X + artifact + PSI-MOD + MOD:00853 + + 2x(18)O labeled deamidated residue + + + + + A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with two (18)O. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively converts an L-lysine to L-lysinium (protonated L-lysine). + 1.01 + C 0 H 1 N 0 O 0 + 1.007276 + 1+ + C 6 H 13 N 2 O 1 + 129.18 + 129.10223 + K + natural + PSI-MOD + MOD:00854 + + Some sources compute the difference formula for charged, quatenary modified lysine based on protonated lysine rather than neutral lysine residue. In such cases, a comparable difference formula can be calculated based on this derivative. + protonated L-lysine (L-lysinium) residue + + + + + A protein modification that effectively converts an L-lysine to L-lysinium (protonated L-lysine). + PubMed:18688235 + + + + + + + + + + + + + + + A protein modification that effectively converts an L-lysinium (N6-protonated L-lysine) residue to an N6,N6,N6-trimethyl-L-lysine. + 42.08 + C 3 H 6 N 0 O 0 + 42.046402 + 1+ + C 9 H 19 N 2 O 1 + 171.26 + 171.14919 + MOD:00854 + natural + Unimod:37 + N6Me3Lys + trimethylk + PSI-MOD + MOD:00855 + + For amino acids residues, amine trimethylation can effectively only be accomplished with an aminium, protonated primary amino, group. This process accounts only for trimethylation and not protonation. The alternative N6Me3+Lys process (MOD:00083) accounts for both protonation and trimethylation. + N6,N6,N6-trimethyl-L-lysine (from L-lysinium residue) + + + + + A protein modification that effectively converts an L-lysinium (N6-protonated L-lysine) residue to an N6,N6,N6-trimethyl-L-lysine. + DeltaMass:0 + OMSSA:15 + PubMed:12590383 + PubMed:3145979 + PubMed:4304194 + PubMed:6778808 + PubMed:7093227 + PubMed:8453381 + Unimod:37#K + + + + + N6Me3Lys + + + + + + trimethylk + + + + + + + + + + + A protein modification that effectively converts an L-alanine residue to an L-alaninium (protonated L-alanine). + 1.01 + C 0 H 1 N 0 O 0 + 1.007276 + 1+ + C 3 H 7 N 1 O 1 + 73.09 + 73.052216 + A + natural + N-term + PSI-MOD + MOD:00856 + + protonated L-alanine (L-alaninium) residue + + + + + A protein modification that effectively converts an L-alanine residue to an L-alaninium (protonated L-alanine). + PubMed:18688235 + + + + + + + + + + + + + + + A protein modification that effectively converts an L-alaninium (protonated L-alanine) residue to an N,N,N-trimethyl-L-alanine. + 42.08 + C 3 H 6 N 0 O 0 + 42.046402 + 1+ + C 6 H 13 N 1 O 1 + 115.18 + 115.09917 + MOD:00856 + natural + N-term + Unimod:37 + N2Me3Ala + PSI-MOD + MOD:00857 + + For amino acids residues, amine trimethylation can effectively only be accomplished with an aminium, protonated primary amino, group. This process accounts only for trimethylation and not protonation. The alternative N2Me3+Ala process (MOD:00071) accounts for both protonation and trimethylation. + N,N,N-trimethyl-L-alanine (from L-alaninium) + + + + + A protein modification that effectively converts an L-alaninium (protonated L-alanine) residue to an N,N,N-trimethyl-L-alanine. + PubMed:12590383 + PubMed:332162 + PubMed:3979397 + PubMed:6778808 + PubMed:7715456 + Unimod:37#A + + + + + N2Me3Ala + + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to D-alanine. + -16.0 + C 0 H 0 N 0 O -1 + -15.994915 + C 3 H 5 N 1 O 1 + 71.08 + 71.03712 + S + natural + uniprot.ptm:PTM-0113 + (R)-2-aminopropanoic acid + D-Ala(Ser) + D-alanine + MOD_RES D-alanine (Ser) + PSI-MOD + MOD:00858 + D-alanine (Ser) + + + + + A protein modification that effectively converts an L-serine residue to D-alanine. + PubMed:7961627 + RESID:AA0191#SER + + + + + (R)-2-aminopropanoic acid + + + + + + D-Ala(Ser) + + + + + + D-alanine + + + + + + MOD_RES D-alanine (Ser) + + + + + + + + + + A protein modification that can be derived from different natural residues by different chemical processes. + X + natural + PSI-MOD + MOD:00859 + + modified residue that can arise from different natural residues + + + + + A protein modification that can be derived from different natural residues by different chemical processes. + PubMed:18688235 + + + + + + + + + A protein modification that produces an amino acid residue containing an exogenous sulfur atom. + PSI-MOD + MOD:00860 + + sulfur containing modified residue + + + + + A protein modification that produces an amino acid residue containing an exogenous sulfur atom. + PubMed:18688235 + + + + + + + + + A protein modification that produces an amino acid residue containing a phosphorus atom. + PSI-MOD + MOD:00861 + + phosphorus containing modified residue + + + + + A protein modification that produces an amino acid residue containing a phosphorus atom. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to D-alanine. + C 3 H 5 N 1 O 1 + 71.08 + 71.03712 + X + natural + (R)-2-aminopropanoic acid + D-alanine + MOD_RES D-alanine (Ala) + MOD_RES D-alanine (Ser) + PSI-MOD + MOD:00862 + D-alanine + + + + + A protein modification that effectively converts a source amino acid residue to D-alanine. + ChEBI:29949 + PubMed:7287302 + PubMed:7961627 + RESID:AA0191 + + + + + (R)-2-aminopropanoic acid + + + + + + D-alanine + + + + + + MOD_RES D-alanine (Ala) + + + + + + MOD_RES D-alanine (Ser) + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to D-allo-threonine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 4 H 7 N 1 O 2 + 101.1 + 101.047676 + T + natural + uniprot.ptm:PTM-0310 + (2R,3R)-2-amino-3-hydroxybutanoic acid + D-Thr + D-threonine + MOD_RES D-threonine + PSI-MOD + MOD:00863 + D-allo-threonine + + + + + A protein modification that effectively converts an L-threonine residue to D-allo-threonine. + ChEBI:32826 + PubMed:18025465 + PubMed:6893271 + RESID:AA0199 + + + + + (2R,3R)-2-amino-3-hydroxybutanoic acid + + + + + + D-Thr + + + + + + D-threonine + + + + + + MOD_RES D-threonine + + + + + + + + + + + + A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-histidino diiron disulfide. + 171.78 + C 0 Fe 2 H -4 N 0 O 0 S 2 + 171.78381 + 2- + C 15 Fe 2 H 18 N 6 O 4 S 5 + 618.34 + 617.8703 + C, C, C, H + natural + CDGSH domain iron-sulfur cluster + METAL Iron-sulfur (2Fe-2S) + METAL Iron-sulfur (2Fe-2S); via pros nitrogen + di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-N3'-histidinoiron) + tris-L-cysteinyl L-histidino diiron disulfide + PSI-MOD + MOD:00864 + Cross-link 4. + tris-L-cysteinyl L-histidino diiron disulfide + + + + + A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-histidino diiron disulfide. + PubMed:17766439 + PubMed:17766440 + RESID:AA0438 + + + + + CDGSH domain iron-sulfur cluster + + + + + + METAL Iron-sulfur (2Fe-2S) + + + + + + METAL Iron-sulfur (2Fe-2S); via pros nitrogen + + + + + + di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-N3'-histidinoiron) + + + + + + tris-L-cysteinyl L-histidino diiron disulfide + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to N-aspartyl-glycosylsphingolipidinositolethanolamine. + 123.05 + C 2 H 6 N 1 O 3 P 1 + 123.00853 + C 6 H 12 N 2 O 7 P 1 + 255.14 + 255.03821 + D + hypothetical + C-term + uniprot.ptm:PTM-0322 + GSIAsp + LIPID GPI-like-anchor amidated aspartate + N-aspartyl-glycosylsphingolipidinositolethanolamine + PSI-MOD + MOD:00865 + N-aspartyl-glycosylsphingolipidinositolethanolamine + + + + + A protein modification that effectively converts an L-aspartic acid residue to N-aspartyl-glycosylsphingolipidinositolethanolamine. + RESID:AA0439 + + + + + GSIAsp + + + + + + LIPID GPI-like-anchor amidated aspartate + + + + + + N-aspartyl-glycosylsphingolipidinositolethanolamine + + + + + + + + + + + A protein modification that effectively converts an L-proline residue to one of several dihydroxylated proline residues, such as (2S,3R,4R)-3,4-dihydroxyproline or (2S,3R,4S)-3,4-dihydroxyproline. + 32.0 + C 0 H 0 N 0 O 2 + 31.989828 + C 5 H 7 N 1 O 3 + 129.12 + 129.04259 + P + natural + uniprot.ptm:PTM-0024 + Hy2Pro + PSI-MOD + MOD:00866 + dihydroxylated proline + + + + + A protein modification that effectively converts an L-proline residue to one of several dihydroxylated proline residues, such as (2S,3R,4R)-3,4-dihydroxyproline or (2S,3R,4S)-3,4-dihydroxyproline. + PubMed:18688235 + + + + + Hy2Pro + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-cysteine converted to an L-selenocysteine residue to form L-cysteinyl-L-selenocystine. + 44.9 + C 0 H -2 N 0 O 0 S -1 Se 1 + 45.9288 + C 6 H 8 N 2 O 2 S 1 Se 1 + 251.17 + 251.94717 + C, C + natural + (R,R)-2-amino-3-[3-(2-aminopropanoic acid)sulfanyl]selanylpropanoic acid + CROSSLNK Cysteinyl-selenocysteine (Cys-Sec) + CROSSLNK Cysteinyl-selenocysteine (Sec-Cys) + L-cysteinyl-L-selenocysteine + PSI-MOD + MOD:00867 + Cross-link 2. + L-cysteinyl-L-selenocysteine (Cys-Cys) + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-cysteine converted to an L-selenocysteine residue to form L-cysteinyl-L-selenocystine. + PubMed:10801974 + PubMed:12911312 + PubMed:17177418 + RESID:AA0358#CYS + + + + + (R,R)-2-amino-3-[3-(2-aminopropanoic acid)sulfanyl]selanylpropanoic acid + + + + + + CROSSLNK Cysteinyl-selenocysteine (Cys-Sec) + + + + + + CROSSLNK Cysteinyl-selenocysteine (Sec-Cys) + + + + + + L-cysteinyl-L-selenocysteine + + + + + + + + + + A protein modification that inserts or replaces a residue with a natural, non-standard encoded residue, such as N-formyl-L-methionine, L-selenocysteine, or L-pyrrolysine. + X + natural + PSI-MOD + MOD:00868 + + These are produced exclusively by modification of amino acids acylated to special tRNA before incorporation by ribosomes into proteins. For this reason, they have also been referred to as pre-translational modifications. + natural, non-standard encoded residue + + + + + A protein modification that inserts or replaces a residue with a natural, non-standard encoded residue, such as N-formyl-L-methionine, L-selenocysteine, or L-pyrrolysine. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-alanine. + -44.01 + C -1 H 0 N 0 O -2 + -43.98983 + C 3 H 5 N 1 O 1 + 71.08 + 71.03712 + D + natural + uniprot.ptm:PTM-0314 + (2S)-2-aminopropanoic acid + 2-aminopropionic acid + 2-azanylpropanoic acid + Asp(Ala) + L-alanine + MOD_RES Beta-decarboxylated aspartate + alpha-alanine + alpha-aminopropionic acid + PSI-MOD + MOD:00869 + This has been reported to occur by a natural process of beta-decarboxylation. + L-alanine residue (Asp) + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-alanine. + PubMed:17138938 + RESID:AA0001#ASP + + + + + (2S)-2-aminopropanoic acid + + + + + + 2-aminopropionic acid + + + + + + 2-azanylpropanoic acid + + + + + + Asp(Ala) + + + + + + L-alanine + + + + + + MOD_RES Beta-decarboxylated aspartate + + + + + + alpha-alanine + + + + + + alpha-aminopropionic acid + + + + + + + + + + A protein modification produced by formation of an adduct with phenyl isocyanate. + 119.12 + C 7 H 5 N 1 O 1 + 119.03712 + X + artifact + N-term + Unimod:411 + PSI-MOD + Phenylisocyanate + phenyl isocyanate + MOD:00870 + + From Unimod with no citation. + phenyl isocyanate derivatized residue + + + + + A protein modification produced by formation of an adduct with phenyl isocyanate. + Unimod:411 + + + + + Phenylisocyanate + + + + + + phenyl isocyanate + + + + + + + + + + + + + + + + A protein modification produced by formation of an adduct with (2)H5-phenyl isocyanate. + 124.07 + C 7 (2)H 5 N 1 O 1 + 124.0685 + X + artifact + N-term + Unimod:412 + PSI-MOD + Phenylisocyanate:2H(5) + d5-phenyl isocyanate + MOD:00871 + + From Unimod with no citation. + (2)H5-phenyl isocyanate derivatized residue + + + + + A protein modification produced by formation of an adduct with (2)H5-phenyl isocyanate. + Unimod:412 + + + + + Phenylisocyanate:2H(5) + + + + + + d5-phenyl isocyanate + + + + + + + + + OBSOLETE because redundant and identical to MOD:01970. Remap to MOD:01970. + MOD:01970 + 129.12 + C 5 H 7 N 1 O 3 + 129.04259 + C 10 H 14 N 2 O 6 + 258.23 + 258.08517 + E + natural + Unimod:450 + N alpha -(gamma-Glutamyl)-Glu + PSI-MOD + Glu + monoglutamyl + MOD:00872 + L-isoglutamyl monoglutamic acid + true + + + + + OBSOLETE because redundant and identical to MOD:01970. Remap to MOD:01970. + PubMed:10747868 + PubMed:15525938 + PubMed:1680872 + RESID:AA0202#var + Unimod:450 + + + + + N alpha -(gamma-Glutamyl)-Glu + + + + + + Glu + + + + + + monoglutamyl + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamic acid, forming an isopeptide bond with a diglutamic acid. + 258.23 + C 10 H 14 N 2 O 6 + 258.08517 + C 15 H 21 N 3 O 9 + 387.35 + 387.12778 + E + natural + Unimod:451 + PSI-MOD + GluGlu + diglutamyl + MOD:00873 + L-isoglutamyl diglutamic acid + + + + + A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamic acid, forming an isopeptide bond with a diglutamic acid. + DeltaMass:0 + PubMed:10747868 + PubMed:1680872 + RESID:AA0202#var + Unimod:451 + + + + + GluGlu + + + + + + diglutamyl + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamyl-glutamic acid, forming an isopeptide bond with a triglutamic acid. + 387.35 + C 15 H 21 N 3 O 9 + 387.12778 + C 20 H 28 N 4 O 12 + 516.46 + 516.17035 + E + natural + Unimod:452 + N alpha -(gamma-Glutamyl)-Glu3 + PSI-MOD + GluGluGlu + triglutamyl + MOD:00874 + From DeltaMass: Average Mass: 388. + L-isoglutamyl triglutamic acid + + + + + A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamyl-glutamic acid, forming an isopeptide bond with a triglutamic acid. + DeltaMass:0 + PubMed:10747868 + PubMed:1680872 + RESID:AA0202#var + Unimod:452 + + + + + N alpha -(gamma-Glutamyl)-Glu3 + + + + + + GluGluGlu + + + + + + triglutamyl + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamyl-glutamyl-glutamic acid, forming an isopeptide bond with a tetraglutamic acid. + 516.46 + C 20 H 28 N 4 O 12 + 516.17035 + C 25 H 35 N 5 O 15 + 645.57 + 645.21295 + E + natural + Unimod:453 + PSI-MOD + GluGluGluGlu + tetraglutamyl + MOD:00875 + L-isoglutamyl tetraglutamic acid + + + + + A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamyl-glutamyl-glutamic acid, forming an isopeptide bond with a tetraglutamic acid. + PubMed:10747868 + PubMed:1680872 + RESID:AA0202#var + Unimod:453 + + + + + GluGluGluGlu + + + + + + tetraglutamyl + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexosamine sugar group through a glycosidic bond. + 161.16 + C 6 H 11 N 1 O 4 + 161.0688 + X + natural + Unimod:454 + Hexosamines (GalN, GlcN) + PSI-MOD + HexN + Hexosamine + MOD:00876 + hexosaminylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexosamine sugar group through a glycosidic bond. + Unimod:454 + + + + + Hexosamines (GalN, GlcN) + + + + + + HexN + + + + + + Hexosamine + + + + + + + + + + dimethyl pimelimidate modification from Unimod + 154.21 + C 8 H 14 N 2 O 1 + 154.11061 + X + artifact + Unimod:455 + PSI-MOD + One end of crosslink attached, one end free + Xlink:DMP-s + MOD:00877 + imidoester crosslink dimethyl pimelimidate singly attached + + + + + dimethyl pimelimidate modification from Unimod + URL:http://www.piercenet.com/files/0668ss5.pdf + Unimod:455 + + + + + One end of crosslink attached, one end free + + + + + + Xlink:DMP-s + + + + + + + + + + dimethyl pimelimidate modification from Unimod - Mechanism of the reaction of imidoesters with amines + 122.17 + C 7 H 10 N 2 + 122.0844 + X + artifact + Unimod:456 + PSI-MOD + Both ends of crosslink attached to same peptide + Xlink:DMP + MOD:00878 + imidoester crosslink dimethyl pimelimidate doubly attached + + + + + dimethyl pimelimidate modification from Unimod - Mechanism of the reaction of imidoesters with amines + PubMed:7171546 + URL:http://dx.doi.org/10.1021/ja00877a017 + Unimod:456 + + + + + Both ends of crosslink attached to same peptide + + + + + + Xlink:DMP + + + + + + + + + + modification from Unimod + 175.19 + C 13 H 5 N 1 + 175.0422 + X + artifact + Unimod:457 + PSI-MOD + NDA + naphthalene-2,3-dicarboxaldehyde + MOD:00879 + naphthalene-2,3-dicarboxaldehyde + + + + + modification from Unimod + PubMed:2081203 + Unimod:457 + + + + + NDA + + + + + + naphthalene-2,3-dicarboxaldehyde + + + + + + + + + + + + + + + + A protein modification produced by formation of an adduct with 6x(13)C labeled 4-sulfophenyl isothiocyanate. + 220.99 + (12)C 1 (13)C 6 H 5 N 1 O 3 S 2 + 220.99121 + X + artifact + Unimod:464 + PSI-MOD + 4-sulfophenyl isothiocyanate (Heavy C13) + SPITC:13C(6) + MOD:00880 + 6x(13)C labeled 4-sulfophenyl isothiocyanate derivatized residue + + + + + A protein modification produced by formation of an adduct with 6x(13)C labeled 4-sulfophenyl isothiocyanate. + PubMed:15536630 + PubMed:16526082 + Unimod:464 + + + + + 4-sulfophenyl isothiocyanate (Heavy C13) + + + + + + SPITC:13C(6) + + + + + + + + + OBSOLETE because Unimod entry 465 megerd with 199. Remap to MOD:00552 DiMethyl-CH2D. + MOD:00552 + 32.06 + C 2 (2)H 4 + 32.056408 + X + artifact + Unimod:465 + PSI-MOD + MOD:00881 + N-reductive amination-D + true + + + + + OBSOLETE because Unimod entry 465 megerd with 199. Remap to MOD:00552 DiMethyl-CH2D. + PubMed:9252331 + Unimod:465 + + + + + + + + + A protein modification that effectively converts an L-serine residue to S-(2-aminoethyl)cysteine. + 59.13 + C 2 H 5 N 1 O -1 S 1 + 59.019356 + C 5 H 10 N 2 O 1 S 1 + 146.21 + 146.05139 + S + artifact + Unimod:472 + Aminoethyl Cysteinyl (AECys) + PSI-MOD + AEC-MAEC + aminoethylcysteine + MOD:00882 + From DeltaMass: Average Mass: 146 Abbreviation:-AECys_ Formula:C5H10O2N1S1 Monoisotopic Mass Change:146.051 Average Mass Change:146.214 References:PE Sciex. + S-(2-aminoethyl)cysteine (Ser) + + + + + A protein modification that effectively converts an L-serine residue to S-(2-aminoethyl)cysteine. + DeltaMass:171 + PubMed:12923550 + Unimod:472#S + + + + + Aminoethyl Cysteinyl (AECys) + + + + + + AEC-MAEC + + + + + + aminoethylcysteine + + + + + + + + + + A protein modification that effectively replaces a 1-carboxyl group (usually referred to as the alpha-carboxyl) with a carboxamido group. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + X + natural + C-term + Unimod:2 + Amide formation (C terminus) + ResN + alpha-amidated residue + ctermamide + PSI-MOD + Amidated + Amidation + MOD:00883 + + The normal biological process involves formation of an amide of an amino acid residue in a peptide sequence where it is followed by a glycine and two basic residues, either arginine or lysine, although in some taxa only one basic residue is required. The peptide is cleaved after the basic residues, glycine is oxidized to hydroxyglycine, which decomposes to release a carboxamide C-terminal [JSG]. + C1-amidated residue + + + + + A protein modification that effectively replaces a 1-carboxyl group (usually referred to as the alpha-carboxyl) with a carboxamido group. + DeltaMass:0 + OMSSA:25 + Unimod:2 + + + + + Amide formation (C terminus) + + + + + + ResN + + + + + + alpha-amidated residue + + + + + + ctermamide + + + + + + Amidated + + + + + + Amidation + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-2-aminoethylcysteine. + 43.07 + C 2 H 5 N 1 O 0 S 0 + 43.0422 + C 5 H 10 N 2 O 1 S 1 + 146.21 + 146.05139 + C + artifact + 4-thialysine + L-cysteine aziridine adduct + S-(2-aminoethyl)-L-cysteine + PSI-MOD + MOD:00884 + + This modified residue is a chemical isolog of L-lysine for trypsin hydolysis produced from L-cysteine by aziridine. + S-aminoethylcysteine (Cys) + + + + + A protein modification that effectively converts an L-cysteine residue to S-2-aminoethylcysteine. + PubMed:1175632 + PubMed:18688235 + + + + + 4-thialysine + + + + + + L-cysteine aziridine adduct + + + + + + S-(2-aminoethyl)-L-cysteine + + + + + + + + + + A protein modification that crosslinks two residues by formation of an ester bond. + PSI-MOD + MOD:00885 + ester crosslinked residues + + + + + A protein modification that crosslinks two residues by formation of an ester bond. + PubMed:18688235 + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to 6'-chloro-L-tryptophan. + 34.44 + C 0 Cl 1 H -1 N 0 O 0 + 33.96103 + C 11 Cl 1 H 9 N 2 O 1 + 220.66 + 220.04034 + W + natural + Unimod:936 + uniprot.ptm:PTM-0052 + (2S)-2-amino-3-(6-chloro-1H-indol-3-yl)propanoic acid + 6'-ClTrp + 6'-chloro-L-tryptophan + MOD_RES 6'-chlorotryptophan + PSI-MOD + MOD:00886 + The Unimod:340 cross-reference to RESID:AA0180 is incorrect. RESID:AA0180 should be cross-referenced by Unimod:936 [JSG]. + 6'-chloro-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to 6'-chloro-L-tryptophan. + PubMed:9033387 + RESID:AA0180 + Unimod:936#W + + + + + (2S)-2-amino-3-(6-chloro-1H-indol-3-yl)propanoic acid + + + + + + 6'-ClTrp + + + + + + 6'-chloro-L-tryptophan + + + + + + MOD_RES 6'-chlorotryptophan + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to a methylated aspartic acid, such as aspartic acid 4-methyl ester. + PSI-MOD + MOD:00887 + methylated aspartic acid + + + + + A protein modification that effectively converts an L-aspartic acid residue to a methylated aspartic acid, such as aspartic acid 4-methyl ester. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively converts an L-proline to an L-prolinium (protonated L-proline). + 1.01 + C 0 H 1 N 0 O 0 + 1.007276 + 1+ + C 5 H 9 N 1 O 1 + 99.13 + 99.06786 + P + natural + N-term + PSI-MOD + MOD:00888 + + protonated L-proline (L-prolinium) residue + + + + + A protein modification that effectively converts an L-proline to an L-prolinium (protonated L-proline). + PubMed:18688235 + + + + + + + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-prolinium (charged L-proline) residue to N,N-dimethyl-L-proline. + 28.05 + C 2 H 4 N 0 O 0 + 28.030752 + 1+ + C 7 H 13 N 1 O 1 + 127.19 + 127.09917 + MOD:00888 + natural + N-term + Unimod:36 + PSI-MOD + MOD:00889 + + N,N-dimethyl-L-proline (from L-prolinium) + + + + + A protein modification that effectively converts an L-prolinium (charged L-proline) residue to N,N-dimethyl-L-proline. + Unimod:36#P + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to a phosphorylated L-histidine, such as pros-phosphohistidine, or tele-phosphohistidine. + 79.98 + C 0 H 1 N 0 O 3 P 1 + 79.96633 + C 6 H 8 N 3 O 4 P 1 + 217.12 + 217.02524 + H + natural + Unimod:21 + uniprot.ptm:PTM-0252 + NPhosHis + mod192 + phosphohistidine + PSI-MOD + Phospho + MOD:00890 + + phosphorylated L-histidine + + + + + A protein modification that effectively converts an L-histidine residue to a phosphorylated L-histidine, such as pros-phosphohistidine, or tele-phosphohistidine. + OMSSA:192 + Unimod:21#H + + + + + NPhosHis + + + + + + mod192 + + + + + + phosphohistidine + + + + + + Phospho + + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to D-serine. + C 3 H 5 N 1 O 2 + 87.08 + 87.03203 + X + natural + (R)-2-amino-3-hydroxypropanoic acid + D-Ser + D-serine + PSI-MOD + MOD:00891 + D-serine + + + + + A protein modification that effectively converts a source amino acid residue to D-serine. + ChEBI:29998 + PubMed:6893271 + PubMed:7973665 + RESID:AA0195 + + + + + (R)-2-amino-3-hydroxypropanoic acid + + + + + + D-Ser + + + + + + D-serine + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to D-serine. + -16.06 + C 0 H 0 N 0 O 1 S -1 + -15.977156 + C 3 H 5 N 1 O 2 + 87.08 + 87.03203 + C + natural + uniprot.ptm:PTM-0309 + (R)-2-amino-3-hydroxypropanoic acid + D-serine + MOD_RES D-serine (Cys) + PSI-MOD + MOD:00892 + D-serine (Cys) + + + + + A protein modification that effectively converts an L-cysteine residue to D-serine. + PubMed:18025465 + PubMed:6893271 + RESID:AA0195#CYS + + + + + (R)-2-amino-3-hydroxypropanoic acid + + + + + + D-serine + + + + + + MOD_RES D-serine (Cys) + + + + + + + + + + Natural or modified residues with a mass of 128.0-128.1 Da. + PSI-MOD + MOD:00893 + + residues isobaric at 128.0-128.1 + + + + + Natural or modified residues with a mass of 128.0-128.1 Da. + PubMed:18688235 + + + + + + + + + + Natural or modified resiues with a mass of 128.058578 Da. + PSI-MOD + MOD:00894 + + residues isobaric at 128.058578 Da + + + + + Natural or modified resiues with a mass of 128.058578 Da. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively results from forming an adduct with a compound containing a flavin adenine dinucleotide (FAD) group. + 783.54 + C 27 H 31 N 9 O 15 P 2 + 783.1415 + X + natural + FADRes + PSI-MOD + MOD:00895 + + FAD modified residue + + + + + A protein modification that effectively results from forming an adduct with a compound containing a flavin adenine dinucleotide (FAD) group. + PubMed:18688235 + + + + + FADRes + + + + + + + + + + + A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group. + X + natural + FMNRes + PSI-MOD + MOD:00896 + + FMN modified residue + + + + + A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group. + PubMed:18688235 + + + + + FMNRes + + + + + + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to N-acetyl-S-archeol-L-cysteine. + 677.2 + C 45 H 88 N 0 O 3 S 0 + 676.67334 + C 48 H 93 N 1 O 4 S 1 + 780.34 + 779.68256 + C + natural + N-term + PSI-MOD + MOD:00897 + N-acetyl-S-archeol-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to N-acetyl-S-archeol-L-cysteine. + RESID:AA0043#var + RESID:AA0223#var + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine. + 576.95 + C 37 H 68 N 0 O 4 S 0 + 576.5118 + C 40 H 73 N 1 O 5 S 1 + 680.09 + 679.52094 + C + natural + Unimod:377 + PSI-MOD + Diacylglycerol + diacylglycerol + MOD:00898 + Incidental to RESID:AA0060. + S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine. + PubMed:10896212 + PubMed:4575979 + PubMed:9056182 + RESID:AA0107#var + Unimod:377 + + + + + Diacylglycerol + + + + + + diacylglycerol + + + + + + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-diacylglycerol-L-cysteine. + C + natural + N-term + PSI-MOD + MOD:00899 + N-palmitoyl-S-diacylglycerol-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-diacylglycerol-L-cysteine. + RESID:AA0069#var + RESID:AA0107#var + + + + + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine. + 815.36 + C 53 H 98 N 0 O 5 S 0 + 814.74146 + C 56 H 103 N 1 O 6 S 1 + 918.5 + 917.7506 + C + natural + N-term + (R)-2-hexadecanoylamino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]sulfanylpropanoic acid + 2-hexadecanoylamino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]thiopropanoic acid + PSI-MOD + MOD:00900 + N-palmitoyl-S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine. + PubMed:18688235 + + + + + (R)-2-hexadecanoylamino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]sulfanylpropanoic acid + + + + + + 2-hexadecanoylamino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]thiopropanoic acid + + + + + + + + + + A protein modification that modifies an L-alanine. + A + ModAla + PSI-MOD + MOD:00901 + + modified L-alanine residue + + + + + A protein modification that modifies an L-alanine. + PubMed:18688235 + + + + + ModAla + + + + + + + + + + A protein modification that modifies an L-arginine residue. + R + ModArg + PSI-MOD + MOD:00902 + + modified L-arginine residue + + + + + A protein modification that modifies an L-arginine residue. + PubMed:18688235 + + + + + ModArg + + + + + + + + + + A protein modification that modifies an L-asparagine residue. + N + ModAsn + PSI-MOD + MOD:00903 + + modified L-asparagine residue + + + + + A protein modification that modifies an L-asparagine residue. + PubMed:18688235 + + + + + ModAsn + + + + + + + + + + A protein modification that modifies an L-aspartic acid residue. + D + ModAsp + PSI-MOD + MOD:00904 + + modified L-aspartic acid residue + + + + + A protein modification that modifies an L-aspartic acid residue. + PubMed:18688235 + + + + + ModAsp + + + + + + + + + + A protein modification that modifies an L-cysteine residue. + C + ModCys + PSI-MOD + MOD:00905 + + modified L-cysteine residue + + + + + A protein modification that modifies an L-cysteine residue. + PubMed:18688235 + + + + + ModCys + + + + + + + + + + A protein modification that modifies an L-glutamic acid residue. + E + ModGlu + PSI-MOD + MOD:00906 + + modified L-glutamic acid residue + + + + + A protein modification that modifies an L-glutamic acid residue. + PubMed:18688235 + + + + + ModGlu + + + + + + + + + + A protein modification that modifies an L-glutamine residue. + Q + ModGln + PSI-MOD + MOD:00907 + + modified L-glutamine residue + + + + + A protein modification that modifies an L-glutamine residue. + PubMed:18688235 + + + + + ModGln + + + + + + + + + + A protein modification that modifies a glycine residue. + G + ModGly + PSI-MOD + MOD:00908 + + modified glycine residue + + + + + A protein modification that modifies a glycine residue. + PubMed:18688235 + + + + + ModGly + + + + + + + + + + A protein modification that modifies an L-histidine residue. + H + ModHis + PSI-MOD + MOD:00909 + + modified L-histidine residue + + + + + A protein modification that modifies an L-histidine residue. + PubMed:18688235 + + + + + ModHis + + + + + + + + + + A protein modification that modifies an L-isoleucine residue. + I + ModIle + PSI-MOD + MOD:00910 + + modified L-isoleucine residue + + + + + A protein modification that modifies an L-isoleucine residue. + PubMed:18688235 + + + + + ModIle + + + + + + + + + + A protein modification that modifies an L-leucine residue. + L + ModLeu + PSI-MOD + MOD:00911 + + modified L-leucine residue + + + + + A protein modification that modifies an L-leucine residue. + PubMed:18688235 + + + + + ModLeu + + + + + + + + + + A protein modification that modifies an L-lysine residue. + K + ModLys + PSI-MOD + MOD:00912 + + modified L-lysine residue + + + + + A protein modification that modifies an L-lysine residue. + PubMed:18688235 + + + + + ModLys + + + + + + + + + + A protein modification that modifies an L-methionine residue. + M + ModMet + PSI-MOD + MOD:00913 + + modified L-methionine residue + + + + + A protein modification that modifies an L-methionine residue. + PubMed:18688235 + + + + + ModMet + + + + + + + + + + A protein modification that modifies an L-phenylalanine residue. + F + ModPhe + PSI-MOD + MOD:00914 + + modified L-phenylalanine residue + + + + + A protein modification that modifies an L-phenylalanine residue. + PubMed:18688235 + + + + + ModPhe + + + + + + + + + + A protein modification that modifies an L-proline residue. + P + ModPro + PSI-MOD + MOD:00915 + + modified L-proline residue + + + + + A protein modification that modifies an L-proline residue. + PubMed:18688235 + + + + + ModPro + + + + + + + + + + A protein modification that modifies an L-serine residue. + S + ModSer + PSI-MOD + MOD:00916 + + modified L-serine residue + + + + + A protein modification that modifies an L-serine residue. + PubMed:18688235 + + + + + ModSer + + + + + + + + + + A protein modification that modifies an L-threonine residue. + T + ModThr + PSI-MOD + MOD:00917 + + modified L-threonine residue + + + + + A protein modification that modifies an L-threonine residue. + PubMed:18688235 + + + + + ModThr + + + + + + + + + + A protein modification that modifies an L-tryptophan residue. + W + ModTrp + PSI-MOD + MOD:00918 + + modified L-tryptophan residue + + + + + A protein modification that modifies an L-tryptophan residue. + PubMed:18688235 + + + + + ModTrp + + + + + + + + + + A protein modification that modifies an L-tyrosine residue. + Y + ModTyr + PSI-MOD + MOD:00919 + + modified L-tyrosine residue + + + + + A protein modification that modifies an L-tyrosine residue. + PubMed:18688235 + + + + + ModTyr + + + + + + + + + + A protein modification that modifies an L-valine residue. + V + ModVal + PSI-MOD + MOD:00920 + + modified L-valine residue + + + + + A protein modification that modifies an L-valine residue. + PubMed:18688235 + + + + + ModVal + + + + + + + + + New uncategorized Unimod. OBSOLETE because organizational use is no longer required. + PSI-MOD + MOD:00921 + new uncategorized Unimod entries + true + + + + + New uncategorized Unimod. OBSOLETE because organizational use is no longer required. + PubMed:18688235 + + + + + + + + + + modification from Unimod Chemical derivative + 672.84 + C 37 H 44 N 4 O 6 S 1 + 672.29816 + C 40 H 49 N 5 O 7 S 2 + 775.98 + 775.3073 + C + artifact + Unimod:494 + PSI-MOD + Cy3 CyDye DIGE Fluor saturation dye + CyDye-Cy3 + MOD:00922 + Cy3 CyDye DIGE Fluor saturation dye + + + + + modification from Unimod Chemical derivative + Unimod:494 + + + + + Cy3 CyDye DIGE Fluor saturation dye + + + + + + CyDye-Cy3 + + + + + + + + + + + modification from Unimod Chemical derivative + 684.85 + C 38 H 44 N 4 O 6 S 1 + 684.29816 + C 41 H 49 N 5 O 7 S 2 + 787.99 + 787.3073 + C + artifact + Unimod:495 + PSI-MOD + Cy5 CyDye DIGE Fluor saturation dye + CyDye-Cy5 + MOD:00923 + Cy5 CyDye DIGE Fluor saturation dye + + + + + modification from Unimod Chemical derivative + Unimod:495 + + + + + Cy5 CyDye DIGE Fluor saturation dye + + + + + + CyDye-Cy5 + + + + + + + + + + + + + + A protein modification that effectively crosslinks an L-lysine residue and an L-threonine residue by an isopeptide bond to form N6-(L-threonyl)-L-lysine. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 10 H 18 N 3 O 3 + 228.27 + 228.13481 + K, T + natural + C-term + uniprot.ptm:PTM-0326 + (2S)-2-amino-6-([(2S,3R)-2-amino-3-hydroxybutanoyl]amino)hexanoic acid + N6-(L-threonyl)-L-lysine + N6-threonyl-lysine + PSI-MOD + MOD:00924 + Cross-link 2. + N6-(L-threonyl)-L-lysine + + + + + A protein modification that effectively crosslinks an L-lysine residue and an L-threonine residue by an isopeptide bond to form N6-(L-threonyl)-L-lysine. + PubMed:18063774 + RESID:AA0440 + + + + + (2S)-2-amino-6-([(2S,3R)-2-amino-3-hydroxybutanoyl]amino)hexanoic acid + + + + + + N6-(L-threonyl)-L-lysine + + + + + + N6-threonyl-lysine + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a heptose sugar group through a glycosidic bond. + 192.17 + C 7 H 12 O 6 + 192.06339 + X + natural + Unimod:490 + PSI-MOD + Hep + Heptose + MOD:00925 + From Unimod with no citation [JSG]. + heptosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a heptose sugar group through a glycosidic bond. + Unimod:490 + + + + + Hep + + + + + + Heptose + + + + + + + + + Modification from Unimod Non-standard residue. OBSOLETE because not an amino acid modification. From Unimod not an approved entry. + 340.42 + C 21 H 24 O 4 + 340.16745 + X + artifact + Unimod:493 + PSI-MOD + BADGE + Bisphenol A diglycidyl ether derivative + MOD:00926 + Bisphenol A diglycidyl ether derivative + true + + + + + Modification from Unimod Non-standard residue. OBSOLETE because not an amino acid modification. From Unimod not an approved entry. + PubMed:11225353 + Unimod:493 + + + + + BADGE + + + + + + Bisphenol A diglycidyl ether derivative + + + + + + + + + + + A protein modification that effectively replaces two hydrogen atoms of a residue containing common isotopes with two (13)C,3x(2)H labeled methyl groups to form a 2x(13)C,6x(2)H labeled dimethylated residue. + 34.06 + (13)C 2 (2)H 4 + 34.063118 + X + artifact + Unimod:510 + PSI-MOD + DiMethyl-C13HD2 + Dimethyl:2H(4)13C(2) + MOD:00927 + 2x(13)C,4x(2)H labeled dimethylated residue + + + + + A protein modification that effectively replaces two hydrogen atoms of a residue containing common isotopes with two (13)C,3x(2)H labeled methyl groups to form a 2x(13)C,6x(2)H labeled dimethylated residue. + PubMed:16335955 + PubMed:3802193 + Unimod:510 + + + + + DiMethyl-C13HD2 + + + + + + Dimethyl:2H(4)13C(2) + + + + + + + + + + modification from Unimod Chemical derivative + 227.39 + C 14 H 29 N 1 O 1 + 227.22491 + X + artifact + Unimod:513 + PSI-MOD + C8-QAT + [3-(2,5)-Dioxopyrrolidin-1-yloxycarbonyl)-propyl]dimethyloctylammonium + MOD:00928 + Should have children for K and X-N-term [JSG]. + [3-(2,5)-dioxopyrrolidin-1-yloxycarbonyl)-propyl]dimethyloctylammonium + + + + + modification from Unimod Chemical derivative + PubMed:16771548 + Unimod:513 + + + + + C8-QAT + + + + + + [3-(2,5)-Dioxopyrrolidin-1-yloxycarbonyl)-propyl]dimethyloctylammonium + + + + + + + + + + + A modification produced in a non-enzymatic reaction between a lactose carbonyl group and an L-lysine to form a Schiff-base or an Amadori ketosamine lysine adduct. + 342.3 + C 12 H 22 O 11 + 342.1162 + C 18 H 34 N 2 O 12 + 470.47 + 470.21118 + K + natural + Unimod:512 + uniprot.ptm:PTM-0511 + CARBOHYD N-linked (Lac) (glycation) lysine + PSI-MOD + Hex(2) + Lactosylation + MOD:00929 + The term lactosylation used with this meaning is a misnomer [JSG]. + lactose glycated lysine + + + + + A modification produced in a non-enzymatic reaction between a lactose carbonyl group and an L-lysine to form a Schiff-base or an Amadori ketosamine lysine adduct. + PubMed:9606156 + Unimod:512 + + + + + CARBOHYD N-linked (Lac) (glycation) lysine + + + + + + Hex(2) + + + + + + Lactosylation + + + + + + + + + + + tyrosine adduct with substrate analog inhibitor 1,2-dideoxy-2'-methyl-alpha-D-glucopyranoso-[2,1-d]-Delta2'-thiazoline. + 232.27 + C 9 H 14 N 1 O 4 S 1 + 232.06436 + C 18 H 23 N 2 O 6 S 1 + 395.45 + 395.1277 + Y + artifact + Unimod:514 + PSI-MOD + MOD:00930 + propyl-NAG tyrosine adduct + + + + + tyrosine adduct with substrate analog inhibitor 1,2-dideoxy-2'-methyl-alpha-D-glucopyranoso-[2,1-d]-Delta2'-thiazoline. + PubMed:15795231 + Unimod:514 + + + + + + + + + modification from Unimod Other - BHTOH is formed upon metabolism of BHT with P450 enzymes. The BHTOH is further metabolized to its quinone methide (electrophile) which reacts with -SH and -NH2 groups + 234.34 + C 15 H 22 O 2 + 234.16199 + X + artifact + Unimod:498 + PSI-MOD + BHTOH + Michael addition of t-butyl hydroxylated BHT (BHTOH) to C, H or K + MOD:00931 + Michael addition of t-butyl hydroxylated BHT (BHTOH) to C, H or K + + + + + modification from Unimod Other - BHTOH is formed upon metabolism of BHT with P450 enzymes. The BHTOH is further metabolized to its quinone methide (electrophile) which reacts with -SH and -NH2 groups + PubMed:11085420 + Unimod:498 + + + + + BHTOH + + + + + + Michael addition of t-butyl hydroxylated BHT (BHTOH) to C, H or K + + + + + + + + + + + modification from Unimod Isotopic label + 298.02 + Br 1 (12)C 10 (13)C 2 H 13 N 2 O 2 + 298.02274 + Br 1 (12)C 13 (13)C 2 H 18 N 3 O 3 S 1 + 401.03 + 401.03192 + C + artifact + Unimod:499 + PSI-MOD + Heavy IDBEST tag for quantitation + IGBP:13C(2) + MOD:00932 + IDBEST tag for quantitation + + + + + modification from Unimod Isotopic label + PubMed:11821862 + Unimod:499 + + + + + Heavy IDBEST tag for quantitation + + + + + + IGBP:13C(2) + + + + + + + + + + + modification from Unimod Chemical derivative - 5-hydro-5-methylimidazol-4-one, arginine methylglyoxal arginine adduct (+54 amu) + 54.05 + C 3 H 2 O 1 + 54.010567 + C 9 H 14 N 4 O 2 + 210.24 + 210.11168 + R + artifact + Unimod:319 + PSI-MOD + Delta:H(2)C(3)O(1) + MDA adduct +54 + MOD:00933 + Ref. Uchida K, Sakai K, Itakura K, Osawa T, Toyokuni S. 1977. Protein modification by lipid peroxidation products: formation of malondialdehyde-derived N(epsilon)-(2-propenol)lysine in proteins. Arch Biochem Biophys. 346(1):45-52. + methylglyoxal arginine adduct (+54 amu) + + + + + modification from Unimod Chemical derivative - 5-hydro-5-methylimidazol-4-one, arginine methylglyoxal arginine adduct (+54 amu) + Unimod:319#R + + + + + Delta:H(2)C(3)O(1) + + + + + + MDA adduct +54 + + + + + + + + + + + modification from Unimod Post-translational + 306.4 + C 19 H 26 N -2 O 5 + 306.17188 + C 25 H 38 N 2 O 6 + 462.59 + 462.27298 + R + natural + Unimod:506 + PSI-MOD + LG-Hlactam-R + Levuglandinyl - arginine hydroxylactam adduct + MOD:00934 + Levuglandinyl - arginine hydroxylactam adduct + + + + + modification from Unimod Post-translational + Unimod:506 + + + + + LG-Hlactam-R + + + + + + Levuglandinyl - arginine hydroxylactam adduct + + + + + + + + + + + Oxidation of methionine to methionine sulfoxide with neutral loss of CH3SOH. + -64.1 + C -1 H -4 N 0 O -1 S -1 + -63.998287 + C 4 H 5 N 1 O 1 S 0 + 83.09 + 83.03712 + M + artifact + PSI-MOD + MOD:00935 + Originally created from Unimod:507 that was later deleted. + methionine oxidation with neutral loss of 64 Da + + + + + Oxidation of methionine to methionine sulfoxide with neutral loss of CH3SOH. + PubMed:18688235 + PubMed:9004526 + + + + + + + + + modification from Unimod Post-translational + 348.44 + C 20 H 28 O 5 + 348.19366 + X + artifact + Unimod:504 + PSI-MOD + LG-Hlactam-K + Levuglandinyl - lysine hydroxylactam adduct + MOD:00936 + Levuglandinyl - hydroxylactam adduct, K and N-term + + + + + modification from Unimod Post-translational + Unimod:504 + + + + + LG-Hlactam-K + + + + + + Levuglandinyl - lysine hydroxylactam adduct + + + + + + + + + + + modification from Unimod Post-translational + 290.4 + C 19 H 26 N -2 O 4 + 290.17697 + C 25 H 38 N 2 O 5 + 446.59 + 446.27808 + R + artifact + Unimod:505 + PSI-MOD + LG-lactam-R + Levuglandinyl - arginine lactam adduct + MOD:00937 + Levuglandinyl - arginine lactam adduct + + + + + modification from Unimod Post-translational + Unimod:505 + + + + + LG-lactam-R + + + + + + Levuglandinyl - arginine lactam adduct + + + + + + + + + + modification from Unimod Post-translational + 332.44 + C 20 H 28 O 4 + 332.19876 + X + artifact + Unimod:503 + PSI-MOD + LG-lactam-K + Levuglandinyl - lysine lactam adduct + MOD:00938 + Levuglandinyl - lactam adduct, K and N-term + + + + + modification from Unimod Post-translational + PubMed:12590383 + Unimod:503 + + + + + LG-lactam-K + + + + + + Levuglandinyl - lysine lactam adduct + + + + + + + + + + + modification from Unimod Chemical derivative + 129.12 + C 5 H 7 N 1 O 3 + 129.04259 + C 8 H 12 N 2 O 4 S 1 + 232.25 + 232.05177 + C + artifact + Unimod:500 + PSI-MOD + Nmethylmaleimide+water + Nmethylmaleimidehydrolysis + MOD:00939 + hydrolyzed N-methylmaleimide cysteine adduct + + + + + modification from Unimod Chemical derivative + Unimod:500 + + + + + Nmethylmaleimide+water + + + + + + Nmethylmaleimidehydrolysis + + + + + + + + + + A protein modification produced by formation of an adduct with 3-methyl-2-pyridyl isocyanate. + 134.14 + C 7 H 6 N 2 O 1 + 134.04802 + X + artifact + N-term + Unimod:501 + PSI-MOD + 3-methyl-2-pyridyl isocyanate + PyMIC + MOD:00940 + 3-methyl-2-pyridyl isocyanate derivatized residue + + + + + A protein modification produced by formation of an adduct with 3-methyl-2-pyridyl isocyanate. + PubMed:11078590 + Unimod:501 + + + + + 3-methyl-2-pyridyl isocyanate + + + + + + PyMIC + + + + + + + + + + + modification from Unimod Chemical derivative + 118.16 + C 8 H 8 N 1 + 118.065674 + C 11 H 13 N 2 S 1 + 205.3 + 205.07994 + C + artifact + Unimod:488 + PSI-MOD + DHP + Dehydropyrrolizidine alkaloid (dehydroretronecine) on cysteines + MOD:00941 + dehydropyrrolizidine alkaloid (dehydroretronecine) derivatized cysteine + + + + + modification from Unimod Chemical derivative + PubMed:12175151 + Unimod:488 + + + + + DHP + + + + + + Dehydropyrrolizidine alkaloid (dehydroretronecine) on cysteines + + + + + + + + + + + A protein modification that effectively substitutes four (1)H protium atoms with four (2)H deuterium atoms to produce (4,4,5,5-(2)H4)-L-lysine. + 4.03 + (1)H -4 (2)H 4 + 4.025107 + C 6 (1)H 8 (2)H 4 N 2 O 1 + 132.12 + 132.12007 + K + artifact + Unimod:481 + 4,4,5,5-tetradeuterolysine + lys-2H4 + PSI-MOD + 4,4,5,5-D4 Lysine + Label:2H(4) + MOD:00942 + For SILAC experiments. + (4,4,5,5-(2)H4)-L-lysine + + + + + A protein modification that effectively substitutes four (1)H protium atoms with four (2)H deuterium atoms to produce (4,4,5,5-(2)H4)-L-lysine. + OMSSA:180 + Unimod:481 + + + + + 4,4,5,5-tetradeuterolysine + + + + + + lys-2H4 + + + + + + 4,4,5,5-D4 Lysine + + + + + + Label:2H(4) + + + + + + + + + + modification from Unimod Isotopic label + 128.19 + C 7 H 14 N 1 O 1 + 128.10754 + X + artifact + Unimod:476 + PSI-MOD + 4-trimethyllammoniumbutyryl- + TMAB + MOD:00943 + 4-trimethylammoniumbutanoyl derivatized residue + + + + + modification from Unimod Isotopic label + PubMed:12643539 + Unimod:476 + + + + + 4-trimethyllammoniumbutyryl- + + + + + + TMAB + + + + + + + + + + + + + + + + modification from Unimod Isotopic label + 137.16 + C 7 (1)H 5 (2)H 9 N 1 O 1 + 137.16403 + X + artifact + Unimod:477 + PSI-MOD + TMAB:2H(9) + d9-4-trimethyllammoniumbutyryl- + MOD:00944 + d9-4-trimethylammoniumbutanoyl derivatized residue + + + + + modification from Unimod Isotopic label + Unimod:477 + + + + + TMAB:2H(9) + + + + + + d9-4-trimethyllammoniumbutyryl- + + + + + + + + + OBSOLETE because redundant and identical to MOD:00626. Remap to MOD:00626. + MOD:00626 + 421.43 + C 21 H 15 N 3 O 5 S 1 + 421.07324 + S + artifact + PSI-MOD + MOD:00945 + fluorescein-5-thiosemicarbazide adduct + true + + + + + OBSOLETE because redundant and identical to MOD:00626. Remap to MOD:00626. + PubMed:18688235 + + + + + + + + + A protein modification that crosslinks two residues with a covalent bond and the loss of ammonia. + PSI-MOD + MOD:00946 + + crosslinked residues with loss of ammonia + + + + + A protein modification that crosslinks two residues with a covalent bond and the loss of ammonia. + PubMed:18688235 + + + + + + + + + Entries from DeltaMass see http://www.abrf.org/index.cfm/dm.home?AvgMass=all. + PSI-MOD + MOD:00947 + DeltaMass + + + + + Entries from DeltaMass see http://www.abrf.org/index.cfm/dm.home?AvgMass=all. + PubMed:18688235 + + + + + + + + OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass + X + PSI-MOD + MOD:00948 + From DeltaMass: Average Mass: -79 + 5'-dephospho + true + + + + + OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass + DeltaMass:0 + + + + + + + + OBSOLETE because redundant and identical to MOD:01933. Remap to MOD:01933. + MOD:01933 + K + PSI-MOD + MOD:00949 + From DeltaMass: Average Mass: -58 + desmosine + true + + + + + OBSOLETE because redundant and identical to MOD:01933. Remap to MOD:01933. + DeltaMass:0 + + + + + + + + OBSOLETE because this modification has not been seen/reported on since this original publication in 1994 and carboxymethylation of proteins is common enough for this mass shift to have been seen in the intervening 25+ years. modification from DeltaMass + M + PSI-MOD + MOD:00950 + From DeltaMass: Average Mass: -48 Average Mass Change:-48 References:Anal. Biochem. Vol 216 No.1 p141 + decomposed carboxymethylated methionine + true + + + + + OBSOLETE because this modification has not been seen/reported on since this original publication in 1994 and carboxymethylation of proteins is common enough for this mass shift to have been seen in the intervening 25+ years. modification from DeltaMass + DeltaMass:3 + + + + + + + + + + + Covalent modification of a peptide or protein L-glutamic acid residue to gamma-carboxyglutamic acid with secondary loss of a neutral carbon dioxide molecular fragment. + -44.01 + C -1 H 0 N 0 O -2 + -43.98983 + C 5 H 7 N 1 O 3 + 129.12 + 129.04259 + E + artifact + d4CbxGlu + PSI-MOD + MOD:00951 + From DeltaMass: Average Mass: -44 Formula:CO2 Average Mass Change:-44 References:Nakamura T, Yu Z, Fainzilber M, Burlingame AL. Protein Sci (1996) 5, 524-530 Mass spectrometric-based revision of the structure of a cysteine-rich peptide toxin with gamma-carboxyglutamic acid, TxVIIA, from the sea snail, Conus textile. Notes: The elimination of CO2 will regenerate glutamate as if there was no modification. However, peaks appearing with an interval of 44 is quite characteristic. It would be noteworthy to remind that loss of 44 from a gamma-carboxyglutamate-containing peptide may be observed not only as a result of spontaneous decarboxylation but also as an artifact under some ionization conditions such as negative ion mode MALDI. + L-gamma-carboxyglutamic acid with neutral loss of carbon dioxide + + + + + Covalent modification of a peptide or protein L-glutamic acid residue to gamma-carboxyglutamic acid with secondary loss of a neutral carbon dioxide molecular fragment. + DeltaMass:58 + + + + + d4CbxGlu + + + + + + + + + + + + A protein modification that crosslinks an aspartic acid and the following glycine residue with the formation of (2-aminosuccinimidyl)acetic acid and the loss of a water molecule. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 6 H 6 N 2 O 3 + 154.13 + 154.03784 + D, G + hypothetical + uniprot.ptm:PTM-0312 + (2-aminosuccinimidyl)acetic acid + (3-amino-2,5-dioxo-1-pyrrolidinyl)acetic acid + CROSSLNK (2-aminosuccinimidyl)acetic acid (Asp-Gly) + N-(2-aminosuccinyl)glycine + [(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]acetic acid + anhydroaspartyl glycine + aspartimide glycine + PSI-MOD + MOD:00952 + + Cross-link 2; this cross-link is formed by the condensation of an aspartic acid residue with the alpha-amido of the following residue. + (2-aminosuccinimidyl)acetic acid (Asp) + + + + + A protein modification that crosslinks an aspartic acid and the following glycine residue with the formation of (2-aminosuccinimidyl)acetic acid and the loss of a water molecule. + PubMed:10801322 + RESID:AA0441#ASP + + + + + (2-aminosuccinimidyl)acetic acid + + + + + + (3-amino-2,5-dioxo-1-pyrrolidinyl)acetic acid + + + + + + CROSSLNK (2-aminosuccinimidyl)acetic acid (Asp-Gly) + + + + + + N-(2-aminosuccinyl)glycine + + + + + + [(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]acetic acid + + + + + + anhydroaspartyl glycine + + + + + + aspartimide glycine + + + + + + + + + + + + A protein modification that effectively crosslinks an L-glutamic acid residue and an L-serine residue by an ester bond and releasing water to form O-(L-isoglutamyl)-L-serine. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 8 H 10 N 2 O 4 + 198.18 + 198.06406 + E, S + artifact + (2S)-2-amino-5-[(2S)-2-amino-2-carboxyethoxy]-5-oxopentanoic acid + CROSSLNK isoglutamyl serine ester (Ser-Glu) + O(beta)-(gamma-glutamyl)serine + O-(L-isoglutamyl)-L-serine + O-gamma-Glutamyl- (Crosslink to Serine) + O3-(isoglutamyl)-serine + PSI-MOD + MOD:00953 + Cross-link 2; From DeltaMass: with no citation. + O-(L-isoglutamyl)-L-serine (Glu-Ser) + + + + + A protein modification that effectively crosslinks an L-glutamic acid residue and an L-serine residue by an ester bond and releasing water to form O-(L-isoglutamyl)-L-serine. + DeltaMass:0 + PubMed:19035375 + RESID:AA0597#ESX + + + + + (2S)-2-amino-5-[(2S)-2-amino-2-carboxyethoxy]-5-oxopentanoic acid + + + + + + CROSSLNK isoglutamyl serine ester (Ser-Glu) + + + + + + O(beta)-(gamma-glutamyl)serine + + + + + + O-(L-isoglutamyl)-L-serine + + + + + + O-gamma-Glutamyl- (Crosslink to Serine) + + + + + + O3-(isoglutamyl)-serine + + + + + + + + + + A protein modification that crosslinks two residues with a covalent bond and the loss of water. + PSI-MOD + MOD:00954 + + crosslinked residues with loss of water + + + + + A protein modification that crosslinks two residues with a covalent bond and the loss of water. + PubMed:18688235 + + + + + + + + + + + A protein modification that effectively crosslinks an L-serine residue and an L-histidine residue to release water and form tele- or pros-(2-amino-2-carboxyethyl)histidine. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 9 H 10 N 4 O 2 + 206.2 + 206.08038 + H, S + artifact + beta-alaninohistidine + PSI-MOD + MOD:00955 + Cross-link 2; From DeltaMass with no citation or formula: Average Mass: -18. The DeltaMass description "Serine crosslinked to theta or pi carbon of Histidine" is incorrect. The histidine ring nitrogens (not carbons) are designated tele or N-tau (not theta), and pros or N-pi [JSG]. + alaninohistidine (serine crosslinked to tele or pros nitrogen of histidine) + + + + + A protein modification that effectively crosslinks an L-serine residue and an L-histidine residue to release water and form tele- or pros-(2-amino-2-carboxyethyl)histidine. + DeltaMass:0 + + + + + beta-alaninohistidine + + + + + + + + + + modification from DeltaMass + -18.03 + C 1 H 2 N 0 O 0 S -1 + -17.95642 + C 6 H 11 N 1 O 1 + 113.16 + 113.08406 + M + PSI-MOD + MOD:00956 + From DeltaMass: Average Mass: -18 Average Mass Change:-18 Notes: It has the same mass as leucine or isoleucine and can be charged on the methionyl t-RNA. This often happens in minimal media-prepared fermentations that are not supplemented with enough free methionine. It gives a mass change of -18 and can often be confused with dehydration. + misincorporation of norleucine for methionine + + + + + modification from DeltaMass + DeltaMass:10 + + + + + + + + + Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral carbon dioxide molecular fragment. + -44.01 + C -1 H 0 N 0 O -2 + -43.98983 + X + artifact + dCO2ModRes + PSI-MOD + MOD:00957 + modified residue with neutral loss of carbon dioxide + + + + + Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral carbon dioxide molecular fragment. + PubMed:18688235 + + + + + dCO2ModRes + + + + + + + + + + modification from DeltaMass + H, R + PSI-MOD + MOD:00958 + Cross-link 2; From DeltaMass: Average Mass: -5 + crosslink between Arg and His sidechains + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + modification from DeltaMass + Y, Y, Y, Y + PSI-MOD + MOD:00959 + Cross-link 4; From DeltaMass: Average Mass: -4 + 3,3',5,5'-TerTyr (Crosslink) + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + A protein modification that effectively replaces a carboxylic acid group with a hydrogen atom. + -44.01 + C -1 H 0 N 0 O -2 + -43.98983 + X + artifact + PSI-MOD + MOD:00960 + decarboxylated residue + + + + + A protein modification that effectively replaces a carboxylic acid group with a hydrogen atom. + PubMed:18688235 + + + + + + + + + + + + + + + + A protein modification that effectively reduces the disulfide bond of cystine to form two cysteine residues. + 2.02 + C 0 H 2 N 0 O 0 S 0 + 2.01565 + C 6 H 10 N 2 O 2 S 2 + 206.28 + 206.01837 + MOD:00034 + PSI-MOD + MOD:00961 + + Cross-link 2; this modification destroys the cross-link. From DeltaMass: Treatment of cystine (cys-cys) by reducing agents such as dithiothreitol (DTT) or triscarboxyethylphosphine (TCEP) results in cleavage of the disulphide bond and reduction of the sulphur atom of each molecule to create cysteine. + reduction of disulfide crosslink in cystine to two cysteines + + + + + A protein modification that effectively reduces the disulfide bond of cystine to form two cysteine residues. + DeltaMass:333 + + + + + + + + + + A protein modification that by reducing the indole ring system of tryptophan to indoline effectively converts an L-tryptophan residue to 2',3'-dihydrotryptophan. + 2.02 + C 0 H 2 N 0 O 0 S 0 + 2.01565 + C 11 H 12 N 2 O 1 + 188.23 + 188.09496 + W + artifact + PSI-MOD + MOD:00962 + From DeltaMass: References:1. Pearson,D.A., Blanchette,M., Baker,M.L. and Guindon,C.A. (1989) Trialkylsilanes as scavengers for the trifluoroacetic acid deblocking ofprotecting groups in peptide synthesis. Tetrahedron Lett., 30(21), 2739-2742 Notes: Reduction of indole double bond of Trp which occurs when triethylsilane (TES) is used as a scavenger and Trp is incorporated without protection of indole nitrogen [1]. This side reaction is likely to be accompanied by oxidation of indoline ring with formation of intensively colored peptide by-products. Triisopropylsilane (TIPS) does not give this side reaction. See structure at http://www.abrf.org/images/misc/dmass2.gif. [However, the pictured indoline structure is incorrect - JSG]. + 2',3'-dihydrotryptophan + + + + + A protein modification that by reducing the indole ring system of tryptophan to indoline effectively converts an L-tryptophan residue to 2',3'-dihydrotryptophan. + DeltaMass:343 + URL:http://dx.doi.org/10.1016/S0040-4039(00)99113-5 + + + + + + + + Modification from DeltaMass. OBSOLETE because redundant and identical to MOD:00462. Remap to MOD:00462. + MOD:00462 + W + artifact + PSI-MOD + MOD:00963 + From DeltaMass: Average Mass: 4 Monoisotopic Mass Change:3.995 Average Mass Change:3.989 References:Ruoppolo M, Amoresano A, Pucci P, Pascarella S, Polticelli F, Trovato M,Menegatti E, Ascenzi P.Characterization of five new low-molecular-mass trypsin inhibitors fromwhite mustard (Sinapis alba L.) seed.Eur J Biochem. 2000 267:6486-92. Notes: See structure at http://www.abrf.org/images/misc/dmass32.jpg. + Oxidation of Trp to kynurenine + true + + + + + Modification from DeltaMass. OBSOLETE because redundant and identical to MOD:00462. Remap to MOD:00462. + DeltaMass:357 + + + + + + + + + modification from DeltaMass + 12.01 + C 1 H 0 N 0 O 0 + 12.0 + C 7 H 12 N 2 O 1 + 140.19 + 140.09496 + K + artifact + N6-(methylidene)-lysine + PSI-MOD + MOD:00964 + From DeltaMass: Average Mass: 12 Average Mass Change: 12 References: Mathews, W. Rodney; Runge, Thomas A.; Haroldsen, Peter E.; Gaskell, Simon J. (1989) Characterization of impurities in a synthetic renin substrate peptide by fast-atom bombardment mass spectrometry and hybrid tandem mass spectrometry. Rapid Commun. Mass Spectrom. 3(9), 314-19 Notes: Fast-atom bombardment mass spectrometry of a synthetic renin substrate decapeptide (Pro-His-Pro-Phe-His-Leu-Val-Ile-His-D-Lys) indicated the presence of several side products, including a component 12 Da higher in mass. Low-energy collisionally activated ***decompn*** analyses were performed using a hybrid tandem instrument and demonstrated that the heavier side product had two components, in which the structural modification was either at the N- or the C-terminus. Addnl. analyses of the N-acetyl deriv. indicated that for each component the structural modification blocked a site of N-acetylation. It is suggested that the formation of these side products is attributable to the generation of formaldehyde, during removal of the histidine protecting group (benzyloxymethyl), which reacts with the N-terminus of the peptide to give an imidazolidinone structure or with the D- ***lysine***.epsilon.-amine group to yield an ***imine*** . While the precise genesis of the side-products remains speculative, it is clear that the combined strategy of derivatization and tandem mass spectrometry has allowed structural conclusions concerning individual components of an isobaric mixt. + lysine epsilon amino to imine + 12 amu + + + + + modification from DeltaMass + DeltaMass:34 + + + + + N6-(methylidene)-lysine + + + + + + + + + + A protein modification that effectively converts an N-terminal L-cysteine residue by a formadehyde adduct to 4-thiazolidinecarboxylic acid. + 12.01 + C 1 H 0 N 0 O 0 S 0 + 12.0 + C 4 H 6 N 1 O 1 S 1 + 116.16 + 116.01701 + C + artifact + N-term + thioproline + PSI-MOD + MOD:00965 + From DeltaMass: References: Mitchell, M.A., Runge, T.A., Mathews, W.R., Ichhpurani, A.K., Harn, N.K., Dobrowolski, P.J. and Eckenrrrode, F.M. Problems associated with use of the benzylozymethyl protecting group for histidines. Formaldehyde adducts formed during cleavage by hydrogen fluoride. Int. J. Pept. Protein Res. 1990, 36(4), 350-355. Gesquiere, J.-C., Diesis, E. and Tartar, A. Conversion of N-terminal cysteine to thiazolidine carboxylic acid during hydrogen fluoride deprotection of peptides containing pi-N-Bom protected histidine. J. Chem. Soc. Chem. Commun. 1990, (20), 1402-1403. Kumagaye, K.Y., Inui, T., Nakajima, K., Kimura,T. and Sakakibara, S. Suppression of a side reaction associated with Nim-benzyloxymethyl group during synthesis of peptides containing cysteinyl residue at the N-terminus. Pept. Res. 1991, 4(2), 84-87. Colombo, R., Colombo, F. and Jones, J.H. Acid-labile histidine side-chain protection. The N(pi)-t-butoxymethyl group. J. Chem. Soc. Chem. Commun. 1984, (5), 292-293. Notes: Conversion of N-term Cys to thiazolidine during HF deprotection of His(Bom)-containing peptides [1-3]. See structure at http://www.abrf.org/images/misc/dmass12b.gif; modification in red. This modification cannot be excluded during final deprotection/cleavage in Fmoc-chemistry in cases when His(Bum) was employed [4]. For formation of free imino acid see PubMed:1527501. + 4-thiazolidinecarboxylic acid + + + + + A protein modification that effectively converts an N-terminal L-cysteine residue by a formadehyde adduct to 4-thiazolidinecarboxylic acid. + DeltaMass:342 + + + + + thioproline + + + + + + + + + + A protein modification that effectively converts an N-terminal L-tryptophan residue by a formadehyde adduct to 1,2,3,4-tetrahydro-beta-carboline-3-carboxylic acid. + 12.01 + C 1 H 0 N 0 O 0 S 0 + 12.0 + C 12 H 10 N 2 O 1 + 198.22 + 198.07932 + W + artifact + PSI-MOD + MOD:00966 + From DeltaMass: Average Mass: 12 Average Mass Change: 12 References: Lippke, K. P., W. G. Schunack, W. Wenning, W. E. Mueller. 1983..beta.-Carbolines as benzodiazepine receptor ligands. 1. Synthesis andbenzodiazepine receptor interaction of esters of.beta.-carboline-3-carboxylic acid. J. Med. Chem.26: 499-503 Cain, M., R. W. Weber, F. Guzman, J. M. Cook, S. A. Barker, K. C.Rice, J. N. Crawley, S. M. Paul, P. Skolnick. 1982. .beta.-Carbolines:synthesis and neurochemical and pharmacological actions on brainbenzodiazepine receptors.J. Med. Chem. 25: 1081-91 Notes: +12 Da modification corresponds to formaldehyde adduct of Trp having beta-carboline structure (methylene bridge links carbon-2 of indole ring and alfa-N. See structure at http://www.abrf.org/images/misc/dmass12a.gif; modification in red. + 1,2,3,4-tetrahydro-beta-carboline-3-carboxylic acid + + + + + A protein modification that effectively converts an N-terminal L-tryptophan residue by a formadehyde adduct to 1,2,3,4-tetrahydro-beta-carboline-3-carboxylic acid. + DeltaMass:339 + + + + + + + + + A protein modification that effectively cross-links two L-lysine residues to form syndesine, hydroxylysinohydroxynorleucine. + 16.96 + C 0 H -3 N -2 O 3 + 16.95512 + C 12 H 21 N 2 O 5 + 273.31 + 273.14505 + K, K + hydroxylysinohydroxynorleucine + PSI-MOD + MOD:00967 + Cross-link 2; From DeltaMass: Average Mass: 13 Average Mass Change: 13 (incorrect) [JSG]. + syndesine + + + + + A protein modification that effectively cross-links two L-lysine residues to form syndesine, hydroxylysinohydroxynorleucine. + DeltaMass:35 + PubMed:75151974 + + + + + hydroxylysinohydroxynorleucine + + + + + + + + + OBSOLETE because this isn't a protein modification, but rather the difference between two known modifications. modification from DeltaMass + C + artifact + PSI-MOD + MOD:00968 + From DeltaMass: Average Mass: 13 Formula:C2H2O2 vs C3H5ON Monoisotopic Mass Change:13.03 Average Mass Change:13.05 Notes:Residual acrylamide in SDS gels can partly label cysteine residues in proteins (propionamido-Cys, PAM-Cys, DeltaMass +71Da; see entry). Subsequent alkylation of protein bands with iodoacetic acid e.g. in preparation for proteomic analysis, will convert remaining free cysteines into carboxymethyl-Cys (CM-Cys, DeltaMass +58Da; see entry). Peptide mass fingerprinting may therefore potentially reveal the same cysteine-containing peptide in two forms, differing in mass by 13Da. The relative ratios of the peaks will depend on the initial degree of labelling with acrylamide. Use of high quality, deionised acrylamide in the SDS gel will minimise modification of cysteine through this route. Where it remains a problem, deliberate alkylation using acrylamide instead of iodoacetamide will ensure chemical homogeneity of the final product. + CM-Cys vs PAM-Cys + true + + + + + OBSOLETE because this isn't a protein modification, but rather the difference between two known modifications. modification from DeltaMass + DeltaMass:347 + + + + + + + + OBSOLETE because this isn't a protein modification, but rather the difference between two known modifications. modification from DeltaMass + C + artifact + PSI-MOD + MOD:00969 + From DeltaMass: Average Mass: 14 Formula:CH2 Monoisotopic Mass Change:14.016 Average Mass Change:14.027 Notes: Residual acrylamide in SDS gels can partly label cysteine residues in proteins (propionamido-Cys, PAM-Cys, DeltaMass +71Da; see entry). Subsequent alkylation of protein bands with iodoacetamide e.g. in preparation for proteomic analysis, will convert remaining free cysteines into carboxamidomethyl-Cys (CAM-Cys, DeltaMass +57Da; see entry). Peptide mass fingerprinting may therefore potentially reveal the same cysteine-containing peptide in two forms, differing in mass by 14Da. The relative ratios of the peaks will depend on the initial degree of labelling with acrylamide. Use of high quality, deionised acrylamide in the SDS gel will minimise modification of cysteine through this route. Where it remains a problem, deliberate alkylation using acrylamide instead of iodoacetamide will ensure chemical homogeneity of the final product. + CAM-Cys vs PAM-Cys + true + + + + + OBSOLETE because this isn't a protein modification, but rather the difference between two known modifications. modification from DeltaMass + DeltaMass:346 + + + + + + + + + modification from DeltaMass + K + natural + PSI-MOD + MOD:00970 + From DeltaMass: Average Mass: 15 Average Mass Change:15 Notes:In going from Lys to hydroxy-allysine, two separate reactions are involved:1. the oxidative deamination converting Lys to allysine (-CH2NH2 being converted to -CHO) with a net mass change of -1;2.conversion of allysine to delta-hydroxy-allysine (-CH2-CHO being converted to -CH(OH)-CHO) with a mass change of +16. The net change from Lys to hydroxyallysine thus is +15. + delta-hydroxy-allysine (Lys) + + + + + modification from DeltaMass + DeltaMass:37 + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to 2-oxohistidine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 6 H 7 N 3 O 2 + 153.14 + 153.05383 + H + natural + PSI-MOD + MOD:00971 + From DeltaMass: Average Mass: 16 Average Mass Change:16 References:Lewisch, S. A. and Levine, R. L. (1995) Anal. Biochem. 231, 440-446. Determination of 2-oxo-histidine by amino acid analysis Notes:Rod LevineNIHBldg 3, Room 106 MSC 0320Bethesda, MD 20892-0320email: rlevine@nih.govvoice: 1 (301) 496-2310fax: 1 (301) 496-0599 + 2-Oxohistidine + + + + + A protein modification that effectively converts an L-histidine residue to 2-oxohistidine. + DeltaMass:38 + PubMed:8405458 + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to a monobrominated L-phenylalanine, such as L-2'-bromophenylalanine. + 78.9 + Br 1 C 0 H -1 N 0 O 0 + 77.910515 + Br 1 C 9 H 8 N 1 O 1 + 226.07 + 224.97893 + F + natural + Unimod:340 + Br1Phe + PSI-MOD + Bromo + bromination + MOD:00972 + From DeltaMass: Average Mass: 78 Average Mass Change:78 References:Yoshino,K et.al. Biochemistry Vol. 30 pg 6203-9 (1991) Identifidation of a novel amino acid, o-bromo-L-phenylananine, in egg-associated peptides that activate spermatozoa + monobrominated L-phenylalanine + + + + + A protein modification that effectively converts an L-phenylalanine residue to a monobrominated L-phenylalanine, such as L-2'-bromophenylalanine. + Unimod:340#F + + + + + Br1Phe + + + + + + Bromo + + + + + + bromination + + + + + + + + + + modification from DeltaMass + P + artifact + PSI-MOD + MOD:00973 + From DeltaMass: Average Mass: 32 Monoisotopic Mass Change:31.99 Average Mass Change:32 References:Amici A, Levine, RL, Tsai, L, and Stadtman, ER: Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. Journal of Biological Chemistry 264: 3341-3346 1989.Rod Levine (unpublished) + Oxidation of proline (to glutamic acid) + + + + + modification from DeltaMass + DeltaMass:355 + + + + + + + + + + + + + + + modification from DeltaMass + 33.96 + (35)Cl 1 H -1 + 33.96103 + C 9 (35)Cl 1 H 8 N 1 O 2 + 197.02 + 197.02435 + Y + artifact + PSI-MOD + MOD:00974 + From DeltaMass: Average Mass: 34 + (35)Cl labeled 3'-chlorotyrosine + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + + + + + + + modification from DeltaMass + 35.96 + (37)Cl 1 H -1 + 35.958076 + C 9 (37)Cl 1 H 8 N 1 O 2 + 199.02 + 199.02141 + Y + artifact + PSI-MOD + MOD:00975 + From DeltaMass: Average Mass: 36 + (37)Cl labeled 3'-chlorotyrosine + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + modification from DeltaMass - OBSOLETE because redundant and identical to MOD:01072. Remap to MOD:01072. + MOD:01072 + 38.09 + H -1 K 1 + 37.955883 + X + PSI-MOD + MOD:00976 + From DeltaMass: Average Mass: 38 + potassium salt + true + + + + + modification from DeltaMass - OBSOLETE because redundant and identical to MOD:01072. Remap to MOD:01072. + DeltaMass:0 + + + + + + + + + modification from DeltaMass + 43.96 + H -2 Na 2 + 43.963886 + X + PSI-MOD + MOD:00977 + + From DeltaMass: Average Mass: 44 + disodium salt + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + modification from DeltaMass + C + artifact + PSI-MOD + MOD:00978 + From DeltaMass: Average Mass: 51 Average Mass Change: 51 References:Lukszo, Patterson, Albericio, and Kates, Letters in Peptide Science 3, 157-166(1996) Notes:The side reaction can be very significant, and the level to which it occurs depends on how the C-terminal Cys is anchored and what the side-chain protecting group is. The mechanism involves piperidine-mediated beta-elimination of sulfur (with the protecting group on), followed by addition of piperidine across the C-terminaldehydroalanine. Since this last-mentioned step creates a chiral center, a mixture of diastereomers is formed which in special cases can be separatedby HPLC. Another problem with C-terminal Cys is racemization; some references in the review article by Andreu, Albericio, Sole, Munson, Ferrer, and Barany in Pennington-Dunn Peptide Synthesis and Purification Protocols, vol 35, 1994, pp. 91-169. + piperidine adduct to C-terminal Cys + + + + + modification from DeltaMass + DeltaMass:345 + + + + + + + + + modification from DeltaMass + X + artifact + PSI-MOD + MOD:00979 + From DeltaMass: Average Mass: 56 + t-butyl ester (OtBu) and t-butyl (tBu) + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + modification from DeltaMass - OBSOLETE because redundant, the difference component of MOD:01060. Remap to MOD:01060. + MOD:01060 + C + artifact + PSI-MOD + MOD:00980 + From DeltaMass: Average Mass: 57 Abbreviation:CamCys Formula:C2H3NO Monoisotopic Mass Change:57.021 Average Mass Change:57.051 Notes:Cysteine reacts with iodoacetamide to produce carboxamidomethyl cysteine. Alternative names are often used, such as amidocarboxymethylcysteine and carbamoylmethylcysteine + Carboxamidomethyl (on Cysteine) + true + + + + + modification from DeltaMass - OBSOLETE because redundant, the difference component of MOD:01060. Remap to MOD:01060. + DeltaMass:337 + + + + + + + + + + modification from DeltaMass + 60.07 + H -2 K 1 Na 1 + 59.937824 + X + PSI-MOD + MOD:00981 + + From DeltaMass: Average Mass: 60 + sodium and potassium salt + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + + A protein modification that effectively converts an L-serine residue to L-selenocysteine (not known as a natural post-translational modification process). + 62.97 + C 0 H 0 N 0 O -1 Se 1 + 63.921608 + C 3 H 5 N 1 O 1 Se 1 + 150.05 + 150.95363 + S + artifact + Sec(Ser) + Selenocysteine (from Serine) + PSI-MOD + MOD:00982 + [From DeltaMass: Average Mass: 64.] Although selenocysteine-charged tRNA(Sec) is biosynthesized from serine-charged tRNA(Sec), in peptide work selenocysteine is usually considered as either a natural residue or as a modified cysteine residue. This entry is for the artifactual formation of L-selenocysteine from serine. For encoded L-selenocysteine, use MOD:00031 [JSG]. + L-selenocysteine (Ser) + + + + + A protein modification that effectively converts an L-serine residue to L-selenocysteine (not known as a natural post-translational modification process). + DeltaMass:0 + + + + + Sec(Ser) + + + + + + Selenocysteine (from Serine) + + + + + + + + + + modification from DeltaMass + D + artifact + PSI-MOD + MOD:00983 + From DeltaMass: Average Mass: 67 Average Mass Change:67 References:http://www.abrf.org/archives/hmail/0008/0007.html Notes:1.) Get rid of the DBU. It can cause piperidine amides at Asp residues. The tbu ester side chain comes off during synthesis and the residue is trans-amidated with piperidine (+67Da by MS). If you haven't yet seen this, you will. Even "normal" 20% pip/DMF (NMP) will cause this, but less frequently. Literature exists for this; I don't remember the exact reference. David H. Singleton Scientist Pfizer Central Research PO Box 8118-101 Eastern Point Road Groton, CT 06340 (860)441-4404. + Asp transamidation with piperidine + + + + + modification from DeltaMass + DeltaMass:67 + + + + + + + + + + + + + + + modification from DeltaMass + 67.92 + (35)Cl 2 H -2 + 67.92206 + C 9 (35)Cl 2 H 7 N 1 O 2 + 230.99 + 230.98538 + Y + artifact + PSI-MOD + MOD:00984 + From DeltaMass: Average Mass: 68 + (35)Cl labeled 3',5'-dichlorotyrosine + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a halogen atom. + Y + HalTyr + PSI-MOD + MOD:00985 + + halogenated tyrosine + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a halogen atom. + PubMed:18688235 + + + + + HalTyr + + + + + + + + + + + + + + + + modification from DeltaMass + 69.92 + (35)Cl 1 (37)Cl 1 H -2 + 69.919106 + C 9 (35)Cl 1 (37)Cl 1 H 7 N 1 O 2 + 232.98 + 232.98244 + Y + artifact + PSI-MOD + MOD:00986 + From DeltaMass: Average Mass: 70. + (35)Cl and (37)Cl labeled 3',5'-dichlorotyrosine + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a chlorine atom. + Y + ClTyr + PSI-MOD + MOD:00987 + chlorinated tyrosine + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a chlorine atom. + PubMed:18688235 + + + + + ClTyr + + + + + + + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a bromine atom. + Y + BrTyr + PSI-MOD + MOD:00988 + brominated tyrosine + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a bromine atom. + PubMed:18688235 + + + + + BrTyr + + + + + + + + + OBSOLETE because redundant, the difference component of MOD:01079. Remap to MOD:01079. + MOD:01079 + C + artifact + PSI-MOD + MOD:00989 + From DeltaMass with no citation or formula. + acetamidomethyl (Acm) + true + + + + + OBSOLETE because redundant, the difference component of MOD:01079. Remap to MOD:01079. + DeltaMass:0 + + + + + + + + + + + + + + + modification from DeltaMass + 71.92 + (37)Cl 2 H -2 + 71.91615 + C 9 (37)Cl 2 H 7 N 1 O 2 + 234.98 + 234.97948 + Y + artifact + PSI-MOD + MOD:00990 + From DeltaMass: Average Mass: 72 + (37)Cl labeled 3',5'-dichlorotyrosine + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + modification from DeltaMass + 74.08 + C 3 H 6 O 2 + 74.03678 + C 6 H 11 N 1 O 3 S 1 + 177.22 + 177.04596 + C + artifact + PSI-MOD + MOD:00991 + From DeltaMass: Average Mass: 74 with no citation. + S-(sn-1-glyceryl)-L-cysteine + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + modification from DeltaMass + 74.08 + C 3 H 6 O 2 + 74.03678 + C 8 H 13 N 1 O 5 + 203.19 + 203.07938 + E + artifact + PSI-MOD + MOD:00992 + From DeltaMass: Average Mass: 74 Average Mass Change: 74 References: Anal. Biochem. 1993 Vol 208 No. 2 382-386, PubMed:8452236. [DeltaMass] This article only suggests this as a possible modification and does no characterization. Isolation and stuctural evidence for artifactual modification are found in PubMed:18767873 [JSG]. + glutamate 5-glycerol ester + + + + + modification from DeltaMass + DeltaMass:78 + PubMed:18767873 + + + + + + + + + modification from DeltaMass + 76.1 + C 6 H 4 + 76.0313 + X + artifact + OPh + PSI-MOD + MOD:00993 + From DeltaMass: Average Mass: 76, on acidic amino acids + phenyl ester + + + + + modification from DeltaMass + DeltaMass:0 + + + + + OPh + + + + + + + + + + + + + + + + modification from DeltaMass + 77.91 + (79)Br 1 H -1 + 77.910515 + (79)Br 1 C 9 H 8 N 1 O 2 + 240.97 + 240.97385 + Y + artifact + PSI-MOD + MOD:00994 + From DeltaMass: Average Mass: 78 + (79)Br labeled 3'-bromotyrosine + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to (81)Br-L-2'-bromophenylalanine. + 79.91 + (81)Br 1 H -1 + 79.90846 + (81)Br 1 C 9 H 8 N 1 O 1 + 226.98 + 226.97688 + F + artifact + PSI-MOD + MOD:00995 + From DeltaMass: Average Mass: 80 + (81)Br labeled 2'-bromophenylalanine + + + + + A protein modification that effectively converts an L-phenylalanine residue to (81)Br-L-2'-bromophenylalanine. + DeltaMass:0 + + + + + + + + + + + + + + + modification from DeltaMass + 79.91 + (81)Br 1 H -1 + 79.90846 + (81)Br 1 C 9 H 8 N 1 O 2 + 242.97 + 242.97179 + Y + artifact + PSI-MOD + MOD:00996 + From DeltaMass: Average Mass: 80 + (81)Br labeled 3'-bromotyrosine + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + modification from DeltaMass + 82.15 + C 6 H 10 + 82.07825 + X + artifact + OcHex + PSI-MOD + MOD:00997 + From DeltaMass: Average Mass: 82 + cyclohexyl ester + + + + + modification from DeltaMass + DeltaMass:0 + + + + + OcHex + + + + + + + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with an iodine atom. + Y + ITyr + PSI-MOD + MOD:00998 + + iodinated tyrosine + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with an iodine atom. + PubMed:18688235 + + + + + ITyr + + + + + + + + + OBSOLETE because redundant and identical to MOD:00404. Remap to MOD:00404. + MOD:00404 + M + artifact + PSI-MOD + MOD:00999 + From DeltaMass: Average Mass: 83 Formula:C4H5O1N1 Monoisotopic Mass Change:83.037 Average Mass Change:83.09 + homoseryl lactone + true + + + + + OBSOLETE because redundant and identical to MOD:00404. Remap to MOD:00404. + DeltaMass:90 + + + + + + + + + A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one bromine atom. + Y + Br1Tyr + PSI-MOD + MOD:01000 + monobrominated tyrosine + + + + + A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one bromine atom. + PubMed:18688235 + + + + + Br1Tyr + + + + + + + + + + A protein modification that inserts or replaces a residue with a 2-aminoisobutyric acid. + C 4 H 7 N 1 O 1 + 85.11 + 85.052765 + X + artifact + 2-amino-2-methylpropanoic acid + 2-amino-2-methylpropionic acid + 2-methylalanine + Aib + alpha,alpha-dimethylglycine + alpha-aminoisobutyric acid + alpha-methylalanine + PSI-MOD + MOD:01001 + Modification from DeltaMass: Average Mass: 85. + 2-aminoisobutyric acid residue (Aib) + + + + + A protein modification that inserts or replaces a residue with a 2-aminoisobutyric acid. + DeltaMass:0 + + + + + 2-amino-2-methylpropanoic acid + + + + + + 2-amino-2-methylpropionic acid + + + + + + 2-methylalanine + + + + + + Aib + + + + + + alpha,alpha-dimethylglycine + + + + + + alpha-aminoisobutyric acid + + + + + + alpha-methylalanine + + + + + + + + + + modification from DeltaMass + 85.11 + C 4 H 7 N 1 O 1 + 85.052765 + X + artifact + PSI-MOD + MOD:01002 + From DeltaMass: Average Mass: 85 Formula: C 4 H 7 O 1 N 1 Monoisotopic Mass Change: 85.053 Average Mass Change: 85.106 + gamma-aminobutyryl + + + + + modification from DeltaMass + DeltaMass:92 + + + + + + + + + modification from DeltaMass + X + artifact + PSI-MOD + MOD:01003 + From DeltaMass: Average Mass: 86 + t-butyloxymethyl (Bum) + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + modification from DeltaMass + 86.09 + C 3 H 6 N 2 O 1 + 86.04801 + X + artifact + PSI-MOD + MOD:01004 + From DeltaMass: Average Mass: 86 Formula: C 3 H 6 O 2 N 1 Monoisotopic Mass Change: 86.048 Average Mass Change: 86.094 + diaminopropionyl + + + + + modification from DeltaMass + DeltaMass:95 + + + + + + + + + modification from DeltaMass + X + artifact + StBu + PSI-MOD + MOD:01005 + From DeltaMass: Average Mass: 88 + t-butylsulfenyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + StBu + + + + + + + + + + A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two bromine atoms. + Y + Unimod:534 + Br2Tyr + PSI-MOD + Dibromo + MOD:01006 + dibrominated tyrosine + + + + + A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two bromine atoms. + Unimod:534 + + + + + Br2Tyr + + + + + + Dibromo + + + + + + Dibromo + + + + + + + + + + A protein modification that effectively substitutes an anisyl (methoxyphenyl) group for a hydroxyl group, typically at the 4 or para position. + 90.13 + C 7 H 6 + 90.04695 + X + artifact + PSI-MOD + MOD:01007 + From DeltaMass with no citation or formula: Average Mass: 90. + anisyl modified residue + + + + + A protein modification that effectively substitutes an anisyl (methoxyphenyl) group for a hydroxyl group, typically at the 4 or para position. + DeltaMass:0 + + + + + + + + + A protein modification that effectively substitutes a benzyl (phenylmethyl) group for a hydrogen atom. + 90.13 + C 7 H 6 + 90.04695 + X + artifact + PSI-MOD + MOD:01008 + From DeltaMass with no citation or formula: Average Mass: 90 + benzyl (Bzl) and benzyl ester (OBzl) modified residue + + + + + A protein modification that effectively substitutes a benzyl (phenylmethyl) group for a hydrogen atom. + DeltaMass:0 + + + + + + + + + + modification from DeltaMass + -2.02 + C 0 H -2 N 0 O 0 + -2.01565 + C 5 H 5 N 1 O 1 + 95.1 + 95.03712 + P + PSI-MOD + MOD:01009 + From DeltaMass with no citation. + dehydrogenated proline + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + + + A protein modification that effectively substitutes a trifluoroacetyl group for a hydrogen atom. + 96.01 + C 2 F 3 H -1 O 1 + 95.9823 + X + artifact + TFA + PSI-MOD + MOD:01010 + trifluoroacetylated residue + + + + + A protein modification that effectively substitutes a trifluoroacetyl group for a hydrogen atom. + DeltaMass:0 + + + + + TFA + + + + + + + + + + modification from DeltaMass + X + artifact + PSI-MOD + MOD:01011 + From DeltaMass: Average Mass: 97 + N-hydroxysuccinimide (ONSu, OSu) + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + + + + + + + A protein modification that effectively oxidizes the disulfide bond of a cystine crosslink to form two cysteic acid residues. + 98.01 + C 0 H 2 N 0 O 6 S 0 + 97.98514 + C 6 H 10 N 2 O 8 S 2 + 302.27 + 301.98785 + MOD:00034 + artifact + PSI-MOD + MOD:01012 + Cross-link 2. This modification destroys a cross-link. From DeltaMass: Average Mass: 98 Abbreviation: Cya Average Mass Change: 98 Notes: Treatment of cystine by strongly oxidising reagents such as performic acid results in the breakage of the disulphide bond and complete oxidation of the sulphur atoms on each molecule. Such treatment is often carried out prior to amino acid analysis as the resulting cysteic acid is then resistant to acid degradation during the hydrolysis procedure. + oxidation of disulfide crosslink in cystine to two cysteic acids + + + + + A protein modification that effectively oxidizes the disulfide bond of a cystine crosslink to form two cysteic acid residues. + DeltaMass:335 + + + + + + + + + modification from DeltaMass + X + PSI-MOD + MOD:01013 + From DeltaMass: Average Mass: 98 + tetramethylguanidinium termination by-product on amine + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + modification from DeltaMass + X + PSI-MOD + MOD:01014 + From DeltaMass: Average Mass: 98 Formula:H3PO4 or H2SO4 Monoisotopic Mass Change:97.97 Average Mass Change:98 Notes:Proteins may pick up non-covalent salt adducts during purification. Phosphate and sulphate salts are commonly used and may be observed as +98 amu adducts (or multiples thereof) forming ion pairs with basic residues. Monoisotopic masses H2SO4 97.967, H3PO4 97.977 + phosphate/sulphate adduct of proteins + + + + + modification from DeltaMass + DeltaMass:358 + + + + + + + + + A protein modification that inserts or replaces a residue with an isovaline. + C 5 H 9 N 1 O 1 + 99.13 + 99.06841 + X + artifact + 2-amino-2-methylbutanoic acid + Isovalyl (-I-,-Iva-) + Iva + PSI-MOD + MOD:01015 + isovaline residue (Iva) + + + + + A protein modification that inserts or replaces a residue with an isovaline. + DeltaMass:110 + + + + + 2-amino-2-methylbutanoic acid + + + + + + Isovalyl (-I-,-Iva-) + + + + + + Iva + + + + + + + + + + modification from DeltaMass + X + artifact + tBoc + PSI-MOD + MOD:01016 + From DeltaMass: Average Mass: 100 + t-butyloxycarbonyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + tBoc + + + + + + + + + OBSOLETE because redundant and identical to MOD:00403. Remap to MOD:00403. + MOD:00403 + M + artifact + PSI-MOD + MOD:01017 + From DeltaMass: Average Mass: 101 Abbreviation:-Hse- Formula:C4H7O2N Monoisotopic Mass Change:101.048 Average Mass Change:101.105 + homoseryl (-Hse-) + true + + + + + OBSOLETE because redundant and identical to MOD:00403. Remap to MOD:00403. + DeltaMass:113 + + + + + + + + + modification from DeltaMass + X + artifact + Meb + PSI-MOD + MOD:01018 + From DeltaMass: Average Mass: 104 + 4-methylbenzyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + Meb + + + + + + + + + + modification from DeltaMass + X + artifact + HMP + PSI-MOD + MOD:01019 + From DeltaMass: Average Mass: 106 + hydroxymethylphenyl linker + + + + + modification from DeltaMass + DeltaMass:0 + + + + + HMP + + + + + + + + + + modification from DeltaMass + X + artifact + PSI-MOD + MOD:01020 + From DeltaMass: Average Mass: 106 + thioanisyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + modification from DeltaMass + X + artifact + PSI-MOD + MOD:01021 + From DeltaMass: Average Mass: 106 + thiocresyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 2-piperidinecarboxylic acid. + -17.03 + C 0 H -3 N -1 O 0 + -17.026548 + C 6 H 9 N 1 O 1 + 111.14 + 111.06841 + K + artifact + Pip + PSI-MOD + MOD:01022 + 2-piperidinecarboxylic acid + + + + + A protein modification that effectively converts an L-lysine residue to 2-piperidinecarboxylic acid. + DeltaMass:0 + + + + + Pip + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to 3',5'-dibromo-L-tyrosine. + 157.79 + Br 2 C 0 H -2 N 0 O 0 + 155.82103 + Br 2 C 9 H 7 N 1 O 2 + 320.97 + 318.88434 + Y + 3',5'-Br2Tyr + PSI-MOD + MOD:01023 + 3',5'-dibromo-L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to 3',5'-dibromo-L-tyrosine. + DeltaMass:156 + + + + + 3',5'-Br2Tyr + + + + + + + + + + + + A protein modification that effectively converts an L-proline residue to one of several monohydroxylated proline residues, including 3-hydroxy-L-proline and 4-hydroxy-L-proline. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 5 H 7 N 1 O 2 + 113.12 + 113.047676 + P + natural + Unimod:35 + uniprot.ptm:PTM-0149 + Hy1Pro + Hydroxyproline + Hyp + hydroxylationp + PSI-MOD + Oxidation + MOD:01024 + + From DeltaMass: Average Mass: 131. This is the mass of the free amino acid [JSG]. + monohydroxylated proline + + + + + A protein modification that effectively converts an L-proline residue to one of several monohydroxylated proline residues, including 3-hydroxy-L-proline and 4-hydroxy-L-proline. + DeltaMass:0 + OMSSA:62 + Unimod:35#P + + + + + Hy1Pro + + + + + + Hydroxyproline + + + + + + Hyp + + + + + + hydroxylationp + + + + + + Oxidation + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to 3'-bromo-L-tyrosine. + 78.9 + Br 1 H -1 + 77.910515 + Br 1 C 9 H 8 N 1 O 2 + 242.07 + 240.97385 + Y + 3'-BrTyr + PSI-MOD + MOD:01025 + 3'-bromo-L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to 3'-bromo-L-tyrosine. + PubMed:18688235 + + + + + 3'-BrTyr + + + + + + + + + + + A protein modification that inserts or replaces a residue with a norleucine. + C 6 H 11 N 1 O 1 + 113.16 + 113.08406 + X + artifact + Nle + PSI-MOD + MOD:01026 + norleucine residue (Nle) + + + + + A protein modification that inserts or replaces a residue with a norleucine. + DeltaMass:126 + + + + + Nle + + + + + + + + + + modification from DeltaMass + X + artifact + Aoc + PSI-MOD + MOD:01027 + From DeltaMass: Average Mass: 114 + t-amyloxycarbonyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + Aoc + + + + + + + + + + + A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one chlorine atom. + 34.44 + C 0 Cl 1 H -1 N 0 O 0 + 33.96103 + C 9 Cl 1 H 8 N 1 O 2 + 197.62 + 197.02435 + Y + artifact + Cl1Tyr + PSI-MOD + MOD:01028 + monochlorinated L-tyrosine + + + + + A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one chlorine atom. + PubMed:18688235 + + + + + Cl1Tyr + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a succinyl group linked through a carbonyl carbon. + 100.07 + C 4 H 4 O 3 + 100.016045 + X + Unimod:64 + PSI-MOD + Succinic anhydride labeling reagent light form (N-term & K) + MOD:01029 + + From DeltaMass with no citation or formula, Average Mass: 117 [JSG]. + succinylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with a succinyl group linked through a carbonyl carbon. + DeltaMass:0 + Unimod:64 + + + + + Succinic anhydride labeling reagent light form (N-term & K) + + + + + + + + + + modification from DeltaMass + X + artifact + HOBt + PSI-MOD + MOD:01030 + From DeltaMass: Average Mass: 117 + hydroxybenzotriazole ester + + + + + modification from DeltaMass + DeltaMass:0 + + + + + HOBt + + + + + + + + + + modification from DeltaMass + X + artifact + diMeBzl + PSI-MOD + MOD:01031 + From DeltaMass: Average Mass: 118 + dimethylbenzyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + diMeBzl + + + + + + + + + + A protein modification that effectively substitutes a benzyloxymethyl group for a hydrogen atom. + 120.15 + C 8 H 8 O 1 + 120.05752 + X + artifact + Bom + PSI-MOD + MOD:01032 + benzyloxymethyl modified residue + + + + + A protein modification that effectively substitutes a benzyloxymethyl group for a hydrogen atom. + DeltaMass:0 + + + + + Bom + + + + + + + + + + A protein modification that effectively substitutes a p-methoxybenzyl group for a hydrogen atom. + 120.15 + C 8 H 8 O 1 + 120.05752 + X + artifact + Mbzl + Mob + PSI-MOD + MOD:01033 + p-methoxybenzyl modified residue + + + + + A protein modification that effectively substitutes a p-methoxybenzyl group for a hydrogen atom. + DeltaMass:0 + + + + + Mbzl + + + + + + Mob + + + + + + + + + + A protein modification that effectively substitutes a 4-nitrophenyl group for a hydrogen atom. + 121.1 + C 6 H 3 N 1 O 2 + 121.01638 + X + artifact + ONp + p-nitrophenyl + PSI-MOD + MOD:01034 + 4-nitrophenyl modified residue + + + + + A protein modification that effectively substitutes a 4-nitrophenyl group for a hydrogen atom. + DeltaMass:0 + + + + + ONp + + + + + + p-nitrophenyl + + + + + + + + + + modification from DeltaMass + X + artifact + ClBzl + PSI-MOD + MOD:01035 + From DeltaMass: Average Mass: 125 + chlorobenzyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + ClBzl + + + + + + + + + OBSOLETE because redundant and identical to MOD:01181. Remap to MOD:01181. + MOD:01181 + C 5 H 7 N 1 O 3 + 129.12 + 129.04259 + D + PSI-MOD + MOD:01036 + From DeltaMass:148 (name misspelled "aspartamyl", and formula incorrect, N and O reversed) Average Mass: 129 Formula: C5H7O1N3 Monoisotopic Mass Change: 129.042 Average Mass Change: 129.116 + O-methyl aspartyl + true + + + + + OBSOLETE because redundant and identical to MOD:01181. Remap to MOD:01181. + PubMed:18688235 + + + + + + + + + A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two chlorine atoms. + 68.88 + C 0 Cl 2 H -2 N 0 O 0 + 67.92206 + C 9 Cl 2 H 7 N 1 O 2 + 232.06 + 230.98538 + Y + artifact + Cl2Tyr + PSI-MOD + MOD:01037 + dichlorinated tyrosine + + + + + A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two chlorine atoms. + PubMed:18688235 + + + + + Cl2Tyr + + + + + + + + + OBSOLETE because this represents a free amino acid and the corresponding residue is MOD:01026. + PSI-MOD + MOD:01038 + From DeltaMass: Average Mass: 131. + norleucine (Nle) + true + + + + + OBSOLETE because this represents a free amino acid and the corresponding residue is MOD:01026. + DeltaMass:0 + + + + + + + + OBSOLETE because redundant and identical to MOD:00036. Remap to MOD:00036. + MOD:00036 + C 4 H 5 N 1 O 4 + 131.09 + 131.02185 + D + PSI-MOD + MOD:01039 + From DeltaMass:152 (name misspelled "aspartamyl", and formula incorrect, N and O reversed) Average Mass: 131 Formula:C4H5O1N4 Monoisotopic Mass Change:131.022 Average Mass Change:131.088 + hydroxy aspartyl + true + + + + + OBSOLETE because redundant and identical to MOD:00036. Remap to MOD:00036. + PubMed:18688235 + + + + + + + + + A protein modification that inserts or replaces a residue with a penicillamine. + C 5 H 9 N 1 O 1 S 1 + 131.19 + 131.04048 + X + artifact + 2-amino-3-mercapto-3-methylbutanoic acid + 2-amino-3-methyl-3-sulfanylbutanoic acid + 3,3-dimethylcysteine + 3-mercapto-L-valine + Pen + beta,beta-dimethylcysteine + PSI-MOD + MOD:01040 + From DeltaMass: Name misspelled 'bb-dimethyl cystenyl'. No citation provided. + penicillamine residue + + + + + A protein modification that inserts or replaces a residue with a penicillamine. + DeltaMass:154 + + + + + 2-amino-3-mercapto-3-methylbutanoic acid + + + + + + 2-amino-3-methyl-3-sulfanylbutanoic acid + + + + + + 3,3-dimethylcysteine + + + + + + 3-mercapto-L-valine + + + + + + Pen + + + + + + Pen + + + + + + beta,beta-dimethylcysteine + + + + + + + + + + A protein modification that effectively substitutes a benzyloxycarbonyl group for a hydrogen atom. + 134.13 + C 8 H 6 O 2 + 134.03677 + artifact + Z + PSI-MOD + MOD:01041 + benzyloxycarbonyl modified residue + + + + + A protein modification that effectively substitutes a benzyloxycarbonyl group for a hydrogen atom. + DeltaMass:0 + + + + + Z + + + + + + + + + + A protein modification that effectively substitutes a adamantyl group for a hydrogen atom. + 134.22 + C 10 H 14 + 134.10954 + artifact + Ada + PSI-MOD + MOD:01042 + adamantyl modified residue + + + + + A protein modification that effectively substitutes a adamantyl group for a hydrogen atom. + DeltaMass:0 + + + + + Ada + + + + + + + + + + A protein modification that effectively substitutes a p-nitrobenzyl group for the hydrogen atom of a carboxyl group. + 135.12 + C 7 H 5 N 1 O 2 + 135.03203 + artifact + ONb + PSI-MOD + MOD:01043 + p-nitrobenzyl ester modified residue + + + + + A protein modification that effectively substitutes a p-nitrobenzyl group for the hydrogen atom of a carboxyl group. + DeltaMass:0 + + + + + ONb + + + + + + + + + OBSOLETE because redundant and identical to MOD:00080. Remap to MOD:00080. + MOD:00080 + Q + PSI-MOD + MOD:01044 + From DeltaMass with no citation. Formula:C6H10O2N2 (name misspelled, formula for N5-methylglutaminyl, rather than N2-methylglutamyl) + N-methyl glutamyl + true + + + + + OBSOLETE because redundant and identical to MOD:00080. Remap to MOD:00080. + DeltaMass:166 + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to 3',5'-dichloro-L-tyrosine. + 68.88 + C 0 Cl 2 H -2 N 0 O 0 + 67.92206 + C 9 Cl 2 H 7 N 1 O 2 + 232.06 + 230.98538 + Y + artifact + 3',5'-Cl2Tyr + PSI-MOD + MOD:01045 + 3',5'-dichloro-L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to 3',5'-dichloro-L-tyrosine. + PubMed:18688235 + + + + + 3',5'-Cl2Tyr + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to 3'-chloro-L-tyrosine. + 34.44 + C 0 Cl 1 H -1 N 0 O 0 + 33.96103 + C 9 Cl 1 H 8 N 1 O 2 + 197.62 + 197.02435 + Y + artifact + 3'-ClTyr + PSI-MOD + MOD:01046 + 3'-chloro-L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to 3'-chloro-L-tyrosine. + PubMed:18688235 + + + + + 3'-ClTyr + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to a monohydroxylated lysine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 6 H 12 N 2 O 2 + 144.17 + 144.08987 + K + natural + Unimod:35 + Hy1Lys + Hydroxy Lysyl (-Hyl-) + hydroxylationk + PSI-MOD + Oxidation + MOD:01047 + + From DeltaMass: Average Mass: 144 Abbreviation:-Hyl- Formula:C6H12N2O2 Monoisotopic Mass Change:144.09 Average Mass Change:144.174. + monohydroxylated lysine + + + + + A protein modification that effectively converts an L-lysine residue to a monohydroxylated lysine. + DeltaMass:168 + OMSSA:60 + Unimod:35#K + + + + + Hy1Lys + + + + + + Hydroxy Lysyl (-Hyl-) + + + + + + hydroxylationk + + + + + + Oxidation + + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to 2-pyrrolidone-5-carboxylic acid. + C 5 H 6 N 1 O 2 + 112.11 + 112.039856 + X + N-term + PyrGlu + PSI-MOD + MOD:01048 + + From DeltaMass: Average Mass: -18 Average Mass Change: -18.01 References:The conversion of glutamic acid to pyroglutamic was reported for the beta-amiloid protein. Miller et al. Arch. Biochem. Biophy. (1993) 301, 41-52. + 2-pyrrolidone-5-carboxylic acid + + + + + A protein modification that effectively converts a source amino acid residue to 2-pyrrolidone-5-carboxylic acid. + PubMed:18688235 + + + + + PyrGlu + + + + + + + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-histidine residue with a halogen atom. + H + HalHis + PSI-MOD + MOD:01049 + halogenated histidine + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-histidine residue with a halogen atom. + PubMed:18688235 + + + + + HalHis + + + + + + + + + + modification from DeltaMass + A + artifact + PSI-MOD + MOD:01050 + From DeltaMass: Average Mass: 148 Formula:C8H8O2N1 Monoisotopic Mass Change:148.064 Average Mass Change:148.165 + pyridyl alanyl + + + + + modification from DeltaMass + DeltaMass:180 + + + + + + + + + modification from DeltaMass + artifact + NBz + PSI-MOD + MOD:01051 + From DeltaMass: Average Mass: 149 + 2-nitrobenzoyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + NBz + + + + + + + + + + modification from DeltaMass + W + artifact + PSI-MOD + MOD:01052 + From DeltaMass: Average Mass: 150 + dimethoxybenzyl Trp + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + modification from DeltaMass + artifact + Nps + PSI-MOD + MOD:01053 + From DeltaMass: Average Mass: 153 + 2-nitrophenylsulphenyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + Nps + + + + + + + + + + modification from DeltaMass + artifact + 4-toluenesulphonyl + Tos + Tosyl + PSI-MOD + MOD:01054 + From DeltaMass: Average Mass: 154 + 4-toluenesulfonyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + 4-toluenesulphonyl + + + + + + Tos + + + + + + Tosyl + + + + + + + + + + modification from DeltaMass + artifact + Npys + PSI-MOD + MOD:01055 + From DeltaMass: Average Mass: 154 + 3-nitro-2-pyridinesulfenyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + Npys + + + + + + + + + + + + + + + + modification from DeltaMass + 155.82 + (79)Br 2 C 0 H -2 N 0 O 0 + 155.82103 + (79)Br 2 C 9 H 7 N 1 O 2 + 318.88 + 318.88434 + Y + artifact + PSI-MOD + MOD:01056 + From DeltaMass: Average Mass: 156 + (79)Br labeled 3',5'-dibromotyrosine + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + + + + + + + modification from DeltaMass + 157.82 + (79)Br 1 (81)Br 1 C 0 H -2 N 0 O 0 + 157.81898 + (79)Br 1 (81)Br 1 C 9 H 7 N 1 O 2 + 320.88 + 320.8823 + Y + artifact + PSI-MOD + MOD:01057 + From DeltaMass: Average Mass: 158 + (79)Br and (81)Br labeled 3',5'-dibromotyrosine + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + modification from DeltaMass + artifact + Dcb + PSI-MOD + MOD:01058 + From DeltaMass: Average Mass: 159 + dichlorobenzyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + Dcb + + + + + + + + + + + + + + + + modification from DeltaMass + 159.82 + (81)Br 2 C 0 H -2 N 0 O 0 + 159.81693 + (81)Br 2 C 9 H 7 N 1 O 2 + 322.88 + 322.88025 + Y + artifact + PSI-MOD + MOD:01059 + From DeltaMass: Average Mass: 160 + (81)Br labeled 3',5'-dibromotyrosine + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine. + 57.05 + C 2 H 3 N 1 O 1 S 0 + 57.021465 + C 5 H 8 N 2 O 2 S 1 + 160.19 + 160.03065 + C + artifact + Unimod:4 + CamC + CamCys + Carboxamidomethyl (on Cysteine) + Carboxyamidomethyl Cystenyl + S-carbamoylmethyl-L-cysteine + amidocarboxymethylcysteine + carbamidomethylc + carbamoylmethylcysteine + PSI-MOD + Carbamidomethyl + Iodoacetamide derivative + MOD:01060 + + From DeltaMass: (name misspelled "Carboxyamidomethyl Cystenyl") [JSG]. + S-carboxamidomethyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine. + DeltaMass:196 + DeltaMass:337 + OMSSA:3 + PubMed:10504701 + PubMed:11510821 + PubMed:12422359 + PubMed:18306178 + Unimod:4#C + + + + + CamC + + + + + + CamCys + + + + + + Carboxamidomethyl (on Cysteine) + + + + + + Carboxyamidomethyl Cystenyl + + + + + + S-carbamoylmethyl-L-cysteine + + + + + + amidocarboxymethylcysteine + + + + + + carbamidomethylc + + + + + + carbamoylmethylcysteine + + + + + + Carbamidomethyl + + + + + + Iodoacetamide derivative + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine. + 58.04 + C 2 H 2 N 0 O 2 S 0 + 58.005478 + C 5 H 7 N 1 O 3 S 1 + 161.18 + 161.01466 + C + artifact + Unimod:6 + Carboxymethyl Cystenyl + Carboxymethyl cysteine + CmC + carboxymethylc + PSI-MOD + Carboxymethyl + Iodoacetic acid derivative + MOD:01061 + + From DeltaMass with no citation, name misspelled "Carboxymethyl Cystenyl", and formula incorrect, N and O reversed: Average Mass: 161 Abbreviation: -Cmc- Formula: C5H7O1N3S1 Monoisotopic Mass Change: 161.015 Average Mass Change: 161.179 [JSG]. + S-carboxymethyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine. + DeltaMass:0 + DeltaMass:197 + OMSSA:2 + Unimod:6#C + + + + + Carboxymethyl Cystenyl + + + + + + Carboxymethyl cysteine + + + + + + CmC + + + + + + carboxymethylc + + + + + + Carboxymethyl + + + + + + Iodoacetic acid derivative + + + + + + + + + OBSOLETE because duplicate and redundant with MOD:01061. Remap to MOD:01061 + MOD:01061 + C 5 H 7 N 3 O 1 S 1 + 157.19 + 157.03099 + C + artifact + Carboxymethyl Cystenyl + PSI-MOD + MOD:01062 + From DeltaMass:197 (Name misspelled "cystenyl", and formula incorrect, N and O reversed) Abbreviation:-Cmc- Formula:C5H7O1N3S1 Monoisotopic Mass Change:161.015 Average Mass Change:161.179 + carboxymethyl cysteinyl + true + + + + + OBSOLETE because duplicate and redundant with MOD:01061. Remap to MOD:01061 + DeltaMass:197 + + + + + Carboxymethyl Cystenyl + + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to a monomethylated phenylalanine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 10 H 11 N 1 O 1 + 161.2 + 161.08406 + F + NMePhe + PSI-MOD + MOD:01063 + + From DeltaMass: Average Mass: 161 Formula: C10H11O1N1 Monoisotopic Mass Change: 161.084 Average Mass Change: 161.205. No citation provided. It is not obvious whether the DeltaMass entry is supposed to represent N-methylphenylalanine, alpha-methylphenylalanine, 2'-, 3'-, or 4'-methylphenylalanine [JSG]. + monomethylated phenylalanine + + + + + A protein modification that effectively converts an L-phenylalanine residue to a monomethylated phenylalanine. + DeltaMass:198 + + + + + NMePhe + + + + + + + + + + modification from DeltaMass + PSI-MOD + MOD:01064 + From DeltaMass: Average Mass: 162 + inositol + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + A modification produced in a non-enzymatic reaction between a carbohydrate carbonyl group (C1 of aldohexose or C2 of fructose) and a protein N-terminal amino group to form a Schiff-base or an Amadori ketosamine (or aminoketose) residue adduct. + 162.14 + C 6 H 10 O 5 + 162.05283 + N-term + Unimod:41 + PSI-MOD + MOD:01065 + From DeltaMass: Average Mass: 162 + hexose glycated N-terminal + + + + + A modification produced in a non-enzymatic reaction between a carbohydrate carbonyl group (C1 of aldohexose or C2 of fructose) and a protein N-terminal amino group to form a Schiff-base or an Amadori ketosamine (or aminoketose) residue adduct. + DeltaMass:0 + Unimod:41#N-term + + + + + + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-phenylalanine residue with a halogen atom. + F + HalPhe + PSI-MOD + MOD:01066 + halogenated phenylalanine + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-phenylalanine residue with a halogen atom. + PubMed:18688235 + + + + + HalPhe + + + + + + + + + + modification from DeltaMass + artifact + PSI-MOD + MOD:01067 + From DeltaMass: Average Mass: 162 Average Mass Change:162 Notes: (from the ABRF discussion list archive) There may be ... things in the reagent K that would allow cleavage of the peptide to occur at the wrong place...in this case it removes the dimethoxybenzyl group first inactivating that site for cleavage, and it goes after tne next amide bond closer to the resin. Try the TFA/TIS/water/EDT cocktail...TFA = 92%, TIS =3%, and water is at 5%. .. had this issue on longer peptides.. and by increasing the amount of water a little bit... able to elminate this problem. + linker attached to peptide in Fmoc peptide synthesis + + + + + modification from DeltaMass + DeltaMass:341 + + + + + + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-tryptophan residue with a halogen atom. + W + HalTrp + PSI-MOD + MOD:01068 + halogenated tryptophan + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-tryptophan residue with a halogen atom. + PubMed:18688235 + + + + + HalTrp + + + + + + + + + + A protein modification that effectively substitutes a 2,4-dinitrophenyl group for a hydrogen atom. + 166.09 + C 6 H 2 N 2 O 4 + 166.00145 + artifact + Dnp + PSI-MOD + MOD:01069 + 2,4-dinitrophenyl modified residue + + + + + A protein modification that effectively substitutes a 2,4-dinitrophenyl group for a hydrogen atom. + DeltaMass:0 + + + + + Dnp + + + + + + + + + + A protein modification that effectively substitutes a pentafluorophenyl group for a hydrogen atom. + 166.05 + C 6 F 5 H -1 + 165.98419 + artifact + Pfp + PSI-MOD + MOD:01070 + From DeltaMass: name mispelled "pentaflourophenyl" + pentafluorophenyl modified residue + + + + + A protein modification that effectively substitutes a pentafluorophenyl group for a hydrogen atom. + DeltaMass:0 + + + + + Pfp + + + + + + + + + + A protein modification that effectively substitutes a diphenylmethyl group for a hydrogen atom. + 166.22 + C 13 H 10 + 166.07825 + X + artifact + Dpm + PSI-MOD + MOD:01071 + diphenylmethyl modified residue + + + + + A protein modification that effectively substitutes a diphenylmethyl group for a hydrogen atom. + DeltaMass:0 + + + + + Dpm + + + + + + + + + + A protein modification that effectively substitutes one potassium atom for one hydrogen atom. + 38.09 + H -1 K 1 + 37.955883 + X + K1Res + PSI-MOD + MOD:01072 + + monopotassium salt + + + + + A protein modification that effectively substitutes one potassium atom for one hydrogen atom. + DeltaMass:0 + + + + + K1Res + + + + + + + + + + A protein modification that effectively substitutes a 2-chlorobenzyloxycarbonyl group for a hydrogen atom. + 169.58 + C 8 Cl 1 H 6 O 2 + 169.00563 + X + artifact + Clz + PSI-MOD + MOD:01073 + 2-chlorobenzyloxycarbonyl modified residue + + + + + A protein modification that effectively substitutes a 2-chlorobenzyloxycarbonyl group for a hydrogen atom. + DeltaMass:0 + + + + + Clz + + + + + + + + + + A protein modification that effectively substitutes a napthylacetyl group for a hydrogen atom. + 169.2 + C 12 H 9 O 1 + 169.06534 + X + artifact + PSI-MOD + MOD:01074 + napthylacetyl modified residue + + + + + A protein modification that effectively substitutes a napthylacetyl group for a hydrogen atom. + DeltaMass:0 + + + + + + + + + A protein modification that effectively substitutes a mercury atom or a cluster containing mercury for hydrogen atoms, or that coordinates a mercury ion. + HgRes + PSI-MOD + MOD:01075 + mercury containing modified residue + + + + + A protein modification that effectively substitutes a mercury atom or a cluster containing mercury for hydrogen atoms, or that coordinates a mercury ion. + PubMed:18688235 + + + + + HgRes + + + + + + + + + modification from DeltaMass - OBSOLETE because redundant and identical to MOD:00414. Remap to MOD:00414. + MOD:00414 + C 7 H 14 N 4 O 1 + 170.22 + 170.11676 + R + PSI-MOD + MOD:01076 + From DeltaMass: Average Mass: 170 Formula:C7H14O4N1 Monoisotopic Mass Change:170.117 Average Mass Change:170.215 + N-methyl arginyl + true + + + + + modification from DeltaMass - OBSOLETE because redundant and identical to MOD:00414. Remap to MOD:00414. + DeltaMass:215 + + + + + + + + + modification from DeltaMass + artifact + PSI-MOD + MOD:01077 + From DeltaMass: Average Mass: 172 Average Mass Change:172 References:[1]. Sieber,P.(1987) Modification of tryptophan residues during acidolysis of4-methoxy-2,3,6-trimethylbenzenesulfonyl groups. Effects of scavengers. Tetrahedron Lett., 28(15),1637-1640. Notes: TFA-cyclic dithioketal by-product is formed when Trp-containing peptide is subjected to prolonged TFA/EDT treatment [1]. See structure at http://www.abrf.org/images/misc/dmass172.gif. Additional discussion of this adduct, and how to avoid it, can befound in Methods in Enzymology 289, 67 (1997) + ethanedithiol/TFA cyclic adduct + + + + + modification from DeltaMass + DeltaMass:216 + + + + + + + + + A protein modification that effectively converts an L-threonine residue to S-(2-aminoethyl)-3-methylcysteine. + 59.13 + C 2 H 5 N 1 O -1 S 1 + 59.019356 + C 6 H 12 N 2 O 1 S 1 + 160.24 + 160.06703 + T + artifact + Unimod:472 + 2-amino-3-(2-aminoethyl)sulfanyl-3-methylbutanoic acid + S-aminoethyl-3-methylcysteine + PSI-MOD + AEC-MAEC + beta-methylaminoethylcysteine + MOD:01078 + From DeltaMass: Average Mass: 146 Abbreviation:-AECys_ Formula:C5H10O2N1S1 Monoisotopic Mass Change:146.051 Average Mass Change:146.214 References:PE Sciex. + S-(2-aminoethyl)-3-methylcysteine (Thr) + + + + + A protein modification that effectively converts an L-threonine residue to S-(2-aminoethyl)-3-methylcysteine. + PubMed:12923550 + Unimod:472#T + + + + + 2-amino-3-(2-aminoethyl)sulfanyl-3-methylbutanoic acid + + + + + + S-aminoethyl-3-methylcysteine + + + + + + AEC-MAEC + + + + + + beta-methylaminoethylcysteine + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-[(acetylamino)methyl]-L-cysteine. + 71.08 + C 3 H 5 N 1 O 1 S 0 + 71.03712 + C 6 H 10 N 2 O 2 S 1 + 174.22 + 174.0463 + C + artifact + Acetamidomethyl Cystenyl + Acm-Cys + N-(hydroxymethyl)acetamide derivatized L-cysteine + S-(acetamido)methyl-L-cysteine + PSI-MOD + MOD:01079 + From DeltaMass: (name misspelled "Acetamidomethyl Cystenyl") Average Mass: 174 Formula: C 6 H 10 O 2 N 2 S 1 Monoisotopic Mass Change: 174.046 Average Mass Change: 174.221. [These are aggregate masses, not delta masses.] See Organic Syntheses, Coll. Vol. 6, p.5 (1988); Vol. 59, p.190 (1979); http://www.orgsyn.org/orgsyn/orgsyn/prepContent.asp?prep=cv6p0005 [JSG]. + S-(acetylamino)methyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-[(acetylamino)methyl]-L-cysteine. + DeltaMass:218 + PubMed:8572278 + + + + + Acetamidomethyl Cystenyl + + + + + + Acm-Cys + + + + + + N-(hydroxymethyl)acetamide derivatized L-cysteine + + + + + + S-(acetamido)methyl-L-cysteine + + + + + + + + + OBSOLETE because this is identical to MOD:00417. modification from DeltaMass + MOD:00417 + C 6 H 10 N 2 O 2 S 1 + 174.22 + 174.0463 + C + artifact + Acrylamidyl Cystenyl + PSI-MOD + MOD:01080 + From DeltaMass: (name misspelled "Acrylamidyl Cystenyl") Average Mass: 174 Formula: C6H10O2N2S1 Monoisotopic Mass Change: 174.046 Average Mass Change: 174.221 + acrylamidyl cysteinyl + true + + + + + OBSOLETE because this is identical to MOD:00417. modification from DeltaMass + DeltaMass:219 + + + + + Acrylamidyl Cystenyl + + + + + + + + + + modification from DeltaMass + 178.14 + C 6 H 10 O 6 + 178.04774 + PSI-MOD + MOD:01081 + From DeltaMass: Average Mass: 177. CAUTION - mass does not match formula. + delta-glycosyloxy- (of lysine) or beta-glycosyloxy- (of phenylalanine or tyrosine) + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + OBSOLETE because redundant with MOD:00757, remap. modification from DeltaMass + MOD:00757 + 178.14 + C 6 H 10 O 6 + 178.04774 + C 11 H 17 N 1 O 6 + 259.26 + 259.1056 + P + PSI-MOD + MOD:01082 + From DeltaMass: Average Mass: 177. Caution: Formula does not match mass. The natural glycosylating sugar of hydroxyproline is galactose. + 4-glycosyloxy- (hexosyl, C6) (of proline) + true + + + + + OBSOLETE because redundant with MOD:00757, remap. modification from DeltaMass + DeltaMass:0 + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-benzyl-L-serine. + 90.13 + C 7 H 6 + 90.04695 + C 10 H 11 N 1 O 2 + 177.2 + 177.07898 + S + artifact + PSI-MOD + MOD:01083 + O-benzyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-benzyl-L-serine. + DeltaMass:0 + + + + + + + + + A protein modification that by reaction of iodoacetic acid effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a carboxymethyl group. + 58.04 + C 2 H 2 O 2 + 58.005478 + X + artifact + N-term + Unimod:6 + Carboxymethyl (on Cysteine) + PSI-MOD + Carboxymethyl + Iodoacetic acid derivative + MOD:01084 + + iodoacetic acid derivatized amino-terminal residue + + + + + A protein modification that by reaction of iodoacetic acid effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a carboxymethyl group. + Unimod:6#N-term + + + + + Carboxymethyl (on Cysteine) + + + + + + Carboxymethyl + + + + + + Iodoacetic acid derivative + + + + + + + + + + + A protein modification that effectively replaces the N-terminal hydrogen atom of a N-terminal histidine residue with a gluconoyl group linked through a glycosidic bond. modification from DeltaMass + 179.15 + C 6 H 11 O 6 + 179.05556 + C 12 H 18 N 3 O 7 + 316.29 + 316.11447 + H + natural + N-term + PSI-MOD + MOD:01085 + Occurs on His-tagged proteins expresssed in E. coli. From DeltaMass: Average Mass: 178 Formula: C6H10O6 Monoisotopic Mass Change: 178.05 Average Mass Change: 178.14 References: Geoghegan, K. F., H. B. Dixon, et al. (1999). Spontaneous alpha-N-6-phosphogluconoylation of a His tag in Escherichia coli: the cause of extra mass of 258 or 178 Da in fusion proteins. Anal Biochem 267(1): 169-84. Mass listed here is 179 because it's N-terminal. + alpha-N-gluconoylated L-histidine + + + + + A protein modification that effectively replaces the N-terminal hydrogen atom of a N-terminal histidine residue with a gluconoyl group linked through a glycosidic bond. modification from DeltaMass + DeltaMass:226 + PubMed:9918669 + + + + + + + + + modification from DeltaMass + artifact + 4Nz + PSI-MOD + MOD:01086 + From DeltaMass: Average Mass: 179 + p-nitrobenzyloxycarbonyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + 4Nz + + + + + + + + + + A protein modification that effectively substitutes a 2,4,5-trichlorophenyl group for a hydrogen atom. + 179.42 + C 6 Cl 3 H 1 + 177.91438 + artifact + PSI-MOD + MOD:01087 + 2,4,5-trichlorophenyl modified residue + + + + + A protein modification that effectively substitutes a 2,4,5-trichlorophenyl group for a hydrogen atom. + DeltaMass:0 + + + + + + + + + A protein modification that effectively substitutes a 2,4,6-trimethyloxybenzyl group for a hydrogen atom. + 180.2 + C 10 H 12 O 3 + 180.07864 + X + artifact + Tmob + PSI-MOD + MOD:01088 + 2,4,6-trimethyloxybenzyl modified residue + + + + + A protein modification that effectively substitutes a 2,4,6-trimethyloxybenzyl group for a hydrogen atom. + DeltaMass:0 + + + + + Tmob + + + + + + + + + + modification from DeltaMass + artifact + Xan + PSI-MOD + MOD:01089 + From DeltaMass: Average Mass: 180 + xanthyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + Xan + + + + + + + + + + A protein modification that by reaction of iodoacetamide effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a carboxamidomethyl group. + 57.05 + C 2 H 3 N 1 O 1 + 57.021465 + X + artifact + N-term + Unimod:4 + (carbamoylmethyl)amino + PSI-MOD + Carbamidomethyl + Iodoacetamide derivative + MOD:01090 + + iodoacetamide derivatized amino-terminal residue + + + + + A protein modification that by reaction of iodoacetamide effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a carboxamidomethyl group. + PubMed:11327326 + PubMed:11510821 + PubMed:12422359 + Unimod:4#N-term + + + + + (carbamoylmethyl)amino + + + + + + Carbamidomethyl + + + + + + Iodoacetamide derivative + + + + + + + + + + + A protein modification that effectively substitutes one hydrogen atom of an L-phenylalanine residue with one chlorine atom. + 34.44 + C 0 Cl 1 H -1 N 0 O 0 + 33.96103 + C 9 Cl 1 H 8 N 1 O 1 + 181.62 + 181.02945 + F + artifact + Cl1Phe + PSI-MOD + MOD:01091 + From DeltaMass: Average Mass: 182 Formula:C9H8O1N1Cl1 Monoisotopic Mass Change:181.029 Average Mass Change:181.623 + monochlorinated L-phenylalanine + + + + + A protein modification that effectively substitutes one hydrogen atom of an L-phenylalanine residue with one chlorine atom. + DeltaMass:233 + + + + + Cl1Phe + + + + + + + + + + modification from DeltaMass + artifact + Mts + PSI-MOD + MOD:01092 + From DeltaMass: Average Mass: 182 + mesitylene-2-sulfonyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + Mts + + + + + + + + + + modification from DeltaMass + C 9 H 16 N 2 O 2 + 184.24 + 184.12119 + K + artifact + PSI-MOD + MOD:01093 + From DeltaMass: Average Mass: 184 Formula: C9H16O2N2 Monoisotopic Mass Change: 184.12 Average Mass Change: 184.24 with no citation. + isopropyl lysyl + + + + + modification from DeltaMass + DeltaMass:236 + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-carboxymethyl-L-lysine. + 58.04 + C 2 H 2 O 2 + 58.005478 + C 8 H 14 N 2 O 3 + 186.21 + 186.10045 + K + artifact + Unimod:6 + Carboxymethyl Lysyl + PSI-MOD + Carboxymethyl + Iodoacetic acid derivative + MOD:01094 + + From DeltaMass:237 (with no citation, formula incorrect, N and O reversed) Average Mass: 186 Formula: C8H14O2N3 Monoisotopic Mass Change: 186.1 Average Mass Change: 186.211 [JSG]. + N6-carboxymethyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-carboxymethyl-L-lysine. + DeltaMass:237 + Unimod:6#K + + + + + Carboxymethyl Lysyl + + + + + + Carboxymethyl + + + + + + Iodoacetic acid derivative + + + + + + + + + Modification from DeltaMass. OBSOLETE because not an amino acid modification. + C 10 H 8 N 1 O 3 + 190.18 + 190.05042 + X + artifact + PSI-MOD + MOD:01095 + From DeltaMass with no citation, formula incorrect, N and O reversed: Formula: C10H8O1N3 Monoisotopic Mass Change: 190.05 Average Mass Change: 190.18. + Matrix alpha cyano MH+ + true + + + + + Modification from DeltaMass. OBSOLETE because not an amino acid modification. + DeltaMass:240 + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-benzyl-L-threonine. + 90.13 + C 7 H 6 + 90.04695 + C 11 H 13 N 1 O 2 + 191.23 + 191.09464 + T + artifact + PSI-MOD + MOD:01096 + O-benzyl-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-benzyl-L-threonine. + DeltaMass:0 + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-benzyl-L-cysteine. + 90.13 + C 7 H 6 + 90.04695 + C 10 H 11 N 1 O 1 S 1 + 193.26 + 193.05614 + C + artifact + PSI-MOD + MOD:01097 + From DeltaMass: misspelled "Benzyl Cystenyl". + S-benzyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-benzyl-L-cysteine. + DeltaMass:242 + + + + + + + + + A protein modification that inserts or replaces a residue with a naphthylalanine. + C 13 H 11 N 1 O 1 + 197.24 + 197.08406 + X + artifact + PSI-MOD + MOD:01098 + From DeltaMass: Average Mass: 197 Formula: C13H11O1N1 Monoisotopic Mass Change: 197.084 Average Mass Change: 197.238. No citation provided. It is not obvious which isomer of naphthylalanine this DeltaMass entry is supposed to represent [JSG]. + naphthylalanine residue + + + + + A protein modification that inserts or replaces a residue with a naphthylalanine. + DeltaMass:243 + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to succinyl beta-aspartyl anhydride. + 82.06 + C 4 H 2 N 0 O 2 + 82.00548 + C 8 H 8 N 1 O 5 + 198.15 + 198.04025 + D + artifact + N-term + succinyl aspartamyl + PSI-MOD + MOD:01099 + From DeltaMass with no citation (name misspelled "aspartamyl", and formula incorrect, N and O reversed) Average Mass: 198 Formula: C8H8O1N5 Monoisotopic Mass Change: 198.04 Average Mass Change: 198.156 [JSG]. + succinyl beta-aspartyl anhydride + + + + + A protein modification that effectively converts an L-aspartic acid residue to succinyl beta-aspartyl anhydride. + DeltaMass:244 + + + + + succinyl aspartamyl + + + + + + + + + + modification from DeltaMass + artifact + PSI-MOD + MOD:01100 + From DeltaMass: Average Mass: 201 with no citation. + HMP (hydroxymethylphenyl)/TFA adduct + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + OBSOLETE because erroneous and apparently redundant to MOD:00111. Remap to MOD:00111. + MOD:00111 + PSI-MOD + MOD:01101 + Modification from DeltaMass: Average Mass: 206. This entry with no other information available appears to be the same as the entry at 204 for "Farnesylation" but with an incorrect mass. + S-Farnesyl- + true + + + + + OBSOLETE because erroneous and apparently redundant to MOD:00111. Remap to MOD:00111. + DeltaMass:0 + + + + + + + + OBSOLETE because redundant and identical to MOD:00504. Remap to MOD:00504. + MOD:00504 + natural + PSI-MOD + MOD:01102 + From DeltaMass: Average Mass: 206 Formula: C14 H22 O1 Monoisotopic Mass Change: 206.167 Average Mass Change: 206.324 References: Neubert TA, Johnson RS, Hurley JB, Walsh KA (1992). The rod transducin alpha subunit amino terminus is heterogeneously fatty acylated. J Biol Chem. 267(26), 18274-7. Notes: Modification of protein N-terminus with (cis,cis-delta 5, delta 8)-tetradecadienoyl group (myristoylation with 2 double bonds) + myristoylation-4H (two double bonds) + true + + + + + OBSOLETE because redundant and identical to MOD:00504. Remap to MOD:00504. + DeltaMass:348 + + + + + + + + OBSOLETE because redundant and identical to MOD:00503. Remap to MOD:00503. + MOD:00503 + natural + PSI-MOD + MOD:01103 + From DeltaMass with no citation or formula: Average Mass: 208. + myristoleylation (one double bond) + true + + + + + OBSOLETE because redundant and identical to MOD:00503. Remap to MOD:00503. + DeltaMass:0 + + + + + + + + + modification from DeltaMass + artifact + Mtr + PSI-MOD + MOD:01104 + From DeltaMass: Average Mass: 212 with no citation. + 4-methoxy-2,3,6-trimethylbenzenesulfonyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + Mtr + + + + + + + + + + modification from DeltaMass + artifact + BrZ + PSI-MOD + MOD:01105 + From DeltaMass: Average Mass: 213 with no citation. + 2-bromobenzyloxycarbonyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + BrZ + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to N-formyl-L-tryptophan. + 28.01 + C 1 H 0 N 0 O 1 + 27.994915 + C 12 H 10 N 2 O 2 + 214.22 + 214.07423 + W + artifact + formyl tryptophanyl + PSI-MOD + MOD:01106 + From DeltaMass with no citation or formula: Average Mass: 214. It is not clear what this is supposed to represent. The mass corresponds to an N-formyl tryptophan (either N2 or N1'), but neither of these modifications has been reported as commonly encountered. It may have been confused with N'-formyl-L-kynurenine, see MOD:00464 [JSG] + N-formyl-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to N-formyl-L-tryptophan. + DeltaMass:0 + + + + + formyl tryptophanyl + + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to O5-benzyl-L-glutamate. + 90.13 + C 7 H 6 + 90.04695 + C 12 H 13 N 1 O 3 + 219.24 + 219.08954 + E + artifact + PSI-MOD + MOD:01107 + From DeltaMass with no citation: (formula incorrect, N and O reversed; mass incorrect, aggregate not delta) Average Mass: 219 Formula: C12H13O1N3 Monoisotopic Mass Change: 219.241 Average Mass Change: 219.09 [JSG]. + O5-benzyl-L-glutamate + + + + + A protein modification that effectively converts an L-glutamic acid residue to O5-benzyl-L-glutamate. + DeltaMass:258 + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to 2-amino-5-(4-methoxyphenyl)-5-oxopentanoic acid, glutamtic acid anisole adduct. + 90.13 + C 7 H 6 + 90.04695 + C 12 H 13 N 1 O 3 + 219.24 + 219.08954 + E + artifact + anisole adducted glutamyl + PSI-MOD + MOD:01108 + From DeltaMass with no citation: (formula incorrect, N and O reversed; mass incorrect, aggregate not delta) Average Mass: 219 Formula: C12H13O1N3 Monoisotopic Mass Change: 219.241 Average Mass Change: 219.09 [JSG]. + 2-amino-5-(4-methoxyphenyl)-5-oxopentanoic acid (Glu) + + + + + A protein modification that effectively converts an L-glutamic acid residue to 2-amino-5-(4-methoxyphenyl)-5-oxopentanoic acid, glutamtic acid anisole adduct. + DeltaMass:259 + + + + + anisole adducted glutamyl + + + + + + + + + + modification from DeltaMass + artifact + PSI-MOD + MOD:01109 + From DeltaMass: Average Mass: 222 with no citation. + 9-fluorenylmethyloxycarbonyl (Fmoc) + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an L-cysteine residue with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20). + C + IpCys + PSI-MOD + MOD:01110 + + isoprenylated cysteine + + + + + A protein modification that effectively replaces a hydrogen atom of an L-cysteine residue with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20). + PubMed:18688235 + + + + + IpCys + + + + + + + + + + A protein modification that effectively substitutes a dimethoxybenzhydryl group for a hydrogen atom. + 226.27 + C 15 H 14 O 2 + 226.09938 + artifact + 4,4'-dimethoxybenzhydryl + Mbh + bis(4-methoxyphenyl)methyl + PSI-MOD + MOD:01111 + From DeltaMass: Average Mass: 226 with no citation. A reagent, typically 4,4'-dimethoxybenzhydryl chloride, used as a protecting group for the carboxamido group of asparagine and glutamine during chemical peptide synthesis [JSG]. + dimethoxybenzhydryl modified residue + + + + + A protein modification that effectively substitutes a dimethoxybenzhydryl group for a hydrogen atom. + DeltaMass:0 + + + + + 4,4'-dimethoxybenzhydryl + + + + + + Mbh + + + + + + bis(4-methoxyphenyl)methyl + + + + + + + + + + modification from DeltaMass + 105.1 + C 6 H 3 N 1 O 1 + 105.02146 + C 12 H 15 N 3 O 2 + 233.27 + 233.11642 + K + artifact + nicotinyl lysyl + PSI-MOD + MOD:01112 + From DeltaMass: (name misspelled "nicotinyl"; formula incorrect, N and O reversed; mass incorrect, aggregate not delta) Average Mass: 233 Formula: C12H15O3N2 Monoisotopic Mass Change: 233.116 Average Mass Change: 233.271 + nicotinoyl lysine + + + + + modification from DeltaMass + DeltaMass:266 + + + + + nicotinyl lysyl + + + + + + + + + + modification from DeltaMass + artifact + Bpoc + PSI-MOD + MOD:01113 + From DeltaMass: Average Mass: 238 with no citation. + 2-(p-biphenyl)isopropyl-oxycarbonyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + Bpoc + + + + + + + + + + modification from DeltaMass + 242.32 + C 19 H 14 + 242.10954 + artifact + Trityl + Trt + PSI-MOD + MOD:01114 + From DeltaMass: Average Mass: 242 Average Mass Change: 242.3 Notes: blocking group used in peptide synthesis for C,H,Q,N + triphenylmethyl + + + + + modification from DeltaMass + DeltaMass:270 + + + + + Trityl + + + + + + Trt + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of an L-tryptophan residue with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20). + W + IpTrp + PSI-MOD + MOD:01115 + isoprenylated tryptophan + + + + + A protein modification that effectively replaces a hydrogen atom of an L-tryptophan residue with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20). + PubMed:18688235 + + + + + IpTrp + + + + + + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine methyl ester. + 218.38 + C 16 H 26 N 0 O 0 S 0 + 218.20345 + C 19 H 32 N 1 O 2 S 1 + 338.53 + 338.21536 + C + natural + C-term + SFarnOMeCys + PSI-MOD + MOD:01116 + + S-farnesyl-L-cysteine methyl ester + + + + + A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine methyl ester. + PubMed:15609361 + RESID:AA0102#var + RESID:AA0105#var + + + + + SFarnOMeCys + + + + + + + + + + modification from DeltaMass + artifact + Pbf + PSI-MOD + MOD:01117 + From DeltaMass: Average Mass: 252 with no citation. + pentamethyldihydrobenzofuransulfonyl + + + + + modification from DeltaMass + DeltaMass:0 + + + + + Pbf + + + + + + + + + + + A protein modification that effectively replaces the N-terminal hydrogen atom of a N-terminal histidine residue with a 6-phosphogluconoyl group linked through a glycosidic bond. modification from DeltaMass + 259.12 + C 6 H 12 O 9 P 1 + 259.02188 + C 12 H 19 N 3 O 10 P 1 + 396.27 + 396.0808 + H + natural + N-term + PSI-MOD + MOD:01118 + Occurs on His-tagged proteins expresssed in E. coli.From DeltaMass: Average Mass: 258 Formula: C6H10O6HPO3 Monoisotopic Mass Change: 258.01 Average Mass Change: 258.12 References: Geoghegan, K. F., H. B. Dixon, et al. (1999). Spontaneous alpha-N-6-phosphogluconoylation of a His tag in Escherichia coli: the cause of extra mass of 258 or 178 Da in fusion proteins. Anal Biochem 267(1): 169-84. Mass is one Da higher because this is an N-terminal modification + alpha-N-6-phosphogluconoylated L-histidine + + + + + A protein modification that effectively replaces the N-terminal hydrogen atom of a N-terminal histidine residue with a 6-phosphogluconoyl group linked through a glycosidic bond. modification from DeltaMass + DeltaMass:275 + PubMed:9918669 + + + + + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine methyl ester. + 286.5 + C 21 H 34 N 0 O 0 S 0 + 286.26605 + C 24 H 40 N 1 O 2 S 1 + 406.65 + 406.27798 + C + natural + C-term + SGergerOMeCys + PSI-MOD + MOD:01119 + + S-geranylgeranyl-L-cysteine methyl ester + + + + + A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine methyl ester. + PubMed:1483450 + PubMed:15609361 + RESID:AA0104#var + RESID:AA0105#var + + + + + SGergerOMeCys + + + + + + + + + + A protein modification that is produced by formation of an adduct with 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride, Pmc chloride. + 266.36 + C 14 H 18 O 3 S 1 + 266.09766 + X + artifact + 2,2,5,7,8-pentamethyl-3,4-dihydro-2H-chromene-6-sulfonyl + 2,2,5,7,8-pentamethyl-6-chromansulfonyl + 2,2,5,7,8-pentamethyl-chromane-6-sulfonyl + 2,2,5,7,8-pentamethylchroman-6-sulfonyl + 2,2,5,7,8-pentamethylchroman-6-sulphonyl + 3,4-dihydro-2,2,5,7,8-pentamethyl-2H-1-benzopyran-6-sulfonyl + Pmc + PmcRes + PSI-MOD + MOD:01120 + From DeltaMass: Average Mass: 266 Notes: blocking group for Arg in peptide synthesis. CAS:112160-39-1 [JSG]. + 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride derivatized residue + + + + + A protein modification that is produced by formation of an adduct with 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride, Pmc chloride. + DeltaMass:0 + + + + + 2,2,5,7,8-pentamethyl-3,4-dihydro-2H-chromene-6-sulfonyl + + + + + + 2,2,5,7,8-pentamethyl-6-chromansulfonyl + + + + + + 2,2,5,7,8-pentamethyl-chromane-6-sulfonyl + + + + + + 2,2,5,7,8-pentamethylchroman-6-sulfonyl + + + + + + 2,2,5,7,8-pentamethylchroman-6-sulphonyl + + + + + + 3,4-dihydro-2,2,5,7,8-pentamethyl-2H-1-benzopyran-6-sulfonyl + + + + + + Pmc + + + + + + PmcRes + + + + + + + + + + modification from DeltaMass + artifact + Mmt + PSI-MOD + MOD:01121 + From DeltaMass: Average Mass: 272 Average Mass Change: 272 + monomethoxytrityl + + + + + modification from DeltaMass + DeltaMass:280 + + + + + Mmt + + + + + + + + + OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass + PSI-MOD + MOD:01122 + From DeltaMass: Average Mass: 289 with no citation. + 5'phos dCytidinyl + true + + + + + OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass + DeltaMass:0 + + + + + + + + OBSOLETE because redundant and identical to MOD:01123. Remap to MOD:01123. + MOD:01123 + Y + PSI-MOD + MOD:01123 + From DeltaMass: Average Mass: 289 + monoiodated tyrosine + true + + + + + OBSOLETE because redundant and identical to MOD:01123. Remap to MOD:01123. + DeltaMass:0 + + + + + + + + + modification from DeltaMass + 162.14 + C 6 H 10 N 0 O 5 + 162.05283 + C 12 H 22 N 2 O 6 + 290.32 + 290.1478 + K + PSI-MOD + MOD:01124 + From DeltaMass: (formula incorrect, N and O reversed; mass incorrect, aggregate not delta) Average Mass: 290 Formula: C12H22O2N6 Monoisotopic Mass Change: 290.148 Average Mass Change: 290.317 + aldohexosyl lysyl + + + + + modification from DeltaMass + DeltaMass:285 + + + + + + + + OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass + PSI-MOD + MOD:01125 + From DeltaMass: Average Mass: 304 with no citation. + 5'phos dThymidinyl + true + + + + + OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass + DeltaMass:0 + + + + + + + + OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass + PSI-MOD + MOD:01126 + From DeltaMass: Average Mass: 305 with no citation. + 5'phos Cytidinyl + true + + + + + OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass + DeltaMass:0 + + + + + + + + OBSOLETE because redundant and identical to MOD:01166. Remap to MOD:01166. + MOD:01166 + PSI-MOD + MOD:01127 + From DeltaMass: Average Mass: 306 Formula: C9H11O2N8P1 Monoisotopic Mass Change: 306.025 Average Mass Change: 306.17 + 5'phos Uridinyl + true + + + + + OBSOLETE because redundant and identical to MOD:01166. Remap to MOD:01166. + DeltaMass:292 + + + + + + + + + modification from DeltaMass + NeuGc + PSI-MOD + MOD:01128 + From DeltaMass: Average Mass: 307 with no citation. + N-glycolneuraminic acid + + + + + modification from DeltaMass + DeltaMass:0 + + + + + NeuGc + + + + + + + + + OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass + PSI-MOD + MOD:01129 + From DeltaMass: Average Mass: 313 Formula: C10H12O5N5P1 Monoisotopic Mass Change: 313.058 Average Mass Change: 313.211 + 5'phos dAdenosyl + true + + + + + OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass + DeltaMass:295 + + + + + + + + + modification from DeltaMass + artifact + PSI-MOD + MOD:01130 + From DeltaMass: Average Mass: 327 Formula: C17H17O3N4 Monoisotopic Mass Change: 327.122 Average Mass Change: 327.342 + SucPhencarb Lysyl + + + + + modification from DeltaMass + DeltaMass:297 + + + + + + + + OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass + PSI-MOD + MOD:01131 + From DeltaMass: Average Mass: 329 + 5'phos dGuanosyl + true + + + + + OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass + DeltaMass:0 + + + + + + + + OBSOLETE because redundant and identical to MOD:01165. Remap to MOD:01165. + MOD:01165 + PSI-MOD + MOD:01132 + From DeltaMass: Average Mass: 329 + 5'phos Adenosinyl + true + + + + + OBSOLETE because redundant and identical to MOD:01165. Remap to MOD:01165. + DeltaMass:0 + + + + + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine methyl ester. + 234.38 + C 16 H 26 N 0 O 1 S 0 + 234.19836 + C 19 H 32 N 1 O 3 S 1 + 354.53 + 354.2103 + C + natural + C-term + S12HyFarnOMeCys + PSI-MOD + MOD:01133 + S-12-hydroxyfarnesyl-L-cysteine methyl ester + + + + + A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine methyl ester. + PubMed:17790543 + RESID:AA0103#var + RESID:AA0105#var + + + + + S12HyFarnOMeCys + + + + + + + + + + modification from DeltaMass + artifact + PSI-MOD + MOD:01134 + From DeltaMass: Average Mass: 359 Formula: C21H11O6 Monoisotopic Mass Change: 359.055 Average Mass Change: 359.315 Notes: Using the DHB matrix at low pH the carboxyl group and one of the oxygens on the flurorescein molecule are protinated so the delta mass is 2Da higher than most text book illustrations would indicate. See Bioconjugate Techniques by Greg Hermanson, Academic Press, page 305, figure 204. Text books of course just show the coupling reaction at neutral or basic pH. + fluorescein labelling of peptide N-terminal using NHS ester + + + + + modification from DeltaMass + DeltaMass:306 + + + + + + + + + modification from DeltaMass + PSI-MOD + MOD:01135 + From DeltaMass: Average Mass: 365 with no citation. + Hex-HexNAc + + + + + modification from DeltaMass + DeltaMass:0 + + + + + + + + OBSOLETE because this is a small molecule contaminant and not a modification to a polypeptide. modification from DeltaMass + artifact + PSI-MOD + MOD:01136 + From DeltaMass: Average Mass: 391 Average Mass Change: 391 Notes: A common plasticizer, and, unfortunaltely, a common contaminate. A sodium adduct is often associated with this peak at 413. + dioctyl phthalate + true + + + + + OBSOLETE because this is a small molecule contaminant and not a modification to a polypeptide. modification from DeltaMass + DeltaMass:309 + + + + + + + + + + A protein modification that is produced by reaction of a lysine residue with 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride, Pmc chloride, to form N6-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-lysine. + 266.36 + C 14 H 18 O 3 S 1 + 266.09766 + C 20 H 30 N 2 O 4 S 1 + 394.53 + 394.19263 + K + artifact + PMC lysyl + PmcLys + PSI-MOD + MOD:01137 + From DeltaMass: Average Mass: Formula: C20H30O2N4S1 Monoisotopic Mass Change: 394.192 Average Mass Change: 394.534 + N6-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-lysine + + + + + A protein modification that is produced by reaction of a lysine residue with 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride, Pmc chloride, to form N6-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-lysine. + DeltaMass:310 + + + + + PMC lysyl + + + + + + PmcLys + + + + + + + + + OBSOLETE because no evidence has been seen for this protein modification. modification from DeltaMass + C + artifact + PSI-MOD + MOD:01138 + [probably aminoethyldansyl, JSG] From DeltaMass: (name misspelled "Aedans Cystenyl", and formula incorrect, N and O reversed) Average Mass: 409 Abbreviation: Aedans-Cys Formula: C17H19O3N5S2 Monoisotopic Mass Change: 409.077 Average Mass Change: 409.482 + Aedans Cystenyl + true + + + + + OBSOLETE because no evidence has been seen for this protein modification. modification from DeltaMass + DeltaMass:311 + + + + + + + + OBSOLETE because this is a MS contaminant, not a known modification to a polypeptide. modification from DeltaMass + artifact + PSI-MOD + MOD:01139 + From DeltaMass: Mass: Average Mass Change: 413 Notes: A common plasticizer, and, unfortunaltely, a common contaminate. A sodium adduct is often associated with this peak at 413. + dioctyl phthalate sodium adduct + true + + + + + OBSOLETE because this is a MS contaminant, not a known modification to a polypeptide. modification from DeltaMass + DeltaMass:312 + + + + + + + + + + A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two iodine atoms. + 251.79 + C 0 H -2 I 2 N 0 O 0 + 251.79329 + C 9 H 7 I 2 N 1 O 2 + 414.97 + 414.85663 + Y + natural + Unimod:130 + 3,5-Diiodination (of Tyrosine) + I2Tyr + diiodinationy + PSI-MOD + Diiodo + di-Iodination + MOD:01140 + + diiodinated tyrosine + + + + + A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two iodine atoms. + DeltaMass:0 + OMSSA:35 + PubMed:15627961 + Unimod:130#Y + + + + + 3,5-Diiodination (of Tyrosine) + + + + + + I2Tyr + + + + + + diiodinationy + + + + + + Diiodo + + + + + + di-Iodination + + + + + + + + + + + A protein modification that is produced by reaction with 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride, Pmc chloride, to form omega-N-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-arginine. + 266.36 + C 14 H 18 O 3 S 1 + 266.09766 + C 20 H 30 N 4 O 4 S 1 + 422.54 + 422.19876 + R + artifact + PMC arginyl + PmcArg + PSI-MOD + MOD:01141 + From DeltaMass: Average Mass: Formula: C20H30O4N4S1 Monoisotopic Mass Change: 422.199 Average Mass Change: 422.547 + omega-N-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-arginine + + + + + A protein modification that is produced by reaction with 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride, Pmc chloride, to form omega-N-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-arginine. + DeltaMass:314 + + + + + PMC arginyl + + + + + + PmcArg + + + + + + + + + + + A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound 15,16-dihydrobiliverdin. + 584.67 + C 33 H 36 N 4 O 6 S 0 + 584.2635 + C 36 H 41 N 5 O 7 S 1 + 687.81 + 687.27264 + C + natural + (16R)-18-ethenyl-8,12-bis(2-carboxyethyl)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,7,13,17-tetramethyl-15,16-dihydrobilin-1,19(21H,24H)-dione + 15,16-Dhbv + 15,16-dihydrobiliverdin IXalpha + 15,16-dihydrobiliverdin cysteine adduct + 18-ethenyl-8,12-bis(2-carboxyethyl)-3-(2-(cysteinyl-S)-ethyl)-2,7,13,17-tetramethylbiladiene-ab-1,19(16H,21H)-dione + 3'-cysteinyl-15,16-dihydrobiliverdin + 3alpha-cysteinyl-15,16-dihydrobiliverdin + BINDING 15,16-dihydrobiliverdin (covalent; via 1 link) + DBV + S-15,16-dihydrobiliverdin-L-cysteine + PSI-MOD + MOD:01142 + S-15,16-dihydrobiliverdin-L-cysteine + + + + + A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound 15,16-dihydrobiliverdin. + PubMed:10430868 + PubMed:15504407 + PubMed:1559975 + PubMed:3208761 + RESID:AA0428 + + + + + (16R)-18-ethenyl-8,12-bis(2-carboxyethyl)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,7,13,17-tetramethyl-15,16-dihydrobilin-1,19(21H,24H)-dione + + + + + + 15,16-Dhbv + + + + + + 15,16-dihydrobiliverdin IXalpha + + + + + + 15,16-dihydrobiliverdin cysteine adduct + + + + + + 18-ethenyl-8,12-bis(2-carboxyethyl)-3-(2-(cysteinyl-S)-ethyl)-2,7,13,17-tetramethylbiladiene-ab-1,19(16H,21H)-dione + + + + + + 3'-cysteinyl-15,16-dihydrobiliverdin + + + + + + 3alpha-cysteinyl-15,16-dihydrobiliverdin + + + + + + BINDING 15,16-dihydrobiliverdin (covalent; via 1 link) + + + + + + DBV + + + + + + S-15,16-dihydrobiliverdin-L-cysteine + + + + + + + + + + + A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound 15,16-dihydrobiliverdin. + 584.67 + C 33 H 36 N 4 O 6 S 0 + 584.2635 + C 39 H 46 N 6 O 8 S 2 + 790.95 + 790.28186 + C, C + natural + (16R)-8,12-bis(2-carboxyethyl)-3-[2-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-18-[(1Xi)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,7,13,17-tetramethyl-15,16-dihydrobilin-1,19(21H,24H)-dione + 15,16-Dhbv + 15,16-dihydrobiliverdin IXalpha + 15,16-dihydrobiliverdin cysteine adduct + 15,16-dihydrobiliverdin-bis-L-cysteine + 3'',18'-biscysteinyl-15,16-dihydrobiliverdin + 3beta,18alpha-biscysteinyl-15,16-dihydrobiliverdin + 8,12-bis(2-carboxyethyl)-3-(2-(cysteinyl-S)-ethyl)-18-(1-(cysteinyl-S)-ethyl)-2,7,13,17-tetramethylbiladiene-ab-1,19(16H,21H)-dione + BINDING 15,16-dihydrobiliverdin (covalent; via 2 links) + DBV + PSI-MOD + MOD:01143 + Cross-link 2. + 15,16-dihydrobiliverdin-bis-L-cysteine + + + + + A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound 15,16-dihydrobiliverdin. + PubMed:1559975 + PubMed:2222853 + PubMed:3208761 + PubMed:8420941 + RESID:AA0429 + + + + + (16R)-8,12-bis(2-carboxyethyl)-3-[2-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-18-[(1Xi)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,7,13,17-tetramethyl-15,16-dihydrobilin-1,19(21H,24H)-dione + + + + + + 15,16-Dhbv + + + + + + 15,16-dihydrobiliverdin IXalpha + + + + + + 15,16-dihydrobiliverdin cysteine adduct + + + + + + 15,16-dihydrobiliverdin-bis-L-cysteine + + + + + + 3'',18'-biscysteinyl-15,16-dihydrobiliverdin + + + + + + 3beta,18alpha-biscysteinyl-15,16-dihydrobiliverdin + + + + + + 8,12-bis(2-carboxyethyl)-3-(2-(cysteinyl-S)-ethyl)-18-(1-(cysteinyl-S)-ethyl)-2,7,13,17-tetramethylbiladiene-ab-1,19(16H,21H)-dione + + + + + + BINDING 15,16-dihydrobiliverdin (covalent; via 2 links) + + + + + + DBV + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine. + 550.91 + C 35 H 66 N 0 O 4 S 0 + 550.4961 + C 38 H 71 N 1 O 5 S 1 + 654.05 + 653.5053 + C + natural + S-(sn-1-Dipalmitoyl-glyceryl)- (on Cysteine) + PSI-MOD + MOD:01144 + + From DeltaMass: Average Mass: 524 + S-(sn-1-2,3-dipalmitoylglycerol)-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine. + DeltaMass:0 + PubMed:10896212 + PubMed:4575979 + PubMed:9056182 + RESID:AA0107#var + + + + + S-(sn-1-Dipalmitoyl-glyceryl)- (on Cysteine) + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to N-tau-(ADP-ribosyl)diphthamide. + 684.51 + C 22 H 36 N 7 O 14 P 2 + 684.179 + 1+ + C 28 H 43 N 10 O 15 P 2 + 821.65 + 821.2379 + H + natural + uniprot.ptm:PTM-0672 + MOD_RES ADP-ribosyldiphthamide + PSI-MOD + MOD:01145 + From DeltaMass: (name misspelled "N theta -(ADP-ribosyl) diphthamide (of Histidine)") Average Mass: 648 + N-tau-(ADP-ribosyl)diphthamide + + + + + A protein modification that effectively converts an L-histidine residue to N-tau-(ADP-ribosyl)diphthamide. + ChEBI:82697 + DeltaMass:0 + + + + + MOD_RES ADP-ribosyldiphthamide + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-(6-FAD)-L-cystine. + 783.54 + C 27 H 31 N 9 O 15 P 2 S 0 + 783.1415 + C 30 H 36 N 10 O 16 P 2 S 1 + 886.68 + 886.1507 + C + hypothetical + S6FADCys + PSI-MOD + FAD + MOD:01146 + + From DeltaMass: Average Mass: 784 with no citation. This modification has not been reported [JSG]. + S-(6-FAD)-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-(6-FAD)-L-cystine. + DeltaMass:0 + + + + + S6FADCys + + + + + + FAD + + + + + + + + + + + modification from DeltaMass + 1038.95 + C 40 H 66 N 2 O 29 + 1038.3751 + C 44 H 72 N 4 O 31 + 1153.06 + 1152.4181 + N + natural + GNO:G20956ZV + Unimod:1761 + PSI-MOD + MOD:01147 + From DeltaMass: Average Mass: 1,039 + dHex1Hex3HexNAc2 N4-glycosylated asparagine + + + + + modification from DeltaMass + DeltaMass:0 + Unimod:1761 + + + + + + + + + + + + + + + + + A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a ubiquitin. + K + natural + PSI-MOD + MOD:01148 + + ubiquitinylated lysine + + + + + A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a ubiquitin. + PubMed:11125103 + PubMed:18688235 + + + + + + + + + + + + + + + + + A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a sumo (Small Ubiquitin-related MOdifier) protein. + K + natural + PSI-MOD + MOD:01149 + + sumoylated lysine + + + + + A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a sumo (Small Ubiquitin-related MOdifier) protein. + PubMed:12612601 + PubMed:18688235 + + + + + + + + + + + + + + + + + A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a nedd8 protein. + K + natural + PSI-MOD + MOD:01150 + + neddylated lysine + + + + + A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a nedd8 protein. + PubMed:11125103 + PubMed:12612601 + PubMed:18688235 + + + + + + + + + Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid phosphorylated residue with a secondary loss of a neutral trihydrogen phosphate molecular fragment. + -97.99 + C 0 H -3 N 0 O -4 P -1 + -97.9769 + X + artifact + PSI-MOD + MOD:01151 + + phosphorylated residue with neutral loss of phosphate + + + + + Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid phosphorylated residue with a secondary loss of a neutral trihydrogen phosphate molecular fragment. + PubMed:18688235 + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a carboxylic acid group. + 44.01 + C 1 H 0 N 0 O 2 + 43.98983 + X + Unimod:299 + PSI-MOD + Carboxy + Carboxylation + MOD:01152 + + carboxylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with a carboxylic acid group. + Unimod:299 + + + + + Carboxy + + + + + + Carboxylation + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an methylsulfanyl group (thiomethyl group). + 46.09 + C 1 H 2 N 0 O 0 S 1 + 45.98772 + X + Unimod:39 + PSI-MOD + Beta-methylthiolation + Methylthio + MOD:01153 + + methylthiolated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an methylsulfanyl group (thiomethyl group). + Unimod:39 + + + + + Beta-methylthiolation + + + + + + Methylthio + + + + + + + + + + + A protein modification that effectively converts a source amino acid to pyruvic acid. + C 3 H 3 O 2 + 71.06 + 71.013306 + X + N-term + 2-oxopropanoic acid + MOD_RES Pyruvic acid (Cys) + MOD_RES Pyruvic acid (Ser) + pyruvic acid + PSI-MOD + MOD:01154 + + pyruvic acid + + + + + A protein modification that effectively converts a source amino acid to pyruvic acid. + PubMed:10085076 + PubMed:3042771 + PubMed:8464063 + RESID:AA0127 + + + + + 2-oxopropanoic acid + + + + + + MOD_RES Pyruvic acid (Cys) + + + + + + MOD_RES Pyruvic acid (Ser) + + + + + + pyruvic acid + + + + + + + + + + A protein modification that effectively results from forming an adduct with a compound containing a lipid-like group either through acylation, alkylation, or amidation. + PSI-MOD + MOD:01155 + + lipoconjugated residue + + + + + A protein modification that effectively results from forming an adduct with a compound containing a lipid-like group either through acylation, alkylation, or amidation. + PubMed:18688235 + + + + + + + + + Modified amino acid residue derived from a natural amino acid by a real or hypothetical chemical process. + PSI-MOD + MOD:01156 + + protein modification categorized by chemical process + + + + + Modified amino acid residue derived from a natural amino acid by a real or hypothetical chemical process. + PubMed:18688235 + + + + + + + + + A protein modification considered either as modified amino acid residues derived from natural amino acids, as a replacement by another natural amino acid, or as a replacement by an unnatural amino acid. + PSI-MOD + MOD:01157 + + protein modification categorized by amino acid modified + + + + + A protein modification considered either as modified amino acid residues derived from natural amino acids, as a replacement by another natural amino acid, or as a replacement by an unnatural amino acid. + PubMed:18688235 + + + + + + + + + + + + + + + + A protein modification that modifies an L-selenocysteine residue. + U + PSI-MOD + MOD:01158 + + modified L-selenocysteine residue + + + + + A protein modification that modifies an L-selenocysteine residue. + PubMed:18688235 + + + + + + + + + A protein modification that effectively attaches a residue to murein peptidoglycan by either a pentaglycine linker peptide or a peptide-like L-alanyl-D-glutamyl-2,6-diaminopimelic acid linkage. + X + natural + PSI-MOD + MOD:01159 + peptidoglycanated residue + + + + + A protein modification that effectively attaches a residue to murein peptidoglycan by either a pentaglycine linker peptide or a peptide-like L-alanyl-D-glutamyl-2,6-diaminopimelic acid linkage. + PubMed:18688235 + + + + + + + + + A protein modification that effectively results in the loss of an ammonia, usually by a process of vicinal dehydration, rearrangement, and rehydration with release of ammonia, resulting in a loss of nitrogen with no gain of oxygen. + -17.03 + C 0 H -3 N -1 O 0 + -17.026548 + X + Unimod:385 + PSI-MOD + Ammonia-loss + Loss of ammonia + MOD:01160 + + deaminated residue + + + + + A protein modification that effectively results in the loss of an ammonia, usually by a process of vicinal dehydration, rearrangement, and rehydration with release of ammonia, resulting in a loss of nitrogen with no gain of oxygen. + Unimod:385 + + + + + Ammonia-loss + + + + + + Loss of ammonia + + + + + + + + + + A protein modification that effectively removes oxygen atoms from a residue without the removal of hydrogen atoms. + -16.0 + C 0 H 0 N 0 O -1 + -15.994915 + X + Unimod:447 + dOxyRes + PSI-MOD + Deoxy + reduction + MOD:01161 + + deoxygenated residue + + + + + A protein modification that effectively removes oxygen atoms from a residue without the removal of hydrogen atoms. + PubMed:14235557 + Unimod:447 + + + + + dOxyRes + + + + + + Deoxy + + + + + + reduction + + + + + + + + + + modification from Unimod N-linked glycosylation + 1769.62 + C 68 H 112 N 4 O 49 + 1768.6395 + C 72 H 118 N 6 O 51 + 1883.73 + 1882.6825 + N + natural + GNO:G83555HU + Unimod:308 + PSI-MOD + Fucosylated biantennary + dHex(1)Hex(5)HexNAc(4) + MOD:01162 + fucosylated biantennary + + + + + modification from Unimod N-linked glycosylation + Unimod:308 + + + + + Fucosylated biantennary + + + + + + dHex(1)Hex(5)HexNAc(4) + + + + + + + + + + A protein modification that effectively crosslinks an amino acid residue and 5'-phosphoguanosine through either a phosphodiester or a phosphoramide bond. + 345.21 + C 10 H 12 N 5 O 7 P 1 + 345.04742 + X + Unimod:413 + 5'phos Guanosyl + PSI-MOD + Phosphoguanosine + phospho-guanosine + MOD:01163 + From DeltaMass: (formula incorrect, N and O reversed) Average Mass: 345 Formula: C10H12O5N7P1 Monoisotopic Mass Change: 345.047 Average Mass Change: 345.209. + guanylated residue + + + + + A protein modification that effectively crosslinks an amino acid residue and 5'-phosphoguanosine through either a phosphodiester or a phosphoramide bond. + DeltaMass:304 + Unimod:413 + + + + + 5'phos Guanosyl + + + + + + Phosphoguanosine + + + + + + phospho-guanosine + + + + + + + + + + A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through a phosphodiester bond. + 438.33 + C 17 H 19 N 4 O 8 P 1 + 438.09406 + X + Unimod:442 + PSI-MOD + FMN + O3-(riboflavin phosphoryl) + MOD:01164 + + riboflavin-phosphorylated residue + + + + + A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through a phosphodiester bond. + Unimod:442 + + + + + FMN + + + + + + O3-(riboflavin phosphoryl) + + + + + + + + + + A protein modification that effectively crosslinks an amino acid residue and 5'-phosphoadenosine through either a phosphodiester or a phosphoramide bond. + 329.21 + C 10 H 12 N 5 O 6 P 1 + 329.05252 + X + Unimod:405 + 5'phos Adenosinyl + PSI-MOD + AMP binding site + Phosphoadenosine + MOD:01165 + + From DeltaMass: (name misspelled "5'phos adenosinyl") Average Mass: 329 + adenylated residue + + + + + A protein modification that effectively crosslinks an amino acid residue and 5'-phosphoadenosine through either a phosphodiester or a phosphoramide bond. + DeltaMass:0 + Unimod:405 + + + + + 5'phos Adenosinyl + + + + + + AMP binding site + + + + + + Phosphoadenosine + + + + + + + + + + A protein modification that effectively crosslinks an amino acid residue and 5'-phosphouridine through either a phosphodiester or a phosphoramide bond. + 306.17 + C 9 H 11 N 2 O 8 P 1 + 306.0253 + X + Unimod:417 + 5'phos Uridinyl + PSI-MOD + PhosphoUridine + uridine phosphodiester + MOD:01166 + From DeltaMass: (name misspelled "5'phos Uridinyl" and formula incorrect, N and O reversed) Average Mass: 306 Formula: C9H11O2N8P1 Monoisotopic Mass Change: 306.025 Average Mass Change: 306.17 + uridylated residue + + + + + A protein modification that effectively crosslinks an amino acid residue and 5'-phosphouridine through either a phosphodiester or a phosphoramide bond. + DeltaMass:292 + Unimod:417 + + + + + 5'phos Uridinyl + + + + + + PhosphoUridine + + + + + + uridine phosphodiester + + + + + + + + + + modification from Unimod + 1572.02 + C 40 H 47 Mo 1 N 20 O 26 P 4 S 4 + 1572.9857 + X + Unimod:424 + PSI-MOD + MolybdopterinGD + molybdenum bis(molybdopterin guanine dinucleotide) + MOD:01167 + molybdopterin guanine dinucleotide + + + + + modification from Unimod + Unimod:424 + + + + + MolybdopterinGD + + + + + + molybdenum bis(molybdopterin guanine dinucleotide) + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to dehydroalanine. + C 3 H 3 N 1 O 1 + 69.06 + 69.02146 + X + natural + 2,3-didehydroalanine + 2-aminoacrylic acid + 2-aminopropenoic acid + 4-methylidene-imidazole-5-one (MIO) active site + Dha + MOD_RES 2,3-didehydroalanine (Cys) + MOD_RES 2,3-didehydroalanine (Ser) + anhydroserine + dHAla + dehydroalanine + PSI-MOD + MOD:01168 + + dehydroalanine + + + + + A protein modification that effectively converts a source amino acid residue to dehydroalanine. + PubMed:10220322 + PubMed:1547888 + PubMed:1815586 + PubMed:2914619 + PubMed:6838602 + PubMed:7947813 + PubMed:8239649 + RESID:AA0181 + + + + + 2,3-didehydroalanine + + + + + + 2-aminoacrylic acid + + + + + + 2-aminopropenoic acid + + + + + + 4-methylidene-imidazole-5-one (MIO) active site + + + + + + Dha + + + + + + MOD_RES 2,3-didehydroalanine (Cys) + + + + + + MOD_RES 2,3-didehydroalanine (Ser) + + + + + + anhydroserine + + + + + + dHAla + + + + + + dehydroalanine + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to L-oxoalanine. + C 3 H 3 N 1 O 2 + 85.06 + 85.01638 + X + natural + (S)-2-amino-3-oxopropanoic acid + 2-amino-3-oxopropionic acid + L-3-oxoalanine + L-amino-malonic acid semialdehyde + L-aminomalonaldehydic acid + MOD_RES 3-oxoalanine (Cys) + MOD_RES 3-oxoalanine (Ser) + PSI-MOD + C(alpha)-formylglycine + L-serinesemialdehyde + MOD:01169 + + L-3-oxoalanine + + + + + A protein modification that effectively converts a source amino acid residue to L-oxoalanine. + DeltaMass:349 + PubMed:14563551 + PubMed:7628016 + PubMed:8681943 + PubMed:9478923 + RESID:AA0185 + + + + + (S)-2-amino-3-oxopropanoic acid + + + + + + 2-amino-3-oxopropionic acid + + + + + + L-3-oxoalanine + + + + + + L-amino-malonic acid semialdehyde + + + + + + L-aminomalonaldehydic acid + + + + + + MOD_RES 3-oxoalanine (Cys) + + + + + + MOD_RES 3-oxoalanine (Ser) + + + + + + C(alpha)-formylglycine + + + + + + L-serinesemialdehyde + + + + + + + + + + A protein modification that effectively forms a 2-ketoimine of pyruvicacid with a residue amino group. + 70.05 + C 3 H 2 N 0 O 2 + 70.00548 + X + N-term + Unimod:422 + PSI-MOD + N-pyruvic acid 2-iminyl + PyruvicAcidIminyl + MOD:01170 + pyruvic acid iminylated residue + + + + + A protein modification that effectively forms a 2-ketoimine of pyruvicacid with a residue amino group. + Unimod:422 + + + + + N-pyruvic acid 2-iminyl + + + + + + PyruvicAcidIminyl + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-acetyl-L-threonine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + C 6 H 9 N 1 O 3 + 143.14 + 143.05824 + T + natural + Unimod:1 + uniprot.ptm:PTM-0233 + (2S,3R)-3-(acetyloxy)-2-aminobutanoic acid + ACT_SITE O-acetylthreonine intermediate + MOD_RES O-acetylthreonine + O-acetyl-L-threonine + O-acetylthreonine + OAcThr + threonine acetate ester + PSI-MOD + Acetylation + MOD:01171 + + O-acetyl-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-acetyl-L-threonine. + PubMed:16728640 + RESID:AA0423 + Unimod:1#T + + + + + (2S,3R)-3-(acetyloxy)-2-aminobutanoic acid + + + + + + ACT_SITE O-acetylthreonine intermediate + + + + + + MOD_RES O-acetylthreonine + + + + + + O-acetyl-L-threonine + + + + + + O-acetylthreonine + + + + + + OAcThr + + + + + + threonine acetate ester + + + + + + Acetylation + + + + + + + + + + + A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylsphingolipidinositolethanolamine. + 123.05 + C 2 H 6 N 1 O 3 P 1 + 123.00853 + C 5 H 12 N 2 O 5 P 1 + 211.13 + 211.04839 + A + hypothetical + C-term + uniprot.ptm:PTM-0144 + GSIAla + LIPID GPI-like-anchor amidated alanine + N-alanyl-glycosylsphingolipidinositolethanolamine + PSI-MOD + MOD:01172 + N-alanyl-glycosylsphingolipidinositolethanolamine + + + + + A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylsphingolipidinositolethanolamine. + PubMed:12626404 + RESID:AA0424 + + + + + GSIAla + + + + + + LIPID GPI-like-anchor amidated alanine + + + + + + N-alanyl-glycosylsphingolipidinositolethanolamine + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylsphingolipidinositolethanolamine. + 123.05 + C 2 H 6 N 1 O 3 P 1 + 123.00853 + C 6 H 13 N 3 O 6 P 1 + 254.16 + 254.0542 + N + hypothetical + C-term + uniprot.ptm:PTM-0145 + GSIAsn + LIPID GPI-like-anchor amidated asparagine + N-asparaginyl-glycosylsphingolipidinositolethanolamine + PSI-MOD + MOD:01173 + N-asparaginyl-glycosylsphingolipidinositolethanolamine + + + + + A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylsphingolipidinositolethanolamine. + PubMed:12626404 + RESID:AA0425 + + + + + GSIAsn + + + + + + LIPID GPI-like-anchor amidated asparagine + + + + + + N-asparaginyl-glycosylsphingolipidinositolethanolamine + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)-L-cysteine. + 316.44 + C 20 H 28 N 0 O 3 S 0 + 316.20386 + C 23 H 33 N 1 O 4 S 1 + 419.58 + 419.21304 + C + natural + uniprot.ptm:PTM-0447 + (2R)-2-amino-3-([(5Z,9Xi,12E,14Z)-1-hydroxy-1,11-oxoprosta-5,12,14-trien-9-yl]sulfanyl)propanoic acid + (5Z,9Xi,12E,14Z)-9-([(2R)-2-amino-3-carboxyethyl]sulfanyl)-11-oxoprosta-5,12,14-trien-1-oic acid + LIPID S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine + PG-J2Cys + S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)-L-cysteine + PSI-MOD + MOD:01174 + S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)-L-cysteine. + ChEBI:27485 + PubMed:11466314 + PubMed:12684535 + RESID:AA0426 + + + + + (2R)-2-amino-3-([(5Z,9Xi,12E,14Z)-1-hydroxy-1,11-oxoprosta-5,12,14-trien-9-yl]sulfanyl)propanoic acid + + + + + + (5Z,9Xi,12E,14Z)-9-([(2R)-2-amino-3-carboxyethyl]sulfanyl)-11-oxoprosta-5,12,14-trien-1-oic acid + + + + + + LIPID S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine + + + + + + PG-J2Cys + + + + + + S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)-L-cysteine + + + + + + + + + + + A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycourobilin. + 586.69 + C 33 H 38 N 4 O 6 S 0 + 586.2791 + C 36 H 43 N 5 O 7 S 1 + 689.83 + 689.2883 + C + natural + (2S,3R,16R)-18-ethenyl-3-[(1R)-1-([(R)-2-amino-2-carboxyethyl]sulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-4,5,15,16-tetrahydrobiline-1,19(21H,22H,24H)-dione + 18-ethenyl-3-[1-(2-amino-2-carboxyethylsulfanyl)ethyl]-2,3,15,16-dihydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid + BINDING Phycourobilin chromophore (covalent; via 1 link) + PUB + PUBCys + S-phycourobilin-L-cysteine + phycourobilin cysteine adduct + PSI-MOD + MOD:01175 + S-phycourobilin-L-cysteine + + + + + A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycourobilin. + PubMed:1903388 + PubMed:3208761 + PubMed:3838747 + RESID:AA0427 + + + + + (2S,3R,16R)-18-ethenyl-3-[(1R)-1-([(R)-2-amino-2-carboxyethyl]sulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-4,5,15,16-tetrahydrobiline-1,19(21H,22H,24H)-dione + + + + + + 18-ethenyl-3-[1-(2-amino-2-carboxyethylsulfanyl)ethyl]-2,3,15,16-dihydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid + + + + + + BINDING Phycourobilin chromophore (covalent; via 1 link) + + + + + + PUB + + + + + + PUBCys + + + + + + S-phycourobilin-L-cysteine + + + + + + phycourobilin cysteine adduct + + + + + + + + + + + A protein modification that effectively cross-links an L-lysine residue and an L-lysine residue converted to allysine with a carbon-nitrogen bond to form L-dehydrolysinonorleucine. + -19.05 + C 0 H -5 N -1 O 0 + -19.042198 + C 12 H 19 N 3 O 2 + 237.3 + 237.14772 + K, K + natural + (2S)-2-amino-6-([(5S)-5-amino-5-carboxypentylidene]amino)hexanoic acid + 6-(N6-L-didehydrolysino)-L-norleucine + CROSSLNK Dehydrolysinonorleucine (Lys-Lys) + L-dehydrolysinonorleucine + N6-[(5S)-5-amino-5-carboxypentylidene]-L-lysine + XLNK6NleN6Lys + dehydrolysinorleucine [misspelling] + dehydrolysylnorleucine + didehydrolysinonorleucine + PSI-MOD + MOD:01176 + Cross-link 2. + L-dehydrolysinonorleucine + + + + + A protein modification that effectively cross-links an L-lysine residue and an L-lysine residue converted to allysine with a carbon-nitrogen bond to form L-dehydrolysinonorleucine. + PubMed:16929109 + RESID:AA0430 + + + + + (2S)-2-amino-6-([(5S)-5-amino-5-carboxypentylidene]amino)hexanoic acid + + + + + + 6-(N6-L-didehydrolysino)-L-norleucine + + + + + + CROSSLNK Dehydrolysinonorleucine (Lys-Lys) + + + + + + L-dehydrolysinonorleucine + + + + + + N6-[(5S)-5-amino-5-carboxypentylidene]-L-lysine + + + + + + XLNK6NleN6Lys + + + + + + dehydrolysinorleucine [misspelling] + + + + + + dehydrolysylnorleucine + + + + + + didehydrolysinonorleucine + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to 1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine. + 90.08 + C 3 H 6 N 0 O 3 + 90.03169 + C 9 H 13 N 3 O 4 + 227.22 + 227.0906 + H + natural + uniprot.ptm:PTM-0416 + (S)-2-amino-3-[1-(1,2,3-trihydroxypropan-2-yl)-1H-imidazol-4-yl]propanoic acid + 1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine + 1-[1,2-dihydroxy-1-(hydroxymethyl)ethyl]-L-histidine + MOD_RES Tele-(1,2,3-trihydroxypropan-2-yl)histidine + N(epsilon)-histidine dihydroxyacetone adduct + N(tau)-(1,2,3-trihydroxypropan-2-yl)histidine + NtauDHAHis + tele-(1,2,3-trihydroxypropan-2-yl)histidine + PSI-MOD + MOD:01177 + 1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine + + + + + A protein modification that effectively converts an L-histidine residue to 1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine. + PubMed:16760471 + RESID:AA0431 + + + + + (S)-2-amino-3-[1-(1,2,3-trihydroxypropan-2-yl)-1H-imidazol-4-yl]propanoic acid + + + + + + 1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine + + + + + + 1-[1,2-dihydroxy-1-(hydroxymethyl)ethyl]-L-histidine + + + + + + MOD_RES Tele-(1,2,3-trihydroxypropan-2-yl)histidine + + + + + + N(epsilon)-histidine dihydroxyacetone adduct + + + + + + N(tau)-(1,2,3-trihydroxypropan-2-yl)histidine + + + + + + NtauDHAHis + + + + + + tele-(1,2,3-trihydroxypropan-2-yl)histidine + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to S-(aspart-4-yloxy) thiocarbonate. + 76.07 + C 1 H 0 N 0 O 2 S 1 + 75.9619 + C 5 H 5 N 1 O 5 S 1 + 191.16 + 190.98885 + D + hypothetical + (2S)-2-amino-4-(carboxysulfanyl)oxy-4-oxobutanoic acid + 4-aspartyloxysulfanylcarbonate + AspOSCO2H + O-carboxysulfanyl-4-oxo-L-homoserine + S-(aspart-4-yloxy) thiocarbonate + PSI-MOD + MOD:01178 + This modification was originally observed in an Entamoeba histolytica enzyme expressed in Escherichia coli. It was not chemically confirmed or characterized. It did not appear in a later model at higher resolution by the same group. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. + S-(aspart-4-yloxy) thiocarbonate + + + + + A protein modification that effectively converts an L-aspartic acid residue to S-(aspart-4-yloxy) thiocarbonate. + PubMed:16627948 + RESID:AA0432 + + + + + (2S)-2-amino-4-(carboxysulfanyl)oxy-4-oxobutanoic acid + + + + + + 4-aspartyloxysulfanylcarbonate + + + + + + AspOSCO2H + + + + + + O-carboxysulfanyl-4-oxo-L-homoserine + + + + + + S-(aspart-4-yloxy) thiocarbonate + + + + + + + + + + + A protein modification that effectively converts an L-alanine residue to N,N-dimethyl-L-alanine. + 28.05 + C 2 H 4 N 0 O 0 + 28.0313 + C 5 H 10 N 1 O 1 + 100.14 + 100.07624 + A + natural + N-term + uniprot.ptm:PTM-0178 + (S)-1-carboxy-N,N-dimethylaminoethane + (S)-2-(dimethylamino)propanoic acid + MOD_RES N,N-dimethylalanine + N,N-dimethyl-L-alanine + N,N-dimethylalanine + NMe2Ala + PSI-MOD + MOD:01179 + N,N-dimethyl-L-alanine + + + + + A protein modification that effectively converts an L-alanine residue to N,N-dimethyl-L-alanine. + PubMed:17691833 + PubMed:387091 + RESID:AA0433 + + + + + (S)-1-carboxy-N,N-dimethylaminoethane + + + + + + (S)-2-(dimethylamino)propanoic acid + + + + + + MOD_RES N,N-dimethylalanine + + + + + + N,N-dimethyl-L-alanine + + + + + + N,N-dimethylalanine + + + + + + NMe2Ala + + + + + + + + + + + A protein modification that effectively converts a glycine residue to 2-hydroxyglycine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 2 H 3 N 1 O 2 + 73.05 + 73.01638 + G + artifact + 2-hydroxyglycine + 2HyGly + alpha-hydroxyglycine + amino(hydroxy)acetic acid + aminohydroxyacetic acid + PSI-MOD + MOD:01180 + CAUTION - peptides of 2-hydroxyglycine are known to be unstable, decaying to break the peptide backbone or to form peptidyl amides [see J. Am. Chem. Soc. 111, 1933-1934, 1989, and J. Org. Chem. 57, 3916-3921, 1992]. If computer analysis of tandem mass-spectrometric results predicts this modification, then it is most probable that there are multiple isobaric peptides differing in the location of multiple hydroxylation modifications [JSG]. + 2-hydroxyglycine observational artifact + + + + + A protein modification that effectively converts a glycine residue to 2-hydroxyglycine. + ChEBI:38048 + PubMed:16178056 + PubMed:17431180 + PubMed:17823333 + RESID:AA0434 + + + + + 2-hydroxyglycine + + + + + + 2HyGly + + + + + + alpha-hydroxyglycine + + + + + + amino(hydroxy)acetic acid + + + + + + aminohydroxyacetic acid + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-aspartate 4-methyl ester. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 5 H 7 N 1 O 3 + 129.12 + 129.04259 + D + artifact + Unimod:34 + (2S)-2-amino-4-methoxy-4-oxobutanoic acid + 2-aminobutanedioic acid 4-methyl ester + 4-methyl L-2-aminosuccinic acid + 4-methyl L-aspartate + 4-methyl L-hydrogen aspartate + L-aspartic acid 4-methyl ester + O4MeAsp + aspartic acid 4-methyl ester + aspartic acid beta-methyl ester + meesterd + PSI-MOD + Methyl + MOD:01181 + CAUTION - observations of this modifation are attributable to artifacts produced in preparation. It is extremely unlikely that eukaryotes produce this modification, because an enzyme acting to form the methyl ester of L-aspartyl peptides would interfere with the D-aspartyl peptide repair mechanism [JSG]. + L-aspartic acid 4-methyl ester + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-aspartate 4-methyl ester. + OMSSA:69 + PubMed:1556110 + PubMed:16888766 + PubMed:9629898 + RESID:AA0435 + Unimod:34#D + + + + + (2S)-2-amino-4-methoxy-4-oxobutanoic acid + + + + + + 2-aminobutanedioic acid 4-methyl ester + + + + + + 4-methyl L-2-aminosuccinic acid + + + + + + 4-methyl L-aspartate + + + + + + 4-methyl L-hydrogen aspartate + + + + + + L-aspartic acid 4-methyl ester + + + + + + O4MeAsp + + + + + + aspartic acid 4-methyl ester + + + + + + aspartic acid beta-methyl ester + + + + + + meesterd + + + + + + Methyl + + + + + + + + + + + + A protein modification that crosslinks a cysteine and a histidine residue by forming the adduct 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FAD. + 781.52 + C 27 H 29 N 9 O 15 P 2 S 0 + 781.12585 + C 36 H 41 N 13 O 17 P 2 S 1 + 1021.81 + 1021.1939 + C, H + natural + uniprot.ptm:PTM-0681 + 6-((R)-2-amino-2-carboxyethyl)sulfanyl-8alpha-[4-((S)-2-amino-2-carboxyethyl)imidazol-3-yl]-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine + 6-(S-L-cysteinyl)-8alpha-(N3'-L-histidino)-FAD + 6-(S-cysteinyl)-8alpha-(N(delta1)-histidyl)-FAD + 6-(S-cysteinyl)-8alpha-(N(pi)-histidyl)-FAD + 6-(S-cysteinyl)-8alpha-(N3'-histidyl)-FAD + 6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD + BINDING FAD (covalent; via 2 links) + BINDING FAD (covalent; via 2 links, pros nitrogen) + CROSSLNK 6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-Cys) + SCys6-NprosHis8a-FAD + PSI-MOD + MOD:01182 + + Cross-link 2. + 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FAD + + + + + A protein modification that crosslinks a cysteine and a histidine residue by forming the adduct 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FAD. + PubMed: + RESID:AA0436 + + + + + 6-((R)-2-amino-2-carboxyethyl)sulfanyl-8alpha-[4-((S)-2-amino-2-carboxyethyl)imidazol-3-yl]-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine + + + + + + 6-(S-L-cysteinyl)-8alpha-(N3'-L-histidino)-FAD + + + + + + 6-(S-cysteinyl)-8alpha-(N(delta1)-histidyl)-FAD + + + + + + 6-(S-cysteinyl)-8alpha-(N(pi)-histidyl)-FAD + + + + + + 6-(S-cysteinyl)-8alpha-(N3'-histidyl)-FAD + + + + + + 6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD + + + + + + BINDING FAD (covalent; via 2 links) + + + + + + BINDING FAD (covalent; via 2 links, pros nitrogen) + + + + + + CROSSLNK 6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-Cys) + + + + + + SCys6-NprosHis8a-FAD + + + + + + + + + + + A protein modification that effectively cross-links two L-selenocysteine residues to form L-selenocystine, + -2.02 + C 0 H -2 N 0 O 0 Se 0 + -2.01565 + C 6 H 8 N 2 O 2 Se 2 + 298.08 + 299.89163 + U, U + hypothetical + (R,R)-3,3'-diselane-1,2-diylbis(2-aminopropanoic acid) + 3,3'-diselenobis(2-aminopropanoic acid) + 3,3'-diselenobisalanine + 3,3'-diselenodialanine + CROSSLNK Selenocystine (Sec-Sec) + L-selenocystine + Sec2 + beta,beta'-diamino-beta,beta'-dicarboxydiethyldiselenide + beta,beta'-diselenodialanine + bis(alpha-aminopropionic acid)-beta-diselenide + bis(beta-amino-beta-carboxyethyl)diselenide + diselenocysteine + selenium cystine + PSI-MOD + MOD:01183 + + Cross-link 2; for formation of the same modification by substitution of 2 selenium for 2 sulfur atoms in L-cystine, see MOD:01184. + L-selenocystine (oxidized selenocysteine) (Sec-Sec) + + + + + A protein modification that effectively cross-links two L-selenocysteine residues to form L-selenocystine, + ChEBI:28553 + PubMed:17715293 + PubMed:6076213 + RESID:AA0437 + + + + + (R,R)-3,3'-diselane-1,2-diylbis(2-aminopropanoic acid) + + + + + + 3,3'-diselenobis(2-aminopropanoic acid) + + + + + + 3,3'-diselenobisalanine + + + + + + 3,3'-diselenodialanine + + + + + + CROSSLNK Selenocystine (Sec-Sec) + + + + + + L-selenocystine + + + + + + Sec2 + + + + + + beta,beta'-diamino-beta,beta'-dicarboxydiethyldiselenide + + + + + + beta,beta'-diselenodialanine + + + + + + bis(alpha-aminopropionic acid)-beta-diselenide + + + + + + bis(beta-amino-beta-carboxyethyl)diselenide + + + + + + diselenocysteine + + + + + + selenium cystine + + + + + + + + + + A protein modification that effectively substitutes two selenium atoms for two sulfur atoms in L-cystine to form L-selenocystine. + 91.81 + C 0 H -2 N 0 O 0 S -2 Se 2 + 93.87325 + C 6 H 8 N 2 O 2 Se 2 + 298.08 + 299.89163 + C, C + hypothetical + (R,R)-3,3'-diselane-1,2-diylbis(2-aminopropanoic acid) + 3,3'-diselenobis(2-aminopropanoic acid) + 3,3'-diselenobisalanine + 3,3'-diselenodialanine + CROSSLNK Selenocystine (Sec-Sec) + L-selenocystine + Se2(S2)Cys2 + beta,beta'-diamino-beta,beta'-dicarboxydiethyldiselenide + beta,beta'-diselenodialanine + bis(alpha-aminopropionic acid)-beta-diselenide + bis(beta-amino-beta-carboxyethyl)diselenide + diselenocysteine + selenium cystine + PSI-MOD + MOD:01184 + Cross-link 2; for formation of the same modification by oxidation of two L-selenocysteine residues, see MOD:01183. + L-selenocystine (selenium disubstituted L-cystine) + + + + + A protein modification that effectively substitutes two selenium atoms for two sulfur atoms in L-cystine to form L-selenocystine. + PubMed:17715293 + RESID:AA0437#CYS2 + + + + + (R,R)-3,3'-diselane-1,2-diylbis(2-aminopropanoic acid) + + + + + + 3,3'-diselenobis(2-aminopropanoic acid) + + + + + + 3,3'-diselenobisalanine + + + + + + 3,3'-diselenodialanine + + + + + + CROSSLNK Selenocystine (Sec-Sec) + + + + + + L-selenocystine + + + + + + Se2(S2)Cys2 + + + + + + beta,beta'-diamino-beta,beta'-dicarboxydiethyldiselenide + + + + + + beta,beta'-diselenodialanine + + + + + + bis(alpha-aminopropionic acid)-beta-diselenide + + + + + + bis(beta-amino-beta-carboxyethyl)diselenide + + + + + + diselenocysteine + + + + + + selenium cystine + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-asparagine. + -0.98 + C 0 H 1 N 1 O -1 + -0.984016 + C 4 H 6 N 2 O 2 + 114.1 + 114.04293 + D + natural + (2S)-2-amino-4-butanediamic acid + 2,4-bis(azanyl)-4-oxobutanoic acid + 2,4-diamino-4-oxobutanoic acid + 2-amino-3-carbamoylpropanoic acid + 2-amino-4-butanediamic acid + 2-aminosuccinamic acid + 2-aminosuccinic acid 4-amide + 4NAsp + L-asparagine + MOD_RES Amidated aspartic acid + alpha-amino-beta-carbamylpropionic acid + alpha-aminosuccinamic acid + aspartic acid 4-amide + aspartic acid beta-amide + beta-asparagine + PSI-MOD + MOD:01185 + 4-amidated L-aspartic acid + + + + + A protein modification that effectively converts an L-aspartic acid residue to L-asparagine. + PubMed:17962566 + RESID:AA0003#ASP + + + + + (2S)-2-amino-4-butanediamic acid + + + + + + 2,4-bis(azanyl)-4-oxobutanoic acid + + + + + + 2,4-diamino-4-oxobutanoic acid + + + + + + 2-amino-3-carbamoylpropanoic acid + + + + + + 2-amino-4-butanediamic acid + + + + + + 2-aminosuccinamic acid + + + + + + 2-aminosuccinic acid 4-amide + + + + + + 4NAsp + + + + + + L-asparagine + + + + + + MOD_RES Amidated aspartic acid + + + + + + alpha-amino-beta-carbamylpropionic acid + + + + + + alpha-aminosuccinamic acid + + + + + + aspartic acid 4-amide + + + + + + aspartic acid beta-amide + + + + + + beta-asparagine + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to either N-acetyl-L-threonne, or O-acetyl-Lthreonine. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + T + natural + AcThr + PSI-MOD + MOD:01186 + + monoacetylated L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to either N-acetyl-L-threonne, or O-acetyl-Lthreonine. + PubMed:18688235 + + + + + AcThr + + + + + + + + + + A protein modification that inserts or replaces a residue with an L-pyrrolysine residue, a natural pretranslational modification. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 12 H 19 N 3 O 2 + 237.3 + 237.14772 + O + natural + Unimod:435 + (2S)-2-amino-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]aminohexanoic acid + 2-azanyl-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]azanylhexanoic acid + L-pyrrolysine + N6-(4-methyl-1,2-didehydropyrrolidine-5-carboxyl)-L-lysine + N6-(4-methyl-delta-1-pyrroline-5-carboxyl)-L-lysine + N6-([(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-yl]carbonyl)-L-lysine + NON_STD Pyrrolysine + Pyl + monomethylamine methyltransferase cofactor lysine adduct + PSI-MOD + MOD:01187 + + L-pyrrolysine residue + + + + + A protein modification that inserts or replaces a residue with an L-pyrrolysine residue, a natural pretranslational modification. + ChEBI:21860 + PubMed:11435424 + PubMed:12029131 + PubMed:12029132 + PubMed:15314242 + PubMed:16096277 + RESID:AA0321 + Unimod:435 + + + + + (2S)-2-amino-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]aminohexanoic acid + + + + + + 2-azanyl-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]azanylhexanoic acid + + + + + + L-pyrrolysine + + + + + + N6-(4-methyl-1,2-didehydropyrrolidine-5-carboxyl)-L-lysine + + + + + + N6-(4-methyl-delta-1-pyrroline-5-carboxyl)-L-lysine + + + + + + N6-([(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-yl]carbonyl)-L-lysine + + + + + + NON_STD Pyrrolysine + + + + + + Pyl + + + + + + monomethylamine methyltransferase cofactor lysine adduct + + + + + + + + + + modification from Unimod Isotopic label - + 90.08 + C 4 (1)H 2 (2)H 5 N 1 O 1 + 90.084145 + C 13 (1)H 11 (2)H 5 N 2 O 3 + 253.15 + 253.14748 + Y + artifact + Unimod:212 + PSI-MOD + N-ethyl iodoacetamide-d5 + NEIAA:2H(5) + MOD:01188 + N-ethyl iodoacetamide-d5 - site Y + + + + + modification from Unimod Isotopic label - + PubMed:11710128 + PubMed:12766232 + PubMed:3155470 + PubMed:957432 + Unimod:212#Y + + + + + N-ethyl iodoacetamide-d5 + + + + + + NEIAA:2H(5) + + + + + + + + + + modification from Unimod Isotopic label - + 90.08 + C 4 (1)H 2 (2)H 5 N 1 O 1 + 90.084145 + C 7 (1)H 7 (2)H 5 N 2 O 2 S 1 + 193.09 + 193.09334 + C + artifact + Unimod:212 + PSI-MOD + N-ethyl iodoacetamide-d5 + NEIAA:2H(5) + MOD:01189 + N-ethyl iodoacetamide-d5 - site C + + + + + modification from Unimod Isotopic label - + PubMed:12766232 + Unimod:212#C + + + + + N-ethyl iodoacetamide-d5 + + + + + + NEIAA:2H(5) + + + + + + + + + Modification from Unimod Chemical derivative. OBSOLETE because duplicate and redundant with MOD:01006. Remap to MOD:01006. + MOD:01006 + 157.79 + Br 2 H -2 + 155.82103 + Y + Unimod:534 + PSI-MOD + Dibromo + MOD:01190 + dibromo + true + + + + + Modification from Unimod Chemical derivative. OBSOLETE because duplicate and redundant with MOD:01006. Remap to MOD:01006. + Unimod:534 + + + + + Dibromo + + + + + + Dibromo + + + + + + + + + + modification from Unimod Isotopic label - + 85.11 + C 4 H 7 N 1 O 1 + 85.052765 + C 7 H 12 N 2 O 2 S 1 + 188.25 + 188.06195 + C + artifact + Unimod:211 + PSI-MOD + N-ethyl iodoacetamide-d0 + NEIAA + MOD:01191 + N-ethyl iodoacetamide-d0 - site C + + + + + modification from Unimod Isotopic label - + PubMed:12766232 + Unimod:211#C + + + + + N-ethyl iodoacetamide-d0 + + + + + + NEIAA + + + + + + + + + + modification from Unimod Isotopic label - + 85.11 + C 4 H 7 N 1 O 1 + 85.052765 + C 13 H 16 N 2 O 3 + 248.28 + 248.11609 + Y + artifact + Unimod:211 + PSI-MOD + N-ethyl iodoacetamide-d0 + NEIAA + MOD:01192 + N-ethyl iodoacetamide-d0 - site Y + + + + + modification from Unimod Isotopic label - + PubMed:11760118 + PubMed:12766232 + Unimod:211#Y + + + + + N-ethyl iodoacetamide-d0 + + + + + + NEIAA + + + + + + + + + + + modification from Unimod Chemical derivative - + 121.2 + C 7 H 7 N 1 O -1 S 1 + 121.035 + C 11 H 14 N 2 O 1 S 1 + 222.31 + 222.08269 + T + artifact + Unimod:264 + PSI-MOD + PET + phosphorylation to pyridyl thiol + MOD:01193 + pyridyl thiol modified L-threonine + + + + + modification from Unimod Chemical derivative - + PubMed:1093385 + Unimod:264#T + + + + + PET + + + + + + phosphorylation to pyridyl thiol + + + + + + + + + + + modification from Unimod Chemical derivative - + 121.2 + C 7 H 7 N 1 O -1 S 1 + 121.035 + C 10 H 12 N 2 O 1 S 1 + 208.28 + 208.06703 + S + artifact + Unimod:264 + PSI-MOD + PET + phosphorylation to pyridyl thiol + MOD:01194 + pyridyl thiol modified L-serine + + + + + modification from Unimod Chemical derivative - + PubMed:15279557 + Unimod:264#S + + + + + PET + + + + + + phosphorylation to pyridyl thiol + + + + + + + + + + modification from Unimod Isotopic label - + 104.11 + C 7 H 4 O 1 + 104.026215 + C 13 H 16 N 2 O 2 + 232.28 + 232.12119 + K + artifact + Unimod:136 + PSI-MOD + Benzoyl + labeling reagent light form (N-term & K) + MOD:01195 + benzoyl labeling reagent light form - site K + + + + + modification from Unimod Isotopic label - + PubMed:11813307 + PubMed:12777388 + PubMed:15456300 + Unimod:136#K + + + + + Benzoyl + + + + + + labeling reagent light form (N-term & K) + + + + + + + + + OBSOLETE because redundant, replaced with MOD:01654. Remap to MOD:01654. + MOD:01654 + 233.29 + C 12 H 11 N 1 O 2 S 1 + 233.05106 + C 18 H 23 N 3 O 3 S 1 + 361.46 + 361.14603 + K + artifact + Unimod:139 + PSI-MOD + 5-dimethylaminonaphthalene-1-sulfonyl + Dansyl + MOD:01196 + 5-dimethylaminonaphthalene-1-sulfonyl - site K + true + + + + + OBSOLETE because redundant, replaced with MOD:01654. Remap to MOD:01654. + Unimod:139 + + + + + 5-dimethylaminonaphthalene-1-sulfonyl + + + + + + Dansyl + + + + + + + + + + A protein modification that effectively converts an L-glutamine residue to N-heptosyl-L-glutamine. + 192.17 + C 7 H 12 O 6 + 192.06339 + C 12 H 20 N 2 O 8 + 320.3 + 320.12198 + Q + artifact + Unimod:490 + PSI-MOD + Hep + Heptose + MOD:01197 + From Unimod with no citation [JSG]. + N-heptosyl-L-glutamine + + + + + A protein modification that effectively converts an L-glutamine residue to N-heptosyl-L-glutamine. + Unimod:490#Q + + + + + Hep + + + + + + Heptose + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-heptosyl-L-serine. + 192.17 + C 7 H 12 O 6 + 192.06339 + C 10 H 17 N 1 O 8 + 279.25 + 279.09543 + S + artifact + Unimod:490 + PSI-MOD + Hep + Heptose + MOD:01198 + From Unimod with no citation [JSG]. + O-heptosyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-heptosyl-L-serine. + Unimod:490#S + + + + + Hep + + + + + + Heptose + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to an N-heptosyl-L-arginine. + 192.17 + C 7 H 12 O 6 + 192.06339 + C 13 H 24 N 4 O 7 + 348.36 + 348.1645 + R + artifact + Unimod:490 + PSI-MOD + Hep + Heptose + MOD:01199 + From Unimod with no citation [JSG]. + N-heptosyl-L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to an N-heptosyl-L-arginine. + Unimod:490#R + + + + + Hep + + + + + + Heptose + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-heptosyl-L-threonine. + 192.17 + C 7 H 12 O 6 + 192.06339 + C 11 H 19 N 1 O 8 + 293.27 + 293.11105 + T + artifact + Unimod:490 + PSI-MOD + Hep + Heptose + MOD:01200 + From Unimod with no citation [JSG]. + O-heptosyl-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-heptosyl-L-threonine. + Unimod:490#T + + + + + Hep + + + + + + Heptose + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-heptosyl-L-lysine. + 192.17 + C 7 H 12 O 6 + 192.06339 + C 13 H 24 N 2 O 7 + 320.34 + 320.15836 + K + artifact + Unimod:490 + PSI-MOD + Hep + Heptose + MOD:01201 + From Unimod with no citation [JSG]. + N6-heptosyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-heptosyl-L-lysine. + Unimod:490#K + + + + + Hep + + + + + + Heptose + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to N-heptosyl-L-asparagine. + 192.17 + C 7 H 12 O 6 + 192.06339 + C 11 H 18 N 2 O 8 + 306.27 + 306.10632 + N + artifact + Unimod:490 + PSI-MOD + Hep + Heptose + MOD:01202 + From Unimod with no citation [JSG]. + N-heptosyl-L-asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to N-heptosyl-L-asparagine. + Unimod:490#N + + + + + Hep + + + + + + Heptose + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-[(pyrid-3-yl)acetyl]lysine. + 119.12 + C 7 H 5 N 1 O 1 + 119.03712 + C 13 H 17 N 3 O 2 + 247.3 + 247.13208 + K + artifact + Unimod:25 + PSI-MOD + Pyridylacetyl + pyridylacetyl + MOD:01203 + Produced by reaction with N-[(pyrid-3-yl)acetyl]oxy-succinimide [JSG]. + N6-(pyridylacetyl)lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-[(pyrid-3-yl)acetyl]lysine. + PubMed:9276974 + Unimod:25#K + + + + + Pyridylacetyl + + + + + + pyridylacetyl + + + + + + + + + + modification from Unimod Artifact - + -48.1 + C -1 H -4 S -1 + -48.003372 + C 4 H 5 N 1 O 1 S 0 + 83.09 + 83.03712 + M + artifact + Unimod:526 + PSI-MOD + Dethiomethyl + Prompt loss of side chain from oxidised Met + MOD:01204 + prompt loss of methanethiol from oxidixed methionine + + + + + modification from Unimod Artifact - + PubMed:9004526 + Unimod:526 + + + + + Dethiomethyl + + + + + + Prompt loss of side chain from oxidised Met + + + + + + + + + + + A protein modification that effectively replaces an O3 hydrogen atom of a serine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond. + 947.85 + C 36 H 57 N 3 O 26 + 947.32306 + C 39 H 62 N 4 O 28 + 1034.93 + 1034.3551 + S + natural + Unimod:160 + PSI-MOD + Hex(1)HexNAc(1)NeuAc(2) + Hex1HexNAc1NeuAc2 + MOD:01205 + Hex1HexNAc1NeuAc2 O-glycosylated serine + + + + + A protein modification that effectively replaces an O3 hydrogen atom of a serine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond. + PubMed:7949339 + Unimod:160#S + + + + + Hex(1)HexNAc(1)NeuAc(2) + + + + + + Hex1HexNAc1NeuAc2 + + + + + + + + + + + A protein modification that effectively replaces an O3 hydrogen atom of a threonine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond. + 947.85 + C 36 H 57 N 3 O 26 + 947.32306 + C 40 H 64 N 4 O 28 + 1048.95 + 1048.3707 + T + natural + Unimod:160 + PSI-MOD + Hex(1)HexNAc(1)NeuAc(2) + Hex1HexNAc1NeuAc2 + MOD:01206 + Hex1HexNAc1NeuAc2 O-glycosylated threonine + + + + + A protein modification that effectively replaces an O3 hydrogen atom of a threonine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond. + Unimod:160#T + + + + + Hex(1)HexNAc(1)NeuAc(2) + + + + + + Hex1HexNAc1NeuAc2 + + + + + + + + + + + A protein modification that effectively replaces an N4 hydrogen atom of an asparagine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond. + 947.85 + C 36 H 57 N 3 O 26 + 947.32306 + C 40 H 63 N 5 O 28 + 1061.95 + 1061.366 + N + natural + Unimod:160 + PSI-MOD + Hex(1)HexNAc(1)NeuAc(2) + Hex1HexNAc1NeuAc2 + MOD:01207 + Hex1HexNAc1NeuAc2 N4-glycosylated asparagine + + + + + A protein modification that effectively replaces an N4 hydrogen atom of an asparagine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond. + Unimod:160#N + + + + + Hex(1)HexNAc(1)NeuAc(2) + + + + + + Hex1HexNAc1NeuAc2 + + + + + + + + + + A protein modification that effectively converts a C-terminal residue to the copper(1+) carboxylate salt. + 62.54 + Cu 1 H -1 + 61.921772 + X + C-term + Unimod:531 + cuprous salt + PSI-MOD + Cation:Cu[I] + Replacement of proton by copper + MOD:01208 + copper(1+) carboxylate C-terminal residue + + + + + A protein modification that effectively converts a C-terminal residue to the copper(1+) carboxylate salt. + Unimod:531#C-term + + + + + cuprous salt + + + + + + Cation:Cu[I] + + + + + + Replacement of proton by copper + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to the copper(1+) aspartate salt. + 62.54 + Cu 1 H -1 + 61.921772 + C 4 Cu 1 H 4 N 1 O 3 + 177.63 + 176.94872 + D + Unimod:531 + cuprous salt + PSI-MOD + Cation:Cu[I] + Replacement of proton by copper + MOD:01209 + copper(1+) L-aspartate + + + + + A protein modification that effectively converts an L-aspartic acid residue to the copper(1+) aspartate salt. + Unimod:531#D + + + + + cuprous salt + + + + + + Cation:Cu[I] + + + + + + Replacement of proton by copper + + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to the copper(1+) glutamate salt. + 62.54 + Cu 1 H -1 + 61.921772 + C 5 Cu 1 H 6 N 1 O 3 + 191.65 + 190.96437 + E + Unimod:531 + cuprous salt + PSI-MOD + Cation:Cu[I] + Replacement of proton by copper + MOD:01210 + copper(1+) L-glutamate + + + + + A protein modification that effectively converts an L-glutamic acid residue to the copper(1+) glutamate salt. + Unimod:531#E + + + + + cuprous salt + + + + + + Cation:Cu[I] + + + + + + Replacement of proton by copper + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-(morpholine-2-acetyl)-lysine. + 127.14 + C 6 H 9 N 1 O 2 + 127.06333 + C 12 H 21 N 3 O 3 + 255.32 + 255.1583 + K + artifact + Unimod:29 + N-succinimidylmorpholine-2-acetate N6-derivatized lysine + PSI-MOD + N-Succinimidyl-2-morpholine acetate + SMA + MOD:01211 + The Unimod name "N-Succinimidyl-3-morpholine acetate" appears to have been a typographical error [JSG]. + N6-(morpholine-2-acetyl)-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-(morpholine-2-acetyl)-lysine. + PubMed:10446193 + Unimod:29#K + + + + + N-succinimidylmorpholine-2-acetate N6-derivatized lysine + + + + + + N-Succinimidyl-2-morpholine acetate + + + + + + SMA + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-(carboxamidomethyl)lysine. + 57.05 + C 2 H 3 N 1 O 1 + 57.021465 + C 8 H 15 N 3 O 2 + 185.23 + 185.11642 + K + artifact + Unimod:4 + N6-(2-amino-2-oxoethyl)lysine + N6-(carbamoylmethyl)lysine + carbamidomethylk + PSI-MOD + Carbamidomethyl + Iodoacetamide derivative + MOD:01212 + + iodoacetamide N6-derivatized lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-(carboxamidomethyl)lysine. + OMSSA:27 + PubMed:11510821 + PubMed:12422359 + PubMed:12686488 + Unimod:4#K + + + + + N6-(2-amino-2-oxoethyl)lysine + + + + + + N6-(carbamoylmethyl)lysine + + + + + + carbamidomethylk + + + + + + Carbamidomethyl + + + + + + Iodoacetamide derivative + + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to an iodoacetamide derivatized histidine, either 1'- or 3'-(carboxamidolmethyl)histidine. + 57.05 + C 2 H 3 N 1 O 1 + 57.021465 + C 8 H 10 N 4 O 2 + 194.19 + 194.08038 + H + artifact + Unimod:4 + carbamidometylh + PSI-MOD + Carbamidomethyl + Iodoacetamide derivative + MOD:01213 + + iodoacetamide derivatized histidine + + + + + A protein modification that effectively converts an L-histidine residue to an iodoacetamide derivatized histidine, either 1'- or 3'-(carboxamidolmethyl)histidine. + OMSSA:28 + PubMed:11510821 + PubMed:12422359 + PubMed:15627961 + PubMed:2026710 + Unimod:4#H + + + + + carbamidometylh + + + + + + Carbamidomethyl + + + + + + Iodoacetamide derivative + + + + + + + + + modification from Unimod Chemical derivative - OBSOLETE because redundant, the difference component of MOD:01060. Remap to MOD:01060. + MOD:01060 + 57.05 + C 2 H 3 N 1 O 1 + 57.021465 + C + artifact + Unimod:4 + PSI-MOD + Carbamidomethyl + Iodoacetamide derivative + MOD:01214 + iodoacetamide - site C + true + + + + + modification from Unimod Chemical derivative - OBSOLETE because redundant, the difference component of MOD:01060. Remap to MOD:01060. + PubMed:10504701 + PubMed:11510821 + PubMed:12422359 + Unimod:4#C + + + + + Carbamidomethyl + + + + + + Iodoacetamide derivative + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to O4-(carboxamidomethyl)aspartate. + 57.05 + C 2 H 3 N 1 O 1 + 57.021465 + C 6 H 8 N 2 O 4 + 172.14 + 172.0484 + D + artifact + Unimod:4 + carbamidomethyld + PSI-MOD + Carbamidomethyl + Iodoacetamide derivative + MOD:01215 + + iodoacetamide derivatized aspartic acid + + + + + A protein modification that effectively converts an L-aspartic acid residue to O4-(carboxamidomethyl)aspartate. + OMSSA:29 + PubMed:11510821 + PubMed:12422359 + PubMed:16526082 + Unimod:4#D + + + + + carbamidomethyld + + + + + + Carbamidomethyl + + + + + + Iodoacetamide derivative + + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to O5-(carboxamidomethyl)glutamate. + 57.05 + C 2 H 3 N 1 O 1 + 57.021465 + C 7 H 10 N 2 O 4 + 186.17 + 186.06406 + E + artifact + Unimod:4 + carbamidomethyle + PSI-MOD + Carbamidomethyl + Iodoacetamide derivative + MOD:01216 + + iodoacetamide derivatized glutamic acid + + + + + A protein modification that effectively converts an L-glutamic acid residue to O5-(carboxamidomethyl)glutamate. + OMSSA:30 + PubMed:11510821 + PubMed:12422359 + Unimod:4#E + + + + + carbamidomethyle + + + + + + Carbamidomethyl + + + + + + Iodoacetamide derivative + + + + + + + + + + modification from Unimod Isotopic label - + 155.0 + (12)C 6 H 5 N 1 O 2 S 1 + 155.0041 + (12)C 10 H 10 N 2 O 5 S 1 + 270.03 + 270.03104 + D + artifact + Unimod:285 + PSI-MOD + Light Sulfanilic Acid (SA) C12 + SulfanilicAcid + MOD:01217 + Sulfanilic Acid (SA), light C12 - site D + + + + + modification from Unimod Isotopic label - + PubMed:12872131 + Unimod:285#D + + + + + Light Sulfanilic Acid (SA) C12 + + + + + + SulfanilicAcid + + + + + + + + + + modification from Unimod Isotopic label - + 155.0 + (12)C 6 H 5 N 1 O 2 S 1 + 155.0041 + (12)C 11 H 12 N 2 O 5 S 1 + 284.05 + 284.0467 + E + artifact + Unimod:285 + PSI-MOD + Light Sulfanilic Acid (SA) C12 + SulfanilicAcid + MOD:01218 + Sulfanilic Acid (SA), light C12 - site E + + + + + modification from Unimod Isotopic label - + PubMed:15283597 + Unimod:285#E + + + + + Light Sulfanilic Acid (SA) C12 + + + + + + SulfanilicAcid + + + + + + + + + + modification from Unimod Chemical derivative - + 161.02 + (13)C 6 H 5 N 1 O 2 S 1 + 161.02423 + (12)C 4 (13)C 6 H 10 N 2 O 5 S 1 + 276.05 + 276.05118 + D + artifact + Unimod:286 + PSI-MOD + Heavy Sulfanilic Acid (SA) C13 + SulfanilicAcid:13C(6) + MOD:01219 + Sulfanilic Acid (SA), heavy C13 - site D + + + + + modification from Unimod Chemical derivative - + PubMed:9254591 + PubMed:9750125 + Unimod:286#D + + + + + Heavy Sulfanilic Acid (SA) C13 + + + + + + SulfanilicAcid:13C(6) + + + + + + + + + + modification from Unimod Chemical derivative - + 161.02 + (13)C 6 H 5 N 1 O 2 S 1 + 161.02423 + (12)C 5 (13)C 6 H 12 N 2 O 5 S 1 + 290.07 + 290.06683 + E + artifact + Unimod:286 + PSI-MOD + Heavy Sulfanilic Acid (SA) C13 + SulfanilicAcid:13C(6) + MOD:01220 + Sulfanilic Acid (SA), heavy C13 - site E + + + + + modification from Unimod Chemical derivative - + PubMed:15121203 + PubMed:9254591 + Unimod:286#E + + + + + Heavy Sulfanilic Acid (SA) C13 + + + + + + SulfanilicAcid:13C(6) + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-formyl-L-threonine. + 28.01 + C 1 O 1 + 27.994915 + C 5 H 7 N 1 O 3 + 129.12 + 129.04259 + T + artifact + Unimod:122 + PSI-MOD + Formyl + Formylation + MOD:01221 + From Unimod: Can occur under CNBr cleavage conditions (70% HCOOH). + O-formyl-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-formyl-L-threonine. + PubMed:11861642 + PubMed:15799070 + Unimod:122#T + + + + + Formyl + + + + + + Formylation + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-formyl-L-serine. + 28.01 + C 1 O 1 + 27.994915 + C 4 H 5 N 1 O 3 + 115.09 + 115.02694 + S + artifact + Unimod:122 + PSI-MOD + Formyl + Formylation + MOD:01222 + From Unimod: Can occur under CNBr cleavage conditions (70% HCOOH). + O-formyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-formyl-L-serine. + PubMed:15627961 + PubMed:15799070 + Unimod:122#S + + + + + Formyl + + + + + + Formylation + + + + + + + + + + modification from Unimod Other - + 88.12 + C 3 H 4 O 1 S 1 + 87.99828 + X + artifact + N-term + Unimod:126 + ntermpeptioacetyl + PSI-MOD + 3,3-Dithio-bis-(sulfosuccinimidyl)propionate + Thioacyl + thioacylation of primary amines (N-term and Lys) + MOD:01223 + This Unimod entry is misdescribed as "thioacylation" [JSG]. + thioacylation of primary amines - site N-term + + + + + modification from Unimod Other - + OMSSA:41 + PubMed:11710128 + PubMed:3155470 + PubMed:957432 + Unimod:126#N-term + + + + + ntermpeptioacetyl + + + + + + 3,3-Dithio-bis-(sulfosuccinimidyl)propionate + + + + + + Thioacyl + + + + + + thioacylation of primary amines (N-term and Lys) + + + + + + + + + + modification from Unimod Other - + 88.12 + C 3 H 4 O 1 S 1 + 87.99828 + C 9 H 16 N 2 O 2 S 1 + 216.3 + 216.09325 + K + artifact + Unimod:126 + thioacetylk + PSI-MOD + 3,3-Dithio-bis-(sulfosuccinimidyl)propionate + Thioacyl + thioacylation of primary amines (N-term and Lys) + MOD:01224 + This Unimod entry is misdescribed as "thioacylation" [JSG]. + thioacylation of primary amines - site K + + + + + modification from Unimod Other - + OMSSA:40 + PubMed:11710128 + PubMed:3155470 + PubMed:957432 + Unimod:126#K + + + + + thioacetylk + + + + + + 3,3-Dithio-bis-(sulfosuccinimidyl)propionate + + + + + + Thioacyl + + + + + + thioacylation of primary amines (N-term and Lys) + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue into an L-fluorotyrosine. + 17.99 + F 1 H -1 + 17.990578 + C 9 F 1 H 8 N 1 O 2 + 181.17 + 181.05391 + Y + artifact + Unimod:127 + phef + PSI-MOD + Fluoro + fluorophenylalanine replacement of phenylalanine + MOD:01225 + From Unimod: the citation appears to be correct, but the PMID is not and has been corrected [JSG]. + monofluorinated L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue into an L-fluorotyrosine. + OMSSA:46 + PubMed:8069568 + Unimod:127#Y + + + + + phef + + + + + + Fluoro + + + + + + fluorophenylalanine replacement of phenylalanine + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to an L-fluorotryptophan. + 17.99 + F 1 H -1 + 17.990578 + C 11 F 1 H 9 N 2 O 1 + 204.2 + 204.06989 + W + artifact + Unimod:127 + PSI-MOD + Fluoro + fluorophenylalanine replacement of phenylalanine + MOD:01226 + From Unimod: the citation appears to be correct, but the PMID is not and has been corrected [JSG]. + monofluorinated L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to an L-fluorotryptophan. + PubMed:8069568 + Unimod:127#W + + + + + Fluoro + + + + + + fluorophenylalanine replacement of phenylalanine + + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to an L-fluorophenylalanine. + 17.99 + C 0 F 1 H -1 N 0 O 0 + 17.990578 + C 9 F 1 H 8 N 1 O 1 + 165.17 + 165.05899 + F + artifact + Unimod:127 + phef + PSI-MOD + Fluoro + fluorophenylalanine replacement of phenylalanine + MOD:01227 + From Unimod: the citation appears to be correct, but the PMID is not and has been corrected. From DeltaMass: (element abbreviation in formula incorrect, mass incorrect, and aggregate not delta) Average Mass: 149 Formula: C9H8O1N1Fl1 Average Mass Change: 149 References:PE Sciex with no citation [JSG]. + monofluorinated L-phenylalanine + + + + + A protein modification that effectively converts an L-phenylalanine residue to an L-fluorophenylalanine. + DeltaMass:181 + OMSSA:46 + PubMed:8069568 + Unimod:127#F + + + + + phef + + + + + + Fluoro + + + + + + fluorophenylalanine replacement of phenylalanine + + + + + + + + + + + A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one iodine atom. + 125.9 + H -1 I 1 + 125.896645 + C 9 H 8 I 1 N 1 O 2 + 289.07 + 288.95996 + Y + artifact + Unimod:129 + I1Tyr + iodinationy + PSI-MOD + Iodination + Iodo + MOD:01228 + + From DeltaMass: Average Mass: 289 [name misspelled "monoiodated" - JSG]. + monoiodinated tyrosine + + + + + A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one iodine atom. + DeltaMass:0 + OMSSA:65 + PubMed:1326520 + PubMed:15627961 + PubMed:2026710 + Unimod:129#Y + + + + + I1Tyr + + + + + + iodinationy + + + + + + Iodination + + + + + + Iodo + + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to an L-iodohistidine. + 125.9 + C 0 H -1 I 1 N 0 O 0 + 125.896645 + C 6 H 6 I 1 N 3 O 1 + 263.04 + 262.95557 + H + artifact + Unimod:129 + I1His + PSI-MOD + Iodination + Iodo + MOD:01229 + L-iodohistidine + + + + + A protein modification that effectively converts an L-histidine residue to an L-iodohistidine. + PubMed:15627961 + PubMed:2026710 + Unimod:129#H + + + + + I1His + + + + + + Iodination + + + + + + Iodo + + + + + + + + + + modification from Unimod Isotopic label - + 105.02 + (12)C 6 H 3 N 1 O 1 + 105.02146 + (12)C 12 H 15 N 3 O 2 + 233.12 + 233.11642 + K + artifact + Unimod:365 + PSI-MOD + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form + ICPL + MOD:01230 + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form - site K + + + + + modification from Unimod Isotopic label - + PubMed:15602776 + Unimod:365#K + + + + + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form + + + + + + ICPL + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 3x(13)C labeled N6-propanoyl-L-lysine. + 59.04 + (13)C 3 H 4 O 1 + 59.036278 + (12)C 6 (13)C 3 H 16 N 2 O 2 + 187.13 + 187.13124 + K + artifact + Unimod:59 + PSI-MOD + Propionate labeling reagent heavy form (+3amu), N-term & K + Propionyl:13C(3) + MOD:01231 + + 3x(13)C labeled N6-propanoyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to 3x(13)C labeled N6-propanoyl-L-lysine. + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + PubMed:12442261 + Unimod:59#K + + + + + Propionate labeling reagent heavy form (+3amu), N-term & K + + + + + + Propionyl:13C(3) + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 3x(12)C labeled N6-propanoyl-L-lysine. + 56.03 + (12)C 3 H 4 O 1 + 56.026215 + (12)C 9 H 16 N 2 O 2 + 184.12 + 184.12119 + K + artifact + Unimod:58 + PSI-MOD + Propionate labeling reagent light form (N-term & K) + Propionyl + MOD:01232 + + 3x(12)C labeled N6-propanoyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to 3x(12)C labeled N6-propanoyl-L-lysine. + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + Unimod:58#K + + + + + Propionate labeling reagent light form (N-term & K) + + + + + + Propionyl + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled N6-acetyl-L-lysine. + 45.03 + C 2 (1)H -1 (2)H 3 O 1 + 45.029396 + C 8 (1)H 11 (2)H 3 N 2 O 2 + 173.12 + 173.12436 + K + artifact + Unimod:56 + PSI-MOD + Acetate labeling reagent (N-term & K) (heavy form, +3amu) + Acetyl:2H(3) + MOD:01233 + + 3x(2)H labeled N6-acetyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled N6-acetyl-L-lysine. + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + Unimod:56#K + + + + + Acetate labeling reagent (N-term & K) (heavy form, +3amu) + + + + + + Acetyl:2H(3) + + + + + + + + + + + modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate + 2.0 + (16)O -1 (18)O 1 + 2.004246 + C 3 H 5 N 1 (16)O 1 (18)O 1 + 89.04 + 89.03628 + S + artifact + Unimod:258 + PSI-MOD + Label:18O(1) + O18 Labeling + MOD:01234 + + (18)O monosubstituted L-serine + + + + + modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate + PubMed:11467524 + Unimod:258#S + + + + + Label:18O(1) + + + + + + O18 Labeling + + + + + + + + + + + modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate + 2.0 + (16)O -1 (18)O 1 + 2.004246 + C 4 H 7 N 1 (16)O 1 (18)O 1 + 103.05 + 103.051926 + T + artifact + Unimod:258 + PSI-MOD + Label:18O(1) + O18 Labeling + MOD:01235 + + (18)O monosubstituted L-threonine + + + + + modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate + PubMed:11467524 + PubMed:15549660 + Unimod:258#T + + + + + Label:18O(1) + + + + + + O18 Labeling + + + + + + + + + + + modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate + 2.0 + (16)O -1 (18)O 1 + 2.004246 + C 9 H 9 N 1 (16)O 1 (18)O 1 + 165.07 + 165.06758 + Y + artifact + Unimod:258 + PSI-MOD + Label:18O(1) + O18 Labeling + MOD:01236 + + (18)O monosubstituted L-tyrosine + + + + + modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate + PubMed:11467524 + PubMed:15549660 + Unimod:258#Y + + + + + Label:18O(1) + + + + + + O18 Labeling + + + + + + + + + + A protein modification produced by formation of an adduct of an L-cysteine residue with 4-hydroxynonenal. + 156.22 + C 9 H 16 O 2 + 156.11504 + C 12 H 21 N 1 O 3 S 1 + 259.36 + 259.1242 + C + artifact + Unimod:53 + PSI-MOD + 4-hydroxynonenal (HNE) + HNE + MOD:01237 + 4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG]. + cysteine 4-hydroxynonenal adduct + + + + + A protein modification produced by formation of an adduct of an L-cysteine residue with 4-hydroxynonenal. + PubMed:11327326 + PubMed:15133838 + PubMed:9629898 + Unimod:53#C + + + + + 4-hydroxynonenal (HNE) + + + + + + HNE + + + + + + + + + + A protein modification produced by formation of an adduct of an L-lysine residue with 4-hydroxynonenal. + 156.22 + C 9 H 16 O 2 + 156.11504 + C 15 H 28 N 2 O 3 + 284.4 + 284.21 + K + artifact + Unimod:53 + PSI-MOD + 4-hydroxynonenal (HNE) + HNE + MOD:01238 + 4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG]. + lysine 4-hydroxynonenal adduct + + + + + A protein modification produced by formation of an adduct of an L-lysine residue with 4-hydroxynonenal. + PubMed:11327326 + PubMed:15133838 + PubMed:9629898 + Unimod:53#K + + + + + 4-hydroxynonenal (HNE) + + + + + + HNE + + + + + + + + + + A protein modification produced by formation of an adduct of an L-histidine residue with 4-hydroxynonenal. + 156.22 + C 9 H 16 O 2 + 156.11504 + C 15 H 23 N 3 O 3 + 293.37 + 293.17395 + H + artifact + Unimod:53 + PSI-MOD + 4-hydroxynonenal (HNE) + HNE + MOD:01239 + 4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG]. + histidine 4-hydroxynonenal adduct + + + + + A protein modification produced by formation of an adduct of an L-histidine residue with 4-hydroxynonenal. + PubMed:10717661 + PubMed:11327326 + PubMed:15133838 + Unimod:53#H + + + + + 4-hydroxynonenal (HNE) + + + + + + HNE + + + + + + + + + + + + + + + + + + A protein modification that crosslinks the N6-amino of a peptidyl lysine with the carboxyl of leucyl-arginyl-glycyl-glycine, the C-terminal tetrapeptide of ubiquitin. + 383.45 + C 16 H 29 N 7 O 4 + 383.2281 + C 22 H 41 N 9 O 5 + 511.63 + 511.32306 + K + artifact + Unimod:535 + PSI-MOD + LeuArgGlyGly + Ubiquitination + MOD:01240 + ubiquitination signature tetrapeptidyl lysine + + + + + A protein modification that crosslinks the N6-amino of a peptidyl lysine with the carboxyl of leucyl-arginyl-glycyl-glycine, the C-terminal tetrapeptide of ubiquitin. + PubMed:10504701 + Unimod:535 + + + + + LeuArgGlyGly + + + + + + Ubiquitination + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled L-aspartic acid 4-methyl ester. + 17.03 + C 1 (1)H -1 (2)H 3 + 17.03448 + C 5 (1)H 4 (2)H 3 N 1 O 3 + 132.06 + 132.06142 + D + artifact + Unimod:298 + trideuteromethyld + PSI-MOD + Methyl:2H(3) + deuterated methyl ester + MOD:01241 + 3x(2)H labeled L-aspartic acid 4-methyl ester + + + + + A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled L-aspartic acid 4-methyl ester. + OMSSA:19 + PubMed:12185208 + Unimod:298#D + + + + + trideuteromethyld + + + + + + Methyl:2H(3) + + + + + + deuterated methyl ester + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled L-glutamic acid 5-methyl ester. + 17.03 + C 1 (1)H -1 (2)H 3 + 17.03448 + C 6 (1)H 6 (2)H 3 N 1 O 3 + 146.08 + 146.07707 + E + artifact + Unimod:298 + trideuteromethyle + PSI-MOD + Methyl:2H(3) + deuterated methyl ester + MOD:01242 + 3x(2)H labeled L-glutamic acid 5-methyl ester + + + + + A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled L-glutamic acid 5-methyl ester. + OMSSA:20 + PubMed:1326520 + Unimod:298#E + + + + + trideuteromethyle + + + + + + Methyl:2H(3) + + + + + + deuterated methyl ester + + + + + + + + + + A protein modification that effectively converts a C-terminal residue to the potassium carboxylate salt. + 38.09 + H -1 K 1 + 37.955883 + X + C-term + Unimod:530 + PSI-MOD + Cation:K + Replacement of proton by potassium + MOD:01243 + potassium carboxylate C-terminal residue + + + + + A protein modification that effectively converts a C-terminal residue to the potassium carboxylate salt. + Unimod:530#C-term + + + + + Cation:K + + + + + + Replacement of proton by potassium + + + + + + + + + + + A protein modification that effectively converts an L-glutamioc acid residue to the potassium glutamate salt. + 38.09 + H -1 K 1 + 37.955883 + C 5 H 6 K 1 N 1 O 3 + 167.21 + 166.99847 + E + Unimod:530 + PSI-MOD + Cation:K + Replacement of proton by potassium + MOD:01244 + potassium L-glutamate + + + + + A protein modification that effectively converts an L-glutamioc acid residue to the potassium glutamate salt. + Unimod:530#E + + + + + Cation:K + + + + + + Replacement of proton by potassium + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to the potassium aspartate salt. + 38.09 + H -1 K 1 + 37.955883 + C 4 H 4 K 1 N 1 O 3 + 153.18 + 152.98282 + D + Unimod:530 + PSI-MOD + Cation:K + Replacement of proton by potassium + MOD:01245 + potassium L-aspartate + + + + + A protein modification that effectively converts an L-aspartic acid residue to the potassium aspartate salt. + Unimod:530#D + + + + + Cation:K + + + + + + Replacement of proton by potassium + + + + + + + + + OBSOLETE because redundant and identical to MOD:00812 after formula correction. Remap to MOD:00812. + MOD:00812 + 147.15 + C 6 H 11 O 4 + 147.06573 + C 9 H 16 N 1 O 6 + 234.23 + 234.09776 + S + natural + Unimod:295 + PSI-MOD + Fucose + dHex + MOD:01246 + fucosylated -site S + true + + + + + OBSOLETE because redundant and identical to MOD:00812 after formula correction. Remap to MOD:00812. + PubMed:11344537 + PubMed:15189151 + PubMed:3311742 + PubMed:3578767 + Unimod:295#S + + + + + Fucose + + + + + + dHex + + + + + + + + + OBSOLETE because redundant and identical to MOD:00813 after formula correction. Remap to MOD:00813. + MOD:00813 + 147.15 + C 6 H 11 O 4 + 147.06573 + C 10 H 18 N 1 O 6 + 248.26 + 248.11342 + T + natural + Unimod:295 + PSI-MOD + Fucose + dHex + MOD:01247 + fucosylated -site T + true + + + + + OBSOLETE because redundant and identical to MOD:00813 after formula correction. Remap to MOD:00813. + PubMed:11344537 + PubMed:11857757 + PubMed:15189151 + Unimod:295#T + + + + + Fucose + + + + + + dHex + + + + + + + + + + + A protein modification that is produced by reaction of iodouridine monophosphate with an L-tyrosine residue to form an ether linkage. + 322.17 + C 9 H 11 N 2 O 9 P 1 + 322.0202 + C 18 H 20 N 3 O 11 P 1 + 485.34 + 485.08356 + Y + artifact + Unimod:292 + PSI-MOD + Cross-link of (Iodo)-uracil MP with W,F,Y + IodoU-AMP + MOD:01248 + This has an ether linkage and not a phosphodiester linkage with UMP. + iodouridine monophosphate derivatized tyrosine + + + + + A protein modification that is produced by reaction of iodouridine monophosphate with an L-tyrosine residue to form an ether linkage. + PubMed:11112526 + PubMed:11567090 + PubMed:6540775 + Unimod:292#Y + + + + + Cross-link of (Iodo)-uracil MP with W,F,Y + + + + + + IodoU-AMP + + + + + + + + + + + A protein modification that is produced by reaction of iodouridine monophosphate with an L-tryptophan residue. + 322.17 + C 9 H 11 N 2 O 9 P 1 + 322.0202 + C 20 H 21 N 4 O 10 P 1 + 508.38 + 508.09952 + W + artifact + Unimod:292 + PSI-MOD + Cross-link of (Iodo)-uracil MP with W,F,Y + IodoU-AMP + MOD:01249 + This has a carbon-nitrogen linkage and not a phosphodiester linkage with UMP. + iodouridine monophosphate derivatized tryptophan + + + + + A protein modification that is produced by reaction of iodouridine monophosphate with an L-tryptophan residue. + PubMed:11112526 + PubMed:11567090 + PubMed:6540775 + Unimod:292#W + + + + + Cross-link of (Iodo)-uracil MP with W,F,Y + + + + + + IodoU-AMP + + + + + + + + + + + A protein modification that is produced by reaction of iodouridine monophosphate with an L-phenylalanine residue. + 322.17 + C 9 H 11 N 2 O 9 P 1 + 322.0202 + C 18 H 20 N 3 O 10 P 1 + 469.34 + 469.08862 + F + artifact + Unimod:292 + PSI-MOD + Cross-link of (Iodo)-uracil MP with W,F,Y + IodoU-AMP + MOD:01250 + This has a carbon-carbon linkage and not a phosphodiester linkage with UMP. + iodouridine monophosphate derivatized phenylalanine + + + + + A protein modification that is produced by reaction of iodouridine monophosphate with an L-phenylalanine residue. + PubMed:11112526 + PubMed:11567090 + PubMed:6540775 + Unimod:292#F + + + + + Cross-link of (Iodo)-uracil MP with W,F,Y + + + + + + IodoU-AMP + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-[3-(carboxamidomethylthio)propanoyl]lysine. + 145.18 + C 5 H 7 N 1 O 2 S 1 + 145.01974 + C 11 H 19 N 3 O 3 S 1 + 273.35 + 273.11472 + K + artifact + Unimod:293 + PSI-MOD + 3-(carbamidomethylthio)propanoyl + CAMthiopropanoyl + MOD:01251 + N6-[3-(carboxamidomethylthio)propanoyl]lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-[3-(carboxamidomethylthio)propanoyl]lysine. + PubMed:15121203 + Unimod:293#K + + + + + 3-(carbamidomethylthio)propanoyl + + + + + + CAMthiopropanoyl + + + + + + + + + OBSOLETE because redundant and identical to MOD:00933. Remap to MOD:00933. + MOD:00933 + 54.05 + C 3 H 2 O 1 + 54.010567 + C 9 H 14 N 4 O 2 + 210.24 + 210.11168 + R + artifact + Unimod:319 + PSI-MOD + Delta:H(2)C(3)O(1) + MDA adduct +54 + MOD:01252 + 5-hydro-5-methylimidazol-4-one, methylglyoxal arginine adduct (+54 amu) + true + + + + + OBSOLETE because redundant and identical to MOD:00933. Remap to MOD:00933. + PubMed:9448752 + Unimod:319#R + + + + + Delta:H(2)C(3)O(1) + + + + + + MDA adduct +54 + + + + + + + + + + + modification from Unimod Chemical derivative - Malondialdehyde (MDA) adduct + 54.05 + C 3 H 2 O 1 + 54.010567 + C 9 H 14 N 2 O 2 + 182.22 + 182.10553 + K + artifact + Unimod:319 + PSI-MOD + Delta:H(2)C(3)O(1) + MDA adduct +54 + MOD:01253 + malondialdehyde lysine adduct (+54 amu) + + + + + modification from Unimod Chemical derivative - Malondialdehyde (MDA) adduct + Unimod:319#K + + + + + Delta:H(2)C(3)O(1) + + + + + + MDA adduct +54 + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 4x(2)H labeled dimethylated L-lysine. + 32.06 + C 2 (2)H 4 + 32.056408 + C 8 H 12 (2)H 4 N 2 O 1 + 160.15 + 160.15137 + K + artifact + Unimod:199 + mod189 + PSI-MOD + DiMethyl-CHD2 + Dimethyl:2H(4) + MOD:01254 + + 4x(2)H labeled dimethylated L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to 4x(2)H labeled dimethylated L-lysine. + OMSSA:189 + PubMed:14670044 + Unimod:199#K + + + + + mod189 + + + + + + DiMethyl-CHD2 + + + + + + Dimethyl:2H(4) + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to S-(2-sulfanylethyl)cysteine. + 76.18 + C 2 H 4 O -1 S 2 + 75.98053 + C 5 H 9 N 1 O 1 S 2 + 163.25 + 163.01256 + S + artifact + Unimod:200 + S-(2-mercaptoethyl)cysteine + PSI-MOD + EDT + Ethanedithiol + MOD:01255 + S-(2-sulfanylethyl)cysteine (Ser) + + + + + A protein modification that effectively converts an L-serine residue to S-(2-sulfanylethyl)cysteine. + PubMed:11507762 + Unimod:200#S + + + + + S-(2-mercaptoethyl)cysteine + + + + + + EDT + + + + + + Ethanedithiol + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to 3-methyl-S-(2-sulfanylethyl)cysteine. + 76.18 + C 2 H 4 O -1 S 2 + 75.98053 + C 6 H 11 N 1 O 1 S 2 + 177.28 + 177.02821 + T + artifact + Unimod:200 + beta-methyl-S-(2-mercaptoethyl)cysteine + PSI-MOD + EDT + Ethanedithiol + MOD:01256 + 3-methyl-S-(2-sulfanylethyl)cysteine (Thr) + + + + + A protein modification that effectively converts an L-threonine residue to 3-methyl-S-(2-sulfanylethyl)cysteine. + PubMed:11507762 + Unimod:200#T + + + + + beta-methyl-S-(2-mercaptoethyl)cysteine + + + + + + EDT + + + + + + Ethanedithiol + + + + + + + + + + modification from Unimod Chemical derivative - + 170.17 + C 10 H 6 N 2 O 1 + 170.04802 + C 16 H 18 N 4 O 2 + 298.35 + 298.14297 + K + artifact + Unimod:194 + PSI-MOD + 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate + AccQTag + MOD:01257 + 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate - site K + + + + + modification from Unimod Chemical derivative - + PubMed:12716131 + PubMed:14997490 + Unimod:194#K + + + + + 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate + + + + + + AccQTag + + + + + + + + + + + modification from Unimod Chemical derivative - + 111.1 + C 5 H 5 N 1 O 2 + 111.03203 + C 8 H 10 N 2 O 3 S 1 + 214.24 + 214.04121 + C + artifact + Unimod:314 + PSI-MOD + Nmethylmaleimide + MOD:01258 + N-methylmaleimide modified L-cysteine + + + + + modification from Unimod Chemical derivative - + PubMed:9448752 + Unimod:314#C + + + + + Nmethylmaleimide + + + + + + Nmethylmaleimide + + + + + + + + + + + modification from Unimod Chemical derivative - + 111.1 + C 5 H 5 N 1 O 2 + 111.03203 + C 11 H 17 N 3 O 3 + 239.27 + 239.12698 + K + artifact + Unimod:314 + PSI-MOD + Nmethylmaleimide + MOD:01259 + N-methylmaleimide modified L-lysine + + + + + modification from Unimod Chemical derivative - + PubMed:9448752 + Unimod:314#K + + + + + Nmethylmaleimide + + + + + + Nmethylmaleimide + + + + + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + 362.38 + C 19 H 22 O 7 + 362.13657 + C 28 H 31 N 1 O 9 + 525.55 + 525.1999 + Y + artifact + Unimod:270 + PSI-MOD + Cytopiloyne + nucleophilic addtion to cytopiloyne + MOD:01260 + nucleophilic addtion to cytopiloyne - site Y + true + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + PubMed:15549660 + Unimod:270#Y + + + + + Cytopiloyne + + + + + + nucleophilic addtion to cytopiloyne + + + + + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + 362.38 + C 19 H 22 O 7 + 362.13657 + C 22 H 27 N 1 O 9 + 449.46 + 449.16858 + S + artifact + Unimod:270 + PSI-MOD + Cytopiloyne + nucleophilic addtion to cytopiloyne + MOD:01261 + nucleophilic addtion to cytopiloyne - site S + true + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + PubMed:15549660 + Unimod:270#C + + + + + Cytopiloyne + + + + + + nucleophilic addtion to cytopiloyne + + + + + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + 362.38 + C 19 H 22 O 7 + 362.13657 + C 25 H 34 N 4 O 8 + 518.57 + 518.2377 + R + artifact + Unimod:270 + PSI-MOD + Cytopiloyne + nucleophilic addtion to cytopiloyne + MOD:01262 + nucleophilic addition to cytopiloyne - site R + true + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + PubMed:12590383 + PubMed:15549660 + Unimod:270#R + + + + + Cytopiloyne + + + + + + nucleophilic addtion to cytopiloyne + + + + + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + 362.38 + C 19 H 22 O 7 + 362.13657 + C 25 H 34 N 2 O 8 + 490.55 + 490.2315 + K + artifact + Unimod:270 + PSI-MOD + Cytopiloyne + nucleophilic addtion to cytopiloyne + MOD:01263 + nucleophilic addtion to cytopiloyne - site K + true + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + PubMed:15549660 + Unimod:270#K + + + + + Cytopiloyne + + + + + + nucleophilic addtion to cytopiloyne + + + + + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + 362.38 + C 19 H 22 O 7 + 362.13657 + C 22 H 27 N 1 O 8 S 1 + 465.52 + 465.14575 + C + artifact + Unimod:270 + PSI-MOD + Cytopiloyne + nucleophilic addtion to cytopiloyne + MOD:01264 + nucleophilic addtion to cytopiloyne - site C + true + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + PubMed:15549660 + Unimod:270#C + + + + + Cytopiloyne + + + + + + nucleophilic addtion to cytopiloyne + + + + + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + 362.38 + C 19 H 22 O 7 + 362.13657 + C 24 H 29 N 1 O 8 + 459.5 + 459.18933 + P + artifact + Unimod:270 + PSI-MOD + Cytopiloyne + nucleophilic addtion to cytopiloyne + MOD:01265 + nucleophilic addtion to cytopiloyne - site P + true + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + PubMed:15549660 + Unimod:270#P + + + + + Cytopiloyne + + + + + + nucleophilic addtion to cytopiloyne + + + + + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + 380.39 + C 19 H 24 O 8 + 380.14713 + C 22 H 29 N 1 O 9 S 1 + 483.53 + 483.1563 + C + artifact + Unimod:271 + PSI-MOD + Cytopiloyne+water + nucleophilic addition to cytopiloyne+H2O + MOD:01266 + nucleophilic addition to cytopiloyne+H2O - site C + true + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + PubMed:15549660 + Unimod:271#C + + + + + Cytopiloyne+water + + + + + + nucleophilic addition to cytopiloyne+H2O + + + + + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + 380.39 + C 19 H 24 O 8 + 380.14713 + C 25 H 36 N 2 O 9 + 508.57 + 508.2421 + K + artifact + Unimod:271 + PSI-MOD + Cytopiloyne+water + nucleophilic addition to cytopiloyne+H2O + MOD:01267 + nucleophilic addition to cytopiloyne+H2O - site K + true + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + PubMed:11746907 + PubMed:15549660 + Unimod:271#K + + + + + Cytopiloyne+water + + + + + + nucleophilic addition to cytopiloyne+H2O + + + + + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + 380.39 + C 19 H 24 O 8 + 380.14713 + C 23 H 31 N 1 O 10 + 481.5 + 481.1948 + T + artifact + Unimod:271 + PSI-MOD + Cytopiloyne+water + nucleophilic addition to cytopiloyne+H2O + MOD:01268 + nucleophilic addition to cytopiloyne+H2O - site T + true + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + PubMed:15549660 + Unimod:271#T + + + + + Cytopiloyne+water + + + + + + nucleophilic addition to cytopiloyne+H2O + + + + + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + 380.39 + C 19 H 24 O 8 + 380.14713 + C 25 H 36 N 4 O 9 + 536.58 + 536.2482 + R + artifact + Unimod:271 + PSI-MOD + Cytopiloyne+water + nucleophilic addition to cytopiloyne+H2O + MOD:01269 + nucleophilic addition to cytopiloyne+H2O - site R + true + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + PubMed:15549660 + Unimod:271#R + + + + + Cytopiloyne+water + + + + + + nucleophilic addition to cytopiloyne+H2O + + + + + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + 380.39 + C 19 H 24 O 8 + 380.14713 + C 22 H 29 N 1 O 10 + 467.47 + 467.17914 + S + artifact + Unimod:271 + PSI-MOD + Cytopiloyne+water + nucleophilic addition to cytopiloyne+H2O + MOD:01270 + nucleophilic addition to cytopiloyne+H2O - site S + true + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + PubMed:14670044 + PubMed:15549660 + Unimod:271#S + + + + + Cytopiloyne+water + + + + + + nucleophilic addition to cytopiloyne+H2O + + + + + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + 380.39 + C 19 H 24 O 8 + 380.14713 + C 28 H 33 N 1 O 10 + 543.57 + 543.21045 + Y + artifact + Unimod:271 + PSI-MOD + Cytopiloyne+water + nucleophilic addition to cytopiloyne+H2O + MOD:01271 + nucleophilic addition to cytopiloyne+H2O - site Y + true + + + + + OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative - + PubMed:15549660 + Unimod:271#Y + + + + + Cytopiloyne+water + + + + + + nucleophilic addition to cytopiloyne+H2O + + + + + + + + + + + modification from Unimod Chemical derivative - + 225.31 + C 10 H 15 N 3 O 1 S 1 + 225.09358 + C 16 H 27 N 5 O 2 S 1 + 353.49 + 353.18854 + K + artifact + Unimod:89 + PSI-MOD + Iminobiotin + Iminobiotinylation + MOD:01272 + iminobiotinylation - site K + + + + + modification from Unimod Chemical derivative - + PubMed:9750125 + Unimod:89#K + + + + + Iminobiotin + + + + + + Iminobiotinylation + + + + + + + + + + + A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-serine residue. + 183.23 + C 8 H 9 N 1 O 2 S 1 + 183.0354 + C 11 H 14 N 2 O 4 S 1 + 270.3 + 270.0674 + S + artifact + Unimod:276 + PSI-MOD + AEBS + Aminoethylbenzenesulfonylation + MOD:01273 + O-[4-(2-aminoethyl)benzenesulfonyl] serine + + + + + A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-serine residue. + PubMed:15283597 + PubMed:8597590 + Unimod:276#S + + + + + AEBS + + + + + + Aminoethylbenzenesulfonylation + + + + + + + + + + + A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-histidine residue. + 183.23 + C 8 H 9 N 1 O 2 S 1 + 183.0354 + C 14 H 16 N 4 O 3 S 1 + 320.37 + 320.0943 + H + artifact + Unimod:276 + PSI-MOD + AEBS + Aminoethylbenzenesulfonylation + MOD:01274 + N'-[4-(2-aminoethyl)benzenesulfonyl] derivatized histidine + + + + + A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-histidine residue. + PubMed:8597590 + Unimod:276#H + + + + + AEBS + + + + + + Aminoethylbenzenesulfonylation + + + + + + + + + + + A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-lysine residue. + 183.23 + C 8 H 9 N 1 O 2 S 1 + 183.0354 + C 14 H 21 N 3 O 3 S 1 + 311.4 + 311.13037 + K + artifact + Unimod:276 + PSI-MOD + AEBS + Aminoethylbenzenesulfonylation + MOD:01275 + N6-[4-(2-aminoethyl)benzenesulfonyl]lysine + + + + + A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-lysine residue. + PubMed:8597590 + Unimod:276#K + + + + + AEBS + + + + + + Aminoethylbenzenesulfonylation + + + + + + + + + + + A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-tyrosine residue. + 183.23 + C 8 H 9 N 1 O 2 S 1 + 183.0354 + C 17 H 18 N 2 O 4 S 1 + 346.4 + 346.09872 + Y + artifact + Unimod:276 + PSI-MOD + AEBS + Aminoethylbenzenesulfonylation + MOD:01276 + O4'-[4-(2-aminoethyl)benzenesulfonyl]tyrosine + + + + + A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-tyrosine residue. + PubMed:10906242 + PubMed:8597590 + Unimod:276#Y + + + + + AEBS + + + + + + Aminoethylbenzenesulfonylation + + + + + + + + + + + modification from Unimod Other - + 70.09 + C 4 H 6 O 1 + 70.04186 + C 7 H 11 N 1 O 2 S 1 + 173.23 + 173.05106 + C + artifact + Unimod:253 + PSI-MOD + Crotonaldehyde + MOD:01277 + crotonylated L-cysteine + + + + + modification from Unimod Other - + PubMed:11283024 + Unimod:253#C + + + + + Crotonaldehyde + + + + + + Crotonaldehyde + + + + + + + + + + + modification from Unimod Other - + 70.09 + C 4 H 6 O 1 + 70.04186 + C 10 H 18 N 2 O 2 + 198.27 + 198.13683 + K + artifact + Unimod:253 + PSI-MOD + Crotonaldehyde + MOD:01278 + crotonylated L-lysine + + + + + modification from Unimod Other - + PubMed:11283024 + Unimod:253#K + + + + + Crotonaldehyde + + + + + + Crotonaldehyde + + + + + + + + + + + modification from Unimod Other - + 70.09 + C 4 H 6 O 1 + 70.04186 + C 10 H 13 N 3 O 2 + 207.23 + 207.10078 + H + artifact + Unimod:253 + PSI-MOD + Crotonaldehyde + MOD:01279 + crotonylated L-histidine + + + + + modification from Unimod Other - + PubMed:11283024 + PubMed:1443554 + Unimod:253#H + + + + + Crotonaldehyde + + + + + + Crotonaldehyde + + + + + + + + + + + modification from Unimod Chemical derivative - + 490.7 + C 20 H 34 N 4 O 4 S 3 + 490.17422 + C 24 H 41 N 5 O 6 S 3 + 591.8 + 591.2219 + T + artifact + Unimod:118 + PSI-MOD + EDT-iodo-PEO-biotin + EDT-iodoacetyl-PEO-biotin + MOD:01280 + EDT-iodo-PEO-biotin - site T + + + + + modification from Unimod Chemical derivative - + PubMed:11857757 + PubMed:12175151 + Unimod:118#T + + + + + EDT-iodo-PEO-biotin + + + + + + EDT-iodoacetyl-PEO-biotin + + + + + + + + + + + modification from Unimod Chemical derivative - + 490.7 + C 20 H 34 N 4 O 4 S 3 + 490.17422 + C 23 H 39 N 5 O 6 S 3 + 577.77 + 577.20624 + S + artifact + Unimod:118 + PSI-MOD + EDT-iodo-PEO-biotin + EDT-iodoacetyl-PEO-biotin + MOD:01281 + EDT-iodo-PEO-biotin - site S + + + + + modification from Unimod Chemical derivative - + PubMed:16335955 + Unimod:118#S + + + + + EDT-iodo-PEO-biotin + + + + + + EDT-iodoacetyl-PEO-biotin + + + + + + + + + OBSOLETE because this modification is not supported by the linked literature [PMT] + 56.06 + C 3 H 4 O 1 + 56.026215 + C 9 H 11 N 3 O 2 + 193.21 + 193.08513 + H + artifact + Unimod:206 + PSI-MOD + Acrolein addition +56 + Delta:H(4)C(3)O(1) + MOD:01282 + acrolein addition +56 - site H + true + + + + + OBSOLETE because this modification is not supported by the linked literature [PMT] + PubMed:10825247 + PubMed:15541752 + Unimod:206#H + + + + + Acrolein addition +56 + + + + + + Delta:H(4)C(3)O(1) + + + + + + + + + OBSOLETE because this modification is not supported by the linked literature [PMT] + 56.06 + C 3 H 4 O 1 + 56.026215 + C 9 H 16 N 2 O 2 + 184.24 + 184.12119 + K + artifact + Unimod:206 + PSI-MOD + Acrolein addition +56 + Delta:H(4)C(3)O(1) + MOD:01283 + acrolein addition +56 - site K + true + + + + + OBSOLETE because this modification is not supported by the linked literature [PMT] + PubMed:10825247 + PubMed:15541752 + Unimod:206#K + + + + + Acrolein addition +56 + + + + + + Delta:H(4)C(3)O(1) + + + + + + + + + OBSOLETE because this modification is not supported by the linked literature [PMT] + 56.06 + C 3 H 4 O 1 + 56.026215 + C 6 H 9 N 1 O 2 S 1 + 159.2 + 159.0354 + C + artifact + Unimod:206 + PSI-MOD + Acrolein addition +56 + Delta:H(4)C(3)O(1) + MOD:01284 + acrolein addition +56 - site C + true + + + + + OBSOLETE because this modification is not supported by the linked literature [PMT] + PubMed:10825247 + PubMed:15541752 + PubMed:9254591 + Unimod:206#C + + + + + Acrolein addition +56 + + + + + + Delta:H(4)C(3)O(1) + + + + + + + + + + + A protein modification that effectively converts an L-leucine residue to 6x(13)C,1x(15)N isotope labeled L-leucine. + 7.02 + (12)C -6 (13)C 6 (14)N -1 (15)N 1 + 7.017164 + (13)C 6 H 11 (15)N 1 O 1 + 120.1 + 120.10123 + L + artifact + Unimod:695 + PSI-MOD + 13C(6) 15N(1) Silac label + Label:13C(6)15N(1) + MOD:01285 + 6x(13)C,1x(15)N labeled L-leucine + + + + + A protein modification that effectively converts an L-leucine residue to 6x(13)C,1x(15)N isotope labeled L-leucine. + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + Unimod:695#L + + + + + 13C(6) 15N(1) Silac label + + + + + + Label:13C(6)15N(1) + + + + + + + + + + + A protein modification that effectively converts an L-isoleucine residue to 6x(13)C,1x(15)N isotope labeled L-isoleucine. + 7.02 + (12)C -6 (13)C 6 (14)N -1 (15)N 1 + 7.017164 + (13)C 6 H 11 (15)N 1 O 1 + 120.1 + 120.10123 + I + artifact + Unimod:695 + PSI-MOD + 13C(6) 15N(1) Silac label + Label:13C(6)15N(1) + MOD:01286 + 6x(13)C,1x(15)N labeled L-isoleucine + + + + + A protein modification that effectively converts an L-isoleucine residue to 6x(13)C,1x(15)N isotope labeled L-isoleucine. + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + Unimod:695#I + + + + + 13C(6) 15N(1) Silac label + + + + + + Label:13C(6)15N(1) + + + + + + + + + + + modification from Unimod Isotopic label - + 111.04 + (13)C 6 H 3 N 1 O 1 + 111.041595 + C 6 (13)C 6 H 15 N 3 O 2 + 239.14 + 239.13655 + K + artifact + Unimod:364 + PSI-MOD + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form + ICPL:13C(6) + MOD:01287 + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form - site K + + + + + modification from Unimod Isotopic label - + PubMed:11857757 + PubMed:15602776 + Unimod:364#K + + + + + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form + + + + + + ICPL:13C(6) + + + + + + + + + OBSOLETE because this is not supported by the literature [PMT] + 28.05 + C 2 H 4 + 28.0313 + C 8 H 11 N 3 O 1 + 165.2 + 165.09021 + H + artifact + Unimod:255 + PSI-MOD + Acetaldehyde +28 + Delta:H(4)C(2) + MOD:01288 + acetaldehyde +28 - site H + true + + + + + OBSOLETE because this is not supported by the literature [PMT] + Unimod:255#H + + + + + Acetaldehyde +28 + + + + + + Delta:H(4)C(2) + + + + + + + + + OBSOLETE because this is not supported by the literature [PMT] + 28.05 + C 2 H 4 + 28.0313 + C 8 H 16 N 2 O 1 + 156.23 + 156.12627 + K + artifact + Unimod:255 + PSI-MOD + Acetaldehyde +28 + Delta:H(4)C(2) + MOD:01289 + acetaldehyde +28 - site K + true + + + + + OBSOLETE because this is not supported by the literature [PMT] + Unimod:255#K + + + + + Acetaldehyde +28 + + + + + + Delta:H(4)C(2) + + + + + + + + + OBSOLETE because redundant and identical to MOD:00465. Remap to MOD:00465. + MOD:00465 + 32.0 + O 2 + 31.989828 + C 9 H 9 N 1 O 3 + 179.17 + 179.05824 + F + artifact + Unimod:425 + PSI-MOD + Dioxidation + dihydroxy + MOD:01290 + dihydroxylated residue - site F + true + + + + + OBSOLETE because redundant and identical to MOD:00465. Remap to MOD:00465. + PubMed:11857757 + PubMed:12175151 + PubMed:12686488 + PubMed:9252331 + Unimod:425 + + + + + Dioxidation + + + + + + dihydroxy + + + + + + + + + OBSOLETE because redundant and identical to MOD:00464. Remap to MOD:00464. + MOD:00464 + 32.0 + O 2 + 31.989828 + C 11 H 10 N 2 O 3 + 218.21 + 218.06914 + W + artifact + Unimod:425 + PSI-MOD + Dioxidation + dihydroxy + MOD:01291 + dihydroxylated residue - site W + true + + + + + OBSOLETE because redundant and identical to MOD:00464. Remap to MOD:00464. + PubMed:12643539 + PubMed:12686488 + PubMed:6273432 + PubMed:9252331 + Unimod:425 + + + + + Dioxidation + + + + + + dihydroxy + + + + + + + + + OBSOLETE because redundant and identical to MOD:00075. Map to MOD:00075. + MOD:00075 + 29.06 + C 2 H 5 + 29.039125 + P + natural + Unimod:529 + PSI-MOD + Delta:H(5)C(2) + Dimethylation of proline residue + MOD:01292 + dimethylation of proline residue + true + + + + + OBSOLETE because redundant and identical to MOD:00075. Map to MOD:00075. + Unimod:529 + + + + + Delta:H(5)C(2) + + + + + + Dimethylation of proline residue + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to L-aspartic acid with one (18)O. + 2.99 + H -1 N -1 (18)O 1 + 2.988262 + C 4 H 5 N 1 (16)O 2 (18)O 1 + 117.03 + 117.03119 + N + artifact + Unimod:366 + oxy18 + PSI-MOD + Deamidated:18O(1) + Deamidation in presence of O18 + MOD:01293 + + 1x(18)O labeled deamidated L-asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to L-aspartic acid with one (18)O. + OMSSA:139 + PubMed:8382902 + Unimod:366#N + + + + + oxy18 + + + + + + Deamidated:18O(1) + + + + + + Deamidation in presence of O18 + + + + + + + + + OBSOLETE identical and redundant with MOD:00791. Remap to MOD:00791. + MOD:00791 + 2.99 + H -1 N -1 (18)O 1 + 2.988262 + Q + artifact + PSI-MOD + Deamidated:18O(1) + Deamidation in presence of O18 + MOD:01294 + deamidation in presence of O18 -site Q + true + + + + + OBSOLETE identical and redundant with MOD:00791. Remap to MOD:00791. + PubMed:8382902 + + + + + Deamidated:18O(1) + + + + + + Deamidation in presence of O18 + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to monosodium L-aspartate. + 21.98 + H -1 Na 1 + 21.981943 + C 4 H 4 N 1 Na 1 O 3 + 137.07 + 137.00888 + D + artifact + Unimod:30 + Na1Asp + PSI-MOD + Cation:Na + Sodium adduct + MOD:01295 + + monosodium L-aspartate + + + + + A protein modification that effectively converts an L-aspartic acid residue to monosodium L-aspartate. + PubMed:12216740 + Unimod:30#D + + + + + Na1Asp + + + + + + Cation:Na + + + + + + Sodium adduct + + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to monosodium L-glutamate. + 21.98 + H -1 Na 1 + 21.981943 + C 5 H 6 N 1 Na 1 O 3 + 151.1 + 151.02454 + E + artifact + Unimod:30 + MSG + Na1Glu + PSI-MOD + Cation:Na + Sodium adduct + MOD:01296 + + monosodium L-glutamate + + + + + A protein modification that effectively converts an L-glutamic acid residue to monosodium L-glutamate. + PubMed:12216740 + Unimod:30#E + + + + + MSG + + + + + + Na1Glu + + + + + + Cation:Na + + + + + + Sodium adduct + + + + + + + + + + + A protein modification that effectively converts an L-proline residue to 5x(13)C labeled L-proline. + 5.02 + (12)C -5 (13)C 5 + 5.016774 + (13)C 5 H 7 N 1 O 1 + 102.07 + 102.069534 + P + artifact + Unimod:772 + PSI-MOD + 13C(5) Silac label + Label:13C(5) + MOD:01297 + In PubMed:12716131, fully (13)C labeled proline apparently resulted from the catabolic conversion of (13)C labeled L-arginine during SILAC. + 5x(13)C labeled L-proline + + + + + A protein modification that effectively converts an L-proline residue to 5x(13)C labeled L-proline. + PubMed:12716131 + Unimod:772#P + + + + + 13C(5) Silac label + + + + + + Label:13C(5) + + + + + + + + + + + + + + + + + A protein modification produced by formation of an adduct of an L-cysteine residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4. + 158.24 + C 9 H 18 O 2 + 158.13068 + C 12 H 23 N 1 O 3 S 1 + 261.38 + 261.13986 + C + artifact + Unimod:335 + PSI-MOD + HNE+Delta:H(2) + reduced 4-Hydroxynonenal + MOD:01298 + 4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG]. + reduced cysteine 4-hydroxynonenal adduct + + + + + A protein modification produced by formation of an adduct of an L-cysteine residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4. + PubMed:11910026 + PubMed:15133838 + Unimod:335#C + + + + + HNE+Delta:H(2) + + + + + + reduced 4-Hydroxynonenal + + + + + + + + + + + + + + + + + A protein modification produced by formation of an adduct of an L-histidine residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4. + 158.24 + C 9 H 18 O 2 + 158.13068 + C 15 H 30 N 2 O 3 + 286.42 + 286.22565 + K + artifact + Unimod:335 + PSI-MOD + HNE+Delta:H(2) + reduced 4-Hydroxynonenal + MOD:01299 + 4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG]. + reduced lysine 4-hydroxynonenal adduct + + + + + A protein modification produced by formation of an adduct of an L-histidine residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4. + PubMed:11910026 + PubMed:12148805 + PubMed:15133838 + Unimod:335#K + + + + + HNE+Delta:H(2) + + + + + + reduced 4-Hydroxynonenal + + + + + + + + + + + + + + + + + A protein modification produced by formation of an adduct of an L-histidine residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4. + 158.24 + C 9 H 18 O 2 + 158.13068 + C 15 H 25 N 3 O 3 + 295.38 + 295.1896 + H + artifact + Unimod:335 + PSI-MOD + HNE+Delta:H(2) + reduced 4-Hydroxynonenal + MOD:01300 + 4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG]. + reduced histidine 4-hydroxynonenal adduct + + + + + A protein modification produced by formation of an adduct of an L-histidine residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4. + PubMed:11910026 + PubMed:12148805 + PubMed:15133838 + Unimod:335#H + + + + + HNE+Delta:H(2) + + + + + + reduced 4-Hydroxynonenal + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to 2-amino-3-(methylamino)butanoic acid. + 13.04 + C 1 H 3 N 1 O -1 + 13.031634 + C 5 H 10 N 2 O 1 + 114.15 + 114.079315 + T + artifact + Unimod:337 + PSI-MOD + Methylamine + Michael addition with methylamine + MOD:01301 + In PubMed:11743741 phosphothreonine is converted to dehydrobutyrine in base, then by Michael addition of methylamine to 2-amino-3-(methylamino)butanoic acid. + methylamine Michael addition derivatized threonine + + + + + A protein modification that effectively converts an L-threonine residue to 2-amino-3-(methylamino)butanoic acid. + PubMed:11743741 + Unimod:337#T + + + + + Methylamine + + + + + + Michael addition with methylamine + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to 2-amino-3-(methylamino)propanoic acid. + 13.04 + C 1 H 3 N 1 O -1 + 13.031634 + C 4 H 8 N 2 O 1 + 100.12 + 100.06366 + S + artifact + Unimod:337 + PSI-MOD + Methylamine + Michael addition with methylamine + MOD:01302 + In PubMed:11743741 phosphoserine is converted to dehydroalanine in base, then by Michael addition of methylamine to 2-amino-3-(methylamino)propanoic acid. + methylamine Michael addition derivatized serine + + + + + A protein modification that effectively converts an L-serine residue to 2-amino-3-(methylamino)propanoic acid. + PubMed:11743741 + Unimod:337#S + + + + + Methylamine + + + + + + Michael addition with methylamine + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to an N4-hexosaminyl-L-asparagine. + 161.16 + C 6 H 11 N 1 O 4 + 161.0688 + C 10 H 17 N 3 O 6 + 275.26 + 275.11172 + N + artifact + Unimod:454 + PSI-MOD + HexN + Hexosamine + MOD:01303 + The natural modifications are N4-(N-acetylamino)galactosyl-L-asparagine (MOD:00832) or N4-(N-acetylamino)glucosyl-L-asparagine (MOD:00831) [JSG]. + N4-hexosaminylated asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to an N4-hexosaminyl-L-asparagine. + PubMed:11467524 + Unimod:454#N + + + + + HexN + + + + + + Hexosamine + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to an N4-hexosaminyl-L-lysine, as a synthetic peptide protectting group. + 161.16 + C 6 H 11 N 1 O 4 + 161.0688 + C 12 H 23 N 3 O 5 + 289.33 + 289.16376 + K + artifact + Unimod:454 + PSI-MOD + HexN + Hexosamine + MOD:01304 + N6-hexosaminylated lysine + + + + + A protein modification that effectively converts an L-lysine residue to an N4-hexosaminyl-L-lysine, as a synthetic peptide protectting group. + Unimod:454#K + + + + + HexN + + + + + + Hexosamine + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to N1'-hexosaminyl-L-tryptophan. + 161.16 + C 6 H 11 N 1 O 4 + 161.0688 + C 17 H 21 N 3 O 5 + 347.37 + 347.14813 + W + artifact + Unimod:454 + PSI-MOD + HexN + Hexosamine + MOD:01305 + The natural modification is N1'-mannosyl-L-tryptophan (MOD:00165) [JSG]. + N1'-hexosaminylated tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to N1'-hexosaminyl-L-tryptophan. + Unimod:454#W + + + + + HexN + + + + + + Hexosamine + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-hexosaminyl-L-threonine. + 161.16 + C 6 H 11 N 1 O 4 + 161.0688 + C 10 H 18 N 2 O 6 + 262.26 + 262.1165 + T + natural + Unimod:454 + PSI-MOD + HexN + Hexosamine + MOD:01306 + The natural modifications are O-(N-acetylaminogalactosyl)-L-threonine (MOD:00164) or O-(N-acetylaminoglucosyl)-L-threonine (MOD:00806) [JSG]. + O-hexosaminylated threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-hexosaminyl-L-threonine. + Unimod:454#T + + + + + HexN + + + + + + Hexosamine + + + + + + + + + + + modification from Unimod Chemical derivative - + 525.66 + C 19 H 34 N 4 O 5 P 1 S 3 + 525.1429 + C 22 H 39 N 5 O 7 P 1 S 3 + 612.74 + 612.1749 + S + artifact + Unimod:332 + PSI-MOD + Thiophos-S-S-biotin + thiophosphate labeled with biotin-HPDP + MOD:01307 + thiophosphate labeled with biotin-HPDP -site S + + + + + modification from Unimod Chemical derivative - + Unimod:332#S + + + + + Thiophos-S-S-biotin + + + + + + thiophosphate labeled with biotin-HPDP + + + + + + + + + + + modification from Unimod Chemical derivative - + 525.66 + C 19 H 34 N 4 O 5 P 1 S 3 + 525.1429 + C 23 H 41 N 5 O 7 P 1 S 3 + 626.76 + 626.19055 + T + artifact + Unimod:332 + PSI-MOD + Thiophos-S-S-biotin + thiophosphate labeled with biotin-HPDP + MOD:01308 + thiophosphate labeled with biotin-HPDP -site T + + + + + modification from Unimod Chemical derivative - + Unimod:332#T + + + + + Thiophos-S-S-biotin + + + + + + thiophosphate labeled with biotin-HPDP + + + + + + + + + + + modification from Unimod Chemical derivative - + 525.66 + C 19 H 34 N 4 O 5 P 1 S 3 + 525.1429 + C 28 H 43 N 5 O 7 P 1 S 3 + 688.83 + 688.20624 + Y + artifact + Unimod:332 + PSI-MOD + Thiophos-S-S-biotin + thiophosphate labeled with biotin-HPDP + MOD:01309 + thiophosphate labeled with biotin-HPDP - site Y + + + + + modification from Unimod Chemical derivative - + Unimod:332#Y + + + + + Thiophos-S-S-biotin + + + + + + thiophosphate labeled with biotin-HPDP + + + + + + + + + + + A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent light form group. + 59.07 + C 3 (1)H 9 N 1 + 59.073498 + C 9 (1)H 21 N 3 O 1 + 187.17 + 187.16846 + K + artifact + Unimod:60 + PSI-MOD + GIST-Quat + Quaternary amine labeling reagent light form (N-term & K) + MOD:01310 + quaternary amine labeling reagent light form N6-L-lysine + + + + + A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent light form group. + PubMed:11857757 + Unimod:60#K + + + + + GIST-Quat + + + + + + Quaternary amine labeling reagent light form (N-term & K) + + + + + + + + + + + A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+3amu) form group. + 62.09 + C 3 (1)H 6 (2)H 3 N 1 + 62.09233 + C 9 (1)H 18 (2)H 3 N 3 O 1 + 190.19 + 190.18729 + K + artifact + Unimod:61 + PSI-MOD + GIST-Quat:2H(3) + Quaternary amine labeling reagent heavy (+3amu) form, N-term & K + MOD:01311 + quaternary amine labeling reagent heavy form (+3amu) N6-L-lysine + + + + + A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+3amu) form group. + PubMed:11698400 + PubMed:11857757 + PubMed:11914093 + Unimod:61#K + + + + + GIST-Quat:2H(3) + + + + + + Quaternary amine labeling reagent heavy (+3amu) form, N-term & K + + + + + + + + + + + A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+6amu) form group. + 65.11 + C 3 (1)H 3 (2)H 6 N 1 + 65.11116 + C 9 (1)H 15 (2)H 6 N 3 O 1 + 193.21 + 193.20612 + K + artifact + Unimod:62 + PSI-MOD + GIST-Quat:2H(6) + Quaternary amine labeling reagent heavy form (+6amu), N-term & K + MOD:01312 + Apparently incorrect parent [JSG]. + quaternary amine labeling reagent heavy form (+6amu) N6-L-lysine + + + + + A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+6amu) form group. + PubMed:11857757 + Unimod:62#K + + + + + GIST-Quat:2H(6) + + + + + + Quaternary amine labeling reagent heavy form (+6amu), N-term & K + + + + + + + + + + + A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+9amu) form group. + 68.13 + C 3 (2)H 9 N 1 + 68.12999 + C 9 (1)H 12 (2)H 9 N 3 O 1 + 196.22 + 196.22496 + K + artifact + Unimod:63 + PSI-MOD + GIST-Quat:2H(9) + Quaternary amine labeling reagent heavy form (+9amu), N-term & K + MOD:01313 + quaternary amine labeling reagent heavy form (+9amu) N6-L-lysine + + + + + A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+9amu) form group. + PubMed:11857757 + Unimod:63#K + + + + + GIST-Quat:2H(9) + + + + + + Quaternary amine labeling reagent heavy form (+9amu), N-term & K + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 4x(1)H,4x(12)C-labeled N6-succinyl-L-lysine. + 100.02 + (12)C 4 (1)H 4 O 3 + 100.016045 + (12)C 10 H 16 N 2 O 4 + 228.11 + 228.11101 + K + artifact + Unimod:64 + PSI-MOD + Succinic anhydride labeling reagent light form (K) + Succinyl + MOD:01314 + 4x(1)H,4x(12)C-labeled N6-succinyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to 4x(1)H,4x(12)C-labeled N6-succinyl-L-lysine. + PubMed:11857757 + PubMed:12175151 + PubMed:12716131 + Unimod:64#K + + + + + Succinic anhydride labeling reagent light form (K) + + + + + + Succinyl + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 4x(2)H-labeled N6-succinyl-L-lysine. + 104.04 + C 4 (2)H 4 O 3 + 104.04115 + C 10 (1)H 12 (2)H 4 N 2 O 4 + 232.14 + 232.13611 + K + artifact + Unimod:65 + PSI-MOD + Succinic anhydride labeling reagent, heavy form (+4amu, 4H2), N-term & K + Succinyl:2H(4) + MOD:01315 + 4x(2)H labeled N6-succinyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to 4x(2)H-labeled N6-succinyl-L-lysine. + PubMed:11344537 + PubMed:11857757 + PubMed:12175151 + PubMed:15189151 + Unimod:65#K + + + + + Succinic anhydride labeling reagent, heavy form (+4amu, 4H2), N-term & K + + + + + + Succinyl:2H(4) + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 4x(13)C labeled N6-succinyl-L-lysine. + 104.03 + (13)C 4 H 4 O 3 + 104.029465 + (12)C 6 (13)C 4 H 16 N 2 O 4 + 232.12 + 232.12442 + K + artifact + Unimod:66 + PSI-MOD + Succinic anhydride labeling reagent, heavy form (+4amu, 4C13), K + Succinyl:13C(4) + MOD:01316 + 4x(13)C labeled N6-succinyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to 4x(13)C labeled N6-succinyl-L-lysine. + PubMed:11344537 + PubMed:11857757 + PubMed:12175151 + PubMed:15189151 + Unimod:66#K + + + + + Succinic anhydride labeling reagent, heavy form (+4amu, 4C13), K + + + + + + Succinyl:13C(4) + + + + + + + + + + + modification from Unimod Chemical derivative - + 87.18 + C 4 H 9 N 1 O -1 S 1 + 87.05066 + C 8 H 16 N 2 O 1 S 1 + 188.29 + 188.09833 + T + artifact + Unimod:178 + PSI-MOD + DAET + phosphorylation to amine thiol + MOD:01317 + phosphorylation to amine thiol - site T + + + + + modification from Unimod Chemical derivative - + PubMed:12216740 + Unimod:178#T + + + + + DAET + + + + + + phosphorylation to amine thiol + + + + + + + + + + + modification from Unimod Chemical derivative - + 87.18 + C 4 H 9 N 1 O -1 S 1 + 87.05066 + C 7 H 14 N 2 O 1 S 1 + 174.26 + 174.08269 + S + artifact + Unimod:178 + PSI-MOD + DAET + phosphorylation to amine thiol + MOD:01318 + phosphorylation to amine thiol - site S + + + + + modification from Unimod Chemical derivative - + PubMed:11510821 + PubMed:12216740 + PubMed:12422359 + Unimod:178#S + + + + + DAET + + + + + + phosphorylation to amine thiol + + + + + + + + + + + modification from Unimod Other + 218.34 + C 15 H 22 O 1 + 218.16707 + C 21 H 29 N 3 O 2 + 355.48 + 355.22598 + H + artifact + Unimod:176 + PSI-MOD + BHT + Michael addition of BHT quinone methide to Cysteine and Lysine + MOD:01319 + Secondary adduct, much less common than cysteine. [Unimod] + Michael addition of BHT quinone methide to histidine + + + + + modification from Unimod Other + PubMed:11510821 + PubMed:12422359 + PubMed:9448752 + Unimod:176#H + + + + + BHT + + + + + + Michael addition of BHT quinone methide to Cysteine and Lysine + + + + + + + + + + + modification from Unimod Other + 218.34 + C 15 H 22 O 1 + 218.16707 + C 21 H 34 N 2 O 2 + 346.51 + 346.26202 + K + artifact + Unimod:176 + PSI-MOD + BHT + Michael addition of BHT quinone methide to Cysteine and Lysine + MOD:01320 + Secondary adduct, much less common than cysteine. [Unimod] + Michael addition of BHT quinone methide to lysine + + + + + modification from Unimod Other + PubMed:16078144 + PubMed:9448752 + Unimod:176#K + + + + + BHT + + + + + + Michael addition of BHT quinone methide to Cysteine and Lysine + + + + + + + + + + + modification from Unimod Other + 218.34 + C 15 H 22 O 1 + 218.16707 + C 18 H 27 N 1 O 2 S 1 + 321.48 + 321.17624 + C + artifact + Unimod:176 + PSI-MOD + BHT + Michael addition of BHT quinone methide to Cysteine and Lysine + MOD:01321 + Primary adduct formed. [Unimod] + Michael addition of BHT quinone methide to cysteine + + + + + modification from Unimod Other + PubMed:11510821 + PubMed:12422359 + PubMed:9448752 + Unimod:176#C + + + + + BHT + + + + + + Michael addition of BHT quinone methide to Cysteine and Lysine + + + + + + + + + OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other - + 40.06 + C 3 H 4 + 40.0313 + C 9 H 16 N 2 O 1 + 168.24 + 168.12627 + K + artifact + Unimod:256 + PSI-MOD + Delta:H(4)C(3) + Propionaldehyde +40 + MOD:01322 + propionaldehyde +40 - site K + true + + + + + OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other - + PubMed:15549660 + Unimod:256#K + + + + + Delta:H(4)C(3) + + + + + + Propionaldehyde +40 + + + + + + + + + OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other - + 40.06 + C 3 H 4 + 40.0313 + C 9 H 11 N 3 O 1 + 177.21 + 177.09021 + H + artifact + Unimod:256 + PSI-MOD + Delta:H(4)C(3) + Propionaldehyde +40 + MOD:01323 + propionaldehyde +40 - site H + true + + + + + OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other - + Unimod:256#H + + + + + Delta:H(4)C(3) + + + + + + Propionaldehyde +40 + + + + + + + + + OBSOLETE because this is not supported by the linked literature [PMT] + 26.04 + C 2 H 2 + 26.01565 + C 8 H 9 N 3 O 1 + 163.18 + 163.07455 + H + artifact + Unimod:254 + PSI-MOD + Acetaldehyde +26 + Delta:H(2)C(2) + MOD:01324 + acetaldehyde +26 - site H + true + + + + + OBSOLETE because this is not supported by the linked literature [PMT] + PubMed:7744761 + Unimod:254#H + + + + + Acetaldehyde +26 + + + + + + Delta:H(2)C(2) + + + + + + + + + OBSOLETE because this is not supported by the linked literature [PMT] + 26.04 + C 2 H 2 + 26.01565 + C 8 H 14 N 2 O 1 + 154.21 + 154.11061 + K + artifact + Unimod:254 + PSI-MOD + Acetaldehyde +26 + Delta:H(2)C(2) + MOD:01325 + acetaldehyde +26 - site K + true + + + + + OBSOLETE because this is not supported by the linked literature [PMT] + PubMed:7744761 + Unimod:254#K + + + + + Acetaldehyde +26 + + + + + + Delta:H(2)C(2) + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to 9x(13)C labeled L-tyrosine. + 9.03 + (12)C -9 (13)C 9 + 9.030194 + (13)C 9 H 9 N 1 O 2 + 172.09 + 172.09352 + Y + artifact + Unimod:184 + PSI-MOD + 13C(9) Silac label + Label:13C(9) + MOD:01326 + 9x(13)C labeled L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to 9x(13)C labeled L-tyrosine. + PubMed:11510821 + PubMed:12422359 + PubMed:12716131 + Unimod:184#Y + + + + + 13C(9) Silac label + + + + + + Label:13C(9) + + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to 9x(13)C labeled L-phenylalanine. + 9.03 + (12)C -9 (13)C 9 + 9.030194 + (13)C 9 H 9 N 1 O 1 + 156.1 + 156.0986 + F + artifact + Unimod:184 + PSI-MOD + 13C(9) Silac label + Label:13C(9) + MOD:01327 + 9x(13)C labeled L-phenylalanine + + + + + A protein modification that effectively converts an L-phenylalanine residue to 9x(13)C labeled L-phenylalanine. + PubMed:12716131 + Unimod:184#F + + + + + 13C(9) Silac label + + + + + + Label:13C(9) + + + + + + + + + + + modification from Unimod Chemical derivative - hydroxylethanone + 58.04 + C 2 H 2 O 2 + 58.005478 + C 13 H 12 N 2 O 3 + 244.25 + 244.0848 + W + artifact + Unimod:6 + PSI-MOD + Carboxymethyl + Iodoacetic acid derivative + MOD:01328 + There is no citation for this Unimod entry. Iodoacetic acid derivatization of tryptophan is not mentioned in the citation [JSG]. + iodoacetic acid - site W + + + + + modification from Unimod Chemical derivative - hydroxylethanone + PubMed:17525468 + Unimod:6#W + + + + + Carboxymethyl + + + + + + Iodoacetic acid derivative + + + + + + + + + OBSOLETE because duplicate and redundant with MOD:01061. Remap to MOD:01061 + MOD:01061 + 58.04 + C 2 H 2 O 2 + 58.005478 + C + artifact + Unimod:6 + PSI-MOD + Carboxymethyl + Iodoacetic acid derivative + MOD:01329 + Modification from Unimod Chemical derivative, Unimod:6 site C + iodoacetic acid - site C + true + + + + + OBSOLETE because duplicate and redundant with MOD:01061. Remap to MOD:01061 + DeltaMass:197 + + + + + Carboxymethyl + + + + + + Iodoacetic acid derivative + + + + + + + + + OBSOLETE because identical with MOD:01094. Remap to MOD:01094 + MOD:01094 + 58.04 + C 2 H 2 O 2 + 58.005478 + K + artifact + Unimod:6 + PSI-MOD + Carboxymethyl + Iodoacetic acid derivative + MOD:01330 + a modification from Unimod:6 + iodoacetic acid -site K + true + + + + + OBSOLETE because identical with MOD:01094. Remap to MOD:01094 + PubMed:18688235 + + + + + Carboxymethyl + + + + + + Iodoacetic acid derivative + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to 6x(13)C labeled L-arginine. + 6.02 + (12)C -6 (13)C 6 + 6.020129 + (13)C 6 H 12 N 4 O 1 + 162.12 + 162.12125 + R + artifact + Unimod:188 + arg-13c6 + PSI-MOD + 13C(6) Silac label + Label:13C(6) + MOD:01331 + + 6x(13)C labeled L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to 6x(13)C labeled L-arginine. + OMSSA:136 + PubMed:12716131 + Unimod:188#R + + + + + arg-13c6 + + + + + + 13C(6) Silac label + + + + + + Label:13C(6) + + + + + + + + + + A protein modification that effectively converts an L-leucine residue to 6x(13)C labeled L-leucine. + 6.02 + (12)C -6 (13)C 6 + 6.020129 + (13)C 6 H 11 N 1 O 1 + 119.1 + 119.104195 + L + artifact + Unimod:188 + PSI-MOD + 13C(6) Silac label + Label:13C(6) + MOD:01332 + + 6x(13)C labeled L-leucine + + + + + A protein modification that effectively converts an L-leucine residue to 6x(13)C labeled L-leucine. + PubMed:12716131 + Unimod:188#L + + + + + 13C(6) Silac label + + + + + + Label:13C(6) + + + + + + + + + + A protein modification that effectively converts an L-isoleucine residue to 6x(13)C labeled L-isoleucine. + 6.02 + (12)C -6 (13)C 6 + 6.020129 + (13)C 6 H 11 N 1 O 1 + 119.1 + 119.104195 + I + artifact + Unimod:188 + PSI-MOD + 13C(6) Silac label + Label:13C(6) + MOD:01333 + + 6x(13)C labeled L-isoleucine + + + + + A protein modification that effectively converts an L-isoleucine residue to 6x(13)C labeled L-isoleucine. + PubMed:12716131 + PubMed:12766232 + Unimod:188#I + + + + + 13C(6) Silac label + + + + + + Label:13C(6) + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 6x(13)C labeled L-lysine. + 6.02 + (12)C -6 (13)C 6 + 6.020129 + (13)C 6 H 12 N 2 O 1 + 134.12 + 134.1151 + K + artifact + Unimod:188 + lys-13c6 + PSI-MOD + 13C(6) Silac label + Label:13C(6) + MOD:01334 + + 6x(13)C labeled L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to 6x(13)C labeled L-lysine. + OMSSA:138 + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + PubMed:12716131 + Unimod:188#K + + + + + lys-13c6 + + + + + + 13C(6) Silac label + + + + + + Label:13C(6) + + + + + + + + + + + modification from Unimod Chemical derivative - + 220.99 + (12)C 1 (13)C 6 H 5 N 1 O 3 S 2 + 220.99121 + (12)C 7 (13)C 6 H 17 N 3 O 4 S 2 + 349.09 + 349.08618 + K + artifact + Unimod:464 + PSI-MOD + 4-sulfophenyl isothiocyanate (Heavy C13) + SPITC:13C(6) + MOD:01335 + 6x(13)C labeled 4-sulfophenyl isothiocyanate derivatized lysine + + + + + modification from Unimod Chemical derivative - + PubMed:11467524 + PubMed:16526082 + Unimod:464#K + + + + + 4-sulfophenyl isothiocyanate (Heavy C13) + + + + + + SPITC:13C(6) + + + + + + + + + OBSOLETE - identical and redundant with MOD:00657. Remap to MOD:00657. + MOD:00657 + 15.01 + C 1 H 1 N -1 O 1 + 14.999666 + Q + natural + Unimod:528 + PSI-MOD + Deamidation followed by a methylation + Methyl+Deamidated + MOD:01336 + Modification from Unimod Post-translational - Unimod:528. + deamidation followed by a methylation -site Q + true + + + + + OBSOLETE - identical and redundant with MOD:00657. Remap to MOD:00657. + PubMed:18688235 + + + + + Deamidation followed by a methylation + + + + + + Methyl+Deamidated + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to L-aspartate 4-methyl ester. + 15.01 + C 1 H 1 N -1 O 1 + 14.999666 + C 5 H 7 N 1 O 3 + 129.12 + 129.04259 + N + artifact + Unimod:528 + PSI-MOD + Deamidation followed by a methylation + Methyl+Deamidated + MOD:01337 + The deamidation and methylation of L-asparagine has not been reported as a natural modification. It is extremely unlikely that eukaryotes produce this modification, because a natural process that would form L-aspartic acid 4-methyl ester from either L-aspartic acid or L-asparagine would interfere with the D-aspartyl peptide repair mechanism [JSG]. + deamidated 4-methyl esterified asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to L-aspartate 4-methyl ester. + Unimod:528#N + + + + + Deamidation followed by a methylation + + + + + + Methyl+Deamidated + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-ethyl-L-lysine. + 28.05 + C 2 H 4 + 28.0313 + C 8 H 16 N 2 O 1 + 156.23 + 156.12627 + K + hypothetical + Unimod:280 + PSI-MOD + Ethyl + Ethylation + MOD:01338 + The Unimod citation refers to the formation of glutamate ethyl ester and not to either lysine or N-terminal alkylation [JSG]. + N6-ethyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-ethyl-L-lysine. + PubMed:9629898 + Unimod:280#K + + + + + Ethyl + + + + + + Ethylation + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an ethyl group. + 28.05 + C 2 H 4 + 28.0313 + X + artifact + Unimod:280 + EtRes + PSI-MOD + Ethyl + Ethylation + MOD:01339 + From DeltaMass: Average Mass: 28 with no citation. The Unimod citation refers to the formation of glutamate ethyl ester and not to either lysine or N-terminal alkylation [JSG]. + ethylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an ethyl group. + PubMed:9629898 + Unimod:280 + + + + + EtRes + + + + + + Ethyl + + + + + + Ethylation + + + + + + + + + + + modification from Unimod Isotopic label - + 348.24 + C 16 (1)H 16 (2)H 10 N 4 O 2 S 1 + 348.24042 + C 22 (1)H 28 (2)H 10 N 6 O 3 S 1 + 476.34 + 476.3354 + K + artifact + Unimod:91 + PSI-MOD + ESP-Tag heavy d10 + ESP:2H(10) + MOD:01340 + ESP-Tag heavy d10 - site K + + + + + modification from Unimod Isotopic label - + PubMed:11078590 + PubMed:11085420 + PubMed:11821862 + Unimod:91#K + + + + + ESP-Tag heavy d10 + + + + + + ESP:2H(10) + + + + + + + + + + + modification from Unimod Isotopic label - + 338.47 + C 16 H 26 N 4 O 2 S 1 + 338.17764 + C 22 H 38 N 6 O 3 S 1 + 466.64 + 466.2726 + K + artifact + Unimod:90 + PSI-MOD + ESP + ESP-Tag light d0 + MOD:01341 + ESP-Tag light d0 - site K + + + + + modification from Unimod Isotopic label - + Unimod:90#K + + + + + ESP + + + + + + ESP-Tag light d0 + + + + + + + + + OBSOLETE because redundant and identical to MOD:00530. Remap to MOD:00530. + MOD:00530 + 46.91 + S -1 Se 1 + 47.94445 + C 5 H 9 N 1 O 1 S 0 Se 1 + 178.1 + 178.98494 + M + artifact + Unimod:162 + PSI-MOD + Delta:S(-1)Se(1) + Selenium replaces sulphur + MOD:01342 + selenium substitution for sulfur - site M + true + + + + + OBSOLETE because redundant and identical to MOD:00530. Remap to MOD:00530. + PubMed:12148805 + Unimod:162 + + + + + Delta:S(-1)Se(1) + + + + + + Selenium replaces sulphur + + + + + + + + + OBSOLETE because redundant and identical to MOD:00686. Remap to MOD:00686. + MOD:00686 + 46.91 + S -1 Se 1 + 47.94445 + C 3 H 5 N 1 O 1 S 0 Se 1 + 150.05 + 150.95363 + C + artifact + Unimod:162 + PSI-MOD + Delta:S(-1)Se(1) + Selenium replaces sulphur + MOD:01343 + selenium substitution for sulfur - site C + true + + + + + OBSOLETE because redundant and identical to MOD:00686. Remap to MOD:00686. + PubMed:12148805 + Unimod:162 + + + + + Delta:S(-1)Se(1) + + + + + + Selenium replaces sulphur + + + + + + + + + OBSOLETE because redundant and identical with MOD:00835. Remap to MOD:00835. + MOD:00835 + -2.02 + H -2 + -2.01565 + S + natural + Unimod:401 + PSI-MOD + 2-amino-3-oxo-butanoic_acid + Didehydro + MOD:01344 + dehydrogenated residue - site S + true + + + + + OBSOLETE because redundant and identical with MOD:00835. Remap to MOD:00835. + PubMed:9252331 + PubMed:9276974 + Unimod:401 + + + + + 2-amino-3-oxo-butanoic_acid + + + + + + Didehydro + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to 2-amino-3-oxobutanoic acid. + -2.02 + H -2 + -2.01565 + C 4 H 5 N 1 O 2 + 99.09 + 99.03203 + T + artifact + Unimod:401 + 2-amino-3-ketobutyric acid + 3-ketobutyrine + twoamino3oxobutanoicacid + PSI-MOD + 2-amino-3-oxo-butanoic_acid + Didehydro + MOD:01345 + There is no citation for this modification in the Unimod entry. Although mentioned in PubMed:9252331, there is no citation for it there [JSG]. + 2-amino-3-oxobutanoic acid + + + + + A protein modification that effectively converts an L-threonine residue to 2-amino-3-oxobutanoic acid. + OMSSA:23 + PubMed:12716131 + PubMed:9252331 + Unimod:401#T + + + + + 2-amino-3-ketobutyric acid + + + + + + 3-ketobutyrine + + + + + + twoamino3oxobutanoicacid + + + + + + 2-amino-3-oxo-butanoic_acid + + + + + + Didehydro + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to an N4-hexosyl-L-asparagine. + 162.14 + C 6 H 10 O 5 + 162.05283 + C 10 H 16 N 2 O 7 + 276.25 + 276.09576 + N + natural + Unimod:41 + PSI-MOD + Hex + Hexose + MOD:01346 + N4-hexosylated asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to an N4-hexosyl-L-asparagine. + PubMed:11112526 + PubMed:11567090 + PubMed:15279557 + PubMed:6540775 + Unimod:41#N + + + + + Hex + + + + + + Hexose + + + + + + + + + + + A modification produced in a non-enzymatic reaction between a carbohydrate carbonyl group (C1 of aldohexose or C2 of fructose) and an L-lysine residue to form a Schiff-base or an Amadori ketosamine lysine adduct. + 162.14 + C 6 H 10 O 5 + 162.05283 + C 12 H 22 N 2 O 6 + 290.32 + 290.1478 + K + natural + Unimod:41 + PSI-MOD + Hex + Hexose + MOD:01347 + hexose glycated L-lysine + + + + + A modification produced in a non-enzymatic reaction between a carbohydrate carbonyl group (C1 of aldohexose or C2 of fructose) and an L-lysine residue to form a Schiff-base or an Amadori ketosamine lysine adduct. + DeltaMass:0 + PubMed:15279557 + Unimod:41#K + + + + + Hex + + + + + + Hexose + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to an O-hexosyl-L-threonine. + 162.14 + C 6 H 10 O 5 + 162.05283 + C 10 H 17 N 1 O 7 + 263.25 + 263.1005 + T + natural + Unimod:41 + PSI-MOD + Hex + Hexose + MOD:01348 + O-hexosylated threonine + + + + + A protein modification that effectively converts an L-threonine residue to an O-hexosyl-L-threonine. + PubMed:15279557 + PubMed:8597590 + Unimod:41#T + + + + + Hex + + + + + + Hexose + + + + + + + + + + + modification from Unimod Chemical derivative - + 143.14 + C 6 H 9 N 1 O 3 + 143.05824 + C 9 H 14 N 2 O 4 S 1 + 246.28 + 246.06743 + C + artifact + Unimod:320 + PSI-MOD + Nethylmaleimide+water + Nethylmaleimidehydrolysis + MOD:01349 + Hydolyzed N-ethylmaeimide adduct, a mixture of isobaric 2- and 3-(S-cysteinyl)-4-(ethylamino)-4-oxobutanoic acid [JSG]. + hydrolyzed N-ethylmaleimide cysteine adduct + + + + + modification from Unimod Chemical derivative - + Unimod:320#C + + + + + Nethylmaleimide+water + + + + + + Nethylmaleimidehydrolysis + + + + + + + + + + modification from Unimod Chemical derivative - + 143.14 + C 6 H 9 N 1 O 3 + 143.05824 + C 12 H 21 N 3 O 4 + 271.32 + 271.1532 + K + artifact + Unimod:320 + PSI-MOD + Nethylmaleimide+water + Nethylmaleimidehydrolysis + MOD:01350 + Hydolyzed N-ethylmaeimide adduct, a mixture of isobaric 2- and 3-(N6-lysyl)-4-(ethylamino)-4-oxobutanoic acid [JSG]. + hydrolyzed N-ethylmaleimide lysine adduct + + + + + modification from Unimod Chemical derivative - + Unimod:320#K + + + + + Nethylmaleimide+water + + + + + + Nethylmaleimidehydrolysis + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to a nitrated L-tryptophan. + 45.0 + H -1 N 1 O 2 + 44.985077 + C 11 H 9 N 3 O 3 + 231.21 + 231.06439 + W + artifact + Unimod:354 + nitrow + PSI-MOD + Nitro + Oxidation to nitro + MOD:01351 + One or more isobaric isomers are produced by nitration with peroxynitrite reagent [JSG]. + nitrated L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to a nitrated L-tryptophan. + OMSSA:85 + PubMed:8839040 + PubMed:9252331 + Unimod:354#W + + + + + nitrow + + + + + + Nitro + + + + + + Oxidation to nitro + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to a nitrated L-tyrosine. + 45.0 + H -1 N 1 O 2 + 44.985077 + C 9 H 8 N 2 O 4 + 208.17 + 208.0484 + Y + artifact + Unimod:354 + uniprot.ptm:PTM-0213 + nitroy + PSI-MOD + Nitro + Oxidation to nitro + MOD:01352 + + One or more isobaric isomers are produced by nitration with peroxynitrite reagent [JSG]. + nitrated L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to a nitrated L-tyrosine. + OMSSA:86 + PubMed:14678012 + PubMed:8839040 + PubMed:9252331 + Unimod:354#Y + + + + + nitroy + + + + + + Nitro + + + + + + Oxidation to nitro + + + + + + + + + + + modification from Unimod Chemical derivative - + 41.05 + C 2 H 3 N 1 + 41.02655 + C 8 H 15 N 3 O 1 + 169.23 + 169.1215 + K + artifact + Unimod:141 + PSI-MOD + Amidine + amidination of lysines or N-terminal amines with methyl acetimidate + MOD:01353 + amidination of lysines or N-terminal amines with methyl acetimidate - site K + + + + + modification from Unimod Chemical derivative - + PubMed:12643539 + PubMed:15602776 + PubMed:6273432 + Unimod:141#K + + + + + Amidine + + + + + + amidination of lysines or N-terminal amines with methyl acetimidate + + + + + + + + + + + A protein modification that effectively replaces an N4 hydrogen atom of an asparagine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond. + 657.6 + C 25 H 41 N 2 O 18 + 657.2354 + C 29 H 47 N 4 O 20 + 771.7 + 771.2784 + N + natural + Unimod:149 + PSI-MOD + Hex(1)HexNAc(1)NeuAc(1) + Hex1HexNAc1NeuAc1 + MOD:01354 + Hex1HexNAc1NeuAc1 N4-glycosylated asparagine + + + + + A protein modification that effectively replaces an N4 hydrogen atom of an asparagine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond. + PubMed:11698400 + Unimod:149#N + + + + + Hex(1)HexNAc(1)NeuAc(1) + + + + + + Hex1HexNAc1NeuAc1 + + + + + + + + + + + A protein modification that effectively replaces an O3 hydrogen atom of a threonine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond. + 657.6 + C 25 H 41 N 2 O 18 + 657.2354 + C 29 H 48 N 3 O 20 + 758.7 + 758.28314 + T + natural + Unimod:149 + PSI-MOD + Hex(1)HexNAc(1)NeuAc(1) + Hex1HexNAc1NeuAc1 + MOD:01355 + Hex1HexNAc1NeuAc1 O-glycosylated threonine + + + + + A protein modification that effectively replaces an O3 hydrogen atom of a threonine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond. + Unimod:149#T + + + + + Hex(1)HexNAc(1)NeuAc(1) + + + + + + Hex1HexNAc1NeuAc1 + + + + + + + + + + + A protein modification that effectively replaces an O3 hydrogen atom of a serine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond. + 657.6 + C 25 H 41 N 2 O 18 + 657.2354 + C 28 H 46 N 3 O 20 + 744.68 + 744.26746 + S + natural + Unimod:149 + PSI-MOD + Hex(1)HexNAc(1)NeuAc(1) + Hex1HexNAc1NeuAc1 + MOD:01356 + Hex1HexNAc1NeuAc1 O-glycosylated serine + + + + + A protein modification that effectively replaces an O3 hydrogen atom of a serine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond. + PubMed:7856876 + Unimod:149#S + + + + + Hex(1)HexNAc(1)NeuAc(1) + + + + + + Hex1HexNAc1NeuAc1 + + + + + + + + + + + + + + + + + A protein modification that effectively replaces two hydrogen atoms of an L-lysine residue containing common isotopes with two (13)C,3x(2)H labeled methyl groups to form a 2x(13)C,6x(2)H labeled dimethylated L-lysine. + 34.06 + (13)C 2 (2)H 4 + 34.063118 + (12)C 6 (13)C 2 (1)H 12 (2)H 4 N 2 O 1 + 162.16 + 162.15808 + K + artifact + Unimod:510 + PSI-MOD + DiMethyl-C13HD2 + Dimethyl:2H(4)13C(2) + MOD:01357 + 2x(13)C,4x(2)H labeled dimethylated L-lysine + + + + + A protein modification that effectively replaces two hydrogen atoms of an L-lysine residue containing common isotopes with two (13)C,3x(2)H labeled methyl groups to form a 2x(13)C,6x(2)H labeled dimethylated L-lysine. + PubMed:12686488 + PubMed:16335955 + Unimod:510#K + + + + + DiMethyl-C13HD2 + + + + + + Dimethyl:2H(4)13C(2) + + + + + + + + + + modification from Unimod Isotopic label - Use when labelling post-digest + 109.05 + C 6 (1)H -1 (2)H 4 N 1 O 1 + 109.04657 + X + artifact + N-term + Unimod:687 + PSI-MOD + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form + ICPL:2H(4) + MOD:01358 + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form - site N-term + + + + + modification from Unimod Isotopic label - Use when labelling post-digest + PubMed:15602776 + Unimod:687#N-term + + + + + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form + + + + + + ICPL:2H(4) + + + + + + + + + + + modification from Unimod Isotopic label - Use when labelling post-digest + 109.05 + C 6 (1)H -1 (2)H 4 N 1 O 1 + 109.04657 + C 12 (1)H 11 (2)H 4 N 3 O 2 + 237.14 + 237.14154 + K + artifact + Unimod:687 + PSI-MOD + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form + ICPL:2H(4) + MOD:01359 + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form - site K + + + + + modification from Unimod Isotopic label - Use when labelling post-digest + PubMed:15602776 + Unimod:687#K + + + + + Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form + + + + + + ICPL:2H(4) + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to the 4-sulfophenyl isothiocyanate adduct, N6-[(4-sulfophenyl)carbamothioyl]lysine. + 215.24 + C 7 H 5 N 1 O 3 S 2 + 214.97108 + C 13 H 17 N 3 O 4 S 2 + 343.42 + 343.06604 + K + artifact + Unimod:261 + N6-[(4-sulfophenyl)carbamothioyl]lysine + PSI-MOD + 4-sulfophenyl isothiocyanate + SPITC + MOD:01360 + 4-sulfophenyl isothiocyanate N6-derivatized lysine + + + + + A protein modification that effectively converts an L-lysine residue to the 4-sulfophenyl isothiocyanate adduct, N6-[(4-sulfophenyl)carbamothioyl]lysine. + PubMed:14689565 + PubMed:14745769 + PubMed:15549660 + PubMed:16526082 + Unimod:261#K + + + + + N6-[(4-sulfophenyl)carbamothioyl]lysine + + + + + + 4-sulfophenyl isothiocyanate + + + + + + SPITC + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-thiophospho-L-threonine. + 96.04 + H 1 O 2 P 1 S 1 + 95.94349 + C 4 H 8 N 1 O 4 P 1 S 1 + 197.14 + 196.99117 + T + artifact + Unimod:260 + PSI-MOD + Thiophospho + Thiophosphorylation + MOD:01361 + O-thiophospho-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-thiophospho-L-threonine. + PubMed:11507762 + PubMed:12110917 + Unimod:260#T + + + + + Thiophospho + + + + + + Thiophosphorylation + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-thiophospho-L-serine. + 96.04 + H 1 O 2 P 1 S 1 + 95.94349 + C 3 H 6 N 1 O 4 P 1 S 1 + 183.12 + 182.97551 + S + artifact + Unimod:260 + PSI-MOD + Thiophospho + Thiophosphorylation + MOD:01362 + O-thiophospho-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-thiophospho-L-serine. + PubMed:11507762 + PubMed:12110917 + Unimod:260#S + + + + + Thiophospho + + + + + + Thiophosphorylation + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to O4'-thiophospho-L-tyrosine. + 96.04 + H 1 O 2 P 1 S 1 + 95.94349 + C 9 H 10 N 1 O 4 P 1 S 1 + 259.22 + 259.0068 + Y + artifact + Unimod:260 + PSI-MOD + Thiophospho + Thiophosphorylation + MOD:01363 + O4'-thiophospho-L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to O4'-thiophospho-L-tyrosine. + PubMed:12110917 + PubMed:15549660 + Unimod:260#Y + + + + + Thiophospho + + + + + + Thiophosphorylation + + + + + + + + + + + modification from Unimod Chemical derivative - + 421.43 + C 21 H 15 N 3 O 5 S 1 + 421.07324 + C 24 H 20 N 4 O 7 S 1 + 508.51 + 508.10526 + S + artifact + Unimod:478 + PSI-MOD + FTC + fluorescein-5-thiosemicarbazide + MOD:01364 + fluorescein-5-thiosemicarbazide - site S + + + + + modification from Unimod Chemical derivative - + PubMed:11467524 + Unimod:478#S + + + + + FTC + + + + + + fluorescein-5-thiosemicarbazide + + + + + + + + + + + modification from Unimod Chemical derivative - + 421.43 + C 21 H 15 N 3 O 5 S 1 + 421.07324 + C 24 H 20 N 4 O 6 S 2 + 524.57 + 524.0824 + C + artifact + Unimod:478 + PSI-MOD + FTC + fluorescein-5-thiosemicarbazide + MOD:01365 + fluorescein-5-thiosemicarbazide - site C + + + + + modification from Unimod Chemical derivative - + Unimod:478#C + + + + + FTC + + + + + + fluorescein-5-thiosemicarbazide + + + + + + + + + + + modification from Unimod Chemical derivative - + 421.43 + C 21 H 15 N 3 O 5 S 1 + 421.07324 + C 27 H 27 N 5 O 6 S 1 + 549.6 + 549.1682 + K + artifact + Unimod:478 + PSI-MOD + FTC + fluorescein-5-thiosemicarbazide + MOD:01366 + fluorescein-5-thiosemicarbazide - site K + + + + + modification from Unimod Chemical derivative - + Unimod:478#K + + + + + FTC + + + + + + fluorescein-5-thiosemicarbazide + + + + + + + + + + + modification from Unimod Chemical derivative - + 421.43 + C 21 H 15 N 3 O 5 S 1 + 421.07324 + C 26 H 22 N 4 O 6 S 1 + 518.54 + 518.126 + P + artifact + Unimod:478 + PSI-MOD + FTC + fluorescein-5-thiosemicarbazide + MOD:01367 + fluorescein-5-thiosemicarbazide - site P + + + + + modification from Unimod Chemical derivative - + Unimod:478#P + + + + + FTC + + + + + + fluorescein-5-thiosemicarbazide + + + + + + + + + + + modification from Unimod Chemical derivative - + 421.43 + C 21 H 15 N 3 O 5 S 1 + 421.07324 + C 27 H 27 N 7 O 6 S 1 + 577.62 + 577.1744 + R + artifact + Unimod:478 + PSI-MOD + FTC + fluorescein-5-thiosemicarbazide + MOD:01368 + fluorescein-5-thiosemicarbazide - site R + + + + + modification from Unimod Chemical derivative - + PubMed:15525938 + Unimod:478#R + + + + + FTC + + + + + + fluorescein-5-thiosemicarbazide + + + + + + + + + + + + + + + + A protein modification that effectively replaces a carboxamido group with a carboxyl methyl ester group. + 15.01 + C 1 H 1 N -1 O 1 + 14.999666 + X + Unimod:528 + PSI-MOD + Deamidation followed by a methylation + Methyl+Deamidated + MOD:01369 + + deamidated and methyl esterified residue + + + + + A protein modification that effectively replaces a carboxamido group with a carboxyl methyl ester group. + Unimod:528 + + + + + Deamidation followed by a methylation + + + + + + Methyl+Deamidated + + + + + + + + + + + A protein modification that effectively converts a residue containing common isotopes to a 6x(13)C,1x(15)N labeled residue. + 7.02 + (12)C -6 (13)C 6 (14)N -1 (15)N 1 + 7.017164 + X + artifact + Unimod:695 + PSI-MOD + 13C(6) 15N(1) Silac label + Label:13C(6)15N(1) + MOD:01370 + 6x(13)C,1x(15)N labeled residue + + + + + A protein modification that effectively converts a residue containing common isotopes to a 6x(13)C,1x(15)N labeled residue. + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + Unimod:695 + + + + + 13C(6) 15N(1) Silac label + + + + + + Label:13C(6)15N(1) + + + + + + + + + OBSOLETE bcecause identical and redundant with MOD:00851. Remap to MOD:00851. + MOD:00851 + 2.99 + H -1 N -1 (18)O 1 + 2.988262 + X + artifact + PSI-MOD + Deamidated:18O(1) + Deamidation in presence of O18 + MOD:01371 + deamidation in presence of O18 + true + + + + + OBSOLETE bcecause identical and redundant with MOD:00851. Remap to MOD:00851. + PubMed:8382902 + + + + + Deamidated:18O(1) + + + + + + Deamidation in presence of O18 + + + + + + + + + + A protein modification that effectively converts an L-leucine residue to a (2S)-4-hydroxyleucine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 6 H 11 N 1 O 2 + 129.16 + 129.07898 + L + natural + uniprot.ptm:PTM-0665 + (2S)-2-amino-4-hydroxy-4-methylpentanoic acid + (2S)-4-hydroxyleucine + MOD_RES (2S)-4-hydroxyleucine + gamma-hydroxyleucine + PSI-MOD + MOD:01372 + (2S)-4-hydroxyleucine + + + + + A protein modification that effectively converts an L-leucine residue to a (2S)-4-hydroxyleucine. + ChEBI:141825 + PubMed:363352 + PubMed:9164839 + RESID:AA0442 + + + + + (2S)-2-amino-4-hydroxy-4-methylpentanoic acid + + + + + + (2S)-4-hydroxyleucine + + + + + + MOD_RES (2S)-4-hydroxyleucine + + + + + + gamma-hydroxyleucine + + + + + + + + + + A protein modification that effectively converts an L-leucine residue to a (2S,4R)-5-hydroxyleucine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 6 H 11 N 1 O 2 + 129.16 + 129.07898 + L + hypothetical + uniprot.ptm:PTM-0491 + (2S,4R)-2-amino-5-hydroxy-4-methylpentanoic acid + (2S,4R)-5-hydroxyleucine + (4R)-5-hydroxyleucine + MOD_RES (4R)-5-hydroxyleucine + delta-hydroxyleucine + PSI-MOD + MOD:01373 + (2S,4R)-5-hydroxyleucine + + + + + A protein modification that effectively converts an L-leucine residue to a (2S,4R)-5-hydroxyleucine. + ChEBI:141824 + PubMed:16858410 + PubMed:7690768 + PubMed:9164839 + RESID:AA0443 + + + + + (2S,4R)-2-amino-5-hydroxy-4-methylpentanoic acid + + + + + + (2S,4R)-5-hydroxyleucine + + + + + + (4R)-5-hydroxyleucine + + + + + + MOD_RES (4R)-5-hydroxyleucine + + + + + + delta-hydroxyleucine + + + + + + + + + + + A modification that effectively oxygenates C5 of an L-leucine residue to form a (2S,4R)-5-oxoleucine. + 13.98 + C 0 H -2 N 0 O 1 + 13.979265 + C 6 H 9 N 1 O 2 + 127.14 + 127.06333 + L + hypothetical + uniprot.ptm:PTM-0492 + (2S,4R)-2-amino-4-methyl-5-oxopentanoic acid + (2S,4R)-5-oxoleucine + (4R)-5-oxo-L-leucine + PSI-MOD + MOD:01374 + (2S,4R)-5-oxoleucine + + + + + A modification that effectively oxygenates C5 of an L-leucine residue to form a (2S,4R)-5-oxoleucine. + ChEBI:43739 + PubMed:16858410 + RESID:AA0444 + + + + + (2S,4R)-2-amino-4-methyl-5-oxopentanoic acid + + + + + + (2S,4R)-5-oxoleucine + + + + + + (4R)-5-oxo-L-leucine + + + + + + + + + + A protein modification that effectively converts an L-leucine residue to a (2S,4R)-4,5-dihydroxyleucine. + 32.0 + C 0 H 0 N 0 O 2 + 31.989828 + C 6 H 11 N 1 O 3 + 145.16 + 145.0739 + L + natural + uniprot.ptm:PTM-0340 + (2S,4R)-2-amino-4,5-dihydroxy-4-methylpentanoic acid + (2S,4R)-4,5-dihydroxyleucine + (4R)-4,5-dihydroxyleucine + MOD_RES (4R)-4,5-dihydroxyleucine + gamma,delta-dihydroxyleucine + PSI-MOD + MOD:01375 + (2S,4R)-4,5-dihydroxyleucine + + + + + A protein modification that effectively converts an L-leucine residue to a (2S,4R)-4,5-dihydroxyleucine. + ChEBI:141823 + PubMed:6010785 + PubMed:6893271 + RESID:AA0445 + + + + + (2S,4R)-2-amino-4,5-dihydroxy-4-methylpentanoic acid + + + + + + (2S,4R)-4,5-dihydroxyleucine + + + + + + (4R)-4,5-dihydroxyleucine + + + + + + MOD_RES (4R)-4,5-dihydroxyleucine + + + + + + gamma,delta-dihydroxyleucine + + + + + + + + + + A protein modification that effectively converts an L-isoleucine residue to a (2S,3S,4R)-3,4-dihydroxyisoleucine. + 32.0 + C 0 H 0 N 0 O 2 + 31.989828 + C 6 H 11 N 1 O 3 + 145.16 + 145.0739 + I + natural + uniprot.ptm:PTM-0343 + (2S,3S,4R)-2-amino-3,4-dihydroxy-3-methylpentanoic acid + (2S,3S,4R)-3,4-dihydroxyisoleucine + (3S,4R)-3,4-dihydroxyisoleucine + MOD_RES (3S,4R)-3,4-dihydroxyisoleucine + beta,gamma-dihydroxyisoleucine + PSI-MOD + MOD:01376 + (2S,3S,4R)-3,4-dihydroxyisoleucine + + + + + A protein modification that effectively converts an L-isoleucine residue to a (2S,3S,4R)-3,4-dihydroxyisoleucine. + ChEBI:141827 + PubMed:11320328 + RESID:AA0447 + + + + + (2S,3S,4R)-2-amino-3,4-dihydroxy-3-methylpentanoic acid + + + + + + (2S,3S,4R)-3,4-dihydroxyisoleucine + + + + + + (3S,4R)-3,4-dihydroxyisoleucine + + + + + + MOD_RES (3S,4R)-3,4-dihydroxyisoleucine + + + + + + beta,gamma-dihydroxyisoleucine + + + + + + + + + + A protein modification that effectively converts an L-isoleucine residue to a (2S,3R,4S)-4-hydroxyisoleucine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 6 H 11 N 1 O 2 + 129.16 + 129.07898 + I + natural + uniprot.ptm:PTM-0337 + (2S,3R,4S)-2-amino-3-methyl-4-hydroxyvaleric acid + (2S,3R,4S)-2-amino-4-hydroxy-3-methylpentanoic acid + (2S,3R,4S)-4-hydroxyisoleucine + (3R,4S)-4-hydroxyisoleucine + MOD_RES (3R,4S)-4-hydroxyisoleucine + gamma-hydroxyisoleucine + PSI-MOD + MOD:01377 + (2S,3R,4S)-4-hydroxyisoleucine + + + + + A protein modification that effectively converts an L-isoleucine residue to a (2S,3R,4S)-4-hydroxyisoleucine. + ChEBI:141844 + PubMed:363352 + RESID:AA0448 + + + + + (2S,3R,4S)-2-amino-3-methyl-4-hydroxyvaleric acid + + + + + + (2S,3R,4S)-2-amino-4-hydroxy-3-methylpentanoic acid + + + + + + (2S,3R,4S)-4-hydroxyisoleucine + + + + + + (3R,4S)-4-hydroxyisoleucine + + + + + + MOD_RES (3R,4S)-4-hydroxyisoleucine + + + + + + gamma-hydroxyisoleucine + + + + + + + + + + A protein modification that effectively converts an L-isoleucine residue to a (2S,3R,4R)-4,5-dihydroxyisoleucine. + 32.0 + C 0 H 0 N 0 O 2 + 31.989828 + C 6 H 11 N 1 O 3 + 145.16 + 145.0739 + I + natural + uniprot.ptm:PTM-0336 + (2S,3R,4R)-2-amino-4,5-dihydroxy-3-methylpentanoic acid + (2S,3R,4R)-4,5-dihydroxyisoleucine + (3R,4R)-4,5-dihydroxyisoleucine + MOD_RES (3R,4R)-4,5-dihydroxyisoleucine + gamma,delta-dihydroxyisoleucine + PSI-MOD + MOD:01378 + (2S,3R,4R)-4,5-dihydroxyisoleucine + + + + + A protein modification that effectively converts an L-isoleucine residue to a (2S,3R,4R)-4,5-dihydroxyisoleucine. + ChEBI:141826 + PubMed:11805306 + PubMed:18552824 + PubMed:363352 + RESID:AA0449 + + + + + (2S,3R,4R)-2-amino-4,5-dihydroxy-3-methylpentanoic acid + + + + + + (2S,3R,4R)-4,5-dihydroxyisoleucine + + + + + + (3R,4R)-4,5-dihydroxyisoleucine + + + + + + MOD_RES (3R,4R)-4,5-dihydroxyisoleucine + + + + + + gamma,delta-dihydroxyisoleucine + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to 2'-methylsulfonyl-L-tryptophan. + 78.09 + C 1 H 2 N 0 O 2 S 1 + 77.97755 + C 12 H 12 N 2 O 3 S 1 + 264.3 + 264.05685 + W + natural + uniprot.ptm:PTM-0304 + 2'-methylsulfonyl-L-tryptophan + 2-methylsulfonyl-3-((2S)-2-amino-2-carboxyethyl)-1H-indole + MOD_RES 2'-methylsulfonyltryptophan + PSI-MOD + MOD:01379 + 2'-methylsulfonyl-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to 2'-methylsulfonyl-L-tryptophan. + PubMed:6893271 + RESID:AA0450 + + + + + 2'-methylsulfonyl-L-tryptophan + + + + + + 2-methylsulfonyl-3-((2S)-2-amino-2-carboxyethyl)-1H-indole + + + + + + MOD_RES 2'-methylsulfonyltryptophan + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-tryptophan residue by a thioether bond to form 2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide. + 29.98 + C 0 H -2 N 0 O 2 S 0 + 29.974178 + C 14 H 13 N 3 O 4 S 1 + 319.33 + 319.06268 + C, W + natural + uniprot.ptm:PTM-0338 + 2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide + 2-((2R)-2-amino-2carboxyethyl)sulfinyl-3-((2S)-2-amino-2-carboxyethyl)-1H-indole + 6'-hydroxy-S-oxo-tryptathionine + CROSSLNK 2'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-Cys) + PSI-MOD + MOD:01380 + Cross-link 2. + 2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-tryptophan residue by a thioether bond to form 2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide. + PubMed:11805306 + PubMed:18552824 + PubMed:363352 + PubMed:4865716 + RESID:AA0451 + + + + + 2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide + + + + + + 2-((2R)-2-amino-2carboxyethyl)sulfinyl-3-((2S)-2-amino-2-carboxyethyl)-1H-indole + + + + + + 6'-hydroxy-S-oxo-tryptathionine + + + + + + CROSSLNK 2'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-Cys) + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-palmitoleyl-L-serine. + 236.4 + C 16 H 28 N 0 O 1 + 236.21402 + C 19 H 33 N 1 O 3 + 323.48 + 323.24603 + S + natural + uniprot.ptm:PTM-0493 + (2S)-2-amino-3-((9Z)-9-hexadecenoyloxy)propanoic acid + L-serine cis-9-hexadecenoate ester + LIPID O-palmitoleyl serine + O-palmitoleyl-L-serine + O3-palmitoleyl-serine + mod186 + PSI-MOD + MOD:01381 + + O-palmitoleyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-palmitoleyl-L-serine. + OMSSA:186 + PubMed:17141155 + RESID:AA0455 + + + + + (2S)-2-amino-3-((9Z)-9-hexadecenoyloxy)propanoic acid + + + + + + L-serine cis-9-hexadecenoate ester + + + + + + LIPID O-palmitoleyl serine + + + + + + O-palmitoleyl-L-serine + + + + + + O3-palmitoleyl-serine + + + + + + mod186 + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to N,N,N-trimethyl-L-methionine. + 43.09 + C 3 H 7 N 0 O 0 S 0 + 43.054226 + 1+ + C 8 H 17 N 1 O 1 S 1 + 175.29 + 175.10254 + M + natural + N-term + uniprot.ptm:PTM-0503 + (1S)-1-carboxy-N,N,N-trimethyl-3-(methylsulfanyl)propanaminium + (1S)-1-carboxy-N,N,N-trimethyl-3-(methylsulfanyl)propanazanium + 2-trimethylammonio-4-(methylthio)butanoic acid + MOD_RES N,N,N-trimethylmethionine + N,N,N-trimethyl-L-methionine + N,N,N-trimethylmethionine cation + N,N,N-trimethylmethioninium + N2Me3+Met + PSI-MOD + MOD:01382 + + N,N,N-trimethyl-L-methionine + + + + + A protein modification that effectively converts an L-methionine residue to N,N,N-trimethyl-L-methionine. + PubMed:18611379 + RESID:AA0456 + + + + + (1S)-1-carboxy-N,N,N-trimethyl-3-(methylsulfanyl)propanaminium + + + + + + (1S)-1-carboxy-N,N,N-trimethyl-3-(methylsulfanyl)propanazanium + + + + + + 2-trimethylammonio-4-(methylthio)butanoic acid + + + + + + MOD_RES N,N,N-trimethylmethionine + + + + + + N,N,N-trimethyl-L-methionine + + + + + + N,N,N-trimethylmethionine cation + + + + + + N,N,N-trimethylmethioninium + + + + + + N2Me3+Met + + + + + + + + + + + A protein modification that effectively cross-links two L-cysteine residues and oxidizes a sulfur to form L-cystine S-oxide. + 13.98 + C 0 H -2 N 0 O 1 S 0 + 13.979265 + C 6 H 8 N 2 O 3 S 2 + 220.26 + 219.99763 + C, C + hypothetical + uniprot.ptm:PTM-0324 + (2R)-2-amino-3-[([(2R)-2-amino-2-carboxyethyl]sulfanyl)sulfinyl]propanoic acid + CROSSLNK S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys) + L-cystine S-oxide + S-[(2R)-2-amino-3-oxopropyl] (2R)-2-amino-3-oxopropane-1-sulfinothioate + S-cysteinyl 3-(oxidosulfanyl)alanine + cystine sulfoxide + PSI-MOD + MOD:01383 + Cross-link 2. + L-cystine S-oxide + + + + + A protein modification that effectively cross-links two L-cysteine residues and oxidizes a sulfur to form L-cystine S-oxide. + RESID:AA0457 + + + + + (2R)-2-amino-3-[([(2R)-2-amino-2-carboxyethyl]sulfanyl)sulfinyl]propanoic acid + + + + + + CROSSLNK S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys) + + + + + + L-cystine S-oxide + + + + + + S-[(2R)-2-amino-3-oxopropyl] (2R)-2-amino-3-oxopropane-1-sulfinothioate + + + + + + S-cysteinyl 3-(oxidosulfanyl)alanine + + + + + + cystine sulfoxide + + + + + + + + + + A protein modification that effectively converts an L-serine residue to an aminomalonic acid. + 13.98 + C 0 H -2 N 0 O 1 S 0 + 13.979265 + C 3 H 3 N 1 O 3 + 101.06 + 101.01129 + S + hypothetical + uniprot.ptm:PTM-0321 + 2-carboxyglycine + Ama + MOD_RES Aminomalonic acid (Ser) + aminomalonic acid + aminopropanedioic acid + PSI-MOD + MOD:01384 + aminomalonic acid (Ser) + + + + + A protein modification that effectively converts an L-serine residue to an aminomalonic acid. + PubMed:1621954 + PubMed:5415959 + PubMed:6366787 + PubMed:7457858 + RESID:AA0458 + + + + + 2-carboxyglycine + + + + + + Ama + + + + + + MOD_RES Aminomalonic acid (Ser) + + + + + + aminomalonic acid + + + + + + aminopropanedioic acid + + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to 3-hydroxy-L-phenylalanine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 9 H 9 N 1 O 2 + 163.18 + 163.06332 + F + natural + uniprot.ptm:PTM-0346 + (2S,3S)-2-amino-3-hydroxy-3-phenylpropanoic acid + 3-hydoxyphenylalanine + 3-hydroxy-L-phenylalanine + 3-phenyl-L-serine + 3HyPhe + L-threo-3-phenylserine + MOD_RES 3-hydroxyphenylalanine + beta-hydroxyphenylalanine + beta-phenylserine + hydroxylationf + PSI-MOD + MOD:01385 + 3-hydroxy-L-phenylalanine + + + + + A protein modification that effectively converts an L-phenylalanine residue to 3-hydroxy-L-phenylalanine. + ChEBI:16795 + OMSSA:63 + PubMed:10625477 + PubMed:15651011 + PubMed:16734421 + PubMed:1880060 + PubMed:7398618 + PubMed:7844053 + RESID:AA0462 + + + + + (2S,3S)-2-amino-3-hydroxy-3-phenylpropanoic acid + + + + + + 3-hydoxyphenylalanine + + + + + + 3-hydroxy-L-phenylalanine + + + + + + 3-phenyl-L-serine + + + + + + 3HyPhe + + + + + + L-threo-3-phenylserine + + + + + + MOD_RES 3-hydroxyphenylalanine + + + + + + beta-hydroxyphenylalanine + + + + + + beta-phenylserine + + + + + + hydroxylationf + + + + + + + + + + + A protein modification that effectively converts an L-valine residue to 3-hydroxy-L-valine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 5 H 9 N 1 O 2 + 115.13 + 115.06333 + V + natural + uniprot.ptm:PTM-0347 + (2S)-2-amino-3-hydroxy-3-methylbutanoic acid + 3-hydroxy-L-valine + 3-hydroxyvaline + 3HyVal + MOD_RES 3-hydroxyvaline + PSI-MOD + MOD:01386 + 3-hydroxy-L-valine + + + + + A protein modification that effectively converts an L-valine residue to 3-hydroxy-L-valine. + ChEBI:141793 + PubMed:7328054 + RESID:AA0463 + + + + + (2S)-2-amino-3-hydroxy-3-methylbutanoic acid + + + + + + 3-hydroxy-L-valine + + + + + + 3-hydroxyvaline + + + + + + 3HyVal + + + + + + MOD_RES 3-hydroxyvaline + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-methyl-L-threonine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 5 H 9 N 1 O 2 + 115.13 + 115.06333 + T + natural + uniprot.ptm:PTM-0356 + (2S,3R)-2-amino-3-methoxybutanoic acid + MOD_RES O-methylthreonine + O-methyl threonine + O-methyl-L-threonine + OMeThr + threonine methyl ether + PSI-MOD + MOD:01387 + O-methyl-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-methyl-L-threonine. + PubMed:7328054 + RESID:AA0464 + + + + + (2S,3R)-2-amino-3-methoxybutanoic acid + + + + + + MOD_RES O-methylthreonine + + + + + + O-methyl threonine + + + + + + O-methyl-L-threonine + + + + + + OMeThr + + + + + + threonine methyl ether + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue into 1-amino-2-propanol. + -44.01 + C -1 H 0 N 0 O -2 + -43.98983 + C 3 H 8 N 1 O 1 + 74.1 + 74.06059 + T + natural + C-term + uniprot.ptm:PTM-0354 + (2R)-1-aminopropan-2-ol + 1-amino-2-hydroxypropane + 1-amino-2-propanol + 1-methyl-2-aminoethanol + 2-amino-1-methylethanol + 2-hydroxy-1-propylamine + 2-hydroxypropanamine + 2-hydroxypropylamine + MOD_RES Decarboxylated threonine + alpha-aminoisopropyl alcohol + dCbxThr + decarboxylated threonine + isopropanolamine + threamine + PSI-MOD + MOD:01388 + 1-amino-2-propanol + + + + + A protein modification that effectively converts an L-threonine residue into 1-amino-2-propanol. + ChEBI:15675 + PubMed:7328054 + RESID:AA0465 + + + + + (2R)-1-aminopropan-2-ol + + + + + + 1-amino-2-hydroxypropane + + + + + + 1-amino-2-propanol + + + + + + 1-methyl-2-aminoethanol + + + + + + 2-amino-1-methylethanol + + + + + + 2-hydroxy-1-propylamine + + + + + + 2-hydroxypropanamine + + + + + + 2-hydroxypropylamine + + + + + + MOD_RES Decarboxylated threonine + + + + + + alpha-aminoisopropyl alcohol + + + + + + dCbxThr + + + + + + decarboxylated threonine + + + + + + isopropanolamine + + + + + + threamine + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-isoleucine residue to form L-isoleucine thiazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 S 0 + -20.026215 + C 9 H 12 N 2 O 1 S 1 + 196.27 + 196.06703 + C, I + natural + uniprot.ptm:PTM-0361 + 2-[(1S,2S)-1-amino-2-methylbutyl]-1,3-thiazole-4-carboxylic acid + 2-[1-zanyl-2-methylbutyl]-1,3-thiazole-4-carboxylic acid + CROSSLNK Thiazole-4-carboxylic acid (Ile-Cys) + L-isoleucine thiazole-4-carboxylic acid + PSI-MOD + MOD:01389 + Cross-link 2. + L-isoleucine thiazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-isoleucine residue to form L-isoleucine thiazole-4-carboxylic acid. + PubMed:11320328 + RESID:AA0466 + + + + + 2-[(1S,2S)-1-amino-2-methylbutyl]-1,3-thiazole-4-carboxylic acid + + + + + + 2-[1-zanyl-2-methylbutyl]-1,3-thiazole-4-carboxylic acid + + + + + + CROSSLNK Thiazole-4-carboxylic acid (Ile-Cys) + + + + + + L-isoleucine thiazole-4-carboxylic acid + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-valine residue to form L-valine thiazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 S 0 + -20.026215 + C 8 H 10 N 2 O 1 S 1 + 182.24 + 182.05139 + C, V + natural + uniprot.ptm:PTM-0365 + 2-[(1S)-1-amino-2-methylpropyl]-1,3-thiazole-4-carboxylic acid + 2-[1-azanyl-2-methylpropyl]-1,3-thiazole-4-carboxylic acid + CROSSLNK Thiazole-4-carboxylic acid (Val-Cys) + L-valine thiazole-4-carboxylic acid + PSI-MOD + MOD:01390 + Cross-link 2. + L-valine thiazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-valine residue to form L-valine thiazole-4-carboxylic acid. + PubMed:7328054 + RESID:AA0467 + + + + + 2-[(1S)-1-amino-2-methylpropyl]-1,3-thiazole-4-carboxylic acid + + + + + + 2-[1-azanyl-2-methylpropyl]-1,3-thiazole-4-carboxylic acid + + + + + + CROSSLNK Thiazole-4-carboxylic acid (Val-Cys) + + + + + + L-valine thiazole-4-carboxylic acid + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-valine residue, and C-5 methoxymethylates to form L-valine 5-(methoxymethyl)thiazole-4-carboxylic acid. + 24.02 + C 2 H 0 N 0 O 0 S 0 + 24.0 + C 10 H 14 N 2 O 2 S 1 + 226.29 + 226.0776 + C, V + natural + uniprot.ptm:PTM-0373 + 2-[(1S)-1-amino-2-methylpropyl]-5-(methoxymethyl)-1,3-thiazole-4-carboxylic acid + 2-[1-azanyl-2-methylpropyl]-5-(methoxymethyl)-1,3-thiazole-4-carboxylic acid + CROSSLNK 5-(methoxymethyl)thiazole-4-carboxylic acid (Val-Cys) + L-valine 5-(methoxymethyl)thiazole-4-carboxylic acid + PSI-MOD + MOD:01391 + Cross-link 2. + L-valine 5-(methoxymethyl)thiazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-valine residue, and C-5 methoxymethylates to form L-valine 5-(methoxymethyl)thiazole-4-carboxylic acid. + PubMed:10625477 + PubMed:1880060 + PubMed:7844053 + RESID:AA0468 + + + + + 2-[(1S)-1-amino-2-methylpropyl]-5-(methoxymethyl)-1,3-thiazole-4-carboxylic acid + + + + + + 2-[1-azanyl-2-methylpropyl]-5-(methoxymethyl)-1,3-thiazole-4-carboxylic acid + + + + + + CROSSLNK 5-(methoxymethyl)thiazole-4-carboxylic acid (Val-Cys) + + + + + + L-valine 5-(methoxymethyl)thiazole-4-carboxylic acid + + + + + + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-asparagine residue, and C-4 methylates to form L-asparagine 5-methylthiazole-4-carboxylic acid. + -6.0 + C 1 H -2 N 0 O -1 S 0 + -6.010565 + C 8 H 9 N 3 O 2 S 1 + 211.24 + 211.04155 + C, N + natural + uniprot.ptm:PTM-0352 + 2-[(1S)-1,3-bisazanyl-3-oxopropyl]-5-methyl-1,3-thiazole-4-carboxylic acid + 2-[(1S)-1,3-diamino-3-oxopropyl]-5-methyl-1,3-thiazole-4-carboxylic acid + CROSSLNK 5-methylthiazole-4-carboxylic acid (Asn-Cys) + L-asparagine 5-methylthiazole-4-carboxylic acid + PSI-MOD + MOD:01392 + Cross-link 2. + L-asparagine 5-methylthiazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-asparagine residue, and C-4 methylates to form L-asparagine 5-methylthiazole-4-carboxylic acid. + PubMed:10625477 + PubMed:1880060 + PubMed:7844053 + RESID:AA0469 + + + + + 2-[(1S)-1,3-bisazanyl-3-oxopropyl]-5-methyl-1,3-thiazole-4-carboxylic acid + + + + + + 2-[(1S)-1,3-diamino-3-oxopropyl]-5-methyl-1,3-thiazole-4-carboxylic acid + + + + + + CROSSLNK 5-methylthiazole-4-carboxylic acid (Asn-Cys) + + + + + + L-asparagine 5-methylthiazole-4-carboxylic acid + + + + + + + + + + + + A protein modification that crosslinks two serine residues and a cysteine residue by formation of a pyridine-2,5-dicarboxylic acid. + -70.07 + C 0 H -8 N -1 O -3 S 0 + -70.050415 + C 9 H 7 N 2 O 2 S 1 + 207.23 + 207.02283 + C, S, S + natural + uniprot.ptm:PTM-0358 + 6-[(1R)-1-amino-2-sulfanylethyl]pyridine-2,5-dicarboxylic acid + L-cysteine pyridine-2,5-dicarboxylic acid + PSI-MOD + MOD:01393 + Cross-link 3. + L-cysteine pyridine-2,5-dicarboxylic acid + + + + + A protein modification that crosslinks two serine residues and a cysteine residue by formation of a pyridine-2,5-dicarboxylic acid. + PubMed:10625477 + PubMed:1880060 + PubMed:7844053 + RESID:AA0470 + + + + + 6-[(1R)-1-amino-2-sulfanylethyl]pyridine-2,5-dicarboxylic acid + + + + + + L-cysteine pyridine-2,5-dicarboxylic acid + + + + + + + + + + + + A protein modification that crosslinks two serine residues and a cysteine residue by formation of a 5-amino-3,4,5,6-tetrahydropyridine-2,5-dicarboxylic acid. + -53.04 + C 0 H -5 N 0 O -3 S 0 + -53.02387 + C 9 H 11 N 3 O 2 S 1 + 225.27 + 225.0572 + C, S, S + natural + N-term + uniprot.ptm:PTM-0348 + (5R,6R)-5-amino-6-[(1R)-1-amino-2-sulfanylethyl]-3,4,5,6-tetrahydropyridine-2,5-dicarboxylic acid + L-cysteine 5-amino-3,4,5,6-tetrahydropyridine-2,5-dicarboxylic acid + L-cysteine 5-aminopiperideine-2,5-dicarboxylic acid + PSI-MOD + CROSSLNK 5-amino-piperideine-2,5-dicarboxylic acid + MOD:01394 + Cross-link 3. + L-cysteine 5-amino-3,4,5,6-tetrahydropyridine-2,5-dicarboxylic acid + + + + + A protein modification that crosslinks two serine residues and a cysteine residue by formation of a 5-amino-3,4,5,6-tetrahydropyridine-2,5-dicarboxylic acid. + PubMed:11320328 + RESID:AA0471 + + + + + (5R,6R)-5-amino-6-[(1R)-1-amino-2-sulfanylethyl]-3,4,5,6-tetrahydropyridine-2,5-dicarboxylic acid + + + + + + L-cysteine 5-amino-3,4,5,6-tetrahydropyridine-2,5-dicarboxylic acid + + + + + + L-cysteine 5-aminopiperideine-2,5-dicarboxylic acid + + + + + + CROSSLNK 5-amino-piperideine-2,5-dicarboxylic acid + + + + + + + + + + + + A protein modification that effectively results from forming an adduct between an isoleucine residue, a threonine residue and the quinaldate compound 2-carboxy-4-(1-hydroxyethyl)--7,8-dihydroquinolin-8-ol. + 215.21 + C 12 H 9 N 1 O 3 + 215.05824 + C 22 H 28 N 3 O 6 + 430.48 + 430.1978 + I, T + natural + N-term + (7R,8S)-7-[(1S,2S)-1-carboxy-2-methylbutyl]amino-2-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)carbonyl-8-hydroxy-4-[(1S)-1-hydroxyethyl]-7,8-dihydroquinoline + 4-(1-hydroxyethyl)-7-isoleucino-2-(threonin-O3-ylcarbonyl)-7,8-dihydroquinolin-8-ol + BINDING 4-(1-hydroxyethyl)-7,8-dihydroquinolin-8-ol (covalent; via 2 links) + PSI-MOD + MOD:01395 + Cross-link 2. + 4-(1-hydroxyethyl)-7-isoleucino-2-(threonin-O3-ylcarbonyl)-7,8-dihydroquinolin-8-ol + + + + + A protein modification that effectively results from forming an adduct between an isoleucine residue, a threonine residue and the quinaldate compound 2-carboxy-4-(1-hydroxyethyl)--7,8-dihydroquinolin-8-ol. + PubMed:11320328 + RESID:AA0472 + + + + + (7R,8S)-7-[(1S,2S)-1-carboxy-2-methylbutyl]amino-2-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)carbonyl-8-hydroxy-4-[(1S)-1-hydroxyethyl]-7,8-dihydroquinoline + + + + + + 4-(1-hydroxyethyl)-7-isoleucino-2-(threonin-O3-ylcarbonyl)-7,8-dihydroquinolin-8-ol + + + + + + BINDING 4-(1-hydroxyethyl)-7,8-dihydroquinolin-8-ol (covalent; via 2 links) + + + + + + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-proline residue to a 5-hydroxy-3-methyl-L-proline. + 30.03 + C 1 H 2 N 0 O 1 + 30.010565 + C 6 H 9 N 1 O 2 + 127.14 + 127.06333 + P + artifactual + (2S,3S,5Xi)-5-hydroxy-3-methylpyrrolidine-2-carboxylic acid + 5-hydroxy-3-methyl-L-proline + 5-hydroxy-3-methylproline + 5Hy3MePro + MOD_RES 5-hydroxy-3-methylproline (Ile) + beta-methyl-delta-hydroxyproline + PSI-MOD + MOD:01396 + This entry is for the hypothetical formation of 5-hydroxy-3-methyl-L-proline from proline. For the natural production from L-isoleucine, use MOD:01897 [JSG]. + 5-hydroxy-3-methyl-L-proline (Pro) + + + + + A protein modification that effectively converts an L-proline residue to a 5-hydroxy-3-methyl-L-proline. + PubMed:7592021 + PubMed:8557573 + RESID:AA0473 + + + + + (2S,3S,5Xi)-5-hydroxy-3-methylpyrrolidine-2-carboxylic acid + + + + + + 5-hydroxy-3-methyl-L-proline + + + + + + 5-hydroxy-3-methylproline + + + + + + 5Hy3MePro + + + + + + MOD_RES 5-hydroxy-3-methylproline (Ile) + + + + + + beta-methyl-delta-hydroxyproline + + + + + + + + + + + + A protein modification that effectively crosslinks an L-serine residue and an L-threonine residue to form L-serine 5-methyloxazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 + -20.026215 + C 7 H 8 N 2 O 3 + 168.15 + 168.0535 + S, T + natural + uniprot.ptm:PTM-0386 + 2-[(1S)-1-amino-2-hydroxyethyl]-5-methyl-1,3-oxazole-4-carboxylic acid + 2-[1-azanyl-2-hydroxyethyl]-5-methyl-1,3-oxazole-4-carboxylic acid + CROSSLNK 5-methyloxazole-4-carboxylic acid (Ser-Thr) + L-serine 5-methyloxazole-4-carboxylic acid + PSI-MOD + MOD:01397 + Cross-link 2. + L-serine 5-methyloxazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-serine residue and an L-threonine residue to form L-serine 5-methyloxazole-4-carboxylic acid. + PubMed:7592021 + PubMed:8557573 + RESID:AA0474 + + + + + 2-[(1S)-1-amino-2-hydroxyethyl]-5-methyl-1,3-oxazole-4-carboxylic acid + + + + + + 2-[1-azanyl-2-hydroxyethyl]-5-methyl-1,3-oxazole-4-carboxylic acid + + + + + + CROSSLNK 5-methyloxazole-4-carboxylic acid (Ser-Thr) + + + + + + L-serine 5-methyloxazole-4-carboxylic acid + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-propanoyl-L-lysine. + 56.06 + C 3 H 4 N 0 O 1 + 56.026215 + C 9 H 16 N 2 O 2 + 184.24 + 184.12119 + K + natural + Unimod:58 + uniprot.ptm:PTM-0642 + (2S)-2-amino-6-(propanoylamino)hexanoic acid + 2-amino-6-propionylaminocaproic acid + MOD_RES N6-propionyllysine + N(zeta)-propanoyllysine + N6-(1-oxopropyl)-L-lysine + N6-propanoyl-L-lysine + N6-propionyllysine + epsilon-propanoyl-L-lysine + epsilon-propionyl-L-lysine + PSI-MOD + MOD:01398 + + The binding of histone peptides with propanoylated lysine to nuclear bromodomain proteins is non-specific and weaker than binding to the corresponding acetylated lysine peptides [JSG]. + N6-propanoyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-propanoyl-L-lysine. + PubMed:17267393 + PubMed:17684016 + PubMed:20715035 + RESID:AA0475 + Unimod:58#K + + + + + (2S)-2-amino-6-(propanoylamino)hexanoic acid + + + + + + 2-amino-6-propionylaminocaproic acid + + + + + + MOD_RES N6-propionyllysine + + + + + + N(zeta)-propanoyllysine + + + + + + N6-(1-oxopropyl)-L-lysine + + + + + + N6-propanoyl-L-lysine + + + + + + N6-propionyllysine + + + + + + epsilon-propanoyl-L-lysine + + + + + + epsilon-propionyl-L-lysine + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to an N6-(ADP-ribosyl)-L-lysine. + 541.3 + C 15 H 21 N 5 O 13 P 2 + 541.0611 + C 21 H 33 N 7 O 14 P 2 + 669.48 + 669.15607 + K + hypothetical + uniprot.ptm:PTM-0355 + (S)-2-amino-6-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)hexanoic acid + 2-amino-6-(ADP-ribosyl)amino-hexanoic acid + MOD_RES N6-(ADP-ribosyl)lysine + N(zeta)-ADP-ribosyllysine + N6-(ADP-ribosyl)-L-lysine + N6-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-lysine + N6-alpha-D-ribofuranosyl-L-lysine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) + epsilon-ADP-ribosyllysine + PSI-MOD + MOD:01399 + N6-(ADP-ribosyl)-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to an N6-(ADP-ribosyl)-L-lysine. + PubMed:18436469 + RESID:AA0476 + + + + + (S)-2-amino-6-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)hexanoic acid + + + + + + 2-amino-6-(ADP-ribosyl)amino-hexanoic acid + + + + + + MOD_RES N6-(ADP-ribosyl)lysine + + + + + + N(zeta)-ADP-ribosyllysine + + + + + + N6-(ADP-ribosyl)-L-lysine + + + + + + N6-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-lysine + + + + + + N6-alpha-D-ribofuranosyl-L-lysine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) + + + + + + epsilon-ADP-ribosyllysine + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to an L-lysyl-poly(ADP-ribose). + K + natural + C-term + L-lysyl-poly(ADP-ribose) + MOD_RES Lysyl poly(ADP-ribose) + poly[2'-adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with 1alpha-D-ribofuranosyl] (2S)-2,6-diaminohexanoate + PSI-MOD + MOD:01400 + L-lysyl-poly(ADP-ribose) + + + + + A protein modification that effectively converts an L-lysine residue to an L-lysyl-poly(ADP-ribose). + PubMed:6772638 + RESID:AA0477 + + + + + L-lysyl-poly(ADP-ribose) + + + + + + MOD_RES Lysyl poly(ADP-ribose) + + + + + + poly[2'-adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with 1alpha-D-ribofuranosyl] (2S)-2,6-diaminohexanoate + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to a (2S,3S)-3-hydroxyasparagine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 4 H 6 N 2 O 3 + 130.1 + 130.03784 + N + natural + uniprot.ptm:PTM-0370 + (2S,3S)-2,4-diamino-3-hydroxy-4-oxobutanoic acid + (2S,3S)-2-amino-3-hydroxy-4-butanediamic acid + (2S,3S)-3-hydroxyasparagine + (3S)3HyAsn + L-threo-beta-hydroxyasparagine + MOD_RES (3S)-3-hydroxyasparagine + PSI-MOD + MOD:01401 + + (2S,3S)-3-hydroxyasparagine + + + + + A protein modification that effectively converts an L-asparagine residue to a (2S,3S)-3-hydroxyasparagine. + ChEBI:138107 + ChEBI:50789 + PubMed:11823643 + PubMed:12042299 + PubMed:12215170 + PubMed:17573339 + RESID:AA0478 + + + + + (2S,3S)-2,4-diamino-3-hydroxy-4-oxobutanoic acid + + + + + + (2S,3S)-2-amino-3-hydroxy-4-butanediamic acid + + + + + + (2S,3S)-3-hydroxyasparagine + + + + + + (3S)3HyAsn + + + + + + L-threo-beta-hydroxyasparagine + + + + + + MOD_RES (3S)-3-hydroxyasparagine + + + + + + + + + + A protein modification that effectively converts an L-proline residue to a (2S,3R,4R)-3,4-dihydroxyproline. + 32.0 + C 0 H 0 N 0 O 2 + 31.989828 + C 5 H 7 N 1 O 3 + 129.12 + 129.04259 + P + natural + uniprot.ptm:PTM-0368 + (2S,3R,4R)-3,4-dihydroxyproline + (2S,3R,4R)-3,4-dihydroxypyrrolidine-2-carboxylic acid + 2,3-trans-3,4-trans-3,4-dihydroxy-L-proline + 2-alpha-3-beta-4-alpha-3,4-dihydroxyproline + MOD_RES (3R,4R)-3,4-dihydroxyproline + PSI-MOD + MOD:01402 + (2S,3R,4R)-3,4-dihydroxyproline + + + + + A protein modification that effectively converts an L-proline residue to a (2S,3R,4R)-3,4-dihydroxyproline. + ChEBI:141805 + PubMed:6893271 + RESID:AA0479 + + + + + (2S,3R,4R)-3,4-dihydroxyproline + + + + + + (2S,3R,4R)-3,4-dihydroxypyrrolidine-2-carboxylic acid + + + + + + 2,3-trans-3,4-trans-3,4-dihydroxy-L-proline + + + + + + 2-alpha-3-beta-4-alpha-3,4-dihydroxyproline + + + + + + MOD_RES (3R,4R)-3,4-dihydroxyproline + + + + + + + + + + A protein modification that effectively converts an L-leucine residue to a (2S)-4,5,5'-trihydroxyleucine. + 48.0 + C 0 H 0 N 0 O 3 + 47.984745 + C 6 H 11 N 1 O 4 + 161.16 + 161.0688 + L + natural + uniprot.ptm:PTM-0372 + (2S)-2-amino-4,5-dihydroxy-4-(hydroxymethyl)pentanoic acid + (2S)-4,5,5'-trihydroxyleucine + 4,5,5'-trihydroxyleucine + MOD_RES 4,5,4'-trihydroxyleucine + gamma,delta,delta'-trihydroxyleucine + PSI-MOD + MOD:01403 + (2S)-4,5,5'-trihydroxyleucine + + + + + A protein modification that effectively converts an L-leucine residue to a (2S)-4,5,5'-trihydroxyleucine. + PubMed:6893271 + RESID:AA0480 + + + + + (2S)-2-amino-4,5-dihydroxy-4-(hydroxymethyl)pentanoic acid + + + + + + (2S)-4,5,5'-trihydroxyleucine + + + + + + 4,5,5'-trihydroxyleucine + + + + + + MOD_RES 4,5,4'-trihydroxyleucine + + + + + + gamma,delta,delta'-trihydroxyleucine + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-asparagine residue to form L-asparagine thiazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 S 0 + -20.026215 + C 7 H 7 N 3 O 2 S 1 + 197.21 + 197.0259 + C, N + natural + uniprot.ptm:PTM-0359 + 2-[(1S)-1,3-diamino-3-oxopropyl]-1,3-thiazole-4-carboxylic acid + 2-[1,3-bisazanyl-3-oxopropyl]-1,3-thiazole-4-carboxylic acid + CROSSLNK Thiazole-4-carboxylic acid (Asn-Cys) + L-asparagine thiazole-4-carboxylic acid + PSI-MOD + MOD:01404 + Cross-link 2. + L-asparagine thiazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-asparagine residue to form L-asparagine thiazole-4-carboxylic acid. + PubMed:7592021 + PubMed:8557573 + RESID:AA0481 + + + + + 2-[(1S)-1,3-diamino-3-oxopropyl]-1,3-thiazole-4-carboxylic acid + + + + + + 2-[1,3-bisazanyl-3-oxopropyl]-1,3-thiazole-4-carboxylic acid + + + + + + CROSSLNK Thiazole-4-carboxylic acid (Asn-Cys) + + + + + + L-asparagine thiazole-4-carboxylic acid + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-proline residue to form L-proline thiazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 S 0 + -20.026215 + C 8 H 8 N 2 O 1 S 1 + 180.22 + 180.03574 + C, P + natural + 2-[(2S)-pyrrolidin-2-yl]-1,3-thiazole-4-carboxylic acid + CROSSLNK Thiazole-4-carboxylic acid (Pro-Cys) + L-proline thiazole-4-carboxylic acid + PSI-MOD + MOD:01405 + Cross-link 2. + L-proline thiazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-proline residue to form L-proline thiazole-4-carboxylic acid. + PubMed:7592021 + PubMed:8557573 + RESID:AA0482 + + + + + 2-[(2S)-pyrrolidin-2-yl]-1,3-thiazole-4-carboxylic acid + + + + + + CROSSLNK Thiazole-4-carboxylic acid (Pro-Cys) + + + + + + L-proline thiazole-4-carboxylic acid + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-threonine thiazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 S 0 + -20.026215 + C 7 H 8 N 2 O 2 S 1 + 184.21 + 184.03065 + C, T + natural + uniprot.ptm:PTM-0364 + 2-[(1S,2R)-1-amino-2-hydroxypropyl]-1,3-thiazole-4-carboxylic acid + 2-[1-azanyl-2-hydroxypropyl]-1,3-thiazole-4-carboxylic acid + CROSSLNK Thiazole-4-carboxylic acid (Thr-Cys) + L-threonine thiazole-4-carboxylic acid + PSI-MOD + MOD:01406 + Cross-link 2. + L-threonine thiazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-threonine thiazole-4-carboxylic acid. + PubMed:11320328 + RESID:AA0483 + + + + + 2-[(1S,2R)-1-amino-2-hydroxypropyl]-1,3-thiazole-4-carboxylic acid + + + + + + 2-[1-azanyl-2-hydroxypropyl]-1,3-thiazole-4-carboxylic acid + + + + + + CROSSLNK Thiazole-4-carboxylic acid (Thr-Cys) + + + + + + L-threonine thiazole-4-carboxylic acid + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazoline-4-carboxylic acid. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 12 H 12 N 2 O 1 S 1 + 232.3 + 232.06703 + C, F + natural + uniprot.ptm:PTM-0366 + (4R)-2-[(1S)-1-amino-2-phenylethyl]-4,5-dihydro-1,3-thiazole-4-carboxylic acid + 2-[1-azanyl-2-phenylethyl]-4,5-dihydro-1,3-thiazole-4-carboxylic acid + CROSSLNK Thiazoline-4-carboxylic acid (Phe-Cys) + L-phenylalanine thiazoline-4-carboxylic acid + PSI-MOD + MOD:01407 + Cross-link 2. + L-phenylalanine thiazoline-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazoline-4-carboxylic acid. + PubMed:7592021 + PubMed:8557573 + RESID:AA0484 + + + + + (4R)-2-[(1S)-1-amino-2-phenylethyl]-4,5-dihydro-1,3-thiazole-4-carboxylic acid + + + + + + 2-[1-azanyl-2-phenylethyl]-4,5-dihydro-1,3-thiazole-4-carboxylic acid + + + + + + CROSSLNK Thiazoline-4-carboxylic acid (Phe-Cys) + + + + + + L-phenylalanine thiazoline-4-carboxylic acid + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-threonine thiazoline-4-carboxylic acid. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 7 H 10 N 2 O 2 S 1 + 186.23 + 186.0463 + C, T + natural + uniprot.ptm:PTM-0392 + (4S)-2-[(1S,2R)-1-amino-2-hydroxypropyl]-4,5-dihydro-1,3-thiazole-4-carboxylic acid + 2-[1-azanyl-2-hydroxypropyl]-4,5-dihydro-1,3-thiazole-4-carboxylic acid + CROSSLNK (4S)-thiazoline-4-carboxylic acid (Thr-Cys) + L-threonine (4S)-thiazoline-4-carboxylic acid + PSI-MOD + MOD:01408 + Cross-link 2. + L-threonine thiazoline-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-threonine thiazoline-4-carboxylic acid. + PubMed:11320328 + RESID:AA0485 + + + + + (4S)-2-[(1S,2R)-1-amino-2-hydroxypropyl]-4,5-dihydro-1,3-thiazole-4-carboxylic acid + + + + + + 2-[1-azanyl-2-hydroxypropyl]-4,5-dihydro-1,3-thiazole-4-carboxylic acid + + + + + + CROSSLNK (4S)-thiazoline-4-carboxylic acid (Thr-Cys) + + + + + + L-threonine (4S)-thiazoline-4-carboxylic acid + + + + + + + + + + A protein modification that effectively replaces three hydrogen atoms with three hydroxyl groups. + 48.0 + C 0 H 0 N 0 O 3 + 47.984745 + X + Hy3Res + PSI-MOD + MOD:01409 + trihydroxylated residue + + + + + A protein modification that effectively replaces three hydrogen atoms with three hydroxyl groups. + PubMed:18688235 + + + + + Hy3Res + + + + + + + + + + + A protein modification that effectively converts an L-leucine residue to an hydroxylated leucine. + L + HyLeu + PSI-MOD + MOD:01410 + hydroxylated leucine + + + + + A protein modification that effectively converts an L-leucine residue to an hydroxylated leucine. + PubMed:18688235 + + + + + HyLeu + + + + + + + + + + + A protein modification that effectively converts an L-leucine residue to a monohydroxylated leucine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 6 H 11 N 1 O 2 + 129.16 + 129.07898 + L + natural + Hy1Leu + PSI-MOD + MOD:01411 + monohydroxylated leucine + + + + + A protein modification that effectively converts an L-leucine residue to a monohydroxylated leucine. + PubMed:18688235 + + + + + Hy1Leu + + + + + + + + + + + A protein modification that effectively converts an L-leucine residue to a dihydroxylated leucine. + 32.0 + C 0 H 0 N 0 O 2 + 31.989828 + C 6 H 11 N 1 O 3 + 145.16 + 145.0739 + L + natural + Hy2Leu + PSI-MOD + MOD:01412 + dihydroxylated leucine + + + + + A protein modification that effectively converts an L-leucine residue to a dihydroxylated leucine. + PubMed:18688235 + + + + + Hy2Leu + + + + + + + + + + + A protein modification that effectively converts an L-leucine residue to a trihydroxylated leucine. + 48.0 + C 0 H 0 N 0 O 3 + 47.984745 + C 6 H 11 N 1 O 4 + 161.16 + 161.0688 + L + natural + Hy3Leu + PSI-MOD + MOD:01413 + trihydroxylated leucine + + + + + A protein modification that effectively converts an L-leucine residue to a trihydroxylated leucine. + PubMed:18688235 + + + + + Hy3Leu + + + + + + + + + + + A protein modification that effectively converts an L-isoleucine residue to an hydroxylated isoleucine. + I + HyIle + PSI-MOD + MOD:01414 + hydroxylated isoleucine + + + + + A protein modification that effectively converts an L-isoleucine residue to an hydroxylated isoleucine. + PubMed:18688235 + + + + + HyIle + + + + + + + + + + + A protein modification that effectively converts an L-isoleucine residue to a monohydroxylated isoleucine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 6 H 11 N 1 O 2 + 129.16 + 129.07898 + I + natural + Hy1Ile + PSI-MOD + MOD:01415 + monohydroxylated isoleucine + + + + + A protein modification that effectively converts an L-isoleucine residue to a monohydroxylated isoleucine. + PubMed:18688235 + + + + + Hy1Ile + + + + + + + + + + + A protein modification that effectively converts an L-isoleucine residue to a dihydroxylated isoleucine. + 32.0 + C 0 H 0 N 0 O 2 + 31.989828 + C 6 H 11 N 1 O 3 + 145.16 + 145.0739 + I + natural + Hy2Ile + PSI-MOD + MOD:01416 + dihydroxylated isoleucine + + + + + A protein modification that effectively converts an L-isoleucine residue to a dihydroxylated isoleucine. + PubMed:18688235 + + + + + Hy2Ile + + + + + + + + + + + A protein modification that effectively converts an L-proline residue to a monomethylated proline. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 6 H 10 N 1 O 1 + 112.15 + 112.07624 + P + natural + Me1Pro + PSI-MOD + MOD:01417 + + monomethylated proline + + + + + A protein modification that effectively converts an L-proline residue to a monomethylated proline. + PubMed:18688235 + + + + + Me1Pro + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to a methylated threonine, such as O-methyl-L-threonine. + T + natural + MeThr + PSI-MOD + MOD:01418 + methylated threonine + + + + + A protein modification that effectively converts an L-threonine residue to a methylated threonine, such as O-methyl-L-threonine. + PubMed:18688235 + + + + + MeThr + + + + + + + + + + A protein modification that crosslinks two residues by condensation of a serine or threonine hydroxyl with the carbonyl of the preceding residue to form an oxazole or oxazoline ring, or by rearrangement and condensation of a cysteine with the carbonyl of the preceding residue to form a 1,3-oxazole-4-carbothionic acid. + PSI-MOD + MOD:01419 + oxazole/oxazoline ring crosslinked residues + + + + + A protein modification that crosslinks two residues by condensation of a serine or threonine hydroxyl with the carbonyl of the preceding residue to form an oxazole or oxazoline ring, or by rearrangement and condensation of a cysteine with the carbonyl of the preceding residue to form a 1,3-oxazole-4-carbothionic acid. + PubMed:18688235 + + + + + + + + + + A protein modification that crosslinks two residues by condensation of a cysteine thiol with the carbonyl of the preceding residue to form a thiazole or thiazoline ring. + C + natural + PSI-MOD + MOD:01420 + thiazole/thiazoline ring crosslinked residues + + + + + A protein modification that crosslinks two residues by condensation of a cysteine thiol with the carbonyl of the preceding residue to form a thiazole or thiazoline ring. + PubMed:18688235 + + + + + + + + + + A protein modification that crosslinks two residues by condensation of a serine hydroxyl with the carbonyl of the preceding residue to form an oxazole or oxazoline ring. + S + natural + PSI-MOD + MOD:01421 + oxazole/oxazoline ring crosslinked residues (Ser) + + + + + A protein modification that crosslinks two residues by condensation of a serine hydroxyl with the carbonyl of the preceding residue to form an oxazole or oxazoline ring. + PubMed:18688235 + + + + + + + + + + A protein modification that crosslinks two residues by condensation of a threonine hydroxyl with the carbonyl of the preceding residue to form a 5-methyloxazole or 5-methyloxazoline ring. + T + natural + PSI-MOD + MOD:01422 + oxazole/oxazoline ring crosslinked residues (Thr) + + + + + A protein modification that crosslinks two residues by condensation of a threonine hydroxyl with the carbonyl of the preceding residue to form a 5-methyloxazole or 5-methyloxazoline ring. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a palmitoleyl group. + 236.4 + C 16 H 28 N 0 O 1 + 236.21402 + X + natural + Unimod:431 + PSI-MOD + MOD:01423 + + palmitoleylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with a palmitoleyl group. + Unimod:431 + + + + + + + + + A protein modification that effectively results from forming an adduct with a compound containing a quinaldate, kynurenate, or xanthurenate group. + PSI-MOD + MOD:01424 + quinaldate modified residue + + + + + A protein modification that effectively results from forming an adduct with a compound containing a quinaldate, kynurenate, or xanthurenate group. + PubMed:18688235 + + + + + + + + + A protein modification that crosslinks three residues by formation of a pyridinyl ring, such as pyridine-2,5-dicarboxylic acid or 5-aminopiperideine-2,5-dicarboxylic acid. + X + natural + PSI-MOD + MOD:01425 + Cross-link 3. + pyridinyl ring crosslinked residues + + + + + A protein modification that crosslinks three residues by formation of a pyridinyl ring, such as pyridine-2,5-dicarboxylic acid or 5-aminopiperideine-2,5-dicarboxylic acid. + PubMed:18688235 + + + + + + + + + A protein modification that forms an adduct with a particular isotope labeled compound used as a reagent. + PSI-MOD + MOD:01426 + + isotope tagged reagent derivatized residue + + + + + A protein modification that forms an adduct with a particular isotope labeled compound used as a reagent. + PubMed:18688235 + + + + + + + + OBSOLETE because redundant and identical to MOD:00819. Remap to MOD:00819. + MOD:00819 + C 4 H 7 N 1 O 1 + 85.11 + 85.052765 + X + artifact + Abu + PSI-MOD + MOD:01427 + 2-aminobutanoic acid (Abu) + true + + + + + OBSOLETE because redundant and identical to MOD:00819. Remap to MOD:00819. + PubMed:18688235 + + + + + Abu + + + + + + + + + + + A protein modification that forms an adduct with a (13)C labeled compound used as a reagent. + PSI-MOD + MOD:01428 + + (13)C isotope tagged reagent + + + + + A protein modification that forms an adduct with a (13)C labeled compound used as a reagent. + PubMed:18688235 + + + + + + + + + + A protein modification that forms an adduct with a (15)N labeled compound used as a reagent. + PSI-MOD + MOD:01429 + + (15)N isotope tagged reagent + + + + + A protein modification that forms an adduct with a (15)N labeled compound used as a reagent. + PubMed:18688235 + + + + + + + + + + A protein modification that forms an adduct with a (13)C labeled compound used as a reagent. + PSI-MOD + MOD:01430 + + (18)O isotope tagged reagent + + + + + A protein modification that forms an adduct with a (13)C labeled compound used as a reagent. + PubMed:18688235 + + + + + + + + + + A protein modification that forms an adduct with a (2)H labeled compound used as a reagent. + PSI-MOD + MOD:01431 + + (2)H deuterium tagged reagent + + + + + A protein modification that forms an adduct with a (2)H labeled compound used as a reagent. + PubMed:18688235 + + + + + + + + + A protein modification that effectively converts an L-leucine residue to a (2S,4S)-4,5-dihydroxyleucine. + 32.0 + C 0 H 0 N 0 O 2 + 31.989828 + C 6 H 11 N 1 O 3 + 145.16 + 145.0739 + L + natural + uniprot.ptm:PTM-0666 + (2S,4S)-2-amino-4,5-dihydroxy-4-methylpentanoic acid + (2S,4S)-4,5-dihydroxyleucine + (4S)-4,5-dihydroxyleucine + MOD_RES (4S)-4,5-dihydroxyleucine + gamma,delta-dihydroxyleucine + PSI-MOD + MOD:01432 + (2S,4S)-4,5-dihydroxyleucine + + + + + A protein modification that effectively converts an L-leucine residue to a (2S,4S)-4,5-dihydroxyleucine. + ChEBI:141819 + PubMed:3718926 + RESID:AA0446 + + + + + (2S,4S)-2-amino-4,5-dihydroxy-4-methylpentanoic acid + + + + + + (2S,4S)-4,5-dihydroxyleucine + + + + + + (4S)-4,5-dihydroxyleucine + + + + + + MOD_RES (4S)-4,5-dihydroxyleucine + + + + + + gamma,delta-dihydroxyleucine + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue into 1-amino-2-propanone. + -46.03 + C -1 H -2 N 0 O -2 + -46.005478 + C 3 H 6 N 1 O 1 + 72.09 + 72.04494 + T + natural + C-term + uniprot.ptm:PTM-0379 + 1-amino-2-propanone + 1-aminopropan-2-one + 1-aminopropanone + MOD_RES 1-amino-2-propanone + aminoacetone + PSI-MOD + MOD:01433 + 1-amino-2-propanone + + + + + A protein modification that effectively converts an L-threonine residue into 1-amino-2-propanone. + ChEBI:17906 + PubMed:12715872 + PubMed:19196969 + RESID:AA0486 + + + + + 1-amino-2-propanone + + + + + + 1-aminopropan-2-one + + + + + + 1-aminopropanone + + + + + + MOD_RES 1-amino-2-propanone + + + + + + aminoacetone + + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to a 4-hydroxy-L-glutamic acid. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 5 H 7 N 1 O 4 + 145.11 + 145.0375 + E + natural + uniprot.ptm:PTM-0453 + (2S,4Xi)-2-amino-4-hydroxypentanedioic acid + 4-hydroxy-L-glutamic acid + MOD_RES 4-hydroxyglutamate + gamma-hydroxy glutaminic acid + threo-4-hydroxy-L-glutamic acid + PSI-MOD + MOD:01434 + 4-hydroxy-L-glutamic acid + + + + + A protein modification that effectively converts an L-glutamic acid residue to a 4-hydroxy-L-glutamic acid. + ChEBI:141845 + PubMed:893891 + RESID:AA0487 + + + + + (2S,4Xi)-2-amino-4-hydroxypentanedioic acid + + + + + + 4-hydroxy-L-glutamic acid + + + + + + MOD_RES 4-hydroxyglutamate + + + + + + gamma-hydroxy glutaminic acid + + + + + + threo-4-hydroxy-L-glutamic acid + + + + + + + + + + + + A protein modification that effectively results from forming an adduct between a cysteine residue, a glutamic acid residue and the indole compound 2-carboxy-3-methyl-4-hydroxymethyl--indole. + 169.18 + C 11 H 7 N 1 O 1 S 0 + 169.05276 + C 19 H 19 N 3 O 5 S 1 + 401.44 + 401.10455 + C, E + natural + 2-([(1R)-1-amino-1-carboxyeth-2-yl]sulfanyl)carbonyl-3-methyl-4-([(1S)-1-amino-1-carboxy-4-oxobutan-4-yl]oxy)methyl-1H-indole + 2-(cystein-S-ylcarbonyl)-3-methyl-4-(glutam-5-yloxy)methylindole + 2-(cystein-S-ylcarbonyl)-4-[(glutam-5-yloxy)methyl]-3-methyl-1H-indole + BINDING 3-methyl-4-hydroxymethylindole-2-carboxylic acid (covalent; via 2 links) + PSI-MOD + MOD:01435 + Cross-link 2. + 2-(cystein-S-ylcarbonyl)-3-methyl-4-(glutam-5-yloxy)methylindole + + + + + A protein modification that effectively results from forming an adduct between a cysteine residue, a glutamic acid residue and the indole compound 2-carboxy-3-methyl-4-hydroxymethyl--indole. + PubMed:893891 + RESID:AA0488 + + + + + 2-([(1R)-1-amino-1-carboxyeth-2-yl]sulfanyl)carbonyl-3-methyl-4-([(1S)-1-amino-1-carboxy-4-oxobutan-4-yl]oxy)methyl-1H-indole + + + + + + 2-(cystein-S-ylcarbonyl)-3-methyl-4-(glutam-5-yloxy)methylindole + + + + + + 2-(cystein-S-ylcarbonyl)-4-[(glutam-5-yloxy)methyl]-3-methyl-1H-indole + + + + + + BINDING 3-methyl-4-hydroxymethylindole-2-carboxylic acid (covalent; via 2 links) + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to cyclo[(prolylserin)-O-yl] cysteinate. + 166.18 + C 8 H 10 N 2 O 2 S 0 + 166.07423 + C 11 H 16 N 3 O 4 S 1 + 286.33 + 286.08615 + C + natural + C-term + (3,6-dioxopyrrolo[4,5-a]piperazin-2-yl)methyl cysteinate + MOD_RES Cyclo[(prolylserin)-O-yl] cysteinate + [(3S,8aS)-1,4-dioxooctahydropyrrolo[1,2-a]pyrazin-3-yl]methyl (2R)-2-amino-3-sulfanylpropanoate + cyclo[(prolylserin)-O-yl] cysteinate + PSI-MOD + MOD:01436 + cyclo[(prolylserin)-O-yl] cysteinate (Cys) + + + + + A protein modification that effectively converts an L-cysteine residue to cyclo[(prolylserin)-O-yl] cysteinate. + PubMed:7961166 + RESID:AA0489#CYS + + + + + (3,6-dioxopyrrolo[4,5-a]piperazin-2-yl)methyl cysteinate + + + + + + MOD_RES Cyclo[(prolylserin)-O-yl] cysteinate + + + + + + [(3S,8aS)-1,4-dioxooctahydropyrrolo[1,2-a]pyrazin-3-yl]methyl (2R)-2-amino-3-sulfanylpropanoate + + + + + + cyclo[(prolylserin)-O-yl] cysteinate + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue, an L-proline residue, and an L-serine residue to cyclo[(prolylserin)-O-yl] cysteinate. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 11 H 16 N 3 O 4 S 1 + 286.33 + 286.08615 + C, P, S + natural + C-term + uniprot.ptm:PTM-0380 + (3,6-dioxopyrrolo[4,5-a]piperazin-2-yl)methyl cysteinate + MOD_RES Cyclo[(prolylserin)-O-yl] cysteinate + [(3S,8aS)-1,4-dioxooctahydropyrrolo[1,2-a]pyrazin-3-yl]methyl (2R)-2-amino-3-sulfanylpropanoate + cyclo[(prolylserin)-O-yl] cysteinate + PSI-MOD + MOD:01437 + Cross-link 3. + cyclo[(prolylserin)-O-yl] cysteinate (Cys-Pro-Ser cross-link) + + + + + A protein modification that effectively converts an L-cysteine residue, an L-proline residue, and an L-serine residue to cyclo[(prolylserin)-O-yl] cysteinate. + PubMed:7961166 + RESID:AA0489#TRI + + + + + (3,6-dioxopyrrolo[4,5-a]piperazin-2-yl)methyl cysteinate + + + + + + MOD_RES Cyclo[(prolylserin)-O-yl] cysteinate + + + + + + [(3S,8aS)-1,4-dioxooctahydropyrrolo[1,2-a]pyrazin-3-yl]methyl (2R)-2-amino-3-sulfanylpropanoate + + + + + + cyclo[(prolylserin)-O-yl] cysteinate + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-[2-(pyridin-2-yl)ethyl]-L-cysteine. + 105.14 + C 7 H 7 N 1 + 105.057846 + C 10 H 12 N 2 O 1 S 1 + 208.28 + 208.06703 + C + artifact + 2-PEC + 2-vinylpyridine derivatized cysteine residue + Pyridylethyl Cystenyl + S-(pyridin-2-ylethyl)-L-cysteine + PSI-MOD + Pyridylethyl + S-pyridylethylation + MOD:01438 + From DeltaMass: (name misspelled "Pyridylethyl Cystenyl", and formula incorrect, N and O reversed) Formula: C10H12O2N1S1 Monoisotopic Mass Change: 208.067 Average Mass Change: 208.286 + S-[2-(pyridin-2-yl)ethyl]-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-[2-(pyridin-2-yl)ethyl]-L-cysteine. + PubMed:18369855 + PubMed:18688235 + + + + + 2-PEC + + + + + + 2-vinylpyridine derivatized cysteine residue + + + + + + Pyridylethyl Cystenyl + + + + + + S-(pyridin-2-ylethyl)-L-cysteine + + + + + + Pyridylethyl + + + + + + S-pyridylethylation + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-[2-(pyridin-4-yl)ethyl]-L-cysteine. + C + artifact + 4-PEC + Pyridylethyl Cystenyl + S-(pyridin-4-ylethyl)-L-cysteine + PSI-MOD + Pyridylethyl + S-pyridylethylation + MOD:01439 + S-[2-(pyridin-4-yl)ethyl]-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-[2-(pyridin-4-yl)ethyl]-L-cysteine. + PubMed:18688235 + PubMed:6528972 + + + + + 4-PEC + + + + + + Pyridylethyl Cystenyl + + + + + + S-(pyridin-4-ylethyl)-L-cysteine + + + + + + Pyridylethyl + + + + + + S-pyridylethylation + + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to an L-glutamyl semialdehyde. + C 5 H 7 N 1 O 2 + 113.12 + 113.047676 + X + artifact + (S)-2-amino-5-oxopentanoic acid + L-glutamic gamma-semialdehyde + PSI-MOD + MOD:01440 + glutamyl semialdehyde + + + + + A protein modification that effectively converts a source amino acid residue to an L-glutamyl semialdehyde. + PubMed:18688235 + + + + + (S)-2-amino-5-oxopentanoic acid + + + + + + L-glutamic gamma-semialdehyde + + + + + + + + + + A protein modification that inserts or replaces a residue with a natural, standard, encoded residue. + X + natural + PSI-MOD + MOD:01441 + + natural, standard, encoded residue + + + + + A protein modification that inserts or replaces a residue with a natural, standard, encoded residue. + PubMed:18688235 + PubMed:6692818 + + + + + + + + + + + A protein modification that effectively cross-links an L-valine residue and an L-tyrosine residue by an ether bond to form 3-(O4'-L-tyrosyl)-L-valine. + -2.02 + C 0 H -2 N 0 O 0 + -2.01565 + C 14 H 16 N 2 O 3 + 260.29 + 260.1161 + V, Y + natural + uniprot.ptm:PTM-0390 + (2S)-2-amino-3-(4-[(2S)-2-amino-2-carboxyethyl]phenoxy)-3-methylbutanoic acid + 3-(O4'-L-tyrosyl)-L-valine + CROSSLNK 3-(O4'-tyrosyl)-valine (Val-Tyr) + PSI-MOD + MOD:01442 + Cross-link 2. + 3-(O4'-L-tyrosyl)-L-valine + + + + + A protein modification that effectively cross-links an L-valine residue and an L-tyrosine residue by an ether bond to form 3-(O4'-L-tyrosyl)-L-valine. + PubMed:19321420 + RESID:AA0490 + + + + + (2S)-2-amino-3-(4-[(2S)-2-amino-2-carboxyethyl]phenoxy)-3-methylbutanoic acid + + + + + + 3-(O4'-L-tyrosyl)-L-valine + + + + + + CROSSLNK 3-(O4'-tyrosyl)-valine (Val-Tyr) + + + + + + + + + + + + + + + + + + + A protein modification that effectively converts four L-glutamic acid residues and two L-histidine residues to tetrakis-L-glutamato bis-L-N1'-histidino lipid carboxylato manganese iron oxide. + 350.12 + C 14 Fe 1 H 23 Mn 1 N 0 O 3 + 350.03824 + 1- + C 46 Fe 1 H 65 Mn 1 N 10 O 17 + 1140.86 + 1140.3264 + E, E, E, E, H, H + natural + PSI-MOD + MOD:01443 + Cross-link 6. It is not clear whether the lipid carboxylate is a cofactor or a substrate, and its identity is not certain. It was modeled as myristic acid [JSG]. + tetrakis-L-glutamato bis-L-N1'-histidino lipid carboxylato manganese iron oxide + + + + + A protein modification that effectively converts four L-glutamic acid residues and two L-histidine residues to tetrakis-L-glutamato bis-L-N1'-histidino lipid carboxylato manganese iron oxide. + PubMed:19321420 + RESID:AA0491 + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to L-3,3-dihydroxyoalanine. + -0.06 + C 0 H 0 N 0 O 2 S -1 + 0.017758 + C 3 H 5 N 1 O 3 + 103.08 + 103.02694 + C + natural + (S)-2-amino-3,3-dihydroxypropanoic acid + 2-(dihydroxymethyl)glycine + 3,3-dihydroxy-L-alanine + 3,3-dihydroxyalanine + 3-hydroxy-L-serine + 3-oxoalanine hydrate + PSI-MOD + C(alpha)-formylglycine hydrate + MOD:01444 + L-3,3-dihydroxyoalanine (Cys) + + + + + A protein modification that effectively converts an L-cysteine residue to L-3,3-dihydroxyoalanine. + PubMed:11435113 + PubMed:17558559 + RESID:AA0492#CYS + + + + + (S)-2-amino-3,3-dihydroxypropanoic acid + + + + + + 2-(dihydroxymethyl)glycine + + + + + + 3,3-dihydroxy-L-alanine + + + + + + 3,3-dihydroxyalanine + + + + + + 3-hydroxy-L-serine + + + + + + 3-oxoalanine hydrate + + + + + + C(alpha)-formylglycine hydrate + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to L-3,3-dihydroxyoalanine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 3 H 5 N 1 O 3 + 103.08 + 103.02694 + S + natural + (S)-2-amino-3,3-dihydroxypropanoic acid + 2-(dihydroxymethyl)glycine + 3,3-dihydroxy-L-alanine + 3,3-dihydroxyalanine + 3-hydroxy-L-serine + 3-oxoalanine hydrate + PSI-MOD + C(alpha)-formylglycine hydrate + MOD:01445 + L-3,3-dihydroxyoalanine (Ser) + + + + + A protein modification that effectively converts an L-serine residue to L-3,3-dihydroxyoalanine. + PubMed:11435113 + PubMed:17558559 + RESID:AA0492#SER + + + + + (S)-2-amino-3,3-dihydroxypropanoic acid + + + + + + 2-(dihydroxymethyl)glycine + + + + + + 3,3-dihydroxy-L-alanine + + + + + + 3,3-dihydroxyalanine + + + + + + 3-hydroxy-L-serine + + + + + + 3-oxoalanine hydrate + + + + + + C(alpha)-formylglycine hydrate + + + + + + + + + + + + + + + + A protein modification that effectively converts an N-formyl-Lmethionine residue to N-(dihydroxymethyl)-L-methionine. + 18.02 + C 0 H 2 N 0 O 1 S 0 + 18.010565 + C 6 H 12 N 1 O 3 S 1 + 178.23 + 178.05379 + MOD:00030 + hypothetical + N-term + (2S)-2-[(dihydroxymethyl)amino]-4-(methylsulfanyl)butanoic acid + N-(dihydroxymethyl)-L-methionine + N-formyl-L-methionine hydrate + N-orthoformylmethionine + PSI-MOD + MOD:01446 + N-(dihydroxymethyl)-L-methionine (fMet) + + + + + A protein modification that effectively converts an N-formyl-Lmethionine residue to N-(dihydroxymethyl)-L-methionine. + PubMed:12595263 + PubMed:9159480 + RESID:AA0493 + + + + + (2S)-2-[(dihydroxymethyl)amino]-4-(methylsulfanyl)butanoic acid + + + + + + N-(dihydroxymethyl)-L-methionine + + + + + + N-formyl-L-methionine hydrate + + + + + + N-orthoformylmethionine + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to N-(dihydroxymethyl)-L-methionine (not known as a natural, post-translational modification process). + 46.03 + C 1 H 2 N 0 O 2 S 0 + 46.005478 + C 6 H 12 N 1 O 3 S 1 + 178.23 + 178.05379 + M + hypothetical + N-term + (2S)-2-[(dihydroxymethyl)amino]-4-(methylsulfanyl)butanoic acid + N-(dihydroxymethyl)-L-methionine + N-formyl-L-methionine hydrate + N-orthoformylmethionine + PSI-MOD + MOD:01447 + This entry is for the artifactual formation of N-(dihydroxymethyl)-L-methionine from methionine. For N-(dihydroxymethyl)-L-methionine derived from encoded N-formyl-L-methionine, use MOD:01446. + N-(dihydroxymethyl)-L-methionine (Met) + + + + + A protein modification that effectively converts an L-methionine residue to N-(dihydroxymethyl)-L-methionine (not known as a natural, post-translational modification process). + PubMed:12595263 + PubMed:9159480 + RESID:AA0493 + + + + + (2S)-2-[(dihydroxymethyl)amino]-4-(methylsulfanyl)butanoic acid + + + + + + N-(dihydroxymethyl)-L-methionine + + + + + + N-formyl-L-methionine hydrate + + + + + + N-orthoformylmethionine + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to L-3,3-dihydroxyoalanine. + C 3 H 5 N 1 O 3 + 103.08 + 103.02694 + X + natural + (S)-2-amino-3,3-dihydroxypropanoic acid + 2-(dihydroxymethyl)glycine + 3,3-dihydroxy-L-alanine + 3,3-dihydroxyalanine + 3-hydroxy-L-serine + 3-oxoalanine hydrate + PSI-MOD + C(alpha)-formylglycine hydrate + MOD:01448 + L-3,3-dihydroxyoalanine + + + + + A protein modification that effectively converts a source amino acid residue to L-3,3-dihydroxyoalanine. + PubMed:11435113 + PubMed:17558559 + RESID:AA0492 + + + + + (S)-2-amino-3,3-dihydroxypropanoic acid + + + + + + 2-(dihydroxymethyl)glycine + + + + + + 3,3-dihydroxy-L-alanine + + + + + + 3,3-dihydroxyalanine + + + + + + 3-hydroxy-L-serine + + + + + + 3-oxoalanine hydrate + + + + + + C(alpha)-formylglycine hydrate + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-3-oxoalanine residue to L-3,3-dihydroxyoalanine. + 18.02 + C 0 H 2 N 0 O 1 + 18.010565 + C 3 H 5 N 1 O 3 + 103.08 + 103.02694 + MOD:01169 + natural + PSI-MOD + MOD:01449 + L-3,3-dihydroxyoalanine (Oxoalanine) + + + + + A protein modification that effectively converts an L-3-oxoalanine residue to L-3,3-dihydroxyoalanine. + PubMed:11435113 + PubMed:17558559 + PubMed:18688235 + + + + + + + + + + + + + + + A protein modification that modifies an N-formyl-L-methionine residue. + MOD:00030 + N-term + PSI-MOD + MOD:01450 + modified N-formyl-L-methionine residue + + + + + A protein modification that modifies an N-formyl-L-methionine residue. + PubMed:18688235 + + + + + + + + + + + + + + + + A protein modification that converts an L-serine residue to O-phosphopantetheine-L-serine with secondary neutral loss of pantetheine resulting in O-phospho-L-serine. + 79.98 + C 0 H 1 N 0 O 3 P 1 + 79.96633 + C 3 H 6 N 1 O 5 P 1 + 167.06 + 166.99835 + S + artifact + PSI-MOD + MOD:01451 + + Phosphoserine is generated and detected after the facile elimination of pantetheine from the phosphopantetheine tertiary phosphodiester. See MOD:01452 for alternate origin. + O-phospho-L-serine arising from O-phosphopantetheine-L-serine after neutral loss of pantetheine + + + + + A protein modification that converts an L-serine residue to O-phosphopantetheine-L-serine with secondary neutral loss of pantetheine resulting in O-phospho-L-serine. + PubMed:17042494 + PubMed:18688235 + + + + + + + + + + + + + + + + Covalent modification of a peptide or protein amino acid O-phosphopantetheine-L-serine with secondary neutral loss of pantetheine resulting in O-phospho-L-serine. + -260.35 + C -11 H -20 N -2 O -3 P 0 S -1 + -260.11948 + C 3 H 6 N 1 O 5 P 1 + 167.06 + 166.99835 + MOD:00159 + artifact + PSI-MOD + MOD:01452 + + Phosphoserine is generated and detected after the facile elimination of pantethiene from the phosphopantethiene tertiary phosphodiester. See MOD:01451 for alternate origin. + O-phosphopantetheine-L-serine with neutral loss of pantetheine + + + + + Covalent modification of a peptide or protein amino acid O-phosphopantetheine-L-serine with secondary neutral loss of pantetheine resulting in O-phospho-L-serine. + PubMed:17042494 + PubMed:18688235 + + + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to L-glutamate 5-methyl ester. + C 6 H 9 N 1 O 3 + 143.14 + 143.05824 + X + natural + (2S)-2-amino-5-methoxy-5-oxopentanoic acid + (5)-methyl L-hydrogen glutamate + 2-aminopentanedioic acid 5-methyl ester + 5-methyl L-2-aminoglutarate + 5-methyl L-glutamate + 5-methyl esterified L-glutamic acid + L-glutamic acid 5-methyl ester + O-methyl Glutamyl + O5MeGlu + glutamic acid 5-methyl ester + glutamic acid gamma-methyl ester + PSI-MOD + MOD:01453 + + L-glutamic acid 5-methyl ester + + + + + A protein modification that effectively converts a source amino acid residue to L-glutamate 5-methyl ester. + RESID:AA0072 + + + + + (2S)-2-amino-5-methoxy-5-oxopentanoic acid + + + + + + (5)-methyl L-hydrogen glutamate + + + + + + 2-aminopentanedioic acid 5-methyl ester + + + + + + 5-methyl L-2-aminoglutarate + + + + + + 5-methyl L-glutamate + + + + + + 5-methyl esterified L-glutamic acid + + + + + + L-glutamic acid 5-methyl ester + + + + + + O-methyl Glutamyl + + + + + + O5MeGlu + + + + + + glutamic acid 5-methyl ester + + + + + + glutamic acid gamma-methyl ester + + + + + + + + + + + A protein modification that effectively crosslinks an N-terminal L-proline residue and a strand of DNA at the C-1 of a ribose, freeing the nucleotide base and forming N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium. + 1+ + P + natural + N-term + (1Z,2S)-2-carboxy-1-[(3R,4R)-3,4-dihydroxy-5-(phosphonooxy)pentylidene]pyrrolidinium + N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium + PSI-MOD + DNA glycosylase proline Schiff base intermediate + MOD:01454 + This linkage is not a Schiff-base [JSG]. + N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium + + + + + A protein modification that effectively crosslinks an N-terminal L-proline residue and a strand of DNA at the C-1 of a ribose, freeing the nucleotide base and forming N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium. + PubMed:10833024 + PubMed:11847126 + PubMed:9030608 + RESID:AA0494 + + + + + (1Z,2S)-2-carboxy-1-[(3R,4R)-3,4-dihydroxy-5-(phosphonooxy)pentylidene]pyrrolidinium + + + + + + N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium + + + + + + DNA glycosylase proline Schiff base intermediate + + + + + + + + + + A protein modification that effectively replaces a residue hydroxyl or carboxyl hydrogen with a phosphono group (H2PO3 or 'phosphate'). + 79.98 + H 1 O 3 P 1 + 79.96633 + X + OPhosRes + PSI-MOD + MOD:01455 + + O-phosphorylated residue + + + + + A protein modification that effectively replaces a residue hydroxyl or carboxyl hydrogen with a phosphono group (H2PO3 or 'phosphate'). + PubMed:18688235 + + + + + OPhosRes + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue amino or imino group with a phosphono group (H2PO3 or 'phosphate'). + 79.98 + H 1 O 3 P 1 + 79.96633 + X + NPhosRes + PSI-MOD + MOD:01456 + + N-phosphorylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue amino or imino group with a phosphono group (H2PO3 or 'phosphate'). + PubMed:18688235 + + + + + NPhosRes + + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to L-cysteine (not known as a natural, post-translational modification process). + -16.06 + C 0 H 0 N 0 O 1 S -1 + -15.977156 + C 3 H 5 N 1 O 1 S 1 + 103.14 + 103.009186 + C + artifact + Cys(Ser) + PSI-MOD + MOD:01457 + L-cysteine (Ser) + + + + + A protein modification that effectively converts an L-serine residue to L-cysteine (not known as a natural, post-translational modification process). + PubMed:1849824 + PubMed:18688235 + + + + + Cys(Ser) + + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acetyl group. + 42.04 + C 2 H 2 N 0 O 1 + 42.010567 + X + natural + N-term + Unimod:1 + N2AcRes + ntermacetyl + PSI-MOD + MOD:01458 + + alpha-amino acetylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acetyl group. + OMSSA:10 + Unimod:1#N-term + + + + + N2AcRes + + + + + + ntermacetyl + + + + + + + + + + A protein modification that effectively converts an N-terminal residue to an 4x(2)H labeled alpha-dimethylamino N-terminal residue. + 32.06 + C 2 (2)H 4 + 32.056408 + X + artifact + N-term + Unimod:199 + mod190 + PSI-MOD + DiMethyl-CHD2 + Dimethyl:2H(4) + MOD:01459 + + Supposed to be alpha-amino and Lys-N6 derivatized by C(2)H2O and reduction. + 4x(2)H labeled alpha-dimethylamino N-terminal residue + + + + + A protein modification that effectively converts an N-terminal residue to an 4x(2)H labeled alpha-dimethylamino N-terminal residue. + OMSSA:190 + PubMed:14670044 + Unimod:199#N-term + + + + + mod190 + + + + + + DiMethyl-CHD2 + + + + + + Dimethyl:2H(4) + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a methyl group. + X + natural + N-term + N2MeRes + PSI-MOD + MOD:01460 + + alpha-amino methylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a methyl group. + PubMed:18688235 + + + + + N2MeRes + + + + + + + + + + + A protein modification that effectively replaces an L-alanine alpha amino hydrogen with a methyl group. + A + natural + PSI-MOD + MOD:01461 + + N-methylated alanine + + + + + A protein modification that effectively replaces an L-alanine alpha amino hydrogen with a methyl group. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively replaces an L-proline alpha imino hydrogen with a methyl group. + P + natural + N-term + PSI-MOD + MOD:01462 + + N-methylated proline + + + + + A protein modification that effectively replaces an L-proline alpha imino hydrogen with a methyl group. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively replaces an L-methionine alpha amino hydrogen with a methyl group. + M + natural + N-term + PSI-MOD + MOD:01463 + + N-methylated methionine + + + + + A protein modification that effectively replaces an L-methionine alpha amino hydrogen with a methyl group. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to an L-methioninium (protonated L-methionine). + 1.01 + C 0 H 1 N 0 O 0 S 0 + 1.007276 + 1+ + C 5 H 11 N 1 O 1 S 1 + 133.21 + 133.05559 + M + natural + N-term + PSI-MOD + MOD:01464 + + protonated L-methionine (L-methioninium) residue + + + + + A protein modification that effectively converts an L-methionine residue to an L-methioninium (protonated L-methionine). + PubMed:18688235 + + + + + + + + + + + + + + + A protein modification that effectively converts an L-methioninium (protonated L-methionine) residue to an N6,N6,N6-trimethyl-L-methionine. + 42.08 + C 3 H 6 N 0 O 0 S 0 + 42.046402 + 1+ + C 8 H 17 N 1 O 1 S 1 + 175.29 + 175.10254 + MOD:001464 + natural + N-term + N2Me3Met + PSI-MOD + MOD:01465 + + For amino acids residues, amine trimethylation can effectively only be accomplished with an aminium, protonated primary amino, group. This process accounts only for trimethylation and not protonation. The alternative N2Me3+Met process (MOD:01382) accounts for both protonation and trimethylation. + N,N,N-trimethyl-L-methionine (from L-methioninium) + + + + + A protein modification that effectively converts an L-methioninium (protonated L-methionine) residue to an N6,N6,N6-trimethyl-L-methionine. + PubMed:18688235 + + + + + N2Me3Met + + + + + + + + + + + modification from Unimod Chemical derivative + 170.17 + C 11 H 6 O 2 + 170.03677 + C 14 H 11 N 1 O 3 S 1 + 273.31 + 273.04596 + C + artifact + Unimod:302 + PSI-MOD + Menadione + Menadione quinone derivative + MOD:01466 + menadione quinone derivative - site C + + + + + modification from Unimod Chemical derivative + PubMed:15939799 + Unimod:302#K + + + + + Menadione + + + + + + Menadione quinone derivative + + + + + + + + + + + modification from Unimod Chemical derivative + 170.17 + C 11 H 6 O 2 + 170.03677 + C 17 H 18 N 2 O 3 + 298.34 + 298.13174 + K + artifact + Unimod:302 + PSI-MOD + Menadione + Menadione quinone derivative + MOD:01467 + menadione quinone derivative - site K + + + + + modification from Unimod Chemical derivative + PubMed:15939799 + Unimod:302#K + + + + + Menadione + + + + + + Menadione quinone derivative + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) (not known as a natural, post-translational modification process). + 1618.93 + C 40 H 47 Mo 1 N 20 O 26 P 4 S 3 Se 1 + 1620.9302 + C 43 H 52 Mo 1 N 21 O 27 P 4 S 4 Se 1 + 1722.07 + 1723.9395 + C + artifact + Unimod:415 + 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide + L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) + bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-selenocysteinyl-Se-molybdenum + formate dehydrogenase selenocysteine molybdenum cofactor + PSI-MOD + L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) + MolybdopterinGD+Delta:S(-1)Se(1) + molybdopterin-se + MOD:01468 + This entry is for the artifactual formation of L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) from cysteine. For natural formation from L-selenocysteine, use MOD:00253. + L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) (Cys) + + + + + A protein modification that effectively converts an L-cysteine residue to L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) (not known as a natural, post-translational modification process). + PubMed:14235557 + PubMed:2211698 + PubMed:8052647 + PubMed:9036855 + RESID:AA0248#CYS + Unimod:415 + + + + + 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide + + + + + + L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) + + + + + + bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-selenocysteinyl-Se-molybdenum + + + + + + formate dehydrogenase selenocysteine molybdenum cofactor + + + + + + L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) + + + + + + MolybdopterinGD+Delta:S(-1)Se(1) + + + + + + molybdopterin-se + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide) (not known as a natural, post-translational modification process). + 1738.88 + C 40 H 47 N 20 O 26 P 4 S 4 Se 1 W 1 + 1738.9479 + C 43 H 52 N 21 O 27 P 4 S 5 Se 1 W 1 + 1842.02 + 1841.957 + C + artifact + PSI-MOD + MOD:01469 + This entry is for the artifactual formation of L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide) from cysteine. For natural formation from L-selenocysteine, use MOD:00381. + L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide) (Cys) + + + + + A protein modification that effectively converts an L-cysteine residue to L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide) (not known as a natural, post-translational modification process). + PubMed:11372198 + PubMed:12220497 + RESID:AA0376#CYS + + + + + + + + + A protein modification that effectively converts an L-threonine residue to (E)-dehydrobutyrine. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 4 H 5 N 1 O 1 + 83.09 + 83.03712 + T + natural + uniprot.ptm:PTM-0441 + (2E)-2-aminobut-2-enoic acid + (E)-2-amino-2-butenoic acid + (E)-2-aminobutenoic acid + (E)-dehydrobutyrine + (E)dHAbu + 2,3-didehydrobutyrine + 3-methyldehydroalanine + Dehydroamino butyric acid + Dhb + MOD_RES (E)-2,3-didehydrobutyrine + alpha,beta-dehydroaminobutyric acid + anhydrothreonine + methyl-dehydroalanine + PSI-MOD + Dehydrated + Dehydration + MOD:01470 + + (E)-dehydrobutyrine (Thr) + + + + + A protein modification that effectively converts an L-threonine residue to (E)-dehydrobutyrine. + DeltaMass:0 + PubMed:1547888 + PubMed:20805503 + PubMed:3769923 + RESID:AA0547 + + + + + (2E)-2-aminobut-2-enoic acid + + + + + + (E)-2-amino-2-butenoic acid + + + + + + (E)-2-aminobutenoic acid + + + + + + (E)-dehydrobutyrine + + + + + + (E)dHAbu + + + + + + 2,3-didehydrobutyrine + + + + + + 3-methyldehydroalanine + + + + + + Dehydroamino butyric acid + + + + + + Dhb + + + + + + MOD_RES (E)-2,3-didehydrobutyrine + + + + + + alpha,beta-dehydroaminobutyric acid + + + + + + anhydrothreonine + + + + + + methyl-dehydroalanine + + + + + + Dehydrated + + + + + + Dehydration + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to (Z)-dehydrobutyrine. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 4 H 5 N 1 O 1 + 83.09 + 83.03712 + T + natural + uniprot.ptm:PTM-0440 + (2Z)-2-aminobut-2-enoic acid + (Z)-2-amino-2-butenoic acid + (Z)-2-aminobutenoic acid + (Z)-dehydrobutyrine + (Z)dHAbu + 2,3-didehydrobutyrine + 3-methyldehydroalanine + Dehydroamino butyric acid + Dhb + MOD_RES (Z)-2,3-didehydrobutyrine + alpha,beta-dehydroaminobutyric acid + anhydrothreonine + methyl-dehydroalanine + PSI-MOD + Dehydrated + Dehydration + MOD:01471 + + (Z)-dehydrobutyrine (Thr) + + + + + A protein modification that effectively converts an L-threonine residue to (Z)-dehydrobutyrine. + DeltaMass:0 + PubMed:1547888 + PubMed:3769923 + RESID:AA0182 + + + + + (2Z)-2-aminobut-2-enoic acid + + + + + + (Z)-2-amino-2-butenoic acid + + + + + + (Z)-2-aminobutenoic acid + + + + + + (Z)-dehydrobutyrine + + + + + + (Z)dHAbu + + + + + + 2,3-didehydrobutyrine + + + + + + 3-methyldehydroalanine + + + + + + Dehydroamino butyric acid + + + + + + Dhb + + + + + + MOD_RES (Z)-2,3-didehydrobutyrine + + + + + + alpha,beta-dehydroaminobutyric acid + + + + + + anhydrothreonine + + + + + + methyl-dehydroalanine + + + + + + Dehydrated + + + + + + Dehydration + + + + + + + + + + A protein modification that effectively either adds neutral hydrogen atoms (proton and electron), or removes oxygen atoms from a residue with or without the addition of hydrogen atoms. + RedRes + PSI-MOD + MOD:01472 + + reduced residue + + + + + A protein modification that effectively either adds neutral hydrogen atoms (proton and electron), or removes oxygen atoms from a residue with or without the addition of hydrogen atoms. + PubMed:18688235 + + + + + RedRes + + + + + + + + + + A protein modification that effectively adds neutral hydrogen atoms (proton and electron) to a residue. + HRes + PSI-MOD + MOD:01473 + + hydrogenated residue + + + + + A protein modification that effectively adds neutral hydrogen atoms (proton and electron) to a residue. + PubMed:18688235 + + + + + HRes + + + + + + + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-[S-(carboxymethyl)phosphopantetheine]-L-serine. + 398.37 + C 13 H 23 N 2 O 8 P 1 S 1 + 398.09128 + C 16 H 28 N 3 O 10 P 1 S 1 + 485.44 + 485.1233 + S + artifact + PSI-MOD + MOD:01474 + This modification results from the derivatization of the pantetheine sulfhydryl with iodoacetic acid [JSG]. + O-[S-(carboxymethyl)phosphopantetheine]-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-[S-(carboxymethyl)phosphopantetheine]-L-serine. + PubMed:18688235 + + + + + + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-[S-(carboxamidomethyl)phosphopantetheine]-L-serine. + 397.38 + C 13 H 24 N 3 O 7 P 1 S 1 + 397.10727 + C 16 H 29 N 4 O 9 P 1 S 1 + 484.46 + 484.13928 + S + artifact + PSI-MOD + MOD:01475 + This modification results from the derivatization of the pantetheine sulfhydryl with iodoacetamide [JSG]. + O-[S-(carboxamidomethyl)phosphopantetheine]-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-[S-(carboxamidomethyl)phosphopantetheine]-L-serine. + PubMed:18688235 + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to an 2'-fluoro-L-fluorophenylalanine. + 17.99 + C 0 F 1 H -1 N 0 O 0 + 17.990578 + C 9 F 1 H 8 N 1 O 1 + 165.17 + 165.05899 + F + artifact + 2-fluorophenylalanine + o-fluorophenylalanine + ortho-fluorophenylalanine + PSI-MOD + MOD:01476 + 2'-fluoro-L-phenylalanine + + + + + A protein modification that effectively converts an L-phenylalanine residue to an 2'-fluoro-L-fluorophenylalanine. + PubMed:18688235 + PubMed:8172898 + + + + + 2-fluorophenylalanine + + + + + + o-fluorophenylalanine + + + + + + ortho-fluorophenylalanine + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue to an 3'-fluoro-L-fluorophenylalanine. + 17.99 + C 0 F 1 H -1 N 0 O 0 + 17.990578 + C 9 F 1 H 8 N 1 O 1 + 165.17 + 165.05899 + F + artifact + 3-fluorophenylalanine + m-fluorophenylalanine + meta-fluorophenylalanine + PSI-MOD + MOD:01477 + 3'-fluoro-L-phenylalanine + + + + + A protein modification that effectively converts an L-phenylalanine residue to an 3'-fluoro-L-fluorophenylalanine. + PubMed:18688235 + PubMed:8172898 + + + + + 3-fluorophenylalanine + + + + + + m-fluorophenylalanine + + + + + + meta-fluorophenylalanine + + + + + + + + + + A protein modification that effectively converts an L-phenylalanine residue into an 4'-fluoro-L-fluorophenylalanine. + 17.99 + C 0 F 1 H -1 N 0 O 0 + 17.990578 + C 9 F 1 H 8 N 1 O 1 + 165.17 + 165.05899 + F + artifact + 4-fluorophenylalanine + p-fluorophenylalanine + para-fluorophenylalanine + rho-fluorophenylalanine + PSI-MOD + MOD:01478 + 4'-fluoro-L-phenylalanine + + + + + A protein modification that effectively converts an L-phenylalanine residue into an 4'-fluoro-L-fluorophenylalanine. + PubMed:18688235 + PubMed:8172898 + + + + + 4-fluorophenylalanine + + + + + + p-fluorophenylalanine + + + + + + para-fluorophenylalanine + + + + + + rho-fluorophenylalanine + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue into an 4'-fluoro-L-tryptophan. + 17.99 + F 1 H -1 + 17.990578 + C 11 F 1 H 9 N 2 O 1 + 204.2 + 204.06989 + W + artifact + 4-fluorotryptophan + PSI-MOD + MOD:01479 + 4'-fluoro-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue into an 4'-fluoro-L-tryptophan. + PubMed:18688235 + PubMed:8172898 + + + + + 4-fluorotryptophan + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue into an 5'-fluoro-L-tryptophan. + 17.99 + F 1 H -1 + 17.990578 + C 11 F 1 H 9 N 2 O 1 + 204.2 + 204.06989 + W + artifact + 5-fluorotryptophan + PSI-MOD + MOD:01480 + 5'-fluoro-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue into an 5'-fluoro-L-tryptophan. + PubMed:18688235 + PubMed:8172898 + + + + + 5-fluorotryptophan + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue into an 6'-fluoro-L-tryptophan. + 17.99 + F 1 H -1 + 17.990578 + C 11 F 1 H 9 N 2 O 1 + 204.2 + 204.06989 + W + artifact + 6-fluorotryptophan + PSI-MOD + MOD:01481 + 6'-fluoro-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue into an 6'-fluoro-L-tryptophan. + PubMed:18688235 + PubMed:8172898 + + + + + 6-fluorotryptophan + + + + + + + + + + A protein modification that effectively substitutes a calcium atom or a cluster containing calcium for hydrogen atoms, or that coordinates a calcium ion. + CaRes + PSI-MOD + MOD:01482 + + calcium containing modified residue + + + + + A protein modification that effectively substitutes a calcium atom or a cluster containing calcium for hydrogen atoms, or that coordinates a calcium ion. + PubMed:18688235 + + + + + CaRes + + + + + + + + + + + A protein modification that effectively replaces a residue hydroxyl group with a formyloxy group. + 28.01 + C 1 O 1 + 27.994915 + X + artifact + OFoRes + PSI-MOD + MOD:01483 + O-formylated residue + + + + + A protein modification that effectively replaces a residue hydroxyl group with a formyloxy group. + PubMed:18688235 + + + + + OFoRes + + + + + + + + + + + + A protein modification that effectively crosslinks an L-glutamic acid residue and an L-lysine residue by an isopeptide bond to form N6-(L-isoglutamyl)-L-lysine and the release of water. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 11 H 17 N 3 O 3 + 239.27 + 239.12698 + K, E + natural + (2S)-2-amino-6-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid + 2-azanyl-6-([4-azanyl-4-carboxybutanoyl]azanyl)hexanoic acid + 5-glutamyl N6-lysine + N alpha -(gamma-Glutamyl)-lysine + N(epsilon)-(gamma-glutamyl)lysine + N6-(L-isoglutamyl)-L-lysine + PSI-MOD + MOD:01484 + Cross-link 2. This cross-link is usually made by glutamine and releases ammonia, rather than glutamic acid and requiring the consumption of ATP. + N6-(L-isoglutamyl)-L-lysine (Glu) + + + + + A protein modification that effectively crosslinks an L-glutamic acid residue and an L-lysine residue by an isopeptide bond to form N6-(L-isoglutamyl)-L-lysine and the release of water. + ChEBI:21863 + PubMed:19015515 + RESID:AA0124#GLU + + + + + (2S)-2-amino-6-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid + + + + + + 2-azanyl-6-([4-azanyl-4-carboxybutanoyl]azanyl)hexanoic acid + + + + + + 5-glutamyl N6-lysine + + + + + + N alpha -(gamma-Glutamyl)-lysine + + + + + + N(epsilon)-(gamma-glutamyl)lysine + + + + + + N6-(L-isoglutamyl)-L-lysine + + + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. + 144.11 + (12)C 5 (13)C 2 H 12 N 2 (18)O 1 + 144.10593 + X + artifact + Unimod:532 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 114 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ114 + iTRAQ4plex114 + MOD:01485 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-114 reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. + Unimod:532 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 114 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ114 + + + + + + iTRAQ4plex114 + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. + 144.11 + (12)C 5 (13)C 2 H 12 N 2 (18)O 1 + 144.10593 + X + artifact + N-term + Unimod:532 + (4-methylpiperazin-1-yl)acetyl + iTRAQ114nterm + PSI-MOD + Accurate mass for 114 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ114 + iTRAQ4plex114 + MOD:01486 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-114 reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. + OMSSA:167 + Unimod:532#N-term + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ114nterm + + + + + + Accurate mass for 114 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ114 + + + + + + iTRAQ4plex114 + + + + + + + + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. + 144.11 + (12)C 5 (13)C 2 H 12 N 2 (18)O 1 + 144.10593 + (12)C 11 (13)C 2 H 24 N 4 (16)O 1 (18)O 1 + 272.2 + 272.2009 + K + artifact + Unimod:532 + (4-methylpiperazin-1-yl)acetyl + iTRAQ114K + PSI-MOD + Accurate mass for 114 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ114 + iTRAQ4plex114 + MOD:01487 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-114 reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. + OMSSA:168 + Unimod:532#K + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ114K + + + + + + Accurate mass for 114 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ114 + + + + + + iTRAQ4plex114 + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. + 144.11 + (12)C 5 (13)C 2 H 12 N 2 (18)O 1 + 144.10593 + (12)C 14 (13)C 2 H 21 N 3 (16)O 2 (18)O 1 + 307.17 + 307.16925 + Y + artifact + Unimod:532 + (4-methylpiperazin-1-yl)acetyl + iTRAQ114Y + PSI-MOD + Accurate mass for 114 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ114 + iTRAQ4plex114 + MOD:01488 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-114 reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. + OMSSA:169 + Unimod:532#Y + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ114Y + + + + + + Accurate mass for 114 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ114 + + + + + + iTRAQ4plex114 + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. + 144.11 + (12)C 5 (13)C 2 H 12 N 2 (18)O 1 + 144.10593 + (12)C 11 (13)C 2 H 19 N 5 O 1 (18)O 1 + 281.16 + 281.16483 + H + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + iTRAQ4plex114 + MOD:01489 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-114 reporter+balance reagent N'-acylated histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ4plex114 + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. + 144.11 + (12)C 5 (13)C 2 H 12 N 2 (18)O 1 + 144.10593 + (12)C 8 (13)C 2 H 17 N 3 O 2 (18)O 1 + 231.14 + 231.13794 + S + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + iTRAQ4plex114 + MOD:01490 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-114 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ4plex114 + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. + 144.11 + (12)C 5 (13)C 2 H 12 N 2 (18)O 1 + 144.10593 + (12)C 9 (13)C 2 H 19 N 3 O 2 (18)O 1 + 245.15 + 245.1536 + T + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + iTRAQ4plex114 + MOD:01491 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-114 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ4plex114 + + + + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. + 144.1 + (12)C 6 (13)C 1 H 12 (14)N 1 (15)N 1 (18)O 1 + 144.0996 + X + artifact + Unimod:533 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 115 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ115 + iTRAQ4plex115 + MOD:01492 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-115 reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. + Unimod:533 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 115 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ115 + + + + + + iTRAQ4plex115 + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. + 144.1 + (12)C 6 (13)C 1 H 12 (14)N 1 (15)N 1 (18)O 1 + 144.0996 + X + artifact + N-term + Unimod:533 + (4-methylpiperazin-1-yl)acetyl + iTRAQ115nterm + PSI-MOD + Accurate mass for 115 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ115 + iTRAQ4plex115 + MOD:01493 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-115 reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. + OMSSA:170 + Unimod:533#N-term + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ115nterm + + + + + + Accurate mass for 115 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ115 + + + + + + iTRAQ4plex115 + + + + + + + + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. + 144.1 + (12)C 6 (13)C 1 H 12 (14)N 1 (15)N 1 (18)O 1 + 144.0996 + (12)C 12 (13)C 1 H 24 (14)N 3 (15)N 1 (16)O 1 (18)O 1 + 272.19 + 272.19455 + K + artifact + Unimod:533 + (4-methylpiperazin-1-yl)acetyl + iTRAQ115K + PSI-MOD + Accurate mass for 115 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ115 + iTRAQ4plex115 + MOD:01494 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-115 reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. + OMSSA:171 + Unimod:533#K + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ115K + + + + + + Accurate mass for 115 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ115 + + + + + + iTRAQ4plex115 + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. + 144.1 + (12)C 6 (13)C 1 H 12 (14)N 1 (15)N 1 (18)O 1 + 144.0996 + (12)C 15 (13)C 1 H 21 (14)N 2 (15)N 1 (16)O 2 (18)O 1 + 307.16 + 307.16293 + Y + artifact + Unimod:533 + (4-methylpiperazin-1-yl)acetyl + iTRAQ115Y + PSI-MOD + Accurate mass for 115 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ115 + iTRAQ4plex115 + MOD:01495 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-115 reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. + OMSSA:172 + Unimod:533#Y + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ115Y + + + + + + Accurate mass for 115 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ115 + + + + + + iTRAQ4plex115 + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. + 144.1 + (12)C 6 (13)C 1 H 12 (14)N 1 (15)N 1 (18)O 1 + 144.0996 + (12)C 12 (13)C 1 H 19 (14)N 4 (15)N 1 (16)O 1 (18)O 1 + 281.16 + 281.1585 + H + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + iTRAQ4plex115 + MOD:01496 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-115 reporter+balance reagent N'-acylated histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ4plex115 + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. + 144.1 + (12)C 6 (13)C 1 H 12 (14)N 1 (15)N 1 (18)O 1 + 144.0996 + (12)C 9 (13)C 1 H 17 N 1 (14)N 1 (15)N 1 (16)O 2 (18)O 1 + 231.13 + 231.13162 + S + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + iTRAQ4plex115 + MOD:01497 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-115 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ4plex115 + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. + 144.1 + (12)C 6 (13)C 1 H 12 (14)N 1 (15)N 1 (18)O 1 + 144.0996 + (12)C 10 (13)C 1 H 19 (14)N 2 (15)N 1 (16)O 2 (18)O 1 + 245.15 + 245.14728 + T + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + iTRAQ4plex115 + MOD:01498 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-115 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ4plex115 + + + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. + 144.1 + (12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1 + 144.10207 + X + artifact + Unimod:214 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 116 & 117 + iTRAQ + iTRAQ4plex + MOD:01499 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-116 reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. + Unimod:214 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 116 & 117 + + + + + + iTRAQ + + + + + + iTRAQ4plex + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. + 144.1 + (12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1 + 144.10207 + X + artifact + N-term + Unimod:214 + (4-methylpiperazin-1-yl)acetyl + iTRAQ116nterm + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 116 & 117 + iTRAQ + iTRAQ4plex + MOD:01500 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-116 reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. + OMSSA:173 + Unimod:214#N-term + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ116nterm + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 116 & 117 + + + + + + iTRAQ + + + + + + iTRAQ4plex + + + + + + + + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. + 144.1 + (12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1 + 144.10207 + (12)C 10 (13)C 3 H 24 N 2 (14)N 1 (15)N 1 O 1 (16)O 1 + 272.2 + 272.19702 + K + artifact + Unimod:214 + (4-methylpiperazin-1-yl)acetyl + iTRAQ116K + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 116 & 117 + iTRAQ + iTRAQ4plex + MOD:01501 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-116 reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. + OMSSA:174 + Unimod:214#K + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ116K + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 116 & 117 + + + + + + iTRAQ + + + + + + iTRAQ4plex + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. + 144.1 + (12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1 + 144.10207 + (12)C 13 (13)C 3 H 21 N 1 (14)N 1 (15)N 1 O 2 (16)O 1 + 307.17 + 307.1654 + Y + artifact + Unimod:214 + (4-methylpiperazin-1-yl)acetyl + iTRAQ116Y + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 116 & 117 + iTRAQ + iTRAQ4plex + MOD:01502 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-116 reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. + OMSSA:175 + Unimod:214#Y + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ116Y + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 116 & 117 + + + + + + iTRAQ + + + + + + iTRAQ4plex + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. + 144.1 + (12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1 + 144.10207 + (12)C 10 (13)C 3 H 19 N 3 (14)N 1 (15)N 1 (16)O 2 + 281.16 + 281.16098 + H + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + iTRAQ4plex + MOD:01503 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-116 reporter+balance reagent N'-acylated histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ4plex + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. + 144.1 + (12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1 + 144.10207 + (12)C 7 (13)C 3 H 17 (14)N 2 (15)N 1 (16)O 3 + 231.13 + 231.1341 + S + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + iTRAQ4plex + MOD:01504 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-116 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ4plex + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. + 144.1 + (12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1 + 144.10207 + (12)C 8 (13)C 3 H 19 (14)N 2 (15)N 1 (16)O 3 + 245.15 + 245.14973 + T + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + iTRAQ4plex + MOD:01505 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-116 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ4plex + + + + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. + 144.1 + (12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1 + 144.10207 + X + artifact + Unimod:214 + Unimod:889 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Applied Biosystems mTRAQ(TM) reagent + Representative mass and accurate mass for 116 & 117 + iTRAQ + iTRAQ4plex + mTRAQ heavy + MOD:01506 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. + Unimod:214 + Unimod:889 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Applied Biosystems mTRAQ(TM) reagent + + + + + + Representative mass and accurate mass for 116 & 117 + + + + + + iTRAQ + + + + + + iTRAQ4plex + + + + + + mTRAQ heavy + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. + 144.1 + (12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1 + 144.10207 + X + artifact + N-term + Unimod:214 + Unimod:889 + (4-methylpiperazin-1-yl)acetyl + iTRAQ117nterm + mTRAQ heavy on nterm + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Applied Biosystems mTRAQ(TM) reagent + Representative mass and accurate mass for 116 & 117 + iTRAQ + iTRAQ4plex + mTRAQ heavy + MOD:01507 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. + OMSSA:176 + OMSSA:211 + Unimod:214#N-term + Unimod:889#N-term + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ117nterm + + + + + + mTRAQ heavy on nterm + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Applied Biosystems mTRAQ(TM) reagent + + + + + + Representative mass and accurate mass for 116 & 117 + + + + + + iTRAQ + + + + + + iTRAQ4plex + + + + + + mTRAQ heavy + + + + + + + + + + + + A protein modification that effectively replaces the N6-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. + 144.1 + (12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1 + 144.10207 + (12)C 10 (13)C 3 H 24 N 2 (14)N 1 (15)N 1 O 1 (16)O 1 + 272.2 + 272.19702 + K + artifact + Unimod:214 + (4-methylpiperazin-1-yl)acetyl + iTRAQ117K + mTRAQ heavy on K + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Applied Biosystems mTRAQ(TM) reagent + Representative mass and accurate mass for 116 & 117 + iTRAQ + iTRAQ4plex + mTRAQ heavy + MOD:01508 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. + OMSSA:177 + OMSSA:212 + Unimod:214#K + Unimod:889#K + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ117K + + + + + + mTRAQ heavy on K + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Applied Biosystems mTRAQ(TM) reagent + + + + + + Representative mass and accurate mass for 116 & 117 + + + + + + iTRAQ + + + + + + iTRAQ4plex + + + + + + mTRAQ heavy + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. + 144.1 + (12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1 + 144.10207 + (12)C 13 (13)C 3 H 21 N 1 (14)N 1 (15)N 1 O 2 (16)O 1 + 307.17 + 307.1654 + Y + artifact + Unimod:214 + Unimod:889 + (4-methylpiperazin-1-yl)acetyl + iTRAQ117Y + mTRAQ heavy on Y + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Applied Biosystems mTRAQ(TM) reagent + Representative mass and accurate mass for 116 & 117 + iTRAQ + iTRAQ4plex + mTRAQ heavy + MOD:01509 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. + OMSSA:178 + OMSSA:213 + Unimod:214#Y + Unimod:889#Y + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ117Y + + + + + + mTRAQ heavy on Y + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Applied Biosystems mTRAQ(TM) reagent + + + + + + Representative mass and accurate mass for 116 & 117 + + + + + + iTRAQ + + + + + + iTRAQ4plex + + + + + + mTRAQ heavy + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. + 144.1 + (12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1 + 144.10207 + (12)C 10 (13)C 3 H 19 (14)N 4 (15)N 1 (16)O 2 + 281.16 + 281.16098 + H + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + iTRAQ4plex + MOD:01510 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-117 reporter+balance reagent N'-acylated histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ4plex + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. + 144.1 + (12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1 + 144.10207 + (12)C 7 (13)C 3 H 17 (14)N 2 (15)N 1 (16)O 3 + 231.13 + 231.1341 + S + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + iTRAQ4plex + MOD:01511 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-117 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ4plex + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. + 144.1 + (12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1 + 144.10207 + (12)C 8 (13)C 3 H 19 (14)N 2 (15)N 1 (16)O 3 + 245.15 + 245.14973 + T + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + iTRAQ4plex + MOD:01512 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex-117 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ4plex + + + + + + + + + + Modifications that have monoisotopic mass differences from their respective origins that are nominally equal (sometimes called isobaric) at a resolution below 0.1 Da. + PSI-MOD + MOD:01513 + + modifications with monoisotopic mass differences that are nominally equal at a resolution below 0.1 Da + + + + + Modifications that have monoisotopic mass differences from their respective origins that are nominally equal (sometimes called isobaric) at a resolution below 0.1 Da. + PubMed:18688235 + + + + + + + + + Modifications that have monoisotopic mass differences from their respective origins that are nominally equal (sometimes called isobaric) at a resolution below 0.01 Da. + PSI-MOD + MOD:01514 + + modifications with monoisotopic mass differences that are nominally equal at a resolution below 0.01 Da + + + + + Modifications that have monoisotopic mass differences from their respective origins that are nominally equal (sometimes called isobaric) at a resolution below 0.01 Da. + PubMed:18688235 + + + + + + + + + Modifications that have monoisotopic mass differences from their respective origins that are nominally equal (sometimes called isobaric) at a resolution below 0.000001 Da. + PSI-MOD + MOD:01515 + + modifications with monoisotopic mass differences that are nominally equal at a resolution below 0.000001 Da + + + + + Modifications that have monoisotopic mass differences from their respective origins that are nominally equal (sometimes called isobaric) at a resolution below 0.000001 Da. + PubMed:18688235 + + + + + + + + + Modifications that have monoisotopic mass differences from their respective origins of 144.099-144.106 Da. + PSI-MOD + MOD:01516 + + modifications with monoisotopic mass diferences that are nominally equal at 144.099-144.106 Da. + + + + + Modifications that have monoisotopic mass differences from their respective origins of 144.099-144.106 Da. + PubMed:18688235 + + + + + + + + + + Modifications that have monoisotopic mass differences from their respective origins of 144.102062 Da. + PSI-MOD + MOD:01517 + + modifications with monoisotopic mass differences that are nominally equal at 144.102062 Da + + + + + Modifications that have monoisotopic mass differences from their respective origins of 144.102062 Da. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups. + X + artifact + Unimod:214 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01518 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups. + Unimod:214 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + A distinct molecular entity produced from a protein or a protein modification as the result of a fragmentation process. + PSI-MOD + MOD:01519 + + The reporter fragment is either itself a modification consisting of atoms derived from the original amino acid residues, or its detection can be taken as evidence that particular modified residues had been present. + reporter fragment + + + + + A distinct molecular entity produced from a protein or a protein modification as the result of a fragmentation process. + PubMed:18688235 + + + + + + + + + A distinct molecular entity produced as the result of a fragmentation process performed on a particular modified residue. + PSI-MOD + MOD:01520 + + modification reporter fragment + + + + + A distinct molecular entity produced as the result of a fragmentation process performed on a particular modified residue. + PubMed:18688235 + + + + + + + + + A protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex reagent derivatized residue. + PSI-MOD + MOD:01521 + + iTRAQ4plex reporter fragment + + + + + A protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex reagent derivatized residue. + PubMed:18688235 + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 114 reagent derivatized residue. + 1+ + (12)C 5 (13)C 1 H 13 (14)N 2 + 114.11 + 114.11068 + X + artifact + 4-methyl-1-methylidenepiperazin-1-ium + PSI-MOD + MOD:01522 + + iTRAQ4plex-114 reporter fragment + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 114 reagent derivatized residue. + PubMed:18688235 + + + + + 4-methyl-1-methylidenepiperazin-1-ium + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 115 reagent derivatized residue. + 1+ + (12)C 5 (13)C 1 H 13 (14)N 1 (15)N 1 + 115.11 + 115.10771 + X + artifact + 4-methyl-1-methylidenepiperazin-1-ium + PSI-MOD + MOD:01523 + + iTRAQ4plex-115 reporter fragment + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 115 reagent derivatized residue. + PubMed:18688235 + + + + + 4-methyl-1-methylidenepiperazin-1-ium + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 116 reagent derivatized residue. + 1+ + (12)C 4 (13)C 2 H 13 (14)N 1 (15)N 1 + 116.11 + 116.11107 + X + artifact + 4-methyl-1-methylidenepiperazin-1-ium + PSI-MOD + MOD:01524 + + iTRAQ4plex-116 reporter fragment + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 116 reagent derivatized residue. + PubMed:18688235 + + + + + 4-methyl-1-methylidenepiperazin-1-ium + + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 117 reagent derivatized residue. + 1+ + (12)C 3 (13)C 3 H 13 (14)N 1 (15)N 1 + 117.11 + 117.114426 + X + artifact + 4-methyl-1-methylidenepiperazin-1-ium + PSI-MOD + MOD:01525 + + iTRAQ4plex-117, mTRAQ heavy, reporter fragment + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 117 reagent derivatized residue. + PubMed:18688235 + + + + + 4-methyl-1-methylidenepiperazin-1-ium + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance groups. + X + artifact + Unimod:730 + PSI-MOD + MOD:01526 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance groups. + Unimod:730 + + + + + + + + + A distinct molecular entity produced from a particular amino acid residue as the result of a fragmentation process. + PSI-MOD + MOD:01527 + + residue reporter fragment + + + + + A distinct molecular entity produced from a particular amino acid residue as the result of a fragmentation process. + PubMed:18688235 + + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + X + artifact + Unimod:730 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01528 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-113 reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. + Unimod:730 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + X + artifact + N-term + Unimod:730 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01529 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-113 reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. + Unimod:730#N-term + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 13 (13)C 7 H 36 (14)N 5 (15)N 1 (16)O 4 + 432.3 + 432.30032 + K + artifact + Unimod:730 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01530 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-113 reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. + Unimod:730#K + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 16 (13)C 7 H 33 (14)N 4 (15)N 1 (16)O 5 + 467.27 + 467.26868 + Y + artifact + Unimod:730 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01531 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-113 reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. + Unimod:730#Y + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 13 (13)C 7 H 31 (14)N 6 (15)N 1 (16)O 4 + 441.26 + 441.26428 + H + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01532 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-113 reporter+balance reagent N'-acylated histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 10 (13)C 7 H 29 (14)N 4 (15)N 1 (16)O 5 + 391.24 + 391.2374 + S + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01533 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-113 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 11 (13)C 7 H 31 (14)N 4 (15)N 1 (16)O 5 + 405.25 + 405.25305 + T + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01534 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-113 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + X + artifact + Unimod:730 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01535 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-114 reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. + Unimod:730 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + X + artifact + N-term + Unimod:730 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01536 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-114 reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. + Unimod:730#N-term + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 13 (13)C 7 H 36 (14)N 5 (15)N 1 (16)O 4 + 432.3 + 432.30032 + K + artifact + Unimod:730 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01537 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-114 reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. + Unimod:730#K + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 16 (13)C 7 H 33 (14)N 4 (15)N 1 (16)O 5 + 467.27 + 467.26868 + Y + artifact + Unimod:730 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01538 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-114 reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. + Unimod:730#Y + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 13 (13)C 7 H 31 (14)N 6 (15)N 1 (16)O 4 + 441.26 + 441.26428 + H + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01539 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-114 reporter+balance reagent N'-acylated histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 10 (13)C 7 H 29 (14)N 4 (15)N 1 (16)O 5 + 391.24 + 391.2374 + S + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01540 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-114 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 11 (13)C 7 H 31 (14)N 4 (15)N 1 (16)O 5 + 405.25 + 405.25305 + T + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01541 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-114 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + X + artifact + Unimod:731 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 115, 118, 119 & 121 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ8plex:13C(6)15N(2) + MOD:01542 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-115 reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. + Unimod:731 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 115, 118, 119 & 121 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ8plex:13C(6)15N(2) + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + X + artifact + N-term + Unimod:731 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 115, 118, 119 & 121 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ8plex:13C(6)15N(2) + MOD:01543 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-115 reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. + Unimod:731#N-term + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 115, 118, 119 & 121 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ8plex:13C(6)15N(2) + + + + + + + + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 14 (13)C 6 H 36 (14)N 4 (15)N 2 (16)O 4 + 432.29 + 432.294 + K + artifact + Unimod:731 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 115, 118, 119 & 121 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ8plex:13C(6)15N(2) + MOD:01544 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-115 reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. + Unimod:731#K + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 115, 118, 119 & 121 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ8plex:13C(6)15N(2) + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 17 (13)C 6 H 33 (14)N 3 (15)N 2 (16)O 5 + 467.26 + 467.26236 + Y + artifact + Unimod:731 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 115, 118, 119 & 121 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ8plex:13C(6)15N(2) + MOD:01545 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-115 reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. + Unimod:731#Y + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 115, 118, 119 & 121 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ8plex:13C(6)15N(2) + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 14 (13)C 6 H 31 (14)N 5 (15)N 2 (16)O 4 + 441.26 + 441.25797 + H + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01546 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-115 reporter+balance reagent N'-derivatized histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 11 (13)C 6 H 29 (14)N 3 (15)N 2 (16)O 5 + 391.23 + 391.23108 + S + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01547 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-115 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 12 (13)C 6 H 31 (14)N 3 (15)N 2 (16)O 5 + 405.25 + 405.2467 + T + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01548 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-115 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + X + artifact + Unimod:730 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01549 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-116 reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. + Unimod:730 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + X + artifact + N-term + Unimod:730 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01550 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-116 reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. + Unimod:730#N-term + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 13 (13)C 7 H 36 (14)N 5 (15)N 1 (16)O 4 + 432.3 + 432.30032 + K + artifact + Unimod:730 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01551 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-116 reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. + Unimod:730#K + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 16 (13)C 7 H 33 (14)N 4 (15)N 1 (16)O 5 + 467.27 + 467.26868 + Y + artifact + Unimod:730 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01552 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-116 reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. + Unimod:730#Y + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 13 (13)C 7 H 31 (14)N 6 (15)N 1 (16)O 4 + 441.26 + 441.26428 + H + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01553 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-116 reporter+balance reagent N'-acylated histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 10 (13)C 7 H 29 (14)N 4 (15)N 1 (16)O 5 + 391.24 + 391.2374 + S + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01554 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-116 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 11 (13)C 7 H 31 (14)N 4 (15)N 1 (16)O 5 + 405.25 + 405.25305 + T + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01555 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-116 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + X + artifact + Unimod:730 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01556 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-117 reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. + Unimod:730 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + X + artifact + N-term + Unimod:730 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01557 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-117 reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. + Unimod:730#N-term + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 13 (13)C 7 H 36 (14)N 5 (15)N 1 (16)O 4 + 432.3 + 432.30032 + K + artifact + Unimod:730 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01558 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-117 reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. + Unimod:730#K + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 16 (13)C 7 H 33 (14)N 4 (15)N 1 (16)O 5 + 467.27 + 467.26868 + Y + artifact + Unimod:730 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + Representative mass and accurate mass for 113, 114, 116 & 117 + iTRAQ8plex + iTRAQ8plex:13C(7)15N(1) + MOD:01559 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-117 reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. + Unimod:730#Y + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + Representative mass and accurate mass for 113, 114, 116 & 117 + + + + + + iTRAQ8plex + + + + + + iTRAQ8plex:13C(7)15N(1) + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 13 (13)C 7 H 31 (14)N 6 (15)N 1 (16)O 4 + 441.26 + 441.26428 + H + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01560 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-117 reporter+balance reagent N'-acylated histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 10 (13)C 7 H 29 (14)N 4 (15)N 1 (16)O 5 + 391.24 + 391.2374 + S + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01561 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-117 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. + 304.21 + (12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3 + 304.20535 + (12)C 11 (13)C 7 H 31 (14)N 4 (15)N 1 (16)O 5 + 405.25 + 405.25305 + T + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01562 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-117 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + X + artifact + Unimod:731 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 115, 118, 119 & 121 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ8plex:13C(6)15N(2) + MOD:01563 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-118 reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. + Unimod:731 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 115, 118, 119 & 121 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ8plex:13C(6)15N(2) + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + X + artifact + N-term + Unimod:731 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 115, 118, 119 & 121 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ8plex:13C(6)15N(2) + MOD:01564 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-118 reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. + Unimod:731#N-term + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 115, 118, 119 & 121 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ8plex:13C(6)15N(2) + + + + + + + + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 14 (13)C 6 H 36 (14)N 4 (15)N 2 (16)O 4 + 432.29 + 432.294 + K + artifact + Unimod:731 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 115, 118, 119 & 121 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ8plex:13C(6)15N(2) + MOD:01565 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-118 reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. + Unimod:731#K + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 115, 118, 119 & 121 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ8plex:13C(6)15N(2) + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 17 (13)C 6 H 33 (14)N 3 (15)N 2 (16)O 5 + 467.26 + 467.26236 + Y + artifact + Unimod:731 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 115, 118, 119 & 121 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ8plex:13C(6)15N(2) + MOD:01566 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-118 reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. + Unimod:731#Y + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 115, 118, 119 & 121 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ8plex:13C(6)15N(2) + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 14 (13)C 6 H 31 (14)N 5 (15)N 2 (16)O 4 + 441.26 + 441.25797 + H + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01567 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-118 reporter+balance reagent N'-acylated histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 11 (13)C 6 H 29 (14)N 3 (15)N 2 (16)O 5 + 391.23 + 391.23108 + S + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01568 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-118 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 12 (13)C 6 H 31 (14)N 3 (15)N 2 (16)O 5 + 405.25 + 405.2467 + T + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01569 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-118 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + X + artifact + Unimod:731 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 115, 118, 119 & 121 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ8plex:13C(6)15N(2) + MOD:01570 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-119 reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. + Unimod:731 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 115, 118, 119 & 121 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ8plex:13C(6)15N(2) + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + X + artifact + N-term + Unimod:731 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 115, 118, 119 & 121 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ8plex:13C(6)15N(2) + MOD:01571 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-119 reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. + Unimod:731#N-term + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 115, 118, 119 & 121 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ8plex:13C(6)15N(2) + + + + + + + + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 14 (13)C 6 H 36 (14)N 4 (15)N 2 (16)O 4 + 432.29 + 432.294 + K + artifact + Unimod:731 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 115, 118, 119 & 121 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ8plex:13C(6)15N(2) + MOD:01572 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-119 reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. + Unimod:731#K + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 115, 118, 119 & 121 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ8plex:13C(6)15N(2) + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 17 (13)C 6 H 33 (14)N 3 (15)N 2 (16)O 5 + 467.26 + 467.26236 + Y + artifact + Unimod:731 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 115, 118, 119 & 121 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ8plex:13C(6)15N(2) + MOD:01573 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-119 reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. + Unimod:731#Y + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 115, 118, 119 & 121 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ8plex:13C(6)15N(2) + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 14 (13)C 6 H 31 (14)N 5 (15)N 2 (16)O 4 + 441.26 + 441.25797 + H + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01574 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-119 reporter+balance reagent N'-acylated histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 11 (13)C 6 H 29 (14)N 3 (15)N 2 (16)O 5 + 391.23 + 391.23108 + S + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01575 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-119 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 12 (13)C 6 H 31 (14)N 3 (15)N 2 (16)O 5 + 405.25 + 405.2467 + T + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01576 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-119 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + X + artifact + Unimod:731 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 115, 118, 119 & 121 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ8plex:13C(6)15N(2) + MOD:01577 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-121 reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. + Unimod:731 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 115, 118, 119 & 121 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ8plex:13C(6)15N(2) + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + X + artifact + N-term + Unimod:731 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 115, 118, 119 & 121 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ8plex:13C(6)15N(2) + MOD:01578 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-121 reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. + Unimod:731#N-term + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 115, 118, 119 & 121 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ8plex:13C(6)15N(2) + + + + + + + + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 14 (13)C 6 H 36 (14)N 4 (15)N 2 (16)O 4 + 432.29 + 432.294 + K + artifact + Unimod:731 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 115, 118, 119 & 121 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ8plex:13C(6)15N(2) + MOD:01579 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-121 reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. + Unimod:731#K + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 115, 118, 119 & 121 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ8plex:13C(6)15N(2) + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 17 (13)C 6 H 33 (14)N 3 (15)N 2 (16)O 5 + 467.26 + 467.26236 + Y + artifact + Unimod:731 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Accurate mass for 115, 118, 119 & 121 + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + iTRAQ8plex:13C(6)15N(2) + MOD:01580 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-121 reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. + Unimod:731#Y + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Accurate mass for 115, 118, 119 & 121 + + + + + + Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry + + + + + + iTRAQ8plex:13C(6)15N(2) + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 14 (13)C 6 H 31 (14)N 5 (15)N 2 (16)O 4 + 441.26 + 441.25797 + H + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01581 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-121 reporter+balance reagent N'-acylated histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 11 (13)C 6 H 29 (14)N 3 (15)N 2 (16)O 5 + 391.23 + 391.23108 + S + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01582 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-121 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. + 304.2 + (12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3 + 304.19904 + (12)C 12 (13)C 6 H 31 (14)N 3 (15)N 2 (16)O 5 + 405.25 + 405.2467 + T + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01583 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex-121 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + Modifications that have monoisotopic mass differences from their respective origins of 304.199039 Da. + PSI-MOD + MOD:01584 + + modifications with monoisotopic mass differences that are nominally equal at 304.199039 Da + + + + + Modifications that have monoisotopic mass differences from their respective origins of 304.199039 Da. + PubMed:18688235 + + + + + + + + + + + + A protein modification that effectively crosslinks an L-serine residue and a glycine residue by an ester bond to form O-glycyl-L-serine. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 5 H 7 N 2 O 3 + 143.12 + 143.04567 + G, S + natural + C-term + uniprot.ptm:PTM-0422 + (2S)-2-amino-3-[(aminoacetyl)oxy]propanoic acid + CROSSLNK Glycyl serine ester (Gly-Ser) (interchain with S-...) + CROSSLNK Glycyl serine ester (Ser-Gly) (interchain with G-...) + O-(glycyl)-L-serine + O3-(aminoacetyl)serine + serine glycinate ester + PSI-MOD + MOD:01585 + Cross-link 2. + O-glycyl-L-serine + + + + + A protein modification that effectively crosslinks an L-serine residue and a glycine residue by an ester bond to form O-glycyl-L-serine. + PubMed:17502423 + RESID:AA0495 + + + + + (2S)-2-amino-3-[(aminoacetyl)oxy]propanoic acid + + + + + + CROSSLNK Glycyl serine ester (Gly-Ser) (interchain with S-...) + + + + + + CROSSLNK Glycyl serine ester (Ser-Gly) (interchain with G-...) + + + + + + O-(glycyl)-L-serine + + + + + + O3-(aminoacetyl)serine + + + + + + serine glycinate ester + + + + + + + + + + + + + A protein modification that effectively crosslinks an L-threonine residue and a glycine residue by an ester bond to form O-glycyl-L-threonine. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 6 H 9 N 2 O 3 + 157.15 + 157.06131 + G, T + natural + C-term + uniprot.ptm:PTM-0423 + (2S,3R)-2-amino-3-[(aminoacetyl)oxy]butanoic acid + CROSSLNK Glycyl threonine ester (Gly-Thr) (interchain with T-...) + CROSSLNK Glycyl threonine ester (Thr-Gly) (interchain with G-...) + O-(glycyl)-L-threonine + O3-(2-aminoacetyl)threonine + threonine glycinate ester + PSI-MOD + MOD:01586 + Cross-link 2. + O-glycyl-L-threonine + + + + + A protein modification that effectively crosslinks an L-threonine residue and a glycine residue by an ester bond to form O-glycyl-L-threonine. + PubMed:17502423 + RESID:AA0496 + + + + + (2S,3R)-2-amino-3-[(aminoacetyl)oxy]butanoic acid + + + + + + CROSSLNK Glycyl threonine ester (Gly-Thr) (interchain with T-...) + + + + + + CROSSLNK Glycyl threonine ester (Thr-Gly) (interchain with G-...) + + + + + + O-(glycyl)-L-threonine + + + + + + O3-(2-aminoacetyl)threonine + + + + + + threonine glycinate ester + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-(2-aminoethylphosphoryl)-L-serine. + 123.05 + C 2 H 6 N 1 O 3 P 1 + 123.00853 + C 5 H 11 N 2 O 5 P 1 + 210.13 + 210.04056 + S + natural + uniprot.ptm:PTM-0399 + (2S)-2-amino-3-([(2-aminoethoxy)(hydroxy)phosphoryl]oxy)propanoic acid + MOD_RES O-(2-aminoethylphosphoryl)serine + O-(2-aminoethylphosphoryl)-L-serine + O3-(2-aminoethylphosphoryl)-L-serine + O3-(phosphoethanolamine)-L-serine + serine ethanolamine phosphate + serine ethanolamine phosphodiester + PSI-MOD + MOD:01587 + O-(2-aminoethylphosphoryl)-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-(2-aminoethylphosphoryl)-L-serine. + PubMed:15249686 + PubMed:16825186 + PubMed:16949362 + RESID:AA0497 + + + + + (2S)-2-amino-3-([(2-aminoethoxy)(hydroxy)phosphoryl]oxy)propanoic acid + + + + + + MOD_RES O-(2-aminoethylphosphoryl)serine + + + + + + O-(2-aminoethylphosphoryl)-L-serine + + + + + + O3-(2-aminoethylphosphoryl)-L-serine + + + + + + O3-(phosphoethanolamine)-L-serine + + + + + + serine ethanolamine phosphate + + + + + + serine ethanolamine phosphodiester + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-cholinephosphoryl-L-serine. + 166.14 + C 5 H 13 N 1 O 3 P 1 + 166.06276 + 1+ + C 8 H 18 N 2 O 5 P 1 + 253.21 + 253.09479 + S + natural + uniprot.ptm:PTM-0400 + 2-[([(2S)-2-amino-2-carboxyethoxy][hydroxy]phosphoryl)oxy]-N,N,N-trimethylethanaminium + 2-[([(2S)-2-azanyl-2-carboxyethoxy][hydroxy]phosphoryl)oxy]-N,N,N-trimethylethanazanium + MOD_RES O-(2-cholinephosphoryl)serine + O-cholinephosphoryl-L-serine + O3-[(2-[trimethylammonio]ethyl)phosphoryl]-L-serine + O3-phosphocholine-L-serine + serine choline phosphate + serine choline phosphodiester + PSI-MOD + MOD:01588 + O-cholinephosphoryl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-cholinephosphoryl-L-serine. + PubMed:15249686 + PubMed:16825186 + PubMed:16949362 + RESID:AA0498 + + + + + 2-[([(2S)-2-amino-2-carboxyethoxy][hydroxy]phosphoryl)oxy]-N,N,N-trimethylethanaminium + + + + + + 2-[([(2S)-2-azanyl-2-carboxyethoxy][hydroxy]phosphoryl)oxy]-N,N,N-trimethylethanazanium + + + + + + MOD_RES O-(2-cholinephosphoryl)serine + + + + + + O-cholinephosphoryl-L-serine + + + + + + O3-[(2-[trimethylammonio]ethyl)phosphoryl]-L-serine + + + + + + O3-phosphocholine-L-serine + + + + + + serine choline phosphate + + + + + + serine choline phosphodiester + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-(2,4-diacetamido-2,4-dideoxyglucosyl)-L-serine. + 244.25 + C 10 H 16 N 2 O 5 + 244.10593 + C 13 H 21 N 3 O 7 + 331.33 + 331.13794 + S + natural + uniprot.ptm:PTM-0547 + (2S)-2-amino-3-[(2,4-diacetamido-2,4-dideoxy-beta-D-glucopyranosyl)oxy]propanoic acid + CARBOHYD O-linked (DADDGlc) serine + DADDGlc + O-(2,4-diacetamido-2,4-dideoxy-D-glucosyl)-L-serine + O-(2,4-diacetamido-2,4-dideoxy-beta-D-glucopyranosyl)-L-serine + O-[2,4-bis(acetylamino)]glucosyl-L-serine + O-seryl-beta-2,4-bis(acetylamino)glucoside + O3-(2,4-diacetamido-2,4-dideoxy-beta-D-glucopyranosyl)-L-serine + PSI-MOD + MOD:01589 + O-(2,4-diacetamido-2,4-dideoxyglucosyl)-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-(2,4-diacetamido-2,4-dideoxyglucosyl)-L-serine. + PubMed:15249686 + PubMed:16949362 + RESID:AA0499 + + + + + (2S)-2-amino-3-[(2,4-diacetamido-2,4-dideoxy-beta-D-glucopyranosyl)oxy]propanoic acid + + + + + + CARBOHYD O-linked (DADDGlc) serine + + + + + + DADDGlc + + + + + + O-(2,4-diacetamido-2,4-dideoxy-D-glucosyl)-L-serine + + + + + + O-(2,4-diacetamido-2,4-dideoxy-beta-D-glucopyranosyl)-L-serine + + + + + + O-[2,4-bis(acetylamino)]glucosyl-L-serine + + + + + + O-seryl-beta-2,4-bis(acetylamino)glucoside + + + + + + O3-(2,4-diacetamido-2,4-dideoxy-beta-D-glucopyranosyl)-L-serine + + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to 3'-farnesyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan. + 204.36 + C 15 H 24 N 0 O 0 + 204.1878 + C 26 H 34 N 2 O 1 + 390.57 + 390.26712 + W + natural + (2S,3aR,8aS)-3a-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid + 3'-farnesyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan + LIPID 3'-farnesyl-2',N2-cyclotryptophan + PSI-MOD + MOD:01590 + 3'-farnesyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to 3'-farnesyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan. + ChEBI:52950 + PubMed:18323630 + RESID:AA0500 + + + + + (2S,3aR,8aS)-3a-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid + + + + + + 3'-farnesyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan + + + + + + LIPID 3'-farnesyl-2',N2-cyclotryptophan + + + + + + + + + + + Modifications that have monoisotopic mass differences from their respective origins of 304.205359 Da. + PSI-MOD + MOD:01591 + + modifications with monoisotopic mass differences that are nominally equal at 304.205359 Da + + + + + Modifications that have monoisotopic mass differences from their respective origins of 304.205359 Da. + PubMed:18688235 + + + + + + + + + Modifications that have monoisotopic mass differences from their respective origins of 304.199-304.206 Da. + PSI-MOD + MOD:01592 + + modifications with monoisotopic mass differences that are nominally equal at 304.199-304.206 Da + + + + + Modifications that have monoisotopic mass differences from their respective origins of 304.199-304.206 Da. + PubMed:18688235 + + + + + + + + + A protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex reagent derivatized residue. + 4-methyl-1-methylidenepiperazin-1-ium + PSI-MOD + MOD:01593 + + iTRAQ8plex reporter fragment + + + + + A protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex reagent derivatized residue. + PubMed:18688235 + + + + + 4-methyl-1-methylidenepiperazin-1-ium + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-113 reagent derivatized residue. + 1+ + (12)C 6 H 13 (14)N 2 + 113.11 + 113.10732 + X + artifact + 4-methyl-1-methylidenepiperazin-1-ium + PSI-MOD + MOD:01594 + + iTRAQ8plex-113 reporter fragment + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-113 reagent derivatized residue. + PubMed:18688235 + + + + + 4-methyl-1-methylidenepiperazin-1-ium + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-114 reagent derivatized residue. + 1+ + (12)C 5 (13)C 1 H 13 (14)N 2 + 114.11 + 114.11068 + X + artifact + 4-methyl-1-methylidenepiperazin-1-ium + PSI-MOD + MOD:01595 + + iTRAQ8plex-114 reporter fragment + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-114 reagent derivatized residue. + PubMed:18688235 + + + + + 4-methyl-1-methylidenepiperazin-1-ium + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-115 reagent derivatized residue. + 1+ + (12)C 5 (13)C 1 H 13 (14)N 1 (15)N 1 + 115.11 + 115.10771 + X + artifact + 4-methyl-1-methylidenepiperazin-1-ium + PSI-MOD + MOD:01596 + + iTRAQ8plex-115 reporter fragment + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-115 reagent derivatized residue. + PubMed:18688235 + + + + + 4-methyl-1-methylidenepiperazin-1-ium + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-116 reagent derivatized residue. + 1+ + (12)C 4 (13)C 2 H 13 (14)N 1 (15)N 1 + 116.11 + 116.11107 + X + artifact + 4-methyl-1-methylidenepiperazin-1-ium + PSI-MOD + MOD:01597 + + iTRAQ8plex-116 reporter fragment + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-116 reagent derivatized residue. + PubMed:18688235 + + + + + 4-methyl-1-methylidenepiperazin-1-ium + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-117 reagent derivatized residue. + 1+ + (12)C 3 (13)C 3 H 13 (14)N 1 (15)N 1 + 117.11 + 117.114426 + X + artifact + 4-methyl-1-methylidenepiperazin-1-ium + PSI-MOD + MOD:01598 + + iTRAQ8plex-117 reporter fragment + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-117 reagent derivatized residue. + PubMed:18688235 + + + + + 4-methyl-1-methylidenepiperazin-1-ium + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-118 reagent derivatized residue. + 1+ + (12)C 3 (13)C 3 H 13 (15)N 2 + 118.11 + 118.11146 + X + artifact + 4-methyl-1-methylidenepiperazin-1-ium + PSI-MOD + MOD:01599 + + iTRAQ8plex-118 reporter fragment + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-118 reagent derivatized residue. + PubMed:18688235 + + + + + 4-methyl-1-methylidenepiperazin-1-ium + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-119 reagent derivatized residue. + 1+ + (12)C 2 (13)C 4 H 13 (15)N 2 + 119.11 + 119.114815 + X + artifact + 4-methyl-1-methylidenepiperazin-1-ium + PSI-MOD + MOD:01600 + + iTRAQ8plex-119 reporter fragment + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-119 reagent derivatized residue. + PubMed:18688235 + + + + + 4-methyl-1-methylidenepiperazin-1-ium + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-121 reagent derivatized residue. + 1+ + (13)C 6 H 13 (15)N 2 + 121.12 + 121.12152 + X + artifact + 4-methyl-1-methylidenepiperazin-1-ium + PSI-MOD + MOD:01601 + + iTRAQ8plex-121 reporter fragment + + + + + The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-121 reagent derivatized residue. + PubMed:18688235 + + + + + 4-methyl-1-methylidenepiperazin-1-ium + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue, and an L-methionine residue to S-(L-lysyl)-L-methionine sulfilimine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 11 H 19 N 3 O 2 S 1 + 257.35 + 257.1198 + K, M + natural + uniprot.ptm:PTM-0401 + (2S)-2-amino-6-([(E)-[(3S)-3-amino-3-carboxypropyl](methyl)-lambda(4)-sulfanylidene]amino)hexanoic acid + (E)-N6-([(3S)-3-amino-3-carboxypropyl](methyl)-lambda(4)-sulfanylidene)-L-lysine + S-(L-lysyl)-L-methionine sulfilimine + S-lysyl-methionine + PSI-MOD + MOD:01602 + Cross-link 2. + S-(L-lysyl)-L-methionine sulfilimine + + + + + A protein modification that effectively converts an L-lysine residue, and an L-methionine residue to S-(L-lysyl)-L-methionine sulfilimine. + PubMed:12011424 + PubMed:15951440 + PubMed:19729652 + RESID:AA0501 + + + + + (2S)-2-amino-6-([(E)-[(3S)-3-amino-3-carboxypropyl](methyl)-lambda(4)-sulfanylidene]amino)hexanoic acid + + + + + + (E)-N6-([(3S)-3-amino-3-carboxypropyl](methyl)-lambda(4)-sulfanylidene)-L-lysine + + + + + + S-(L-lysyl)-L-methionine sulfilimine + + + + + + S-lysyl-methionine + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 2x(15)N labeled L-lysine. + 1.99 + (14)N -2 (15)N 2 + 1.99407 + C 6 H 12 (15)N 2 O 1 + 130.09 + 130.08904 + K + artifact + Unimod:995 + PSI-MOD + MOD:01603 + + 2x(15)N labeled L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to 2x(15)N labeled L-lysine. + PubMed:18688235 + URL:http://www.sigmaaldrich.com/catalog/ProductDetail.do?N4=609021|ALDRICH&N5=SEARCH_CONCAT_PNO|BRAND_KEY&F=SPEC&lang=en_US0.000000E+000 + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to 4x(15)N labeled L-arginine. + 3.99 + (14)N -4 (15)N 4 + 3.98814 + C 6 H 12 (15)N 4 O 1 + 160.09 + 160.08925 + R + artifact + PSI-MOD + MOD:01604 + + 4x(15)N labeled L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to 4x(15)N labeled L-arginine. + PubMed:18688235 + URL:http://www.sigmaaldrich.com/catalog/ProductDetail.do?N4=600113|ALDRICH&N5=SEARCH_CONCAT_PNO|BRAND_KEY&F=SPEC&lang=en_US0.000000E+000 + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl 2-aminoadipic acid. + 143.14 + C 6 H 9 N 1 O 3 + 143.05824 + C 11 H 16 N 2 O 6 + 272.26 + 272.10083 + E + natural + uniprot.ptm:PTM-0406 + (2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanedioic acid + 5-glutamyl 2-aminoadipic acid + MOD_RES 5-glutamyl 2-aminoadipic acid + N2-(gamma-glutamyl)-2-aminoadipic acid + N2-(isoglutamyl)-2-aminoadipic acid + PSI-MOD + MOD:01605 + 5-glutamyl 2-aminoadipic acid + + + + + A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl 2-aminoadipic acid. + ChEBI:78503 + PubMed:19620981 + RESID:AA0502 + + + + + (2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanedioic acid + + + + + + 5-glutamyl 2-aminoadipic acid + + + + + + MOD_RES 5-glutamyl 2-aminoadipic acid + + + + + + N2-(gamma-glutamyl)-2-aminoadipic acid + + + + + + N2-(isoglutamyl)-2-aminoadipic acid + + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl 2-aminoadipic 6-phosphoric anhydride. + 223.12 + C 6 H 10 N 1 O 6 P 1 + 223.02457 + C 11 H 17 N 2 O 9 P 1 + 352.24 + 352.06717 + E + hypothetical + (2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)-6-oxo-6-(phosphonooxy)hexanoic acid + 5-glutamyl 2-aminoadipic 6-phosphoric anhydride + PSI-MOD + MOD:01606 + 5-glutamyl 2-aminoadipic 6-phosphoric anhydride + + + + + A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl 2-aminoadipic 6-phosphoric anhydride. + PubMed:19620981 + RESID:AA0503 + + + + + (2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)-6-oxo-6-(phosphonooxy)hexanoic acid + + + + + + 5-glutamyl 2-aminoadipic 6-phosphoric anhydride + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl allysine. + 127.14 + C 6 H 9 N 1 O 2 + 127.06333 + C 11 H 16 N 2 O 5 + 256.26 + 256.10593 + E + hypothetical + (2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)-6-oxohexanoic acid + 2-(5-glutamyl)amino-6-oxohexanoic acid + 5-glutamyl allysine + N2-(gamma-glutamyl)allysine + N2-(isoglutamyl)allysine + alpha-(gamma-glutamyl)allysine + PSI-MOD + MOD:01607 + 5-glutamyl allysine + + + + + A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl allysine. + PubMed:19620981 + RESID:AA0504 + + + + + (2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)-6-oxohexanoic acid + + + + + + 2-(5-glutamyl)amino-6-oxohexanoic acid + + + + + + 5-glutamyl allysine + + + + + + N2-(gamma-glutamyl)allysine + + + + + + N2-(isoglutamyl)allysine + + + + + + alpha-(gamma-glutamyl)allysine + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to N2-(L-isoglutamyl)-L-lysine. This is not an isopeptide cross-link. + 128.18 + C 6 H 12 N 2 O 1 + 128.09496 + C 11 H 19 N 3 O 4 + 257.29 + 257.13754 + E + natural + uniprot.ptm:PTM-0407 + (2S)-6-amino-2-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid + 5-glutamyl N2-lysine + MOD_RES 5-glutamyl N2-lysine + N2-(L-isoglutamyl)-L-lysine + N2-(gamma-glutamyl)lysine + alpha-(gamma-glutamyl)lysine + gamma-glutamyl N2-lysine + PSI-MOD + MOD:01608 + N2-(L-isoglutamyl)-L-lysine + + + + + A protein modification that effectively converts an L-glutamic acid residue to N2-(L-isoglutamyl)-L-lysine. This is not an isopeptide cross-link. + PubMed:19620981 + RESID:AA0505 + + + + + (2S)-6-amino-2-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid + + + + + + 5-glutamyl N2-lysine + + + + + + MOD_RES 5-glutamyl N2-lysine + + + + + + N2-(L-isoglutamyl)-L-lysine + + + + + + N2-(gamma-glutamyl)lysine + + + + + + alpha-(gamma-glutamyl)lysine + + + + + + gamma-glutamyl N2-lysine + + + + + + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to 7'-hydroxy-2'-alpha-mannosyl-L-tryptophan. + 178.14 + C 6 H 10 N 0 O 6 + 178.04774 + C 17 H 20 N 2 O 7 + 364.35 + 364.12704 + W + natural + uniprot.ptm:PTM-0504 + (2S)-2-amino-3-[7-hydroxy-2-(alpha-D-mannopyranosyl)-1H-indol-3-yl]propanoic acid + 7'-hydroxy-2'-alpha-mannosyl-L-tryptophan + CARBOHYD C-linked (Man) hydroxytryptophan + PSI-MOD + MOD:01609 + 7'-hydroxy-2'-alpha-mannosyl-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to 7'-hydroxy-2'-alpha-mannosyl-L-tryptophan. + PubMed:19584055 + RESID:AA0506 + + + + + (2S)-2-amino-3-[7-hydroxy-2-(alpha-D-mannopyranosyl)-1H-indol-3-yl]propanoic acid + + + + + + 7'-hydroxy-2'-alpha-mannosyl-L-tryptophan + + + + + + CARBOHYD C-linked (Man) hydroxytryptophan + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to L-threonine methyl ester. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 5 H 10 N 1 O 3 + 132.14 + 132.06607 + T + natural + C-term + uniprot.ptm:PTM-0412 + L-threonine methyl ester + MOD_RES Threonine methyl ester + methyl (2S,3R)-2-amino-3-hydroxybutanoate + methyl L-threoninate + PSI-MOD + MOD:01610 + L-threonine methyl ester + + + + + A protein modification that effectively converts an L-threonine residue to L-threonine methyl ester. + PubMed:19745839 + RESID:AA0507 + + + + + L-threonine methyl ester + + + + + + MOD_RES Threonine methyl ester + + + + + + methyl (2S,3R)-2-amino-3-hydroxybutanoate + + + + + + methyl L-threoninate + + + + + + + + + + + + A protein modification that crosslinks a cysteine and a histidine residue by forming the adduct 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FMN. + 452.32 + C 17 H 17 N 4 O 9 P 1 S 0 + 452.0733 + C 26 H 29 N 8 O 11 P 1 S 1 + 692.6 + 692.1414 + C, H + natural + 6-((R)-2-amino-2-carboxyethyl)sulfanyl-8alpha-[4-((S)-2-amino-2-carboxyethyl)imidazol-3-yl]-riboflavin 5'-trihydrogen phosphate + 6-(S-L-cysteinyl)-8alpha-(N3'-L-histidino)-FMN + 6-(S-cysteinyl)-8alpha-(N(delta)-histidyl)-FMN + 6-(S-cysteinyl)-8alpha-(N(pi)-histidyl)-FMN + 6-(S-cysteinyl)-8alpha-(N3'-histidyl)-FMN + 6-(S-cysteinyl)-8alpha-(pros-histidyl)-FMN + BINDING FMN (covalent; via 2 links) + BINDING FMN (covalent; via 2 links, pros nitrogen) + PSI-MOD + MOD:01611 + + Cross-link 2. + 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FMN + + + + + A protein modification that crosslinks a cysteine and a histidine residue by forming the adduct 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FMN. + PubMed:17935335 + RESID:AA0508 + + + + + 6-((R)-2-amino-2-carboxyethyl)sulfanyl-8alpha-[4-((S)-2-amino-2-carboxyethyl)imidazol-3-yl]-riboflavin 5'-trihydrogen phosphate + + + + + + 6-(S-L-cysteinyl)-8alpha-(N3'-L-histidino)-FMN + + + + + + 6-(S-cysteinyl)-8alpha-(N(delta)-histidyl)-FMN + + + + + + 6-(S-cysteinyl)-8alpha-(N(pi)-histidyl)-FMN + + + + + + 6-(S-cysteinyl)-8alpha-(N3'-histidyl)-FMN + + + + + + 6-(S-cysteinyl)-8alpha-(pros-histidyl)-FMN + + + + + + BINDING FMN (covalent; via 2 links) + + + + + + BINDING FMN (covalent; via 2 links, pros nitrogen) + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to 3'-iodo-L-tyrosine. + 125.9 + C 0 H -1 I 1 N 0 O 0 + 125.896645 + C 9 H 8 I 1 N 1 O 2 + 289.07 + 288.95996 + Y + natural + uniprot.ptm:PTM-0411 + (2S)-2-amino-3-(4-hydroxy-3-iodophenyl)propanoic acid + 3'-iodo-L-tyrosine + 3-iodo-L-tyrosine + 3-iodotyrosine + 4-hydroxy-3-iodo-phenylalanine + MIT + MOD_RES Iodotyrosine + PSI-MOD + MOD:01612 + + 3'-iodo-L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to 3'-iodo-L-tyrosine. + ChEBI:27847 + PubMed:8995307 + RESID:AA0509 + + + + + (2S)-2-amino-3-(4-hydroxy-3-iodophenyl)propanoic acid + + + + + + 3'-iodo-L-tyrosine + + + + + + 3-iodo-L-tyrosine + + + + + + 3-iodotyrosine + + + + + + 4-hydroxy-3-iodo-phenylalanine + + + + + + MIT + + + + + + MOD_RES Iodotyrosine + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to 3',5'-diiodo-L-tyrosine. + 251.79 + C 0 H -2 I 2 N 0 O 0 + 251.79329 + C 9 H 7 I 2 N 1 O 2 + 414.97 + 414.85663 + Y + natural + uniprot.ptm:PTM-0408 + (2S)-2-amino-3-(4-hydroxy-3,5-diiodophenyl)propanoic acid + 3',5'-diiodo-L-tyrosine + 3,5-diiodo-L-tyrosine + 3,5-diiodotyrosine + DIT + MOD_RES Diiodotyrosine + iodogorgoic acid + PSI-MOD + MOD:01613 + + 3',5'-diiodo-L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to 3',5'-diiodo-L-tyrosine. + ChEBI:15768 + PubMed:8995307 + RESID:AA0510 + + + + + (2S)-2-amino-3-(4-hydroxy-3,5-diiodophenyl)propanoic acid + + + + + + 3',5'-diiodo-L-tyrosine + + + + + + 3,5-diiodo-L-tyrosine + + + + + + 3,5-diiodotyrosine + + + + + + DIT + + + + + + MOD_RES Diiodotyrosine + + + + + + iodogorgoic acid + + + + + + + + + + + A protein modification that effectively converts a glycine residue to glycyl phospho-5'-adenosine. + 329.21 + C 10 H 12 N 5 O 6 P 1 + 329.05252 + C 12 H 16 N 6 O 8 P 1 + 403.27 + 403.07672 + G + natural + C-term + uniprot.ptm:PTM-0409 + (2-aminoacetyl)oxy-([(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy)phosphinic acid + ([(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl)-2-aminoethanoate + 5'-adenylic-glyinate + MOD_RES Glycyl adenylate + aminoacetyl [5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl hydrogen phosphate + glycine monoanhydride with 5'-adenylic acid + glycyl 5'-adenylate + glycyl adenosine-5'-phosphate + glycyl phospho-5'-adenosine + glycyladenylate + PSI-MOD + MOD:01614 + glycyl phospho-5'-adenosine + + + + + A protein modification that effectively converts a glycine residue to glycyl phospho-5'-adenosine. + PubMed:16388576 + PubMed:9632726 + RESID:AA0511 + + + + + (2-aminoacetyl)oxy-([(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy)phosphinic acid + + + + + + ([(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl)-2-aminoethanoate + + + + + + 5'-adenylic-glyinate + + + + + + MOD_RES Glycyl adenylate + + + + + + aminoacetyl [5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl hydrogen phosphate + + + + + + glycine monoanhydride with 5'-adenylic acid + + + + + + glycyl 5'-adenylate + + + + + + glycyl adenosine-5'-phosphate + + + + + + glycyl phospho-5'-adenosine + + + + + + glycyladenylate + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a dithioester bond to form glycyl cysteine dithioester. + 14.05 + C 0 H -2 N 0 O -1 S 1 + 13.961506 + C 5 H 7 N 2 O 2 S 2 + 191.24 + 190.99489 + C, G + hypothetical + C-term + uniprot.ptm:PTM-0410 + (2R)-2-amino-3-[(aminoacetyl)disulfanyl]propanoic acid + 2-(glycyldithio)alanine + S-glycyl cysteine persulfide + S-glycyl thiocysteine + glycyl cysteine dithioester + thioglycine cysteine disulfide + PSI-MOD + MOD:01615 + Cross-link 2. + glycyl cysteine dithioester + + + + + A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a dithioester bond to form glycyl cysteine dithioester. + PubMed:11438688 + PubMed:16388576 + RESID:AA0512 + + + + + (2R)-2-amino-3-[(aminoacetyl)disulfanyl]propanoic acid + + + + + + 2-(glycyldithio)alanine + + + + + + S-glycyl cysteine persulfide + + + + + + S-glycyl thiocysteine + + + + + + glycyl cysteine dithioester + + + + + + thioglycine cysteine disulfide + + + + + + + + + + A protein modification that effectively cross-links two L-cysteine residues and adds three sulfur atoms to form trithiocystine. + 94.16 + C 0 H -2 N 0 O 0 S 3 + 93.900566 + C 6 H 8 N 2 O 2 S 5 + 300.44 + 299.91895 + C, C + natural + uniprot.ptm:PTM-0417 + (2R,2'R)-3,3'-pentasulfane-1,5-diylbis(2-aminopropanoic acid) + 3,3'-pentathiobisalanine + bis(2-amino-2-carboxyethyl)pentasulfide + trithiocystine + PSI-MOD + MOD:01616 + Cross-link 2. + trithiocystine + + + + + A protein modification that effectively cross-links two L-cysteine residues and adds three sulfur atoms to form trithiocystine. + PubMed:19438211 + RESID:AA0513 + + + + + (2R,2'R)-3,3'-pentasulfane-1,5-diylbis(2-aminopropanoic acid) + + + + + + 3,3'-pentathiobisalanine + + + + + + bis(2-amino-2-carboxyethyl)pentasulfide + + + + + + trithiocystine + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-(6-phosphomannosyl)-L-threonine. + 242.12 + C 6 H 11 N 0 O 8 P 1 + 242.01915 + C 10 H 18 N 1 O 10 P 1 + 343.22 + 343.06683 + T + natural + uniprot.ptm:PTM-0596 + (2S,3R)-2-amino-3-[6-phosphonooxy-alpha-D-mannopyranosyloxy]butanoic acid + CARBOHYD O-linked (Man6P) threonine + O-(6-phosphomannosyl)-L-threonine + O3-(6-phosphomannosyl)threonine + PSI-MOD + MOD:01617 + O-(6-phosphomannosyl)-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-(6-phosphomannosyl)-L-threonine. + PubMed:20044576 + RESID:AA0514 + + + + + (2S,3R)-2-amino-3-[6-phosphonooxy-alpha-D-mannopyranosyloxy]butanoic acid + + + + + + CARBOHYD O-linked (Man6P) threonine + + + + + + O-(6-phosphomannosyl)-L-threonine + + + + + + O3-(6-phosphomannosyl)threonine + + + + + + + + + + + + + A protein modification that effectively converts an L-alaine residue and an L-asparagine residue to L-alanyl-L-isoaspartyl cyclopeptide. + -17.03 + C 0 H -3 N -1 O 0 + -17.026548 + C 7 H 9 N 2 O 3 + 169.16 + 169.06131 + A, N + natural + N-term + uniprot.ptm:PTM-0418 + (2S,5S)-2-methyl-3,7-dioxo-1,4-diazepane-5-carboxylic acid + 1,4.2-anhydro(L-alanyl-L-aspartic acid) + CROSSLNK Alanine isoaspartyl cyclopeptide (Ala-Asn) + L-alanyl-L-isoaspartyl cyclopeptide + PSI-MOD + MOD:01618 + Cross-link 2. + L-alanyl-L-isoaspartyl cyclopeptide + + + + + A protein modification that effectively converts an L-alaine residue and an L-asparagine residue to L-alanyl-L-isoaspartyl cyclopeptide. + PubMed:19928958 + PubMed:3207697 + RESID:AA0515 + + + + + (2S,5S)-2-methyl-3,7-dioxo-1,4-diazepane-5-carboxylic acid + + + + + + 1,4.2-anhydro(L-alanyl-L-aspartic acid) + + + + + + CROSSLNK Alanine isoaspartyl cyclopeptide (Ala-Asn) + + + + + + L-alanyl-L-isoaspartyl cyclopeptide + + + + + + + + + + + A protein modification that crosslinks two cysteine residues by formation of a chain of two or more bonded sulfur atoms. + PSI-MOD + MOD:01619 + + multisulfide crosslinked residues + + + + + A protein modification that crosslinks two cysteine residues by formation of a chain of two or more bonded sulfur atoms. + PubMed:18688235 + + + + + + + + + + A protein modification that crosslinks two cysteine residues by formation of a chain of three or more bonded sulfur atoms. + PSI-MOD + MOD:01620 + polysulfide crosslinked residues + + + + + A protein modification that crosslinks two cysteine residues by formation of a chain of three or more bonded sulfur atoms. + PubMed:18688235 + + + + + + + + + + A protein modification that crosslinks two or more amino acid residues by forming an adduct with a compound containing a flavin group. + PSI-MOD + MOD:01621 + + flavin crosslinked residues + + + + + A protein modification that crosslinks two or more amino acid residues by forming an adduct with a compound containing a flavin group. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to one of several monohydroxylated tryptophan residues, including 3-hydroxy-L-tryptophan and 7'-hydroxy-L-tryptophan. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 11 H 10 N 2 O 2 + 202.21 + 202.07423 + W + natural + Unimod:35 + oxyw + PSI-MOD + Oxidation + MOD:01622 + monohydroxylated tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to one of several monohydroxylated tryptophan residues, including 3-hydroxy-L-tryptophan and 7'-hydroxy-L-tryptophan. + OMSSA:90 + Unimod:35#W + + + + + oxyw + + + + + + Oxidation + + + + + + + + + + A protein modification that effectively converts a glycine residue to a C-terminal 1-thioglycine. + 16.06 + C 0 H 0 N 0 O -1 S 1 + 15.977156 + C 2 H 3 N 1 S 1 + 73.11 + 72.99862 + G + natural + C-term + PSI-MOD + MOD:01623 + + 1-thioglycine (C-terminal) + + + + + A protein modification that effectively converts a glycine residue to a C-terminal 1-thioglycine. + PubMed:11463785 + PubMed:19145231 + PubMed:9367957 + RESID:AA0265#var + + + + + + + + + + + A protein modification that crosslinks an asparagine and the following glycine residue with the formation of (2-aminosuccinimidyl)acetic acid and the release of ammonia. + -17.03 + C 0 H -3 N -1 O 0 + -17.026548 + C 6 H 6 N 2 O 3 + 154.13 + 154.03784 + G, N + hypothetical + uniprot.ptm:PTM-0450 + (2-aminosuccinimidyl)acetic acid + (3-amino-2,5-dioxo-1-pyrrolidinyl)acetic acid + CROSSLNK (2-aminosuccinimidyl)acetic acid (Asn-Gly) + N-(2-aminosuccinyl)glycine + [(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]acetic acid + anhydroaspartyl glycine + aspartimide glycine + PSI-MOD + MOD:01624 + + Cross-link 2. + (2-aminosuccinimidyl)acetic acid (Asn) + + + + + A protein modification that crosslinks an asparagine and the following glycine residue with the formation of (2-aminosuccinimidyl)acetic acid and the release of ammonia. + PubMed:10801322 + PubMed:2015294 + RESID:AA0441#ASN + + + + + (2-aminosuccinimidyl)acetic acid + + + + + + (3-amino-2,5-dioxo-1-pyrrolidinyl)acetic acid + + + + + + CROSSLNK (2-aminosuccinimidyl)acetic acid (Asn-Gly) + + + + + + N-(2-aminosuccinyl)glycine + + + + + + [(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]acetic acid + + + + + + anhydroaspartyl glycine + + + + + + aspartimide glycine + + + + + + + + + + + A protein modification that effectively converts a glycine residue to 1-thioglycine. + 16.06 + C 0 H 0 N 0 O -1 S 1 + 15.977156 + G + natural + 1-thioglycine + 2-amino-1-sulfanylethanone + MOD_RES 1-thioglycine + S(O)Gly + aminoethanethioic acid + aminothioacetic acid + PSI-MOD + Carboxy->Thiocarboxy + thiocarboxylic acid + MOD:01625 + + This modification occurs naturally in two forms. At an interior peptide location (MOD:00270) it exists as aminoethanethionic acid, or aminoethanethioic O-acid. At the C-terminal (MOD:01623) it exists as aminoethanethiolic acid, or aminoethanethioic S-acid [JSG]. + 1-thioglycine + + + + + A protein modification that effectively converts a glycine residue to 1-thioglycine. + PubMed:11463785 + PubMed:9367957 + RESID:AA0265 + + + + + 1-thioglycine + + + + + + 2-amino-1-sulfanylethanone + + + + + + MOD_RES 1-thioglycine + + + + + + S(O)Gly + + + + + + aminoethanethioic acid + + + + + + aminothioacetic acid + + + + + + Carboxy->Thiocarboxy + + + + + + thiocarboxylic acid + + + + + + + + + + A protein modification that forms L-cystine by forming a disulfide bond that either cross-links two peptidyl L-cysteine residues, or modifies a peptidyl cysteine with a free cysteine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + natural + (2R,2'R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid) + 3,3'-disulfane-1,2-diylbis(2-azanylpropanoic acid) + 3,3'-dithiobis(2-aminopropanoic acid) + 3,3'-dithiobisalanine + 3,3'-dithiodialanine + Cys2 + Cystine ((Cys)2) + L-cystine + beta,beta'-diamino-beta,beta'-dicarboxydiethyldisulfide + beta,beta'-dithiodialanine + bis(alpha-aminopropionic acid)-beta-disulfide + bis(beta-amino-beta-carboxyethyl)disulfide + dicysteine + PSI-MOD + 2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid + MOD:01626 + + This modification occurs naturally in two forms. It exists as a disulfide cross-link of two cysteine residues (MOD:00034), or as a disulfide cross-link of a cysteine residues and a free cysteine (MOD:00765). + L-cystine + + + + + A protein modification that forms L-cystine by forming a disulfide bond that either cross-links two peptidyl L-cysteine residues, or modifies a peptidyl cysteine with a free cysteine. + ChEBI:16283 + PubMed:1988019 + PubMed:2001356 + PubMed:2076469 + PubMed:3083866 + PubMed:366603 + PubMed:7918467 + PubMed:8344916 + RESID:AA0025 + + + + + (2R,2'R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid) + + + + + + 3,3'-disulfane-1,2-diylbis(2-azanylpropanoic acid) + + + + + + 3,3'-dithiobis(2-aminopropanoic acid) + + + + + + 3,3'-dithiobisalanine + + + + + + 3,3'-dithiodialanine + + + + + + Cys2 + + + + + + Cystine ((Cys)2) + + + + + + L-cystine + + + + + + beta,beta'-diamino-beta,beta'-dicarboxydiethyldisulfide + + + + + + beta,beta'-dithiodialanine + + + + + + bis(alpha-aminopropionic acid)-beta-disulfide + + + + + + bis(beta-amino-beta-carboxyethyl)disulfide + + + + + + dicysteine + + + + + + 2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid + + + + + + + + + + + + A protein modification that forms L-cysteinyl-L-selenocysteine either by the natural process of cross-linking an L-cysteine residue and an L-selenocysteine residue, or by the hypothetical process of substituting a selenium for a sulfur atom in cystine. + C 6 H 8 N 2 O 2 S 1 Se 1 + 251.17 + 251.94717 + C, X + natural + PSI-MOD + MOD:01627 + + Cross-link 2. + L-cysteinyl-L-selenocysteine + + + + + A protein modification that forms L-cysteinyl-L-selenocysteine either by the natural process of cross-linking an L-cysteine residue and an L-selenocysteine residue, or by the hypothetical process of substituting a selenium for a sulfur atom in cystine. + PubMed:12911312 + PubMed:18688235 + + + + + + + + + + A protein modification that forms (2-aminosuccinimidyl)acetic acid by crosslinking either an aspartic acid residue or an asparagine residue with the following glycine residue. + C 6 H 6 N 2 O 3 + 154.13 + 154.03784 + G, X + hypothetical + PSI-MOD + MOD:01628 + + Cross-link 2; this cross-link is formed by the condensation of an aspartic acid residue or an asparagine residue with the alpha-amido of the following residue. + (2-aminosuccinimidyl)acetic acid + + + + + A protein modification that forms (2-aminosuccinimidyl)acetic acid by crosslinking either an aspartic acid residue or an asparagine residue with the following glycine residue. + PubMed:10801322 + PubMed:18688235 + + + + + + + + + + A protein modification that forms cyclo[(prolylserin)-O-yl] cysteinate by the natural process of cross-linking an L-cysteine residue an L-proline residue, and an L-serine residue, or by effectively modifying a cysteine residue. + C 11 H 16 N 3 O 4 S 1 + 286.33 + 286.08615 + X + natural + C-term + (3,6-dioxopyrrolo[4,5-a]piperazin-2-yl)methyl cysteinate + MOD_RES Cyclo[(prolylserin)-O-yl] cysteinate + [(3S,8aS)-1,4-dioxooctahydropyrrolo[1,2-a]pyrazin-3-yl]methyl (2R)-2-amino-3-sulfanylpropanoate + cyclo[(prolylserin)-O-yl] cysteinate + PSI-MOD + MOD:01629 + cyclo[(prolylserin)-O-yl] cysteinate + + + + + A protein modification that forms cyclo[(prolylserin)-O-yl] cysteinate by the natural process of cross-linking an L-cysteine residue an L-proline residue, and an L-serine residue, or by effectively modifying a cysteine residue. + PubMed:7961166 + RESID:AA0489 + + + + + (3,6-dioxopyrrolo[4,5-a]piperazin-2-yl)methyl cysteinate + + + + + + MOD_RES Cyclo[(prolylserin)-O-yl] cysteinate + + + + + + [(3S,8aS)-1,4-dioxooctahydropyrrolo[1,2-a]pyrazin-3-yl]methyl (2R)-2-amino-3-sulfanylpropanoate + + + + + + cyclo[(prolylserin)-O-yl] cysteinate + + + + + + + + + + + + + A protein modification that effectively crosslinks either an L-glutamine residue or an L-glutamic acid residue with an L-lysine residue by an isopeptide bond to form N6-(L-isoglutamyl)-L-lysine . + C 11 H 17 N 3 O 3 + 239.27 + 239.12698 + K, X + natural + uniprot.ptm:PTM-0397 + (2S)-2-amino-6-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid + 2-azanyl-6-([4-azanyl-4-carboxybutanoyl]azanyl)hexanoic acid + 5-glutamyl N6-lysine + N alpha -(gamma-Glutamyl)-lysine + N(epsilon)-(gamma-glutamyl)lysine + N6-(L-isoglutamyl)-L-lysine + PSI-MOD + MOD:01630 + + Cross-link 2. + N6-(L-isoglutamyl)-L-lysine + + + + + A protein modification that effectively crosslinks either an L-glutamine residue or an L-glutamic acid residue with an L-lysine residue by an isopeptide bond to form N6-(L-isoglutamyl)-L-lysine . + ChEBI:21863 + DeltaMass:0 + PubMed:2461365 + PubMed:5637041 + PubMed:5656070 + PubMed:8598899 + RESID:AA0124 + + + + + (2S)-2-amino-6-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid + + + + + + 2-azanyl-6-([4-azanyl-4-carboxybutanoyl]azanyl)hexanoic acid + + + + + + 5-glutamyl N6-lysine + + + + + + N alpha -(gamma-Glutamyl)-lysine + + + + + + N(epsilon)-(gamma-glutamyl)lysine + + + + + + N6-(L-isoglutamyl)-L-lysine + + + + + + + + + + + A protein modification that effectively removes or replaces an L-alanine. + -71.08 + C -3 H -5 N -1 O -1 + -71.03712 + A + natural + PSI-MOD + MOD:01631 + + This represents the loss or replacement of an L-alanine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-alanine removal + + + + + A protein modification that effectively removes or replaces an L-alanine. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces an L-arginine. + -156.19 + C -6 H -12 N -4 O -1 + -156.1011 + R + natural + PSI-MOD + MOD:01632 + + This represents the loss or replacement of an L-arginine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-arginine removal + + + + + A protein modification that effectively removes or replaces an L-arginine. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces an L-asparagine. + -114.1 + C -4 H -6 N -2 O -2 + -114.04293 + N + natural + PSI-MOD + MOD:01633 + + This represents the loss or replacement of an L-asparagine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-asparagine removal + + + + + A protein modification that effectively removes or replaces an L-asparagine. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces an L-aspartic acid. + -115.09 + C -4 H -5 N -1 O -3 + -115.02694 + D + natural + PSI-MOD + MOD:01634 + + This represents the loss or replacement of an L-aspartic acid residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-aspartic acid removal + + + + + A protein modification that effectively removes or replaces an L-aspartic acid. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces an L-cysteine. + -103.14 + C -3 H -5 N -1 O -1 S -1 + -103.009186 + C + natural + PSI-MOD + MOD:01635 + + This represents the loss or replacement of an L-cysteine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-cysteine removal + + + + + A protein modification that effectively removes or replaces an L-cysteine. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces an L-glutamic acid. + -129.12 + C -5 H -7 N -1 O -3 + -129.04259 + E + natural + PSI-MOD + MOD:01636 + + This represents the loss or replacement of an L-glutamic acid residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-glutamic acid removal + + + + + A protein modification that effectively removes or replaces an L-glutamic acid. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces an L-glutamine. + -128.13 + C -5 H -8 N -2 O -2 + -128.05858 + Q + natural + PSI-MOD + MOD:01637 + + This represents the loss or replacement of an L-glutamine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-glutamine removal + + + + + A protein modification that effectively removes or replaces an L-glutamine. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces a glycine. + -57.05 + C -2 H -3 N -1 O -1 + -57.021465 + G + natural + PSI-MOD + MOD:01638 + + This represents the loss or replacement of an glycine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + glycine removal + + + + + A protein modification that effectively removes or replaces a glycine. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces an L-histidine. + -137.14 + C -6 H -7 N -3 O -1 + -137.05891 + H + natural + PSI-MOD + MOD:01639 + + This represents the loss or replacement of an L-histidine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-histidine removal + + + + + A protein modification that effectively removes or replaces an L-histidine. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces an L-isoleucine. + -113.16 + C -6 H -11 N -1 O -1 + -113.08406 + I + natural + PSI-MOD + MOD:01640 + + This represents the loss or replacement of an L-isoleucine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-isoleucine removal + + + + + A protein modification that effectively removes or replaces an L-isoleucine. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces an L-leucine. + -113.16 + C -6 H -11 N -1 O -1 + -113.08406 + L + natural + PSI-MOD + MOD:01641 + + This represents the loss or replacement of an L-leucine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-leucine removal + + + + + A protein modification that effectively removes or replaces an L-leucine. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces an L-lysine. + -128.18 + C -6 H -12 N -2 O -1 + -128.09496 + K + natural + PSI-MOD + MOD:01642 + + This represents the loss or replacement of an L-lysine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-lysine removal + + + + + A protein modification that effectively removes or replaces an L-lysine. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces an L-methionine. + -131.19 + C -5 H -9 N -1 O -1 S -1 + -131.04048 + M + natural + Unimod:765 + ntermmcleave + PSI-MOD + Met-loss + MOD:01643 + + This represents the loss or replacement of an L-methionine residue in a polypeptide, including initiator methionine removal in eukaryotes. It may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution [JSG]. + L-methionine removal + + + + + A protein modification that effectively removes or replaces an L-methionine. + OMSSA:9 + PubMed:3327521 + Unimod:765 + + + + + ntermmcleave + + + + + + Met-loss + + + + + + + + + + + A protein modification that effectively removes or replaces an L-phenylalanine. + -147.18 + C -9 H -9 N -1 O -1 + -147.06842 + F + natural + PSI-MOD + MOD:01644 + + This represents the loss or replacement of an L-phenylalanine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-phenylalanine removal + + + + + A protein modification that effectively removes or replaces an L-phenylalanine. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces an L-proline. + -97.12 + C -5 H -7 N -1 O -1 + -97.052765 + P + natural + PSI-MOD + MOD:01645 + + This represents the loss or replacement of an L-proline residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-proline removal + + + + + A protein modification that effectively removes or replaces an L-proline. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces an L-serine. + -87.08 + C -3 H -5 N -1 O -2 + -87.03203 + S + natural + PSI-MOD + MOD:01646 + + This represents the loss or replacement of an L-serine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-serine removal + + + + + A protein modification that effectively removes or replaces an L-serine. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces an L-threonine. + -101.1 + C -4 H -7 N -1 O -2 + -101.047676 + T + natural + PSI-MOD + MOD:01647 + + This represents the loss or replacement of an L-threonine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-threonine removal + + + + + A protein modification that effectively removes or replaces an L-threonine. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces an L-tryptophan. + -186.21 + C -11 H -10 N -2 O -1 + -186.07932 + W + natural + PSI-MOD + MOD:01648 + + This represents the loss or replacement of an L-tryptophan residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-tryptophan removal + + + + + A protein modification that effectively removes or replaces an L-tryptophan. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces an L-tyrosine. + -163.18 + C -9 H -9 N -1 O -2 + -163.06332 + Y + natural + PSI-MOD + MOD:01649 + + This represents the loss or replacement of an L-tyrosine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-tyrosine removal + + + + + A protein modification that effectively removes or replaces an L-tyrosine. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes or replaces an L-valine. + -99.13 + C -5 H -9 N -1 O -1 + -99.06841 + V + natural + PSI-MOD + MOD:01650 + + This represents the loss or replacement of an L-valine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + L-valine removal + + + + + A protein modification that effectively removes or replaces an L-valine. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively removes a natural, standard, encoded residue. + X + natural + PSI-MOD + MOD:01651 + + This represents the loss of an encoded residue in a polypeptide. + natural, standard, encoded residue removal + + + + + A protein modification that effectively removes a natural, standard, encoded residue. + PubMed:18688235 + + + + + + + + + A protein modification that is produced by formation of an adduct with a sulfonyl halide compound used as a reagent. + X + artifact + PSI-MOD + MOD:01652 + These reagents typically react with N6-amino group of lysine residues and a free alpha-amino group of a peptide. + sulfonyl halide reagent derivatized residue + + + + + A protein modification that is produced by formation of an adduct with a sulfonyl halide compound used as a reagent. + PubMed:18688235 + + + + + + + + + A protein modification that is produced by formation of an adduct with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride. + 233.29 + C 12 H 11 N 1 O 2 S 1 + 233.05106 + X + artifact + Unimod:139 + Dansyl (Dns) + DansylRes + PSI-MOD + 5-dimethylaminonaphthalene-1-sulfonyl + Dansyl + MOD:01653 + dansyl chloride derivatized residue + + + + + A protein modification that is produced by formation of an adduct with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride. + DeltaMass:0 + Unimod:139 + + + + + Dansyl (Dns) + + + + + + DansylRes + + + + + + 5-dimethylaminonaphthalene-1-sulfonyl + + + + + + Dansyl + + + + + + + + + + + A protein modification that is produced by reaction with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride, to form N6-Dansyl-lysine. + 233.29 + C 12 H 11 N 1 O 2 S 1 + 233.05106 + C 18 H 23 N 3 O 3 S 1 + 361.46 + 361.14603 + K + artifact + Unimod:139 + N6DansylLys + PSI-MOD + 5-dimethylaminonaphthalene-1-sulfonyl + Dansyl + MOD:01654 + N6-Dansyl derivatized lysine + + + + + A protein modification that is produced by reaction with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride, to form N6-Dansyl-lysine. + Unimod:139#K + + + + + N6DansylLys + + + + + + 5-dimethylaminonaphthalene-1-sulfonyl + + + + + + Dansyl + + + + + + + + + + A protein modification that is produced by reaction with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride, to form an alpha-amino-Dansyl-derivatized residue. + 233.29 + C 12 H 11 N 1 O 2 S 1 + 233.05106 + X + artifact + Unimod:139 + N2DansylRes + PSI-MOD + 5-dimethylaminonaphthalene-1-sulfonyl + Dansyl + MOD:01655 + alpha-amino-Dansyl derivatized residue + + + + + A protein modification that is produced by reaction with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride, to form an alpha-amino-Dansyl-derivatized residue. + Unimod:139#N-term + + + + + N2DansylRes + + + + + + 5-dimethylaminonaphthalene-1-sulfonyl + + + + + + Dansyl + + + + + + + + + + A protein modification that is produced by formation of an adduct with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, Dabsyl chloride. + 287.34 + C 14 H 13 N 3 O 2 S 1 + 287.07285 + X + artifact + 4-([4-(dimethylamino)phenyl]diazenyl)benzenesulfonyl + DabsylRes + PSI-MOD + MOD:01656 + Dabsyl chloride derivatized residue + + + + + A protein modification that is produced by formation of an adduct with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, Dabsyl chloride. + PubMed:18688235 + + + + + 4-([4-(dimethylamino)phenyl]diazenyl)benzenesulfonyl + + + + + + DabsylRes + + + + + + + + + + + A protein modification that is produced by reaction with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, dabsyl chloride, to form N6-Dabsyl-lysine. + 287.34 + C 14 H 13 N 3 O 2 S 1 + 287.07285 + C 20 H 25 N 5 O 3 S 1 + 415.51 + 415.16782 + K + artifact + N6-[4-([4-(dimethylamino)phenyl]diazenyl)benzenesulfonyl]lysine + N6DabsylLys + PSI-MOD + MOD:01657 + N6-Dabsyl derivatized lysine + + + + + A protein modification that is produced by reaction with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, dabsyl chloride, to form N6-Dabsyl-lysine. + PubMed:18688235 + + + + + N6-[4-([4-(dimethylamino)phenyl]diazenyl)benzenesulfonyl]lysine + + + + + + N6DabsylLys + + + + + + + + + + A protein modification that is produced by reaction with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, dabsyl chloride, to form an alpha-amino-Dabsyl-derivatized residue. + 287.34 + C 14 H 13 N 3 O 2 S 1 + 287.07285 + X + artifact + N-term + N2DabsylRes + PSI-MOD + MOD:01658 + alpha-amino-Dabsyl derivatized residue + + + + + A protein modification that is produced by reaction with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, dabsyl chloride, to form an alpha-amino-Dabsyl-derivatized residue. + PubMed:18688235 + + + + + N2DabsylRes + + + + + + + + + + A protein modification that is produced by formation of an adduct with 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate, Uniblue A. + 484.5 + C 22 H 16 N 2 O 7 S 2 + 484.0399 + X + artifact + 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid + 1-amino-9,10-dioxo-4-{[3-(vinylsulfonyl)phenyl]amino}-9,10-dihydroanthracene-2-sulfonic acid + Uniblue A + UniblueARes + PSI-MOD + MOD:01659 + This reagent has a reactive sulfonyl vinyl and typically reacts with the free thiol group of cysteine residues. + Uniblue A derivatized residue + + + + + A protein modification that is produced by formation of an adduct with 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate, Uniblue A. + PubMed:18688235 + + + + + 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid + + + + + + 1-amino-9,10-dioxo-4-{[3-(vinylsulfonyl)phenyl]amino}-9,10-dihydroanthracene-2-sulfonic acid + + + + + + Uniblue A + + + + + + UniblueARes + + + + + + + + + + + A protein modification that is produced by reaction with 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate, Uniblue A, to form Uniblue A cysteine adduct. + 484.5 + C 22 H 16 N 2 O 7 S 2 + 484.0399 + C 25 H 21 N 3 O 8 S 3 + 587.64 + 587.0491 + C + artifact + 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate + 1-amino-9,10-dioxo-4-{[3-(vinylsulfonyl)phenyl]amino}-9,10-dihydroanthracene-2-sulfonate + SUniblueACys + Uniblue A + PSI-MOD + MOD:01660 + + Uniblue A derivatized cysteine + + + + + A protein modification that is produced by reaction with 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate, Uniblue A, to form Uniblue A cysteine adduct. + PubMed:18688235 + + + + + 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate + + + + + + 1-amino-9,10-dioxo-4-{[3-(vinylsulfonyl)phenyl]amino}-9,10-dihydroanthracene-2-sulfonate + + + + + + SUniblueACys + + + + + + Uniblue A + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to pyruvic acid. + -93.13 + C -6 H -7 N -1 O 0 + -93.057846 + C 3 H 3 O 2 + 71.06 + 71.013306 + Y + natural + N-term + uniprot.ptm:PTM-0662 + 2-oxopropanoic acid + MOD_RES Pyruvic acid (Tyr) + pyruvic acid + PSI-MOD + MOD:01661 + pyruvic acid (Tyr) + + + + + A protein modification that effectively converts an L-tyrosine residue to pyruvic acid. + PubMed:10085076 + PubMed:3042771 + PubMed:500639 + PubMed:8464063 + RESID:AA0127#TYR + + + + + 2-oxopropanoic acid + + + + + + MOD_RES Pyruvic acid (Tyr) + + + + + + pyruvic acid + + + + + + + + + + + A protein modification that effectively converts an L-glutamine residue to N5-(ADP-ribosyl)-L-glutamine. + 541.3 + C 15 H 21 N 5 O 13 P 2 + 541.0611 + C 20 H 29 N 7 O 15 P 2 + 669.43 + 669.1197 + Q + natural + (S)-2-amino-4-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)-5-oxopentanoic acid + N5-(ADP-ribosyl)-L-glutamine + N5-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-glutamine + N5-alpha-D-ribofuranosyl-L-glutamine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) + PSI-MOD + MOD:01662 + N5-(ADP-ribosyl)-L-glutamine + + + + + A protein modification that effectively converts an L-glutamine residue to N5-(ADP-ribosyl)-L-glutamine. + PubMed:20185726 + RESID:AA0518 + + + + + (S)-2-amino-4-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)-5-oxopentanoic acid + + + + + + N5-(ADP-ribosyl)-L-glutamine + + + + + + N5-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-glutamine + + + + + + N5-alpha-D-ribofuranosyl-L-glutamine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-(ADP-ribosyl)-L-threonine. + 541.3 + C 15 H 21 N 5 O 13 P 2 + 541.0611 + C 19 H 28 N 6 O 15 P 2 + 642.41 + 642.10876 + T + natural + (S)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]oxy)-butanoic acid + O-(ADP-ribosyl)-L-threonine + O3-(ADP-ribosyl)-L-threonine + O3-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-threonine + O3-alpha-D-ribofuranosyl-L-threonine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) + PSI-MOD + MOD:01663 + O-(ADP-ribosyl)-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-(ADP-ribosyl)-L-threonine. + PubMed:20185726 + RESID:AA0519 + + + + + (S)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]oxy)-butanoic acid + + + + + + O-(ADP-ribosyl)-L-threonine + + + + + + O3-(ADP-ribosyl)-L-threonine + + + + + + O3-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-threonine + + + + + + O3-alpha-D-ribofuranosyl-L-threonine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to a 7'-hydroxy-L-tryptophan. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 11 H 10 N 2 O 2 + 202.21 + 202.07423 + W + natural + uniprot.ptm:PTM-0427 + (2S)-2-amino-3-(7-hydroxy-1H-indol-3-yl)propanoic acid + 7'-hydroxy-L-tryptophan + 7-hydroxy-L-tryptophan + PSI-MOD + MOD:01664 + 7'-hydroxy-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to a 7'-hydroxy-L-tryptophan. + PubMed:20223990 + RESID:AA0520 + + + + + (2S)-2-amino-3-(7-hydroxy-1H-indol-3-yl)propanoic acid + + + + + + 7'-hydroxy-L-tryptophan + + + + + + 7-hydroxy-L-tryptophan + + + + + + + + + + + A protein modification that effectively crosslinks an N-terminal L-valine residue and a strand of DNA at the C-1 of a ribose, freeing the nucleotide base and forming N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-valine. + V + hypothetical + N-term + (2S)-2-[(3R,4R)-3,4-dihydroxy-5-(phosphonooxy)pentylidene]amino-3-methylbutanoic acid + ACT_SITE Schiff-base intermediate with DNA; via amino nitrogen + DNA glycosylase valine Schiff base intermediate + N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-valine + PSI-MOD + MOD:01665 + N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-valine + + + + + A protein modification that effectively crosslinks an N-terminal L-valine residue and a strand of DNA at the C-1 of a ribose, freeing the nucleotide base and forming N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-valine. + PubMed:20185759 + RESID:AA0521 + + + + + (2S)-2-[(3R,4R)-3,4-dihydroxy-5-(phosphonooxy)pentylidene]amino-3-methylbutanoic acid + + + + + + ACT_SITE Schiff-base intermediate with DNA; via amino nitrogen + + + + + + DNA glycosylase valine Schiff base intermediate + + + + + + N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-valine + + + + + + + + + + A protein modification that is produced by formation of an adduct with epicocconone. + 410.42 + C 23 H 22 O 7 + 410.13657 + X + artifact + (6S,9aS)-6-(hydroxymethyl)-3-[(1Z,4E,6E,8E)-1-hydroxy-3-oxodeca-1,4,6,8-tetraen-1-yl]-9a-methyl-5,6-dihydro-2H-furo[3,2-g]isochromene-2,9(9aH)-dione + Deep Purple + LavaPurple + Lightning Fast + PSI-MOD + MOD:01666 + epicocconone derivatized residue + + + + + A protein modification that is produced by formation of an adduct with epicocconone. + PubMed:18688235 + + + + + (6S,9aS)-6-(hydroxymethyl)-3-[(1Z,4E,6E,8E)-1-hydroxy-3-oxodeca-1,4,6,8-tetraen-1-yl]-9a-methyl-5,6-dihydro-2H-furo[3,2-g]isochromene-2,9(9aH)-dione + + + + + + Deep Purple + + + + + + LavaPurple + + + + + + Lightning Fast + + + + + + + + + + + A protein modification that is produced by formation of an adduct with epicocconone. + 410.42 + C 23 H 22 O 7 + 410.13657 + C 29 H 34 N 2 O 8 + 538.6 + 538.2315 + K + artifact + (6Z,7aS)-3-[(1Z,4E,6E,8E)-1-hydroxy-3-oxodeca-1,4,6,8-tetraen-1-yl]-7a-methyl-6-[([(1S)-1-amino-1-carboxylpentyl]amino)methylidene]-5-[(2S)-2,3-dihydroxypropyl]-1-benzofuran-2,7(6H,7aH)-dione + DeepPurple + LavaPurple + Lightning Fast + PSI-MOD + MOD:01667 + N6-epicoccononyl lysine adduct + + + + + A protein modification that is produced by formation of an adduct with epicocconone. + PubMed:18688235 + + + + + (6Z,7aS)-3-[(1Z,4E,6E,8E)-1-hydroxy-3-oxodeca-1,4,6,8-tetraen-1-yl]-7a-methyl-6-[([(1S)-1-amino-1-carboxylpentyl]amino)methylidene]-5-[(2S)-2,3-dihydroxypropyl]-1-benzofuran-2,7(6H,7aH)-dione + + + + + + DeepPurple + + + + + + LavaPurple + + + + + + Lightning Fast + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to O4-(8alpha-FAD)-L-aspartate. + 783.54 + C 27 H 31 N 9 O 15 P 2 + 783.1415 + C 31 H 36 N 10 O 18 P 2 + 898.63 + 898.16846 + D + natural + (2S)-2-amino-4-oxo-4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxybutanoic acid + 8alpha-[(4-aspartyl)oxy]FAD + O4-(8alpha-FAD)-L-aspartate + PSI-MOD + MOD:01668 + + O4-(8alpha-FAD)-L-aspartate + + + + + A protein modification that effectively converts an L-aspartic acid residue to O4-(8alpha-FAD)-L-aspartate. + PubMed:20080101 + RESID:AA0522 + + + + + (2S)-2-amino-4-oxo-4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxybutanoic acid + + + + + + 8alpha-[(4-aspartyl)oxy]FAD + + + + + + O4-(8alpha-FAD)-L-aspartate + + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to N(omega),N(omega),N'(omega)-trimethyl-L-arginine. + 42.08 + C 3 H 6 N 0 O 0 + 42.04695 + C 9 H 18 N 4 O 1 + 198.27 + 198.14806 + R + hypothetical + Unimod:37 + (2S)-2-amino-5-([(dimethylamino)(methylamino)methylidene]amino)pentanoic acid + (2S)-2-amino-5-([(dimethylamino)(methylimino)methyl]amino)pentanoic acid + 2-[(4S)-4-amino-5-oxopentyl]-1,1,3-trimethylguanidine + N(G)-trimethylarginine + N5-[(dimethylamino)(imino)methyl]ornithine + NoNoNo'Me3Arg + omega-N,omega-N,omega-N'-trimethyl-L-arginine + trimethylationr + PSI-MOD + Trimethyl + tri-Methylation + MOD:01669 + trimethyl-L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to N(omega),N(omega),N'(omega)-trimethyl-L-arginine. + OMSSA:117 + PubMed:11704273 + PubMed:602668 + RESID:AA0523 + Unimod:37#R + + + + + (2S)-2-amino-5-([(dimethylamino)(methylamino)methylidene]amino)pentanoic acid + + + + + + (2S)-2-amino-5-([(dimethylamino)(methylimino)methyl]amino)pentanoic acid + + + + + + 2-[(4S)-4-amino-5-oxopentyl]-1,1,3-trimethylguanidine + + + + + + N(G)-trimethylarginine + + + + + + N5-[(dimethylamino)(imino)methyl]ornithine + + + + + + NoNoNo'Me3Arg + + + + + + omega-N,omega-N,omega-N'-trimethyl-L-arginine + + + + + + trimethylationr + + + + + + Trimethyl + + + + + + tri-Methylation + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine. + 34.44 + C 0 Cl 1 H -1 N 0 O 0 + 33.96103 + C 6 Cl 1 H 11 N 2 O 1 + 162.62 + 162.05598 + K + hypothetical + (2S)-2-amino-6-(chloroamino)hexanoic acid + N(zeta)-chlorolysine + N6-chloro-L-lysine + N6ClLys + epsilon-chlorolysine + lysine chloramine + PSI-MOD + MOD:01670 + N6-chloro-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine. + PubMed:16091367 + PubMed:16195462 + PubMed:17260957 + RESID:AA0524 + + + + + (2S)-2-amino-6-(chloroamino)hexanoic acid + + + + + + N(zeta)-chlorolysine + + + + + + N6-chloro-L-lysine + + + + + + N6ClLys + + + + + + epsilon-chlorolysine + + + + + + lysine chloramine + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-(L-isoaspartyl)-L-threonine, using free L-asparagine and releasing ammonia. + 115.09 + C 4 H 5 N 1 O 3 + 115.02694 + C 8 H 12 N 2 O 5 + 216.19 + 216.07462 + T + natural + (2S)-2-amino-4-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-4-oxobutanoic acid + (2S,3R)-2-amino-3-([(4S)-3-amino-3-carboxypropanoyl]oxy)propanoic acid + ACT_SITE O-isoaspartyl threonine intermediate + O(beta)-(beta-aspartyl)threonine + O-(L-isoaspartyl)-L-threonine + O3-(isoaspartyl)-threonine + PSI-MOD + MOD:01671 + This is a threonine active intermediate and not an ester cross-link of peptides [JSG]. + O-(L-isoaspartyl)-L-threonine (active site intermediate) + + + + + A protein modification that effectively converts an L-threonine residue to O-(L-isoaspartyl)-L-threonine, using free L-asparagine and releasing ammonia. + PubMed:8706862 + RESID:AA0525#THR + + + + + (2S)-2-amino-4-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-4-oxobutanoic acid + + + + + + (2S,3R)-2-amino-3-([(4S)-3-amino-3-carboxypropanoyl]oxy)propanoic acid + + + + + + ACT_SITE O-isoaspartyl threonine intermediate + + + + + + O(beta)-(beta-aspartyl)threonine + + + + + + O-(L-isoaspartyl)-L-threonine + + + + + + O3-(isoaspartyl)-threonine + + + + + + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-lysine residue with a halogen atom. + K + PSI-MOD + MOD:01672 + halogenated lysine + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-lysine residue with a halogen atom. + PubMed:18688235 + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an N-acetylaminohexose group through a glycosidic bond. + 203.19 + C 8 H 13 N 1 O 5 + 203.07938 + X + Unimod:43 + HexNAcRes + PSI-MOD + HexNAc + N-Acetylhexosamine + MOD:01673 + + N-acetylaminohexosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an N-acetylaminohexose group through a glycosidic bond. + Unimod:43 + + + + + HexNAcRes + + + + + + HexNAc + + + + + + N-Acetylhexosamine + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminohexosyl)-L-asparagine. + 203.19 + C 8 H 13 N 1 O 5 + 203.07938 + C 12 H 19 N 3 O 7 + 317.3 + 317.1223 + N + natural + Unimod:43 + (S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-hexopyranosyl)amino-4-oxobutanoic acid + HexNAcAsn + N4-(2-acetamido-2-deoxy-beta-D-hexopyranosyl)-L-asparagine + N4-(2-acetylamino-2-deoxy-beta-D-hexopyranosyl)-L-asparagine + N4-(N-acetylhexosaminyl)asparagine + N4-asparagine-beta-N-acetylhexosaminide + N4-glycosyl-L-asparagine + N4-glycosylasparagine + N4HexNAcAsn + hexNAcN + PSI-MOD + HexNAc + N-Acetylhexosamine + MOD:01674 + + N4-(N-acetylamino)hexosyl-L-asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminohexosyl)-L-asparagine. + OMSSA:182 + Unimod:43#N + + + + + (S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-hexopyranosyl)amino-4-oxobutanoic acid + + + + + + HexNAcAsn + + + + + + N4-(2-acetamido-2-deoxy-beta-D-hexopyranosyl)-L-asparagine + + + + + + N4-(2-acetylamino-2-deoxy-beta-D-hexopyranosyl)-L-asparagine + + + + + + N4-(N-acetylhexosaminyl)asparagine + + + + + + N4-asparagine-beta-N-acetylhexosaminide + + + + + + N4-glycosyl-L-asparagine + + + + + + N4-glycosylasparagine + + + + + + N4HexNAcAsn + + + + + + hexNAcN + + + + + + HexNAc + + + + + + N-Acetylhexosamine + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O3-(N-acetylaminohexosyl)-L-serine. + 203.19 + C 8 H 13 N 1 O 5 + 203.07938 + C 11 H 18 N 2 O 7 + 290.27 + 290.1114 + S + natural + Unimod:43 + (S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-hexopyranosyloxy)propanoic acid + O-(2-acetylamino-2-deoxy-beta-D-hexopyranosyl)-L-serine + O-(N-acetylhexosaminyl)serine + O-glycosylserine + O-seryl-beta-N-acetylhexosaminide + O3-(2-acetamido-2-deoxy-beta-D-hexopyranosyl)-L-serine + OHexNAcSer + hexNAcS + PSI-MOD + HexNAc + N-Acetylhexosamine + MOD:01675 + + O-(N-acetylamino)hexosyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O3-(N-acetylaminohexosyl)-L-serine. + OMSSA:184 + Unimod:43#S + + + + + (S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-hexopyranosyloxy)propanoic acid + + + + + + O-(2-acetylamino-2-deoxy-beta-D-hexopyranosyl)-L-serine + + + + + + O-(N-acetylhexosaminyl)serine + + + + + + O-glycosylserine + + + + + + O-seryl-beta-N-acetylhexosaminide + + + + + + O3-(2-acetamido-2-deoxy-beta-D-hexopyranosyl)-L-serine + + + + + + OHexNAcSer + + + + + + hexNAcS + + + + + + HexNAc + + + + + + N-Acetylhexosamine + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminohexosyl)-L-threonine. + 203.19 + C 8 H 13 N 1 O 5 + 203.07938 + C 12 H 20 N 2 O 7 + 304.3 + 304.12704 + T + natural + Unimod:43 + (2S,3R)-2-amino-3-(alpha-D-2-acetamido-2-deoxyhexopyranosyloxy)butanoic acid + O-(N-acetylhexcosaminyl)-L-threonine + O-glycosylthreonine + O3-(N-acetylhexosaminyl)threonine + OHexNAcThr + hexNAcT + PSI-MOD + HexNAc + N-Acetylhexosamine + MOD:01676 + + O-(N-acetylamino)hexosyl-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminohexosyl)-L-threonine. + OMSSA:185 + Unimod:43#T + + + + + (2S,3R)-2-amino-3-(alpha-D-2-acetamido-2-deoxyhexopyranosyloxy)butanoic acid + + + + + + O-(N-acetylhexcosaminyl)-L-threonine + + + + + + O-glycosylthreonine + + + + + + O3-(N-acetylhexosaminyl)threonine + + + + + + OHexNAcThr + + + + + + hexNAcT + + + + + + HexNAc + + + + + + N-Acetylhexosamine + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-proline residue to O4-(N-acetylamino)hexosyl-L-hydroxyproline. + 219.19 + C 8 H 13 N 1 O 6 + 219.07428 + C 13 H 20 N 2 O 7 + 316.31 + 316.12704 + P + natural + (2S,4R)-4-[2-acetamido-2-deoxy-alpha-D-hexopyranosyloxy]pyrrolidine-2-carboxylic acid + 4-(N-acetylhexosaminyloxy)proline + 4-[(2-N-acetylamino)-alpha-D-hexopyranosyl]oxyproline + O4-glycosyl-hydroxyproline + O4HexNAcHyPro + alpha-2-(N-acetylamino)hexopyranosyl-4-hydroxyproline + PSI-MOD + HexNAc + MOD:01677 + + secondary to RESID:AA0030 + O4-(N-acetylamino)hexosyl-L-hydroxyproline + + + + + A protein modification that effectively converts an L-proline residue to O4-(N-acetylamino)hexosyl-L-hydroxyproline. + PubMed:18688235 + + + + + (2S,4R)-4-[2-acetamido-2-deoxy-alpha-D-hexopyranosyloxy]pyrrolidine-2-carboxylic acid + + + + + + 4-(N-acetylhexosaminyloxy)proline + + + + + + 4-[(2-N-acetylamino)-alpha-D-hexopyranosyl]oxyproline + + + + + + O4-glycosyl-hydroxyproline + + + + + + O4HexNAcHyPro + + + + + + alpha-2-(N-acetylamino)hexopyranosyl-4-hydroxyproline + + + + + + HexNAc + + + + + + + + + + + A protein modification that effectively coverts L-lysine to N6-carbamoyl-L-lysine. + 43.02 + C 1 H 1 N 1 O 1 + 43.005814 + C 7 H 13 N 3 O 2 + 171.2 + 171.10078 + K + artifact + Unimod:5 + uniprot.ptm:PTM-0675 + 2-amino-6-ureido-hexanoic acid + MOD_RES N6-carbamoyllysine + N6-(aminocarbonyl)-L-lysine + N6CbmLys + carbamylk + homocitrulline + PSI-MOD + Carbamyl + Carbamylation + MOD:01678 + + This modification can be produced by hydrogen cyanate, either as a reagent or as released by urea degradation in solution [JSG]. + N6-carbamoyl-L-lysine + + + + + A protein modification that effectively coverts L-lysine to N6-carbamoyl-L-lysine. + ChEBI:144369 + DeltaMass:56 + OMSSA:31 + PubMed:10978403 + PubMed:12203680 + Unimod:5#K + + + + + 2-amino-6-ureido-hexanoic acid + + + + + + MOD_RES N6-carbamoyllysine + + + + + + N6-(aminocarbonyl)-L-lysine + + + + + + N6CbmLys + + + + + + carbamylk + + + + + + homocitrulline + + + + + + Carbamyl + + + + + + Carbamylation + + + + + + + + + + A protein modification that effectively replaces a residue alpha amino or imino hydrogen with a carbamoyl group. + 43.02 + C 1 H 1 N 1 O 1 + 43.005814 + X + artifact + N-term + Unimod:5 + N2CbmRes + ntermcarbamyl + PSI-MOD + Carbamyl + Carbamylation + MOD:01679 + + This modification can be produced by hydrogen cyanate, either as a reagent or as released by urea degradation. This modification effectively blocks Edman degradation, and because it can dehydrate to a cyanate group and react with another peptide N-terminal, it can effectively block two peptide molecules [JSG]. + alpha-aminocarbamoylated residue + + + + + A protein modification that effectively replaces a residue alpha amino or imino hydrogen with a carbamoyl group. + DeltaMass:56 + OMSSA:32 + PubMed:10978403 + PubMed:12203680 + Unimod:5#N-term + + + + + N2CbmRes + + + + + + ntermcarbamyl + + + + + + Carbamyl + + + + + + Carbamylation + + + + + + + + + + + A protein modification that effectively replaces one residue alpha amino or imino hydrogen with one methyl group. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + X + natural + N-term + Unimod:34 + N2Me1Res + ntermmethyl + ntermpepmethyl + PSI-MOD + Methyl + Methylation + MOD:01680 + + Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG]. + alpha-amino monomethylated residue + + + + + A protein modification that effectively replaces one residue alpha amino or imino hydrogen with one methyl group. + OMSSA:11 + OMSSA:76 + Unimod:34#N-term + + + + + N2Me1Res + + + + + + ntermmethyl + + + + + + ntermpepmethyl + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + A protein modification that effectively replaces one hydrogen atom of an L-aspartic acid residue with one methyl group. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 5 H 7 N 1 O 3 + 129.12 + 129.04259 + D + artifact + Unimod:34 + Me1Asp + methyld + PSI-MOD + Methyl + Methylation + MOD:01681 + monomethylated L-aspartic acid + + + + + A protein modification that effectively replaces one hydrogen atom of an L-aspartic acid residue with one methyl group. + OMSSA:16 + Unimod:34#D + + + + + Me1Asp + + + + + + methyld + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + A protein modification that effectively replaces one hydrogen atom of an L-cysteine residue with one methyl group. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 4 H 7 N 1 O 1 S 1 + 117.17 + 117.02483 + C + natural + Unimod:34 + Me1Cys + methylc + PSI-MOD + Methyl + Methylation + MOD:01682 + + monomethylated L-cysteine + + + + + A protein modification that effectively replaces one hydrogen atom of an L-cysteine residue with one methyl group. + OMSSA:73 + Unimod:34#C + + + + + Me1Cys + + + + + + methylc + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + + A protein modification that effectively replaces one hydrogen atom of an L-lysine residue with one methyl group. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 7 H 15 N 2 O 2 + 159.21 + 159.11336 + K + natural + Me1Lys + methylk + PSI-MOD + Methyl + Methylation + MOD:01683 + + monomethylated L-lysine + + + + + A protein modification that effectively replaces one hydrogen atom of an L-lysine residue with one methyl group. + OMSSA:0 + + + + + Me1Lys + + + + + + methylk + + + + + + Methyl + + + + + + Methylation + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to a palmitoylated-L-cysteine, such as N-palmitoyl-L-cysteine or S-palmitoyl-L-cysteine. + 238.41 + C 16 H 30 N 0 O 1 S 0 + 238.22966 + C 19 H 35 N 1 O 2 S 1 + 341.55 + 341.23886 + C + natural + Unimod:47 + Hexadecanoylated L-cysteine + PamCys + palmitoylationc + PSI-MOD + Palmitoyl + Palmitoylation + MOD:01684 + + palmitoylated-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to a palmitoylated-L-cysteine, such as N-palmitoyl-L-cysteine or S-palmitoyl-L-cysteine. + OMSSA:92 + Unimod:47 + + + + + Hexadecanoylated L-cysteine + + + + + + PamCys + + + + + + palmitoylationc + + + + + + Palmitoyl + + + + + + Palmitoylation + + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino group with a alpha-palmitoylamino group. + 238.41 + C 16 H 30 N 0 O 1 S 0 + 238.22966 + X + natural + N-term + Unimod:47 + N2PamRes + PSI-MOD + Palmitoyl + Palmitoylation + MOD:01685 + + alpha-amino palmitoylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino group with a alpha-palmitoylamino group. + Unimod:47#N-term + + + + + N2PamRes + + + + + + Palmitoyl + + + + + + Palmitoylation + + + + + + + + + + + A protein modification that effectively replaces two alpha amino hydrogen atoms with two methyl group. + 28.05 + C 2 H 4 + 28.0313 + X + N-term + Unimod:36 + N2Me2Res + ntermpepdimethyl + PSI-MOD + Dimethyl + di-Methylation + MOD:01686 + For alpha-amino acids, both N-alpha-monomethylation and complete N-alpha protonation and trimethylation have been observed, but incomplete dimethylation has not been reported as a natural process. For N-terminal proline residues, dimethylation can only be effectively accomplished with a protonated imino group, whereas this process accounts only for dimethylation and not protonation. See MOD:00889. + alpha-amino dimethylated residue + + + + + A protein modification that effectively replaces two alpha amino hydrogen atoms with two methyl group. + OMSSA:38 + Unimod:36#N-term + + + + + N2Me2Res + + + + + + ntermpepdimethyl + + + + + + Dimethyl + + + + + + di-Methylation + + + + + + + + + + + + + + + + + A protein modification that effectively replaces an alpha-aminium group with a trimethylaminium group. + 42.08 + C 3 H 6 N 0 O 0 + 42.046402 + 1+ + X + natural + N-term + Unimod:37 + N2Me3Res + ntermtrimethyl + PSI-MOD + Trimethyl + tri-Methylation + MOD:01687 + + For amino acids residues, amine trimethylation can effectively only be accomplished with an aminium, protonated primary amino, group. This process accounts only for trimethylation and not protonation. The alternative N2Me3+Res process (MOD:01698) accounts for both protonation and trimethylation. + alpha-amino trimethylated residue + + + + + A protein modification that effectively replaces an alpha-aminium group with a trimethylaminium group. + OMSSA:12 + Unimod:37#N-term + + + + + N2Me3Res + + + + + + ntermtrimethyl + + + + + + Trimethyl + + + + + + tri-Methylation + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to one of the diastereomeric 3-hydroxy-L-asparagine residues. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 4 H 6 N 2 O 3 + 130.1 + 130.03784 + N + natural + Unimod:35 + 3HyAsn + hydroxylationn + monohydroxylated asparagine + PSI-MOD + Oxidation + MOD:01688 + + 3-hydroxy-L-asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to one of the diastereomeric 3-hydroxy-L-asparagine residues. + OMSSA:61 + Unimod:35#N + + + + + 3HyAsn + + + + + + hydroxylationn + + + + + + monohydroxylated asparagine + + + + + + Oxidation + + + + + + + + + + A protein modification that effectively converts a carboxyl-terminal residue to an alpha-carboxyl (1-carboxyl) methyl ester. + 14.03 + C 1 H 2 N 0 O 0 S 0 + 14.01565 + X + natural + C-term + Unimod:34 + C1OMeRes + ctermpepmeester + ctermpepmethyl + PSI-MOD + Methyl + MOD:01689 + + alpha-carboxyl methylated residue + + + + + A protein modification that effectively converts a carboxyl-terminal residue to an alpha-carboxyl (1-carboxyl) methyl ester. + OMSSA:18 + OMSSA:68 + Unimod:34#C-term + + + + + C1OMeRes + + + + + + ctermpepmeester + + + + + + ctermpepmethyl + + + + + + Methyl + + + + + + Methyl + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to N-[(12R)-12-hydroxymyristoyl]-L-cysteine. + 226.36 + C 14 H 26 N 0 O 2 S 0 + 226.19328 + C 17 H 32 N 1 O 3 S 1 + 330.51 + 330.2103 + C + natural + N-term + uniprot.ptm:PTM-0419 + 2-[(12R)-12-hydroxytetradecanoyl]amino-3-sulfanylpropanoic acid + LIPID N-[(12R)-12-hydroxymyristoyl]cysteine + N-[(12R)-12-hydroxymyristoyl]-L-cysteine + N-[(12R)-12-hydroxytetradecanoyl]cysteine + PSI-MOD + MOD:01690 + N-[(12R)-12-hydroxymyristoyl]-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to N-[(12R)-12-hydroxymyristoyl]-L-cysteine. + RESID:AA0516 + + + + + 2-[(12R)-12-hydroxytetradecanoyl]amino-3-sulfanylpropanoic acid + + + + + + LIPID N-[(12R)-12-hydroxymyristoyl]cysteine + + + + + + N-[(12R)-12-hydroxymyristoyl]-L-cysteine + + + + + + N-[(12R)-12-hydroxytetradecanoyl]cysteine + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to N-(12-ketomyristoyl)-L-cysteine. + 224.34 + C 14 H 24 N 0 O 2 S 0 + 224.17763 + C 17 H 30 N 1 O 3 S 1 + 328.49 + 328.19464 + C + natural + N-term + uniprot.ptm:PTM-0420 + 2-(12-oxotetradecanoyl)amino-3-sulfanylpropanoic acid + LIPID N-(12-oxomyristoyl)cysteine + N-(12-ketomyristoyl)-L-cysteine + N-(12-oxotetradecanoyl)cysteine + PSI-MOD + MOD:01691 + N-(12-ketomyristoyl)-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to N-(12-ketomyristoyl)-L-cysteine. + PubMed:19053188 + RESID:AA0517 + + + + + 2-(12-oxotetradecanoyl)amino-3-sulfanylpropanoic acid + + + + + + LIPID N-(12-oxomyristoyl)cysteine + + + + + + N-(12-ketomyristoyl)-L-cysteine + + + + + + N-(12-oxotetradecanoyl)cysteine + + + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl semialdehyde. + -16.0 + C 0 H 0 N 0 O -1 + -15.994915 + C 5 H 7 N 1 O 2 + 113.12 + 113.047676 + E + artifact + gamma-glutamyl semialdehyde + glutamyl 5-semialdehyde + glutamyl aldehyde + PSI-MOD + Deoxy + MOD:01692 + glutamyl semialdehyde (Glu) + + + + + A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl semialdehyde. + PubMed:18688235 + PubMed:743268 + + + + + gamma-glutamyl semialdehyde + + + + + + glutamyl 5-semialdehyde + + + + + + glutamyl aldehyde + + + + + + Deoxy + + + + + + + + + + + A protein modification that effectively replaces a residue alpha amino or imino hydrogen with a (pyrid-3-yl)acetyl group. + 119.12 + C 7 H 5 N 1 O 1 + 119.03712 + X + artifact + N-term + Unimod:25 + ntermpeppyridyl + PSI-MOD + Pyridylacetyl + pyridylacetyl + MOD:01693 + Produced by reaction with N-[(pyrid-3-yl)acetyl]oxy-succinimide [JSG]. + alpha-amino pyridylacetylated residue + + + + + A protein modification that effectively replaces a residue alpha amino or imino hydrogen with a (pyrid-3-yl)acetyl group. + OMSSA:107 + PubMed:9276974 + Unimod:25#N-term + + + + + ntermpeppyridyl + + + + + + Pyridylacetyl + + + + + + pyridylacetyl + + + + + + + + + + A protein modification that effectively results from forming an adduct between an L-cysteine residue and the bioluminescent compound didehydrocoelenterazine to form S-(coelenterazin-3a-yl)-L-cysteine. + 421.46 + C 26 H 19 N 3 O 3 S 0 + 421.14264 + C 29 H 24 N 4 O 4 S 1 + 524.6 + 524.15186 + C + natural + uniprot.ptm:PTM-0428 + (2R)-2-amino-3-([(4-hydroxyphenyl)(8-benzyl-3-oxo-6-[4-hydroxyphenyl]-3,7-dihydroimidazo[1,2-a]pyrazin-2-yl)methyl]sulfanyl)propanoic acid + MOD_RES S-(coelenterazin-3a-yl)cysteine + S-(coelenterazin-3a-yl)-L-cysteine + dehydrocoelenterazine cysteine adduct + symplectin chromophore + PSI-MOD + MOD:01694 + S-(coelenterazin-3a-yl)-L-cysteine + + + + + A protein modification that effectively results from forming an adduct between an L-cysteine residue and the bioluminescent compound didehydrocoelenterazine to form S-(coelenterazin-3a-yl)-L-cysteine. + ChEBI:2311 + PubMed:18997450 + RESID:AA0526 + + + + + (2R)-2-amino-3-([(4-hydroxyphenyl)(8-benzyl-3-oxo-6-[4-hydroxyphenyl]-3,7-dihydroimidazo[1,2-a]pyrazin-2-yl)methyl]sulfanyl)propanoic acid + + + + + + MOD_RES S-(coelenterazin-3a-yl)cysteine + + + + + + S-(coelenterazin-3a-yl)-L-cysteine + + + + + + dehydrocoelenterazine cysteine adduct + + + + + + symplectin chromophore + + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an 3-(carboxamidomethylthio)propanoyl group. + 145.18 + C 5 H 7 N 1 O 2 S 1 + 145.01974 + X + artifact + N-term + Unimod:293 + PSI-MOD + 3-(carbamidomethylthio)propanoyl + CAMthiopropanoyl + MOD:01695 + alpha-amino 3-(carboxamidomethylthio)propanoylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an 3-(carboxamidomethylthio)propanoyl group. + PubMed:15121203 + Unimod:293#N-term + + + + + 3-(carbamidomethylthio)propanoyl + + + + + + CAMthiopropanoyl + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acyl group. + X + natural + N-term + PSI-MOD + MOD:01696 + + alpha-amino acylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acyl group. + PubMed:18688235 + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an 4-(2-aminoethyl)benzenesulfonyl group. + 183.23 + C 8 H 9 N 1 O 2 S 1 + 183.0354 + X + artifact + N-term + Unimod:276 + PSI-MOD + AEBS + Aminoethylbenzenesulfonylation + MOD:01697 + See the comment for MOD:00596 [JSG]. + alpha-amino 4-(2-aminoethyl)benzenesulfonylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an 4-(2-aminoethyl)benzenesulfonyl group. + DeltaMass:235 + PubMed:8597590 + Unimod:276#N-term + + + + + AEBS + + + + + + Aminoethylbenzenesulfonylation + + + + + + + + + + + A protein modification that effectively replaces an amino group with a trimethylaminium group. + 43.09 + C 3 H 7 N 0 O 0 S 0 + 43.054226 + 1+ + X + natural + N-term + N2Me3+Res + PSI-MOD + Trimethyl + tri-Methylation + MOD:01698 + + alpha-amino trimethylated protonated-residue + + + + + A protein modification that effectively replaces an amino group with a trimethylaminium group. + PubMed:18688235 + + + + + N2Me3+Res + + + + + + Trimethyl + + + + + + tri-Methylation + + + + + + + + + + A protein modification that effectively adds a hydrogen cation, a proton, forming a cationic residue. + 1.01 + C 0 H 1 N 0 O 0 + 1.007276 + 1+ + X + natural + H+NRes + PSI-MOD + MOD:01699 + + protonated residue + + + + + A protein modification that effectively adds a hydrogen cation, a proton, forming a cationic residue. + PubMed:18688235 + + + + + H+NRes + + + + + + + + + + A protein modification that effectively adds a proton to a residue alpha-amnino or alpha-imino group forming an alpha-aminium or alpha-iminium group, respectively. + 1.01 + C 0 H 1 N 0 O 0 + 1.007276 + 1+ + X + natural + N-term + N2H+NRes + PSI-MOD + MOD:01700 + + alpha-amino protonated residue + + + + + A protein modification that effectively adds a proton to a residue alpha-amnino or alpha-imino group forming an alpha-aminium or alpha-iminium group, respectively. + PubMed:18688235 + + + + + N2H+NRes + + + + + + + + + + A protein modification that effectively removes a hydrogen cation, a proton, forming an anionic residue. + -1.01 + C 0 H -1 N 0 O 0 + -1.007276 + 1- + X + natural + H-NRes + PSI-MOD + MOD:01701 + + deprotonated residue + + + + + A protein modification that effectively removes a hydrogen cation, a proton, forming an anionic residue. + PubMed:18688235 + + + + + H-NRes + + + + + + + + + + A protein modification that effectively removes a proton from a residue 1-carboxyl group (referred to as the alpha-carboxyl), forming a carboxylate anion. + -1.01 + C 0 H -1 N 0 O 0 + -1.007276 + 1- + X + natural + C-term + C1H-NRes + PSI-MOD + MOD:01702 + + alpha-carboxyl deprotonated residue + + + + + A protein modification that effectively removes a proton from a residue 1-carboxyl group (referred to as the alpha-carboxyl), forming a carboxylate anion. + PubMed:18688235 + + + + + C1H-NRes + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to dehydrobutyrine. + C 4 H 5 N 1 O 1 + 83.09 + 83.03712 + X + Dehydroamino butyric acid + beta-elim-t + dHAbu + dehydro + phospholosst + PSI-MOD + Dehydrated + Dehydration + MOD:01703 + + dehydrobutyrine + + + + + A protein modification that effectively converts a source amino acid residue to dehydrobutyrine. + PubMed:18688235 + + + + + Dehydroamino butyric acid + + + + + + beta-elim-t + + + + + + dHAbu + + + + + + dehydro + + + + + + phospholosst + + + + + + Dehydrated + + + + + + Dehydrated + + + + + + Dehydration + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to dehydrobutyrine, by neutral loss of methyl sulfide. + -48.1 + C -1 H -4 N 0 O 0 S -1 + -48.003372 + C 4 H 5 N 1 O 1 + 83.09 + 83.03712 + M + artifact + dHAbu(Met) + PSI-MOD + MOD:01704 + + It is expected that this neutral loss will produce a mix of (E)- and (Z)-isomers [JSG]. + dehydrobutyrine (Met) + + + + + A protein modification that effectively converts an L-methionine residue to dehydrobutyrine, by neutral loss of methyl sulfide. + PubMed:18688235 + + + + + dHAbu(Met) + + + + + + + + + + A protein modification that effectively replaces a residue hydrogen with an isotope tagged reagent acyl group. + X + artifact + PSI-MOD + MOD:01705 + + isotope tagged reagent acylated residue + + + + + A protein modification that effectively replaces a residue hydrogen with an isotope tagged reagent acyl group. + PubMed:18688235 + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an isotope tagged reagent acyl group. + X + artifact + PSI-MOD + MOD:01706 + + isotope tagged reagent N-acylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an isotope tagged reagent acyl group. + PubMed:18688235 + + + + + + + + + A protein modification that effectively replaces a residue hydroxyl group with an isotope tagged reagent acyloxy group. + X + artifact + PSI-MOD + MOD:01707 + isotope tagged reagent O-acylated residue + + + + + A protein modification that effectively replaces a residue hydroxyl group with an isotope tagged reagent acyloxy group. + PubMed:18688235 + + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an isotope tagged reagent acyl group. + X + artifact + N-term + PSI-MOD + MOD:01708 + + isotope tagged reagent alpha-amino acylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an isotope tagged reagent acyl group. + PubMed:18688235 + + + + + + + + + A protein modification that effectively replaces a residue amino- or imino-hydrogen with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups. + X + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01709 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex reporter+balance reagent N-acylated residue + + + + + A protein modification that effectively replaces a residue amino- or imino-hydrogen with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + A protein modification that effectively replaces a residue amino- or imino-hydrogen with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance groups. + X + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01710 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex reporter+balance reagent N-acylated residue + + + + + A protein modification that effectively replaces a residue amino- or imino-hydrogen with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance groups. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups. + X + artifact + N-term + Unimod:214 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01711 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups. + Unimod:214#N-term + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance groups. + X + artifact + N-term + Unimod:214 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01712 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance groups. + Unimod:214#N-term + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + A protein modification that effectively replaces a residue hydroxyl with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance acyloxy groups. + X + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01713 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ4plex reporter+balance reagent O-acylated residue + + + + + A protein modification that effectively replaces a residue hydroxyl with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance acyloxy groups. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + A protein modification that effectively replaces a residue hydroxyl with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance acyloxy groups. + X + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + MOD:01714 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + iTRAQ8plex reporter+balance reagent O-acylated residue + + + + + A protein modification that effectively replaces a residue hydroxyl with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance acyloxy groups. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with a Proteome Sciences TMT6plex reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + X + artifact + Unimod:214 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01715 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with a Proteome Sciences TMT6plex reporter+balance group. + Unimod:214 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-126 reagent acylated residue. + 2,6-dimethyl-1-methylidenepiperidinium + cysTMT6plex reporter fragment + PSI-MOD + MOD:01716 + + TMT6plex reporter fragment + + + + + The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-126 reagent acylated residue. + PubMed:18688235 + + + + + 2,6-dimethyl-1-methylidenepiperidinium + + + + + + cysTMT6plex reporter fragment + + + + + + + + + + A protein modification that effectively replaces a residue amino- or imino-hydrogen with a Proteome Sciences TMT6plex reporter+balance group. + X + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01717 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex reporter+balance reagent N-acylated residue + + + + + A protein modification that effectively replaces a residue amino- or imino-hydrogen with a Proteome Sciences TMT6plex reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a Proteome Sciences TMT6plex reporter+balance group. + X + artifact + N-term + Unimod:214 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01718 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a Proteome Sciences TMT6plex reporter+balance group. + Unimod:214#N-term + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + A protein modification that effectively replaces a residue hydroxyl with one of the Proteome Sciences TMT6plex reagent reporter+balance acyloxy groups. + X + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01719 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex reporter+balance reagent O-acylated residue + + + + + A protein modification that effectively replaces a residue hydroxyl with one of the Proteome Sciences TMT6plex reagent reporter+balance acyloxy groups. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-126 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + X + artifact + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01720 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-126 reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-126 reporter+balance group. + Unimod:737 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-126 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + X + artifact + N-term + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01721 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-126 reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-126 reporter+balance group. + Unimod:737#N-term + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-126 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 14 (13)C 4 H 32 (14)N 3 (15)N 1 O 3 + 357.26 + 357.2579 + K + artifact + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01722 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-126 reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-126 reporter+balance group. + Unimod:737#K + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-126 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 17 (13)C 4 H 29 (14)N 2 (15)N 1 O 4 + 392.23 + 392.22626 + Y + artifact + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01723 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-126 reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-126 reporter+balance group. + Unimod:737#Y + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-126 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 14 (13)C 4 H 27 (14)N 4 (15)N 1 O 3 + 366.22 + 366.22183 + H + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01724 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-126 reporter+balance reagent N'-acylated histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-126 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-126 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 11 (13)C 4 H 25 (14)N 2 (15)N 1 O 4 + 316.19 + 316.19495 + S + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01725 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-126 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-126 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-126 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 12 (13)C 4 H 27 (14)N 2 (15)N 1 O 4 + 330.21 + 330.2106 + T + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01726 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-126 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-126 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-126 reagent acylated residue. + 1+ + (12)C 8 H 16 (14)N 1 + 126.13 + 126.12772 + X + artifact + 2,6-dimethyl-1-methylidenepiperidinium + cysTMT6plex-126 reporter fragment + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01727 + + TMT6plex-126 reporter fragment + + + + + The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-126 reagent acylated residue. + PubMed:18688235 + + + + + 2,6-dimethyl-1-methylidenepiperidinium + + + + + + cysTMT6plex-126 reporter fragment + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-127 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + X + artifact + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01728 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-127 reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-127 reporter+balance group. + Unimod:737 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-127 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + X + artifact + N-term + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01729 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-127 reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-127 reporter+balance group. + Unimod:737#N-term + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-127 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 14 (13)C 4 H 32 (14)N 3 (15)N 1 O 3 + 357.26 + 357.2579 + K + artifact + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01730 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-127 reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-127 reporter+balance group. + Unimod:737#K + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-127 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16 + 229.16293 + Y + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01731 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-127 reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-127 reporter+balance group. + Unimod:737#Y + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-127 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 14 (13)C 4 H 27 (14)N 4 (15)N 1 O 3 + 366.22 + 366.22183 + H + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01732 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-127 reporter+balance reagent N'-acylated histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-127 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-127 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 11 (13)C 4 H 25 (14)N 2 (15)N 1 O 4 + 316.19 + 316.19495 + S + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01733 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-127 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-127 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-127 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 12 (13)C 4 H 27 (14)N 2 (15)N 1 O 4 + 330.21 + 330.2106 + T + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01734 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-127 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-127 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-127 reagent acylated residue. + 1+ + (12)C 7 (13)C 1 H 16 (14)N 1 + 127.13 + 127.13108 + X + artifact + 2,6-dimethyl-1-methylidenepiperidinium + cysTMT6plex-127 reporter fragment + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01735 + + TMT6plex-127 reporter fragment + + + + + The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-127 reagent acylated residue. + PubMed:18688235 + + + + + 2,6-dimethyl-1-methylidenepiperidinium + + + + + + cysTMT6plex-127 reporter fragment + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-128 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + X + artifact + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01736 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-128 reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-128 reporter+balance group. + Unimod:737 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-128 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + X + artifact + N-term + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01737 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-128 reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-128 reporter+balance group. + Unimod:737#N-term + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-128 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 14 (13)C 4 H 32 (14)N 3 (15)N 1 O 3 + 357.26 + 357.2579 + K + artifact + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01738 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-128 reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-128 reporter+balance group. + Unimod:737#K + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-128 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 17 (13)C 4 H 29 (14)N 2 (15)N 1 O 4 + 392.23 + 392.22626 + Y + artifact + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01739 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-128 reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-128 reporter+balance group. + Unimod:737#Y + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-128 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 14 (13)C 4 H 27 (14)N 4 (15)N 1 O 3 + 366.22 + 366.22183 + H + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01740 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-128 reporter+balance reagent N'-acylated histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-128 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-128 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 11 (13)C 4 H 25 (14)N 2 (15)N 1 O 4 + 316.19 + 316.19495 + S + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01741 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-128 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-128 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-128 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 12 (13)C 4 H 27 (14)N 2 (15)N 1 O 4 + 330.21 + 330.2106 + T + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01742 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-128 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-128 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-128 reagent acylated residue. + 1+ + (12)C 6 (13)C 2 H 16 (14)N 1 + 128.13 + 128.13443 + X + artifact + 2,6-dimethyl-1-methylidenepiperidinium + cysTMT6plex-128 reporter fragment + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01743 + + TMT6plex-128 reporter fragment + + + + + The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-128 reagent acylated residue. + PubMed:18688235 + + + + + 2,6-dimethyl-1-methylidenepiperidinium + + + + + + cysTMT6plex-128 reporter fragment + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-129 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + X + artifact + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01744 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-129 reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-129 reporter+balance group. + Unimod:737 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-129 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + X + artifact + N-term + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01745 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-129 reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-129 reporter+balance group. + Unimod:737#N-term + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-129 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 14 (13)C 4 H 32 (14)N 3 (15)N 1 O 3 + 357.26 + 357.2579 + K + artifact + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01746 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-129 reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-129 reporter+balance group. + Unimod:737#K + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-129 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 17 (13)C 4 H 29 (14)N 2 (15)N 1 O 4 + 392.23 + 392.22626 + Y + artifact + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01747 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-129 reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-129 reporter+balance group. + Unimod:737#Y + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-129 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 14 (13)C 4 H 27 (14)N 4 (15)N 1 O 3 + 366.22 + 366.22183 + H + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01748 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-129 reporter+balance reagent N'-acylated histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-129 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-129 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 11 (13)C 4 H 25 (14)N 2 (15)N 1 O 4 + 316.19 + 316.19495 + S + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01749 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-129 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-129 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-129 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 12 (13)C 4 H 27 (14)N 2 (15)N 1 O 4 + 330.21 + 330.2106 + T + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01750 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-129 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-129 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-129 reagent acylated residue. + 1+ + (12)C 5 (13)C 3 H 16 (14)N 1 + 129.14 + 129.13779 + X + artifact + 2,6-dimethyl-1-methylidenepiperidinium + cysTMT6plex-129 reporter fragment + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01751 + + TMT6plex-129 reporter fragment + + + + + The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-129 reagent acylated residue. + PubMed:18688235 + + + + + 2,6-dimethyl-1-methylidenepiperidinium + + + + + + cysTMT6plex-129 reporter fragment + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-130 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + X + artifact + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01752 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-130 reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-130 reporter+balance group. + Unimod:737 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-130 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + X + artifact + N-term + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01753 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-130 reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-130 reporter+balance group. + Unimod:737#N-term + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-130 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 14 (13)C 4 H 32 (14)N 3 (15)N 1 O 3 + 357.26 + 357.2579 + K + artifact + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01754 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-130 reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-130 reporter+balance group. + Unimod:737#K + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-130 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 17 (13)C 4 H 29 (14)N 2 (15)N 1 O 4 + 392.23 + 392.22626 + Y + artifact + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01755 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-130 reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-130 reporter+balance group. + Unimod:737#Y + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-130 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 14 (13)C 4 H 27 (14)N 4 (15)N 1 O 3 + 366.22 + 366.22183 + H + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01756 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-130 reporter+balance reagent N'-acylated histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-130 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-130 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 11 (13)C 4 H 25 (14)N 2 (15)N 1 O 4 + 316.19 + 316.19495 + S + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01757 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-130 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-130 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-130 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 12 (13)C 4 H 27 (14)N 2 (15)N 1 O 4 + 330.21 + 330.2106 + T + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01758 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-130 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-130 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-130 reagent acylated residue. + 1+ + (12)C 4 (13)C 4 H 16 (14)N 1 + 130.14 + 130.14114 + X + artifact + 2,6-dimethyl-1-methylidenepiperidinium + cysTMT6plex-130 reporter fragment + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01759 + + TMT6plex-130 reporter fragment + + + + + The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-130 reagent acylated residue. + PubMed:18688235 + + + + + 2,6-dimethyl-1-methylidenepiperidinium + + + + + + cysTMT6plex-130 reporter fragment + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-131 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + X + artifact + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + cysTMT6plex-131 reporter fragment + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01760 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-131 reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-131 reporter+balance group. + Unimod:737 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + cysTMT6plex-131 reporter fragment + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-131 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + X + artifact + N-term + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01761 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-131 reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-131 reporter+balance group. + Unimod:737#N-term + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-131 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 14 (13)C 4 H 32 (14)N 3 (15)N 1 O 3 + 357.26 + 357.2579 + K + artifact + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01762 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-131 reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-131 reporter+balance group. + Unimod:737#K + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-131 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 17 (13)C 4 H 29 (14)N 2 (15)N 1 O 4 + 392.23 + 392.22626 + Y + artifact + Unimod:737 + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01763 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-131 reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-131 reporter+balance group. + Unimod:737#Y + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-131 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 14 (13)C 4 H 27 (14)N 4 (15)N 1 O 3 + 366.22 + 366.22183 + H + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01764 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-131 reporter+balance reagent N'-acylated histidine + + + + + A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-131 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-131 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 11 (13)C 4 H 25 (14)N 2 (15)N 1 O 4 + 316.19 + 316.19495 + S + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01765 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-131 reporter+balance reagent O3-acylated serine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-131 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-131 reporter+balance group. + 229.16 + (12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2 + 229.16293 + (12)C 12 (13)C 4 H 27 (14)N 2 (15)N 1 O 4 + 330.21 + 330.2106 + T + artifact + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01766 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + TMT6plex-131 reporter+balance reagent O3-acylated threonine + + + + + A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-131 reporter+balance group. + PubMed:18688235 + + + + + 3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-131 reagent acylated residue. + 1+ + (12)C 4 (13)C 4 H 16 (15)N 1 + 131.14 + 131.13818 + X + artifact + 2,6-dimethyl-1-methylidenepiperidinium + PSI-MOD + Sixplex Tandem Mass Tag(TM) + TMT6plex + MOD:01767 + TMT6plex-131 reporter fragment + + + + + The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-131 reagent acylated residue. + PubMed:18688235 + + + + + 2,6-dimethyl-1-methylidenepiperidinium + + + + + + Sixplex Tandem Mass Tag(TM) + + + + + + TMT6plex + + + + + + + + + + + A protein modification that effectively replaces a residue hydroxyl group with a palmitoleyloxy group. + 236.4 + C 16 H 28 N 0 O 1 + 236.21402 + X + natural + PSI-MOD + MOD:01768 + + O-palmitoleylated residue + + + + + A protein modification that effectively replaces a residue hydroxyl group with a palmitoleyloxy group. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-palmitoleyl-L-threonine. + 236.4 + C 16 H 28 N 0 O 1 + 236.21402 + C 20 H 35 N 1 O 3 + 337.5 + 337.2617 + T + natural + Unimod:431 + (2S,3R)-2-amino-3-((Z)-9-hexadecenoyloxy)butanoic acid + L-threonine cis-9-hexadecenoate ester + O-palmitoleylated L-threonine + O3-palmitoleyl-threonine + mod188 + PSI-MOD + Palmitoleyl + palmitoleyl + MOD:01769 + + O-palmitoleyl-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-palmitoleyl-L-threonine. + OMSSA:188 + PubMed:6642431 + PubMed:8413602 + RESID:AA0079#var + Unimod:431#T + + + + + (2S,3R)-2-amino-3-((Z)-9-hexadecenoyloxy)butanoic acid + + + + + + L-threonine cis-9-hexadecenoate ester + + + + + + O-palmitoleylated L-threonine + + + + + + O3-palmitoleyl-threonine + + + + + + mod188 + + + + + + Palmitoleyl + + + + + + palmitoleyl + + + + + + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-palmitoyl-L-threonine amide. + 254.44 + C 16 H 32 N 1 O 1 + 254.24838 + C 20 H 39 N 2 O 3 + 355.54 + 355.29608 + T + natural + C-term + (2S,3R)-2-amino-3-(hexadecanoyloxy)butanamide + OPamThrN + PSI-MOD + MOD:01770 + O-palmitoyl-L-threonine amide + + + + + A protein modification that effectively converts an L-threonine residue to O-palmitoyl-L-threonine amide. + PubMed:8413602 + RESID:AA0079#var + RESID:AA0097#var + + + + + (2S,3R)-2-amino-3-(hexadecanoyloxy)butanamide + + + + + + OPamThrN + + + + + + + + + + + + + + + + The farnesyl cation protein modification reporter fragment produced by fragmentation of some farnesyl modified residues. + 1+ + C 15 H 25 + 205.36 + 205.19508 + X + natural + (2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ylium + Farn+ + farnesyl cation + PSI-MOD + MOD:01771 + + farnesyl reporter fragment + + + + + The farnesyl cation protein modification reporter fragment produced by fragmentation of some farnesyl modified residues. + PubMed:15609361 + PubMed:18688235 + + + + + (2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ylium + + + + + + Farn+ + + + + + + farnesyl cation + + + + + + + + + + + + + + + + The palmityl cation protein modification reporter fragment produced by fragmentation of some palmitoyl modified residues. + 1+ + C 16 H 31 O 1 + 239.42 + 239.23694 + X + natural + Pam+ + PSI-MOD + palmityl cation + MOD:01772 + + palmityl reporter fragment + + + + + The palmityl cation protein modification reporter fragment produced by fragmentation of some palmitoyl modified residues. + PubMed:18688235 + PubMed:8413602 + + + + + Pam+ + + + + + + palmityl cation + + + + + + + + + + + + + + + + + Covalent modification of a trimethyllysine residue with secondary loss of a neutral trimethylamine molecular fragment. + -59.11 + C -3 H -9 N -1 O 0 + -59.074047 + 1+ + C 6 H 10 N 1 O 1 + 112.15 + 112.07569 + MOD:00083 + artifact + dMe3N6Me3+Lys + PSI-MOD + MOD:01773 + + N6,N6,N6-trimethyl-L-lysine with neutral loss of trimethylamine + + + + + Covalent modification of a trimethyllysine residue with secondary loss of a neutral trimethylamine molecular fragment. + PubMed:17205979 + PubMed:18688235 + + + + + dMe3N6Me3+Lys + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-octanoyl-L-lysine. + 126.2 + C 8 H 14 N 0 O 1 + 126.10446 + C 14 H 26 N 2 O 2 + 254.37 + 254.19943 + K + natural + (2S)-2-amino-6-(octanoylamino)hexanoic acid + N(zeta)-octanoyllysine + N6-(1-oxooctyl)-L-lysine + N6-octanoyl-L-lysine + epsilon-octanoyllysine + PSI-MOD + MOD:01774 + + N6-octanoyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-octanoyl-L-lysine. + PubMed:12591875 + PubMed:2215217 + RESID:AA0527 + + + + + (2S)-2-amino-6-(octanoylamino)hexanoic acid + + + + + + N(zeta)-octanoyllysine + + + + + + N6-(1-oxooctyl)-L-lysine + + + + + + N6-octanoyl-L-lysine + + + + + + epsilon-octanoyllysine + + + + + + + + + + A protein modification that effectively converts an L-glutamine residue to 5-glutamyl serotonin. + 159.19 + C 10 H 9 N 1 O 1 + 159.06842 + C 15 H 17 N 3 O 3 + 287.32 + 287.12698 + Q + natural + (2S)-2-amino-5-([2-(5-hydroxy-1H-indol-3-yl)ethyl]amino)-5-oxopentanoic acid + 5-glutamyl serotonin + N2-(gamma-glutamyl)-5-hydoxytryptamine + N5-[2-(5-hydroxy-3-indolyl)ethyl]glutamine + PSI-MOD + MOD:01775 + 5-glutamyl serotonin + + + + + A protein modification that effectively converts an L-glutamine residue to 5-glutamyl serotonin. + PubMed:11805836 + PubMed:14697203 + RESID:AA0528 + + + + + (2S)-2-amino-5-([2-(5-hydroxy-1H-indol-3-yl)ethyl]amino)-5-oxopentanoic acid + + + + + + 5-glutamyl serotonin + + + + + + N2-(gamma-glutamyl)-5-hydoxytryptamine + + + + + + N5-[2-(5-hydroxy-3-indolyl)ethyl]glutamine + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-methylthiocarbonylaminoethylcysteine. + 117.17 + C 4 H 7 N 1 O 1 S 1 + 117.02483 + C 7 H 12 N 2 O 2 S 2 + 220.31 + 220.03403 + C + artifact + (2R)-2-amino-3-([2-([(methylsulfanyl)carbonyl]amino)ethyl]sulfanyl)propanoic acid + L-cysteine N-(methylthiocarbonyl)aziridine adduct + MTCTK + N6-methylthiocarbonyl-4-thialysine + S-[2-([(methylthio)carbonyl]amino)ethyl]-L-cysteine + PSI-MOD + MOD:01776 + This modified residue is a chemical analog of N6-acetyl-L-lysine produced from L-cysteine by methylthiocarbonylaziridine (MTCA, S-methyl aziridine-1-carbothioate). + S-methylthiocarbonylaminoethylcysteine (Cys) + + + + + A protein modification that effectively converts an L-cysteine residue to S-methylthiocarbonylaminoethylcysteine. + PubMed:18688235 + PubMed:20608637 + + + + + (2R)-2-amino-3-([2-([(methylsulfanyl)carbonyl]amino)ethyl]sulfanyl)propanoic acid + + + + + + L-cysteine N-(methylthiocarbonyl)aziridine adduct + + + + + + MTCTK + + + + + + N6-methylthiocarbonyl-4-thialysine + + + + + + S-[2-([(methylthio)carbonyl]amino)ethyl]-L-cysteine + + + + + + + + + + A protein modification that effectively converts a C-terminal glycine residue to S-(glycyl)-L-cysteine by forming a thioester bond with a free L-cysteine. + 103.14 + C 3 H 5 N 1 O 1 S 1 + 103.009186 + C 5 H 9 N 2 O 3 S 1 + 177.2 + 177.03339 + G + natural + C-term + (2R)-2-amino-3-[(aminoacetyl)sulfanyl]propanoic acid + 1-(cystein-S-yl)-glycinate + MOD_RES CysO-cysteine adduct + S-(2-amino-1-oxoethyl)cysteine + S-(glycyl)-L-cysteine + glycine cysteine thioester + PSI-MOD + MOD:01777 + This is not the cross-linking of two peptides, but the modification of a C-terminal glycine by formation of an thioester bond with a free cysteine. For the cross-linking of two peptide see MOD:00211 [JSG]. + S-(glycyl)-L-cysteine (Gly) + + + + + A protein modification that effectively converts a C-terminal glycine residue to S-(glycyl)-L-cysteine by forming a thioester bond with a free L-cysteine. + ChEBI:22050 + PubMed:17726030 + PubMed:18359941 + PubMed:18771296 + PubMed:18799456 + PubMed:18842002 + PubMed:3306404 + RESID:AA0206 + + + + + (2R)-2-amino-3-[(aminoacetyl)sulfanyl]propanoic acid + + + + + + 1-(cystein-S-yl)-glycinate + + + + + + MOD_RES CysO-cysteine adduct + + + + + + S-(2-amino-1-oxoethyl)cysteine + + + + + + S-(glycyl)-L-cysteine + + + + + + glycine cysteine thioester + + + + + + + + + + A protein modification that effectively converts a C-terminal glycine residue to N-(glycyl)-L-cysteine by forming a peptide bond with a free L-cysteine. + 103.14 + C 3 H 5 N 1 O 1 S 1 + 103.009186 + C 5 H 9 N 2 O 3 S 1 + 177.2 + 177.03339 + G + hypothetical + C-term + uniprot.ptm:PTM-0433 + (2R)-2-[(aminoacetyl)amino]-3-sulfanylpropanoic acid + MOD_RES CysO-cysteine adduct + N-(2-amino-1-oxoethyl)cysteine + N-(glycyl)-L-cysteine + PSI-MOD + MOD:01778 + N-(glycyl)-L-cysteine + + + + + A protein modification that effectively converts a C-terminal glycine residue to N-(glycyl)-L-cysteine by forming a peptide bond with a free L-cysteine. + PubMed:18771296 + PubMed:18799456 + PubMed:18842002 + RESID:AA0529 + + + + + (2R)-2-[(aminoacetyl)amino]-3-sulfanylpropanoic acid + + + + + + MOD_RES CysO-cysteine adduct + + + + + + N-(2-amino-1-oxoethyl)cysteine + + + + + + N-(glycyl)-L-cysteine + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-(L-lysyl)-L-lysine by formation of an isopeptide bond between the carboxyl group of a free lysine and the N6-amino group of the peptidyl L-lysine. + 128.18 + C 6 H 12 N 2 O 1 + 128.09496 + C 12 H 24 N 4 O 2 + 256.35 + 256.1899 + K + natural + (2S)-2-amino-6-([(2S)-2,6-diaminohexanoyl]amino)hexanoic acid + N6-(L-lysyl)-L-lysine + N6-(alpha-lysyl)-lysine + PSI-MOD + MOD:01779 + This is not the cross-linking of two peptides, but the modification of a peptidyl lysine by formation of an isopeptide bond with a free lysine [JSG]. + N6-(L-lysyl)-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-(L-lysyl)-L-lysine by formation of an isopeptide bond between the carboxyl group of a free lysine and the N6-amino group of the peptidyl L-lysine. + PubMed:18201202 + PubMed:20729861 + RESID:AA0530 + + + + + (2S)-2-amino-6-([(2S)-2,6-diaminohexanoyl]amino)hexanoic acid + + + + + + N6-(L-lysyl)-L-lysine + + + + + + N6-(alpha-lysyl)-lysine + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-(beta-lysyl)-L-5-hydroxylysine by formation of an isopeptide bond between the carboxyl group of a free beta-lysine and the N6-amino group of a peptidyl L-lysine. + 144.17 + C 6 H 12 N 2 O 2 + 144.08987 + C 12 H 24 N 4 O 3 + 272.35 + 272.18484 + K + hypothetical + uniprot.ptm:PTM-0474 + (2S)-2-amino-6-([(3R)-3,6-diaminohexanoyl]amino)-5-hydroxyhexanoic acid + 5-hydroxy-N6-(beta-lysyl)-L-lysine + 5-hydroxy-N6-[(3R)-beta-lysyl]lysine + EF-P lysine derivative + MOD_RES N6-(3,6-diaminohexanoyl)-5-hydroxylysine + N6-[(3R)-3,6-diaminohexanoyl]-L-5-hydroxylysine + lysyl spermidine derivative [misidentification] + PSI-MOD + MOD:01780 + N6-(beta-lysyl)-L-5-hydroxylysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-(beta-lysyl)-L-5-hydroxylysine by formation of an isopeptide bond between the carboxyl group of a free beta-lysine and the N6-amino group of a peptidyl L-lysine. + PubMed:18201202 + PubMed:20729861 + RESID:AA0531 + + + + + (2S)-2-amino-6-([(3R)-3,6-diaminohexanoyl]amino)-5-hydroxyhexanoic acid + + + + + + 5-hydroxy-N6-(beta-lysyl)-L-lysine + + + + + + 5-hydroxy-N6-[(3R)-beta-lysyl]lysine + + + + + + EF-P lysine derivative + + + + + + MOD_RES N6-(3,6-diaminohexanoyl)-5-hydroxylysine + + + + + + N6-[(3R)-3,6-diaminohexanoyl]-L-5-hydroxylysine + + + + + + lysyl spermidine derivative [misidentification] + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-butanoyl-L-lysine. + 70.09 + C 4 H 6 N 0 O 1 + 70.04186 + C 10 H 18 N 2 O 2 + 198.27 + 198.13683 + K + hypothetical + Unimod:1289 + uniprot.ptm:PTM-0637 + (2S)-2-amino-6-(butanoylamino)hexanoic acid + (2S)-2-azanyl-6-(butanoylamino)hexanoic acid + 2-amino-6-butyrylaminocaproic acid + MOD_RES N6-butyryllysine + N(zeta)-butanoyllysine + N6-(1-oxobutyl)-L-lysine + N6-butanoyl-L-lysine + N6-butyryllysine + epsilon-butanoyl-L-lysine + epsilon-butyryl-L-lysine + PSI-MOD + MOD:01781 + The binding of histone peptides with butanoylated lysine to nuclear bromodomain proteins is non-specific and weaker than binding to the corresponding acetylated lysine peptides [JSG]. + N6-butanoyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-butanoyl-L-lysine. + PubMed:17267393 + PubMed:20715035 + RESID:AA0532 + Unimod:1289 + + + + + (2S)-2-amino-6-(butanoylamino)hexanoic acid + + + + + + (2S)-2-azanyl-6-(butanoylamino)hexanoic acid + + + + + + 2-amino-6-butyrylaminocaproic acid + + + + + + MOD_RES N6-butyryllysine + + + + + + N(zeta)-butanoyllysine + + + + + + N6-(1-oxobutyl)-L-lysine + + + + + + N6-butanoyl-L-lysine + + + + + + N6-butyryllysine + + + + + + epsilon-butanoyl-L-lysine + + + + + + epsilon-butyryl-L-lysine + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to N-methyl-L-serine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 4 H 7 N 1 O 2 + 101.1 + 101.047676 + S + natural + uniprot.ptm:PTM-0432 + (2S)-3-hydroxy-2-(methylamino)propanoic acid + MOD_RES N-methylserine + N-methyl-L-serine + N-methylserine + PSI-MOD + MOD:01782 + + N-methyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to N-methyl-L-serine. + PubMed:20668449 + RESID:AA0533 + + + + + (2S)-3-hydroxy-2-(methylamino)propanoic acid + + + + + + MOD_RES N-methylserine + + + + + + N-methyl-L-serine + + + + + + N-methylserine + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to N,N-dimethyl-L-serine. + 28.05 + C 2 H 4 N 0 O 0 + 28.0313 + C 5 H 10 N 1 O 2 + 116.14 + 116.07115 + S + natural + N-term + uniprot.ptm:PTM-0431 + (2S)-2-(dimethylamino)propanoic acid + MOD_RES N,N-dimethylserine + N,N-dimethyl-L-serine + N,N-dimethylserine + PSI-MOD + MOD:01783 + N,N-dimethyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to N,N-dimethyl-L-serine. + PubMed:20668449 + RESID:AA0534 + + + + + (2S)-2-(dimethylamino)propanoic acid + + + + + + MOD_RES N,N-dimethylserine + + + + + + N,N-dimethyl-L-serine + + + + + + N,N-dimethylserine + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to N,N,N-trimethyl-L-serine. + 43.09 + C 3 H 7 N 0 O 0 + 43.054226 + 1+ + C 6 H 13 N 1 O 2 + 131.17 + 131.09409 + S + natural + N-term + uniprot.ptm:PTM-0430 + (1S)-1-carboxy-2-hydroxy-N,N,N-trimethylethanaminium + (1S)-1-carboxy-2-hydroxy-N,N,N-trimethylethanazanium + (2S)-2-trimethylammonio-3-hydroxypropanoic acid + MOD_RES N,N,N-trimethylserine + N,N,N-trimethyl-L-serine + N,N,N-trimethylserine cation + N,N,N-trimethylserinium + PSI-MOD + MOD:01784 + + N,N,N-trimethyl-L-serine + + + + + A protein modification that effectively converts an L-serine residue to N,N,N-trimethyl-L-serine. + PubMed:20668449 + PubMed:3979397 + RESID:AA0535 + + + + + (1S)-1-carboxy-2-hydroxy-N,N,N-trimethylethanaminium + + + + + + (1S)-1-carboxy-2-hydroxy-N,N,N-trimethylethanazanium + + + + + + (2S)-2-trimethylammonio-3-hydroxypropanoic acid + + + + + + MOD_RES N,N,N-trimethylserine + + + + + + N,N,N-trimethyl-L-serine + + + + + + N,N,N-trimethylserine cation + + + + + + N,N,N-trimethylserinium + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-(L-isoglutamyl)-L-threonine, using free L-glutamine and releasing ammonia. + 129.12 + C 5 H 7 N 1 O 3 + 129.04259 + C 9 H 14 N 2 O 5 + 230.22 + 230.09027 + T + hypothetical + (2S)-2-amino-5-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-5-oxopentanoic acid + (2S,3R)-2-amino-3-([(4S)-4-amino-4-carboxybutanoyl]oxy)-propanoic acid + 5-(threon-O3-yl)glutamate + O(beta)-(gamma-glutamyl)threonine + O-(L-isoglutamyl)-L-threonine + O3-(isoglutamyl)threonine + PSI-MOD + MOD:01785 + This is not an ester cross-link of peptides [JSG]. + O-(L-isoglutamyl)-L-threonine (active site intermediate) + + + + + A protein modification that effectively converts an L-threonine residue to O-(L-isoglutamyl)-L-threonine, using free L-glutamine and releasing ammonia. + PubMed:8706862 + RESID:AA0536#THR + + + + + (2S)-2-amino-5-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-5-oxopentanoic acid + + + + + + (2S,3R)-2-amino-3-([(4S)-4-amino-4-carboxybutanoyl]oxy)-propanoic acid + + + + + + 5-(threon-O3-yl)glutamate + + + + + + O(beta)-(gamma-glutamyl)threonine + + + + + + O-(L-isoglutamyl)-L-threonine + + + + + + O3-(isoglutamyl)threonine + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to 3'-nitro-L-tyrosine. + 45.0 + C 0 H -1 N 1 O 2 + 44.985077 + C 9 H 8 N 2 O 4 + 208.17 + 208.0484 + Y + natural + uniprot.ptm:PTM-0434 + (2S)-2-amino-3-(4-hydroxy-3-nitrophenyl)propanoic acid + 3'-nitro-L-tyrosine + 3-nitro-L-tyrosine + 3-nitrotyrosine + MOD_RES 3'-Nitrotyrosine + m-nitrotyrosine + meta-nitrotyrosine + PSI-MOD + MOD:01786 + + 3'-nitro-L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to 3'-nitro-L-tyrosine. + ChEBI:44454 + PubMed:16944230 + PubMed:5339594 + RESID:AA0537 + + + + + (2S)-2-amino-3-(4-hydroxy-3-nitrophenyl)propanoic acid + + + + + + 3'-nitro-L-tyrosine + + + + + + 3-nitro-L-tyrosine + + + + + + 3-nitrotyrosine + + + + + + MOD_RES 3'-Nitrotyrosine + + + + + + m-nitrotyrosine + + + + + + meta-nitrotyrosine + + + + + + + + + + + A protein modification that effectively cross-links two L-tyrosine residues through their 5' positions by amine nitrogen to form 5'-(L-tyros-5'-yl)amino-L-tyrosine. + 13.0 + C 0 H -1 N 1 O 0 + 12.995249 + C 18 H 17 N 3 O 4 + 339.35 + 339.12192 + Y, Y + hypothetical + uniprot.ptm:PTM-0320 + (2S,2'S)-3,3'-[iminobis(4-hydroxybenzene-3,1-diyl)]bis(2-aminopropanoic acid) + 5'-(L-tyros-5'-yl)amino-L-tyrosine + 5'-[(tyros-5'-yl)amino]tyrosine + 5'-tyrosyl-5'-aminotyrosine + CROSSLNK 5'-tyrosyl-5'-aminotyrosine (Tyr-Tyr) (interchain) + bis(LTQ) linkage + PSI-MOD + MOD:01787 + Cross-link 2. + 5'-(L-tyros-5'-yl)amino-L-tyrosine + + + + + A protein modification that effectively cross-links two L-tyrosine residues through their 5' positions by amine nitrogen to form 5'-(L-tyros-5'-yl)amino-L-tyrosine. + PubMed:18781570 + RESID:AA0459 + + + + + (2S,2'S)-3,3'-[iminobis(4-hydroxybenzene-3,1-diyl)]bis(2-aminopropanoic acid) + + + + + + 5'-(L-tyros-5'-yl)amino-L-tyrosine + + + + + + 5'-[(tyros-5'-yl)amino]tyrosine + + + + + + 5'-tyrosyl-5'-aminotyrosine + + + + + + CROSSLNK 5'-tyrosyl-5'-aminotyrosine (Tyr-Tyr) (interchain) + + + + + + bis(LTQ) linkage + + + + + + + + + + + A protein modification that effectively converts an N-terminal L-histidine residue to histidine immonium ion. + -27.0 + C -1 H 1 N 0 O -1 + -26.987638 + 1+ + C 5 H 8 N 3 O 0 + 110.14 + 110.07127 + H + artifact + 2-(1H-imidazolyl)ethaniminium + PSI-MOD + MOD:01788 + + This fragment corresponds to the first ion in an a+ series. + histidine immonium ion + + + + + A protein modification that effectively converts an N-terminal L-histidine residue to histidine immonium ion. + PubMed:17074506 + PubMed:18688235 + + + + + 2-(1H-imidazolyl)ethaniminium + + + + + + + + + + + A protein modification that effectively converts an N-terminal L-phenylalanine residue to phenylalanine immonium ion. + -27.0 + C -1 H 1 N 0 O -1 + -26.987638 + 1+ + C 8 H 10 N 1 O 0 + 120.17 + 120.08077 + F + artifact + 2-phenylethaniminium + PSI-MOD + MOD:01789 + + This fragment corresponds to the first ion in an a+ series. + phenylalanine immonium ion + + + + + A protein modification that effectively converts an N-terminal L-phenylalanine residue to phenylalanine immonium ion. + PubMed:17074506 + PubMed:18688235 + + + + + 2-phenylethaniminium + + + + + + + + + + + A protein modification that effectively converts an an N-terminal L-tyrosine residue to tyrosine immonium ion. + -27.0 + C -1 H 1 N 0 O -1 + -26.987638 + 1+ + C 8 H 10 N 1 O 1 + 136.17 + 136.07568 + Y + artifact + 2-(4-hydroxyphenyl)ethaniminium + PSI-MOD + MOD:01790 + + This fragment corresponds to the first ion in an a+ series. + tyrosine immonium ion + + + + + A protein modification that effectively converts an an N-terminal L-tyrosine residue to tyrosine immonium ion. + PubMed:17074506 + PubMed:18688235 + + + + + 2-(4-hydroxyphenyl)ethaniminium + + + + + + + + + + + + + + + + + A protein modification that effectively converts an N-terminal phosphohistidine residue to phosphohistidine immonium ion. + -27.0 + C -1 H 1 N 0 O -1 + -26.987638 + 1+ + C 5 H 9 N 3 O 3 P 1 + 190.12 + 190.0376 + MOD:00890 + artifact + 2-(1H-imidazolyl)ethaniminium + PSI-MOD + MOD:01791 + + This fragment corresponds to the first ion in an a+ series. + phosphohistidine immonium ion + + + + + A protein modification that effectively converts an N-terminal phosphohistidine residue to phosphohistidine immonium ion. + PubMed:17690871 + PubMed:18688235 + PubMed:20847263 + + + + + 2-(1H-imidazolyl)ethaniminium + + + + + + + + + + + + + + + + + A protein modification that effectively converts an N-terminal O4'-phospho-L-tyrosine residue to tyrosine immonium ion. + -27.0 + C -1 H 1 N 0 O -1 + -26.987638 + 1+ + C 8 H 11 N 1 O 4 P 1 + 216.15 + 216.04202 + MOD:00048 + artifact + 2-(4-phosphonoxyphenyl)ethaniminium + PSI-MOD + MOD:01792 + + This fragment corresponds to the first ion in an a+ series. + phosphotyrosine immonium ion + + + + + A protein modification that effectively converts an N-terminal O4'-phospho-L-tyrosine residue to tyrosine immonium ion. + PubMed:17690871 + PubMed:18688235 + + + + + 2-(4-phosphonoxyphenyl)ethaniminium + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine sulfoxide. + 73.05 + C 2 H 3 N 1 O 2 + 73.01638 + C 5 H 8 N 2 O 3 S 1 + 176.19 + 176.02556 + C + artifact + CamCO + S-carbamoylmethyl-L-cysteine sulfoxide + PSI-MOD + MOD:01793 + S-carboxamidomethyl-L-cysteine sulfoxide + + + + + A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine sulfoxide. + PubMed:11212008 + PubMed:17689096 + PubMed:18306178 + PubMed:18688235 + + + + + CamCO + + + + + + S-carbamoylmethyl-L-cysteine sulfoxide + + + + + + + + + + + A protein modification that effectively replaces the methyl group of a residue containing common isotopes with a 1x(13)C,3x(2)H labeled monomethylated residue. + 18.04 + (13)C 1 (1)H -1 (2)H 3 + 18.037834 + X + artifact + PSI-MOD + Methyl:2H(3)13C(1) + MOD:01794 + 1x(13)C,3x(2)H labeled monomethylated residue + + + + + A protein modification that effectively replaces the methyl group of a residue containing common isotopes with a 1x(13)C,3x(2)H labeled monomethylated residue. + PubMed:18688235 + + + + + Methyl:2H(3)13C(1) + + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue containing common isotopes to 1x(13)C,3x(2)H C(6)-labeled L-methionine. + 4.02 + (12)C -1 (13)C 1 (1)H -3 (2)H 3 + 4.022185 + (12)C 4 (13)C 1 (1)H 6 (2)H 3 N 1 O 1 S 1 + 135.06 + 135.06267 + M + artifact + PSI-MOD + Methyl:2H(3)13C(1) + MOD:01795 + 1x(13)C,3x(2)H C(6)-labeled L-methionine + + + + + A protein modification that effectively converts an L-methionine residue containing common isotopes to 1x(13)C,3x(2)H C(6)-labeled L-methionine. + PubMed:15782174 + PubMed:18688235 + + + + + Methyl:2H(3)13C(1) + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue containing common isotopes to 1x(13)C,3x(2)H C(6)-labeled L-methionine sulfoxide. + 20.02 + (12)C -1 (13)C 1 (1)H -3 (2)H 3 O 1 + 20.0171 + (12)C 4 (13)C 1 (1)H 6 (2)H 3 N 1 O 2 S 1 + 151.06 + 151.05759 + M + artifact + PSI-MOD + MOD:01796 + 1x(13)C,3x(2)H C(6)-labeled L-methionine sulfoxide + + + + + A protein modification that effectively converts an L-methionine residue containing common isotopes to 1x(13)C,3x(2)H C(6)-labeled L-methionine sulfoxide. + PubMed:15782174 + PubMed:18688235 + + + + + + + + + + + + + + + A protein modification that effectively converts an N-terminal 1'-phosphohistidine residue to 1'-phosphohistidine immonium ion. + -27.0 + C -1 H 1 N 0 O -1 + -26.987638 + 1+ + C 5 H 9 N 3 O 3 P 1 + 190.12 + 190.0376 + MOD:00044 + artifact + 2-((1-phosphono-1H-imidazol-4-yl)ethaniminium + Ntau-phosphorylated L-histidine + PSI-MOD + MOD:01797 + This fragment corresponds to the first ion in an a+ series. + 1'-phosphohistidine immonium ion + + + + + A protein modification that effectively converts an N-terminal 1'-phosphohistidine residue to 1'-phosphohistidine immonium ion. + PubMed:17690871 + PubMed:18688235 + PubMed:20847263 + + + + + 2-((1-phosphono-1H-imidazol-4-yl)ethaniminium + + + + + + Ntau-phosphorylated L-histidine + + + + + + + + + + + + + + + + A protein modification that effectively converts an N-terminal 3'-phosphohistidine residue to 3'-phosphohistidine immonium ion. + -27.0 + C -1 H 1 N 0 O -1 + -26.987638 + 1+ + C 5 H 9 N 3 O 3 P 1 + 190.12 + 190.0376 + MOD:00045 + artifact + 2-(1-phosphono-1H-imidazol-5-yl)ethaniminium + Npi-phosphorylated L-histidine + PSI-MOD + MOD:01798 + This fragment corresponds to the first ion in an a+ series. + 3'-phosphohistidine immonium ion + + + + + A protein modification that effectively converts an N-terminal 3'-phosphohistidine residue to 3'-phosphohistidine immonium ion. + PubMed:18688235 + + + + + 2-(1-phosphono-1H-imidazol-5-yl)ethaniminium + + + + + + Npi-phosphorylated L-histidine + + + + + + + + + + + A protein modification that effectively converts an L-alanine residue to a methylated serine, such as N-methylserine, N,N-dimethylserine, or N,N,N-trimethylserine. + S + MeSer + PSI-MOD + MOD:01799 + + methylated serine + + + + + A protein modification that effectively converts an L-alanine residue to a methylated serine, such as N-methylserine, N,N-dimethylserine, or N,N,N-trimethylserine. + PubMed:18688235 + + + + + MeSer + + + + + + + + + + + A protein modification that effectively replaces an L-serine alpha amino hydrogen with a methyl group. + S + natural + N-term + PSI-MOD + MOD:01800 + + N-methylated serine + + + + + A protein modification that effectively replaces an L-serine alpha amino hydrogen with a methyl group. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively converts an L-serine residue to an L-serinium (protonated L-serine). + 1.01 + C 0 H 1 N 0 O 0 + 1.007276 + 1+ + C 3 H 7 N 1 O 2 + 89.09 + 89.04713 + S + natural + N-term + PSI-MOD + MOD:01801 + + protonated L-serine (L-serinium) residue + + + + + A protein modification that effectively converts an L-serine residue to an L-serinium (protonated L-serine). + PubMed:18688235 + + + + + + + + + + + + + + + A protein modification that effectively converts an L-serinium (protonated L-serine) residue to an N,N,N-trimethyl-L-serine. + 42.08 + C 3 H 6 N 0 O 0 + 42.046402 + 1+ + C 6 H 13 N 1 O 2 + 131.17 + 131.09409 + MOD:01801 + natural + N-term + N2Me3Ala + PSI-MOD + MOD:01802 + + For amino acids residues, amine trimethylation can effectively only be accomplished with an aminium, protonated primary amino, group. This process accounts only for trimethylation and not protonation. The alternative N2Me3+Ser process (MOD:00071) accounts for both protonation and trimethylation. + N,N,N-trimethyl-L-serine (from L-serinium) + + + + + A protein modification that effectively converts an L-serinium (protonated L-serine) residue to an N,N,N-trimethyl-L-serine. + PubMed:18688235 + + + + + N2Me3Ala + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to a methylated threonine, such as O-methyl-L-threonine or L-threonine methyl ester. + T + natural + OMeThr + PSI-MOD + MOD:01803 + O-methylated threonine + + + + + A protein modification that effectively converts an L-threonine residue to a methylated threonine, such as O-methyl-L-threonine or L-threonine methyl ester. + PubMed:18688235 + + + + + OMeThr + + + + + + + + + + + A protein modification that effectively results from forming an adduct with a glycosylphosphate through a phosphodiester bond. + PSI-MOD + MOD:01804 + glycosylphosphorylated residue + + + + + A protein modification that effectively results from forming an adduct with a glycosylphosphate through a phosphodiester bond. + PubMed:18688235 + + + + + + + + + + + A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue by an isopeptide bond with formation of N-(L-isoaspartyl)-glycine and the release of water. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 6 H 7 N 2 O 3 + 155.13 + 155.04567 + D, G + natural + N-term + uniprot.ptm:PTM-0490 + (2S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid + 2-amino-N4-(carboxymethyl)-butanediamic acid + CROSSLNK Isoaspartyl glycine isopeptide (Asp-Gly) + CROSSLNK Isoaspartyl glycine isopeptide (Gly-Asp) + N-(L-isoaspartyl)-glycine + N-beta-aspartylglycine + N4-(carboxymethyl)-asparagine + isoaspartyl glycine + PSI-MOD + MOD:01805 + Cross-link 2. + N-(L-isoaspartyl)-glycine (Asp) + + + + + A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue by an isopeptide bond with formation of N-(L-isoaspartyl)-glycine and the release of water. + ChEBI:21479 + PubMed:1826288 + PubMed:18671394 + RESID:AA0126 + + + + + (2S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid + + + + + + 2-amino-N4-(carboxymethyl)-butanediamic acid + + + + + + CROSSLNK Isoaspartyl glycine isopeptide (Asp-Gly) + + + + + + CROSSLNK Isoaspartyl glycine isopeptide (Gly-Asp) + + + + + + N-(L-isoaspartyl)-glycine + + + + + + N-beta-aspartylglycine + + + + + + N4-(carboxymethyl)-asparagine + + + + + + isoaspartyl glycine + + + + + + + + + + + A protein modification that effectively converts an L-leucine residue to N,N-dimethyl-L-leucine. + 28.05 + C 2 H 4 N 0 O 0 + 28.0313 + C 8 H 16 N 1 O 1 + 142.22 + 142.12318 + L + hypothetical + N-term + uniprot.ptm:PTM-0435 + (2S)-2-(dimethylamino)-4-methylpentanoic acid + 2-(dimethylamino)-4-methylvaleric acid + 2-(dimethylazanyl)-4-methylpentanoic acid + MOD_RES N,N-dimethylleucine + N,N-dimethyl-L-leucine + N,N-dimethylleucine + PSI-MOD + MOD:01806 + N,N-dimethyl-L-leucine + + + + + A protein modification that effectively converts an L-leucine residue to N,N-dimethyl-L-leucine. + PubMed:19522542 + RESID:AA0538 + + + + + (2S)-2-(dimethylamino)-4-methylpentanoic acid + + + + + + 2-(dimethylamino)-4-methylvaleric acid + + + + + + 2-(dimethylazanyl)-4-methylpentanoic acid + + + + + + MOD_RES N,N-dimethylleucine + + + + + + N,N-dimethyl-L-leucine + + + + + + N,N-dimethylleucine + + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to N-formyl-L-glutamic acid. + 28.01 + C 1 H 0 N 0 O 1 + 27.994915 + C 6 H 8 N 1 O 4 + 158.13 + 158.04533 + E + artifact + N-term + (2S)-2-(formylamino)pentanedioic acid + 2-(formylazanyl)pentanedioic acid + 2-formamidopentanedioic acid + 2-formylaminopentanedioic acid + N-formyl-L-glutamic acid + PSI-MOD + MOD:01807 + N-formyl-L-glutamic acid + + + + + A protein modification that effectively converts an L-glutamic acid residue to N-formyl-L-glutamic acid. + PubMed:18001127 + RESID:AA0539 + + + + + (2S)-2-(formylamino)pentanedioic acid + + + + + + 2-(formylazanyl)pentanedioic acid + + + + + + 2-formamidopentanedioic acid + + + + + + 2-formylaminopentanedioic acid + + + + + + N-formyl-L-glutamic acid + + + + + + + + + + + A protein modification that effectively replaces an L-leucine alpha amino hydrogen with a methyl group. + L + MeLeu + PSI-MOD + MOD:01808 + + N-methylated leucine + + + + + A protein modification that effectively replaces an L-leucine alpha amino hydrogen with a methyl group. + PubMed:18688235 + + + + + MeLeu + + + + + + + + + + + A protein modification that effectively converts a residue containing common isotopes to a 5x(13)C,1x(15)N labeled residue. + 6.01 + (12)C -5 (13)C 5 (14)N -1 (15)N 1 + 6.013809 + X + artifact + Unimod:268 + PSI-MOD + 13C(5) 15N(1) Silac label + Label:13C(5)15N(1) + MOD:01809 + 5x(13)C,1x(15)N labeled residue + + + + + A protein modification that effectively converts a residue containing common isotopes to a 5x(13)C,1x(15)N labeled residue. + PubMed:12771378 + Unimod:268 + + + + + 13C(5) 15N(1) Silac label + + + + + + Label:13C(5)15N(1) + + + + + + + + + + + A protein modification that effectively converts an L-proline residue to 5x(13)C,1x(15)N labeled L-proline. + 6.01 + (12)C -5 (13)C 5 (14)N -1 (15)N 1 + 6.013809 + (13)C 5 H 7 (15)N 1 O 1 + 103.07 + 103.066574 + P + artifact + Unimod:268 + PSI-MOD + 13C(5) 15N(1) Silac label + Label:13C(5)15N(1) + MOD:01810 + 5x(13)C,1x(15)N labeled L-proline + + + + + A protein modification that effectively converts an L-proline residue to 5x(13)C,1x(15)N labeled L-proline. + PubMed:12771378 + Unimod:268#P + + + + + 13C(5) 15N(1) Silac label + + + + + + Label:13C(5)15N(1) + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to 5x(13)C,1x(15)N labeled L-methionine. + 6.01 + (12)C -5 (13)C 5 (14)N -1 (15)N 1 + 6.013809 + (13)C 5 H 9 (15)N 1 O 1 S 1 + 137.05 + 137.05429 + M + artifact + Unimod:268 + PSI-MOD + 13C(5) 15N(1) Silac label + Label:13C(5)15N(1) + MOD:01811 + 5x(13)C,1x(15)N labeled L-methionine + + + + + A protein modification that effectively converts an L-methionine residue to 5x(13)C,1x(15)N labeled L-methionine. + PubMed:12771378 + Unimod:268#M + + + + + 13C(5) 15N(1) Silac label + + + + + + Label:13C(5)15N(1) + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to 5x(13)C,1x(15)N labeled L-methionine sulfoxide. + 6.01 + (12)C -5 (13)C 5 (14)N -1 (15)N 1 + 6.013809 + (13)C 5 H 9 (15)N 1 O 2 S 1 + 153.05 + 153.04921 + M + artifact + Unimod:268 + PSI-MOD + 13C(5) 15N(1) Silac label + Label:13C(5)15N(1) + MOD:01812 + 5x(13)C,1x(15)N labeled L-methionine sulfoxide + + + + + A protein modification that effectively converts an L-methionine residue to 5x(13)C,1x(15)N labeled L-methionine sulfoxide. + PubMed:12771378 + Unimod:268#M + + + + + 13C(5) 15N(1) Silac label + + + + + + Label:13C(5)15N(1) + + + + + + + + + + + A protein modification that effectively substitutes a morpholine-2-acetyl group for a hydrogen atom. + 127.14 + C 6 H 9 N 1 O 2 + 127.06333 + X + artifact + Unimod:29 + N-succinimidylmorpholine-2-acetate derivative + PSI-MOD + N-Succinimidyl-2-morpholine acetate + SMA + MOD:01813 + The Unimod name "N-Succinimidyl-3-morpholine acetate" appears to have been a typographical error [JSG]. + morpholine-2-acetylated residue + + + + + A protein modification that effectively substitutes a morpholine-2-acetyl group for a hydrogen atom. + PubMed:10446193 + Unimod:29 + + + + + N-succinimidylmorpholine-2-acetate derivative + + + + + + N-Succinimidyl-2-morpholine acetate + + + + + + SMA + + + + + + + + + + + + A protein modification that effectively cross-links a cysteine and two serine residues to form L-cysteine 3-hydroxy-2,5-pyridinedicarboxylic acid. + -54.07 + C 0 H -8 N -1 O -2 S 0 + -54.055504 + C 9 H 7 N 2 O 3 S 1 + 223.23 + 223.01773 + C, S, S + natural + uniprot.ptm:PTM-0454 + 6-[(1R)-1-amino-2-sulfanylethyl]-3-hydroxypyridine-2,5-dicarboxylic acid + 6-[1-azanyl-2-sulfanylethyl]-3-hydroxypyridine-2,5-dicarboxylic acid + L-cysteine 3-hydroxy-2,5-pyridinedicarboxylic acid + PSI-MOD + CROSSLNK 3-hydroxypyridine-2,5-dicarboxylic acid (Ser-Cys) + MOD:01814 + Cross-link 3. + L-cysteine 3-hydroxy-2,5-pyridinedicarboxylic acid + + + + + A protein modification that effectively cross-links a cysteine and two serine residues to form L-cysteine 3-hydroxy-2,5-pyridinedicarboxylic acid. + PubMed:18406324 + PubMed:19678698 + PubMed:893891 + RESID:AA0540 + + + + + 6-[(1R)-1-amino-2-sulfanylethyl]-3-hydroxypyridine-2,5-dicarboxylic acid + + + + + + 6-[1-azanyl-2-sulfanylethyl]-3-hydroxypyridine-2,5-dicarboxylic acid + + + + + + L-cysteine 3-hydroxy-2,5-pyridinedicarboxylic acid + + + + + + CROSSLNK 3-hydroxypyridine-2,5-dicarboxylic acid (Ser-Cys) + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-glutamic acid residue to form L-glutamate thiazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 S 0 + -20.026215 + C 8 H 8 N 2 O 3 S 1 + 212.22 + 212.02556 + C, E + natural + uniprot.ptm:PTM-0456 + 2-[(1S)-1-amino-3-carboxypropyl]-1,3-thiazole-4-carboxylic acid + 2-[-1-azanyl-3-carboxypropyl]-1,3-thiazole-4-carboxylic acid + CROSSLNK Thiazole-4-carboxylic acid (Glu-Cys) + L-glutamate thiazole-4-carboxylic acid + PSI-MOD + MOD:01815 + Cross-link 2. + L-glutamate thiazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-glutamic acid residue to form L-glutamate thiazole-4-carboxylic acid. + PubMed:18406324 + PubMed:19678698 + PubMed:893891 + RESID:AA0541 + + + + + 2-[(1S)-1-amino-3-carboxypropyl]-1,3-thiazole-4-carboxylic acid + + + + + + 2-[-1-azanyl-3-carboxypropyl]-1,3-thiazole-4-carboxylic acid + + + + + + CROSSLNK Thiazole-4-carboxylic acid (Glu-Cys) + + + + + + L-glutamate thiazole-4-carboxylic acid + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to a 2'-hydroxy-L-tryptophan. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 11 H 10 N 2 O 2 + 202.21 + 202.07423 + W + artifact + (2S)-2-amino-3-(2-hydroxy-1H-indol-3-yl)propanoic acid + 2'-hydroxy-L-tryptophan + 2-azanyl-3-(2-hydroxy-1H-indol-3-yl)propanoic acid + 2-hydroxy-L-tryptophan + 2-hydroxy-tryptophan + PSI-MOD + MOD:01816 + 2'-hydroxy-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to a 2'-hydroxy-L-tryptophan. + PubMed:11714714 + RESID:AA0542 + + + + + (2S)-2-amino-3-(2-hydroxy-1H-indol-3-yl)propanoic acid + + + + + + 2'-hydroxy-L-tryptophan + + + + + + 2-azanyl-3-(2-hydroxy-1H-indol-3-yl)propanoic acid + + + + + + 2-hydroxy-L-tryptophan + + + + + + 2-hydroxy-tryptophan + + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to a 2'-oxo-L-tryptophan. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 11 H 10 N 2 O 2 + 202.21 + 202.07423 + W + artifact + (2S)-2-amino-3-[(3S)-2-oxo-2,3-dihydro-1H-indol-3-yl]propanoic acid + 2'-oxo-L-tryptophan + 2-azanyl-3-[(3S)-2-oxo-2,3-dihydro-1H-indol-3-yl]propanoic acid + 2-oxo-L-tryptophan + 2-oxotryptophan + PSI-MOD + MOD:01817 + 2'-oxo-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to a 2'-oxo-L-tryptophan. + PubMed:9461080 + RESID:AA0543 + + + + + (2S)-2-amino-3-[(3S)-2-oxo-2,3-dihydro-1H-indol-3-yl]propanoic acid + + + + + + 2'-oxo-L-tryptophan + + + + + + 2-azanyl-3-[(3S)-2-oxo-2,3-dihydro-1H-indol-3-yl]propanoic acid + + + + + + 2-oxo-L-tryptophan + + + + + + 2-oxotryptophan + + + + + + + + + + + A protein modification that effectively cross-links two tryptophan residues to form 1'-(L-tryptophan-3'-yl)-L-tryptophan. + -2.02 + C 0 H -2 N 0 O 0 + -2.01565 + C 22 H 18 N 4 O 2 + 370.41 + 370.14297 + W, W + natural + uniprot.ptm:PTM-0544 + (2S,2'S)-3,3'-(3'H-1,3'-biindole-3,3'-diyl)bis(2-aminopropanoic acid) + 1-(L-tryptophan-3-yl)-L-tryptophan + 2-amino-3-[2-[2-amino-3-(2-carboxyethyl)-1H-indol-4-yl]-1H-indol-3-yl]propanoic acid + 3-[(2S)-2-amino-2-carboxyethyl]-3-(3-[(2S)-2-amino-2-carboxyethyl]-1H-indol-2-yl)-1H-indole + 3-[2-azanyl-2-carboxyethyl]-3-(3-[2-azanyl-2-carboxyethyl]-1H-indol-2-yl)-1H-indole + ditryptophan + PSI-MOD + MOD:01818 + Cross-link 2. + 1'-(L-tryptophan-3'-yl)-L-tryptophan + + + + + A protein modification that effectively cross-links two tryptophan residues to form 1'-(L-tryptophan-3'-yl)-L-tryptophan. + PubMed:20600836 + RESID:AA0544 + + + + + (2S,2'S)-3,3'-(3'H-1,3'-biindole-3,3'-diyl)bis(2-aminopropanoic acid) + + + + + + 1-(L-tryptophan-3-yl)-L-tryptophan + + + + + + 2-amino-3-[2-[2-amino-3-(2-carboxyethyl)-1H-indol-4-yl]-1H-indol-3-yl]propanoic acid + + + + + + 3-[(2S)-2-amino-2-carboxyethyl]-3-(3-[(2S)-2-amino-2-carboxyethyl]-1H-indol-2-yl)-1H-indole + + + + + + 3-[2-azanyl-2-carboxyethyl]-3-(3-[2-azanyl-2-carboxyethyl]-1H-indol-2-yl)-1H-indole + + + + + + ditryptophan + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-succinyl-L-lysine. + 100.07 + C 4 H 4 N 0 O 3 + 100.016045 + C 10 H 16 N 2 O 4 + 228.25 + 228.11101 + K + natural + uniprot.ptm:PTM-0438 + (2S)-2-amino-6-[(3-carboxypropanoyl)amino]hexanoic acid + 2-azanyl-6-[(3-carboxypropanoyl)azanyl]hexanoic acid + 4-[[(5S)-5-amino-6-hydroxy-6-oxohexyl]amino]-4-oxobutanoate + MOD_RES N6-succinyllysine + N(epsilon)-(succinyl)lysine + N6-succinyl-L-lysine + succinyllysine + PSI-MOD + MOD:01819 + + N6-succinyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-succinyl-L-lysine. + PubMed:16582421 + PubMed:21151122 + RESID:AA0545 + + + + + (2S)-2-amino-6-[(3-carboxypropanoyl)amino]hexanoic acid + + + + + + 2-azanyl-6-[(3-carboxypropanoyl)azanyl]hexanoic acid + + + + + + 4-[[(5S)-5-amino-6-hydroxy-6-oxohexyl]amino]-4-oxobutanoate + + + + + + MOD_RES N6-succinyllysine + + + + + + N(epsilon)-(succinyl)lysine + + + + + + N6-succinyl-L-lysine + + + + + + succinyllysine + + + + + + + + + + + A protein modification that effectively replaces a cysteine sulhydryl hydrogen with an isotope tagged sulfhydryl reagent group. + C + artifact + PSI-MOD + MOD:01820 + + isotope tagged sufhydryl reagent modified cysteine + + + + + A protein modification that effectively replaces a cysteine sulhydryl hydrogen with an isotope tagged sulfhydryl reagent group. + PubMed:18688235 + + + + + + + + + + + A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex reporter+balance group. + C + artifact + Unimod:985 + S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl + PSI-MOD + cysTMT6plex + cysteine-reactive Sixplex Tandem Mass Tag(TM) + MOD:01821 + + The reagent consists of a reporter group, a balance group and a protein sulfhydryl reactive pyridine disulfanyl group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + cysTMT6plex reporter+balance reagent cysteine disulfide + + + + + A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex reporter+balance group. + URL:http://www.piercenet.com/files/2162220.pdf + Unimod:985 + + + + + S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl + + + + + + cysTMT6plex + + + + + + cysteine-reactive Sixplex Tandem Mass Tag(TM) + + + + + + + + + + A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-zero reporter+balance group. + 299.17 + (12)C 14 H 25 (14)N 3 O 2 S 1 + 299.16675 + (12)C 17 H 32 (14)N 4 O 4 S 2 + 420.19 + 420.1865 + C + artifact + Unimod:984 + S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl + PSI-MOD + Native cysteine-reactive Tandem Mass Tag(TM) + cysTMT + MOD:01822 + + The reagent consists of a reporter group, a balance group and a protein sulfhydryl reactive pyridine disulfanyl group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + cysTMT6plex-zero reporter+balance reagent cysteine disulfide + + + + + A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-zero reporter+balance group. + URL:http://www.piercenet.com/files/2162220.pdf + Unimod:984 + + + + + S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl + + + + + + Native cysteine-reactive Tandem Mass Tag(TM) + + + + + + cysTMT + + + + + + + + + + A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-126 reporter+balance group. + 304.18 + (12)C 10 (13)C 4 H 25 (14)N 2 (15)N 1 O 2 S 1 + 304.17722 + (12)C 13 (13)C 4 H 32 (14)N 3 (15)N 1 O 4 S 2 + 425.2 + 425.19696 + C + artifact + Unimod:985 + S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl + PSI-MOD + cysTMT6plex + cysteine-reactive Sixplex Tandem Mass Tag(TM) + MOD:01823 + + The reagent consists of a reporter group, a balance group and a protein sulfhydryl reactive pyridine disulfanyl group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + cysTMT6plex-126 reporter+balance reagent cysteine disulfide + + + + + A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-126 reporter+balance group. + PubMed:18688235 + URL:http://www.piercenet.com/files/2162220.pdf + + + + + S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl + + + + + + cysTMT6plex + + + + + + cysteine-reactive Sixplex Tandem Mass Tag(TM) + + + + + + + + + + A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-127 reporter+balance group. + 304.18 + (12)C 10 (13)C 4 H 25 (14)N 2 (15)N 1 O 2 S 1 + 304.17722 + (12)C 13 (13)C 4 H 32 (14)N 3 (15)N 1 O 4 S 2 + 425.2 + 425.19696 + C + artifact + S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl + PSI-MOD + cysTMT6plex + cysteine-reactive Sixplex Tandem Mass Tag(TM) + MOD:01824 + + The reagent consists of a reporter group, a balance group and a protein sulfhydryl reactive pyridine disulfanyl group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + cysTMT6plex-127 reporter+balance reagent cysteine disulfide + + + + + A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-127 reporter+balance group. + PubMed:18688235 + URL:http://www.piercenet.com/files/2162220.pdf + + + + + S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl + + + + + + cysTMT6plex + + + + + + cysteine-reactive Sixplex Tandem Mass Tag(TM) + + + + + + + + + + A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-128 reporter+balance group. + 304.18 + (12)C 10 (13)C 4 H 25 (14)N 2 (15)N 1 O 2 S 1 + 304.17722 + (12)C 13 (13)C 4 H 32 (14)N 3 (15)N 1 O 4 S 2 + 425.2 + 425.19696 + C + artifact + S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl + PSI-MOD + cysTMT6plex + cysteine-reactive Sixplex Tandem Mass Tag(TM) + MOD:01825 + + The reagent consists of a reporter group, a balance group and a protein sulfhydryl reactive pyridine disulfanyl group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + cysTMT6plex-128 reporter+balance reagent cysteine disulfide + + + + + A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-128 reporter+balance group. + PubMed:18688235 + URL:http://www.piercenet.com/files/2162220.pdf + + + + + S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl + + + + + + cysTMT6plex + + + + + + cysteine-reactive Sixplex Tandem Mass Tag(TM) + + + + + + + + + + A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-129 reporter+balance group. + 304.18 + (12)C 10 (13)C 4 H 25 (14)N 2 (15)N 1 O 2 S 1 + 304.17722 + (12)C 13 (13)C 4 H 32 (14)N 3 (15)N 1 O 4 S 2 + 425.2 + 425.19696 + C + artifact + S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl + PSI-MOD + cysTMT6plex + cysteine-reactive Sixplex Tandem Mass Tag(TM) + MOD:01826 + + The reagent consists of a reporter group, a balance group and a protein sulfhydryl reactive pyridine disulfanyl group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + cysTMT6plex-129 reporter+balance reagent cysteine disulfide + + + + + A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-129 reporter+balance group. + PubMed:18688235 + URL:http://www.piercenet.com/files/2162220.pdf + + + + + S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl + + + + + + cysTMT6plex + + + + + + cysteine-reactive Sixplex Tandem Mass Tag(TM) + + + + + + + + + + A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-130 reporter+balance group. + 304.18 + (12)C 10 (13)C 4 H 25 (14)N 2 (15)N 1 O 2 S 1 + 304.17722 + (12)C 13 (13)C 4 H 32 (14)N 3 (15)N 1 O 4 S 2 + 425.2 + 425.19696 + C + artifact + S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl + PSI-MOD + cysTMT6plex + cysteine-reactive Sixplex Tandem Mass Tag(TM) + MOD:01827 + + The reagent consists of a reporter group, a balance group and a protein sulfhydryl reactive pyridine disulfanyl group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + cysTMT6plex-130 reporter+balance reagent cysteine disulfide + + + + + A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-130 reporter+balance group. + PubMed:18688235 + URL:http://www.piercenet.com/files/2162220.pdf + + + + + S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl + + + + + + cysTMT6plex + + + + + + cysteine-reactive Sixplex Tandem Mass Tag(TM) + + + + + + + + + + A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-131 reporter+balance group. + 304.18 + (12)C 10 (13)C 4 H 25 (14)N 2 (15)N 1 O 2 S 1 + 304.17722 + (12)C 13 (13)C 4 H 32 (14)N 3 (15)N 1 O 4 S 2 + 425.2 + 425.19696 + C + artifact + S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl + PSI-MOD + cysTMT6plex + cysteine-reactive Sixplex Tandem Mass Tag(TM) + MOD:01828 + + The reagent consists of a reporter group, a balance group and a protein sulfhydryl reactive pyridine disulfanyl group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + cysTMT6plex-131 reporter+balance reagent cysteine disulfide + + + + + A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-131 reporter+balance group. + PubMed:18688235 + URL:http://www.piercenet.com/files/2162220.pdf + + + + + S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl + + + + + + cysTMT6plex + + + + + + cysteine-reactive Sixplex Tandem Mass Tag(TM) + + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine sulfoxide. + 58.04 + C 2 H 2 N 0 O 2 S 0 + 58.005478 + C 5 H 7 N 1 O 3 S 1 + 161.18 + 161.01466 + C + artifact + CmCO + PSI-MOD + MOD:01829 + S-carboxymethyl-L-cysteine sulfoxide + + + + + A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine sulfoxide. + PubMed:17689096 + PubMed:18688235 + + + + + CmCO + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine sulfone. + 74.03 + C 2 H 2 N 0 O 3 S 0 + 74.0004 + C 5 H 7 N 1 O 4 S 1 + 177.17 + 177.00958 + C + artifact + CmCO2 + PSI-MOD + MOD:01830 + S-carboxymethyl-L-cysteine sulfone + + + + + A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine sulfone. + PubMed:18688235 + + + + + CmCO2 + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine sulfone. + 89.05 + C 2 H 3 N 1 O 3 + 89.01129 + C 5 H 8 N 2 O 4 S 1 + 192.19 + 192.02048 + C + artifact + CamCO2 + S-carbamoylmethyl-L-cysteine sulfone + PSI-MOD + MOD:01831 + S-carboxamidomethyl-L-cysteine sulfone + + + + + A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine sulfone. + PubMed:18688235 + + + + + CamCO2 + + + + + + S-carbamoylmethyl-L-cysteine sulfone + + + + + + + + + + A protein modification that effectively converts a residue containing common isotopes to a 5x(13)C-labeled residue. + 5.02 + (12)C -5 (13)C 5 + 5.016774 + X + artifact + Unimod:772 + PSI-MOD + 13C(5) Silac label + Label:13C(5) + MOD:01832 + 5x(13)C-labeled residue + + + + + A protein modification that effectively converts a residue containing common isotopes to a 5x(13)C-labeled residue. + PubMed:12771378 + Unimod:772 + + + + + 13C(5) Silac label + + + + + + Label:13C(5) + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine. + 5.02 + (12)C -5 (13)C 5 H 0 N 0 O 0 S 0 + 5.016774 + (13)C 5 H 9 N 1 O 1 S 1 + 136.06 + 136.05727 + M + artifact + PSI-MOD + MOD:01833 + 5x(13)C-labeled L-methionine + + + + + A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine. + PubMed:18688235 + url: + + + + + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine sulfoxide. + 5.02 + (12)C -5 (13)C 5 H 0 N 0 O 0 S 0 + 5.016774 + (13)C 5 H 9 N 1 O 2 S 1 + 152.05 + 152.05217 + MOD:00719 + artifact + PSI-MOD + MOD:01834 + 5x(13)C-labeled L-methionine sulfoxide + + + + + A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine sulfoxide. + PubMed:18688235 + + + + + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine sulfone. + 5.02 + (12)C -5 (13)C 5 H 0 N 0 O 0 S 0 + 5.016774 + (13)C 5 H 9 N 1 O 3 S 1 + 168.05 + 168.04709 + MOD:00256 + artifact + PSI-MOD + MOD:01835 + 5x(13)C-labeled L-methionine sulfone + + + + + A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine sulfone. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-[([1-(6-nitro-2H-1,3-benzodioxol-5-yl)ethoxy]carbonyl]lysine. + 237.17 + C 10 H 7 N 1 O 6 + 237.02734 + C 16 H 19 N 3 O 7 + 365.34 + 365.1223 + K + artifact + (2S)-2-amino-6-[([1-(6-nitro-1,3-benzodioxol-5-yl)ethoxy]carbonyl)amino]hexanoic acid + [(alpha-methyl-6-nitro-piperonyloxy)carbonyl]lysine + PSI-MOD + MOD:01836 + N6-[([1-(6-nitro-2H-1,3-benzodioxol-5-yl)ethoxy]carbonyl]lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-[([1-(6-nitro-2H-1,3-benzodioxol-5-yl)ethoxy]carbonyl]lysine. + PubMed:18688235 + PubMed:20218600 + PubMed:21271704 + + + + + (2S)-2-amino-6-[([1-(6-nitro-1,3-benzodioxol-5-yl)ethoxy]carbonyl)amino]hexanoic acid + + + + + + [(alpha-methyl-6-nitro-piperonyloxy)carbonyl]lysine + + + + + + + + + + A protein modification that effectively cross-links two L-cysteine residues with a thioether bond to form L-lanthionine. + -34.08 + C 0 H -2 N 0 O 0 S -1 + -33.98772 + C 6 H 8 N 2 O 2 S 1 + 172.2 + 172.03065 + C, C + hypothetical + (2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid) + (R)-S-(2-amino-2-carboxyethyl)-L-cysteine + (R,R)-2,6-diamino-4-thiaheptanedioic acid + (R,R)-3,3'-thiobis-(2-aminopropanoic acid) + (R,R)-bis(2-amino-2-carboxyethyl)sulfide + 2-amino-3-(2-amino-2-carboxyethyl)sulfanylpropanoic acid + 3,3'-thiobis-L-alanine + L-lanthionine + PSI-MOD + MOD:01837 + Cross-link 2. + L-lanthionine (Cys-Cys) + + + + + A protein modification that effectively cross-links two L-cysteine residues with a thioether bond to form L-lanthionine. + ChEBI:21347 + PubMed:20805503 + PubMed:6007887 + RESID:AA0110#CYS2 + + + + + (2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid) + + + + + + (R)-S-(2-amino-2-carboxyethyl)-L-cysteine + + + + + + (R,R)-2,6-diamino-4-thiaheptanedioic acid + + + + + + (R,R)-3,3'-thiobis-(2-aminopropanoic acid) + + + + + + (R,R)-bis(2-amino-2-carboxyethyl)sulfide + + + + + + 2-amino-3-(2-amino-2-carboxyethyl)sulfanylpropanoic acid + + + + + + 3,3'-thiobis-L-alanine + + + + + + L-lanthionine + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to L-lysinoalanine. + 87.08 + C 3 H 5 N 1 O 2 + 87.03203 + C 9 H 17 N 3 O 3 + 215.25 + 215.12698 + K + natural + uniprot.ptm:PTM-0439 + (2R,9S)-lysinoalanine + (2S)-2-amino-6-([(2R)-2-amino-2-carboxyethyl]amino)hexanoic acid + L-lysinoalanine + LAL + MOD_RES Lysino-D-alanine (Lys) + N-epsilon-(2-amino-2-carboxyethyl)-L-lysine + N6-(2-amino-2-carboxyethyl)-L-lysine + alaninolysine + lysino-D-alanine + PSI-MOD + MOD:01838 + This entry is for the modification of peptidyl lysine by a free serine. For the crosslink of peptidyl serine and peptidyl lysine see MOD:00132. + L-lysinoalanine (Lys) + + + + + A protein modification that effectively converts an L-lysine residue to L-lysinoalanine. + PubMed:19155267 + PubMed:2544544 + RESID:AA0123#LYS + + + + + (2R,9S)-lysinoalanine + + + + + + (2S)-2-amino-6-([(2R)-2-amino-2-carboxyethyl]amino)hexanoic acid + + + + + + L-lysinoalanine + + + + + + LAL + + + + + + MOD_RES Lysino-D-alanine (Lys) + + + + + + N-epsilon-(2-amino-2-carboxyethyl)-L-lysine + + + + + + N6-(2-amino-2-carboxyethyl)-L-lysine + + + + + + alaninolysine + + + + + + lysino-D-alanine + + + + + + + + + + + + A protein modification that effectively cross-links either two L-cysteine residues, or an L-cysteine residue and an L-serine residue by a thioether bond to form L-lanthionine. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 6 H 8 N 2 O 2 S 1 + 172.2 + 172.03065 + C, X + artifact + PSI-MOD + MOD:01839 + Cross-link 2. For the natural form of the lanthionine cross-link see MOD:00120 meso-lanthionine [JSG]. + L-lanthionine + + + + + A protein modification that effectively cross-links either two L-cysteine residues, or an L-cysteine residue and an L-serine residue by a thioether bond to form L-lanthionine. + PubMed:18688235 + + + + + + + + + + + A protein modification that effectively converts an L-isoleucine residue to L-allo-isoleucine. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 6 H 11 N 1 O 1 + 113.16 + 113.08406 + I + natural + uniprot.ptm:PTM-0442 + (2S,3R)-2-amino-3-methylpentanoic acid + 2-azanyl-3-methylpentanoic acid + 3-methyl-norvaline + L-allo-isoleucine + L-threo-isoleucine + MOD_RES L-allo-isoleucine + allo-L-isoleucine + alpha-amino-beta-methylvaleric acid + PSI-MOD + MOD:01840 + L-allo-isoleucine + + + + + A protein modification that effectively converts an L-isoleucine residue to L-allo-isoleucine. + ChEBI:43433 + PubMed:20805503 + RESID:AA0546 + + + + + (2S,3R)-2-amino-3-methylpentanoic acid + + + + + + 2-azanyl-3-methylpentanoic acid + + + + + + 3-methyl-norvaline + + + + + + L-allo-isoleucine + + + + + + L-threo-isoleucine + + + + + + MOD_RES L-allo-isoleucine + + + + + + allo-L-isoleucine + + + + + + alpha-amino-beta-methylvaleric acid + + + + + + + + + + + A protein modification that effectively cross-links either two or an L-cysteine residue and an L-serine residue by a thioether bond to form a lanthionine, either D- or L- or meso-lanthionine. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 6 H 8 N 2 O 2 S 1 + 172.2 + 172.03065 + C, X + artifact + 2,6-diamino-4-thiaheptanedioic acid + 2-amino-3-(2-amino-2-carboxyethyl)sulfanylpropanoic acid + 3,3'-thiobis-(2-aminopropanoic acid) + 3,3'-thiobis-L-alanine + S-(2-amino-2-carboxyethyl)-L-cysteine + bis(2-amino-2-carboxyethyl)sulfanediyl + bis(2-amino-2-carboxyethyl)sulfide + PSI-MOD + MOD:01841 + Cross-link 2. [JSG]. + lanthionine + + + + + A protein modification that effectively cross-links either two or an L-cysteine residue and an L-serine residue by a thioether bond to form a lanthionine, either D- or L- or meso-lanthionine. + PubMed:18688235 + + + + + 2,6-diamino-4-thiaheptanedioic acid + + + + + + 2-amino-3-(2-amino-2-carboxyethyl)sulfanylpropanoic acid + + + + + + 3,3'-thiobis-(2-aminopropanoic acid) + + + + + + 3,3'-thiobis-L-alanine + + + + + + S-(2-amino-2-carboxyethyl)-L-cysteine + + + + + + bis(2-amino-2-carboxyethyl)sulfanediyl + + + + + + bis(2-amino-2-carboxyethyl)sulfide + + + + + + + + + + A protein modification that effectively converts two L-cysteine residues to S-(2-aminovinyl)-L-cysteine. + -80.1 + C -1 H -4 N 0 O -2 S -1 + -79.9932 + C 5 H 7 N 2 O 1 S 1 + 143.18 + 143.02791 + C, C + natural + C-term + uniprot.ptm:PTM-0443 + (2R)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid + (R,Z)-S-(2-aminovinyl)cysteine + S-(2-aminovinyl)-L-cysteine + PSI-MOD + MOD:01842 + Cross-link 2. + S-(2-aminovinyl)-L-cysteine + + + + + A protein modification that effectively converts two L-cysteine residues to S-(2-aminovinyl)-L-cysteine. + PubMed:20805503 + RESID:AA0548 + + + + + (2R)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid + + + + + + (R,Z)-S-(2-aminovinyl)cysteine + + + + + + S-(2-aminovinyl)-L-cysteine + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to 5'-chloro-L-tryptophan. + 34.44 + C 0 Cl 1 H -1 N 0 O 0 + 33.96103 + C 11 Cl 1 H 9 N 2 O 1 + 220.66 + 220.04034 + W + natural + uniprot.ptm:PTM-0444 + (2S)-2-amino-3-(5-chloro-1H-indol-3-yl)propanoic acid + 5'-chloro-L-tryptophan + MOD_RES 5'-chlorotryptophan + PSI-MOD + MOD:01843 + 5'-chloro-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to 5'-chloro-L-tryptophan. + PubMed:18215770 + RESID:AA0549 + + + + + (2S)-2-amino-3-(5-chloro-1H-indol-3-yl)propanoic acid + + + + + + 5'-chloro-L-tryptophan + + + + + + MOD_RES 5'-chlorotryptophan + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue and an L-leucine residue to 2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid. + -5.06 + C 0 H -7 N -1 O 1 S 0 + -5.062935 + C 9 H 10 N 1 O 3 S 1 + 212.24 + 212.03813 + C, L + natural + N-term + uniprot.ptm:PTM-0448 + (4Z)-4-[hydroxy(sulfanyl)methylidene]-2-(3-methylbutanoyl)-1,3-oxazol-5(4H)-one [tautomer] + 2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid + 5-hydroxy-2-(3-methylbutanoyl)-1,3-oxazole-4-carbothioic O-acid + MOD_RES 2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid (Leu-Cys) + PSI-MOD + MOD:01844 + Cross-link 2. + 2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid + + + + + A protein modification that effectively converts an L-cysteine residue and an L-leucine residue to 2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid. + PubMed:15361623 + PubMed:18729522 + PubMed:20961038 + PubMed:21254756 + RESID:AA0550 + + + + + (4Z)-4-[hydroxy(sulfanyl)methylidene]-2-(3-methylbutanoyl)-1,3-oxazol-5(4H)-one [tautomer] + + + + + + 2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid + + + + + + 5-hydroxy-2-(3-methylbutanoyl)-1,3-oxazole-4-carbothioic O-acid + + + + + + MOD_RES 2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid (Leu-Cys) + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue and an L-proline residue to L-proline 5-hydroxyoxazole-4-carbothionic acid. + -4.03 + C 0 H -4 N 0 O 0 S 0 + -4.0313 + C 8 H 8 N 2 O 2 S 1 + 196.22 + 196.03065 + C, P + natural + uniprot.ptm:PTM-0449 + (4Z)-4-[hydroxy(sulfanyl)methylidene]-2-[(2S)-pyrrolidin-2-yl]-1,3-oxazol-5(4H)-one [tautomer] + 5-hydroxy-2-[(2S)-pyrrolidin-2-yl]-1,3-oxazole-4-carbothioic O-acid + CROSSLNK Proline 5-hydroxy-oxazole-4-carbothionic acid (Pro-Cys) + L-proline 5-hydroxy-oxazole-4-carbothionic acid + PSI-MOD + MOD:01845 + Cross-link 2. + L-proline 5-hydroxyoxazole-4-carbothionic acid + + + + + A protein modification that effectively converts an L-cysteine residue and an L-proline residue to L-proline 5-hydroxyoxazole-4-carbothionic acid. + PubMed:15361623 + PubMed:18729522 + PubMed:20961038 + PubMed:21254756 + RESID:AA0551 + + + + + (4Z)-4-[hydroxy(sulfanyl)methylidene]-2-[(2S)-pyrrolidin-2-yl]-1,3-oxazol-5(4H)-one [tautomer] + + + + + + 5-hydroxy-2-[(2S)-pyrrolidin-2-yl]-1,3-oxazole-4-carbothioic O-acid + + + + + + CROSSLNK Proline 5-hydroxy-oxazole-4-carbothionic acid (Pro-Cys) + + + + + + L-proline 5-hydroxy-oxazole-4-carbothionic acid + + + + + + + + + + + A protein modification that effectively converts two L-cysteine residues, and a copper atom to the methanobactin OB3b copper complex. + 85.46 + C 0 Cu 1 H -10 N 0 O 2 S 0 + 84.84118 + C 6 Cu 1 H 0 N 2 O 4 S 2 + 291.74 + 290.85956 + C, C + natural + N-term + METAL copper [Cu-methanobactin OB3b complex] + bis[4-(hydroxy[sulfanyl-kappaS]methylidene)-1,3-oxazol-5(4H)-onato-kappaN]copper + methanobactin OB3b copper complex + PSI-MOD + MOD:01846 + Cross-link 2. + methanobactin OB3b copper complex + + + + + A protein modification that effectively converts two L-cysteine residues, and a copper atom to the methanobactin OB3b copper complex. + PubMed:15361623 + PubMed:18729522 + PubMed:20961038 + PubMed:21254756 + RESID:AA0552 + + + + + METAL copper [Cu-methanobactin OB3b complex] + + + + + + bis[4-(hydroxy[sulfanyl-kappaS]methylidene)-1,3-oxazol-5(4H)-onato-kappaN]copper + + + + + + methanobactin OB3b copper complex + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteine sulfinyl phosphate. + 111.98 + C 0 H 1 N 0 O 5 P 1 S 0 + 111.95616 + C 3 H 6 N 1 O 6 P 1 S 1 + 215.12 + 214.96535 + C + hypothetical + (2R)-2-amino-3-[(phosphonooxy)sulfinyl]propanoic acid + L-cysteine sulfinyl phosphate + cysteine sulfinic phosphoryl ester + PSI-MOD + MOD:01847 + L-cysteine sulfinyl phosphate + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteine sulfinyl phosphate. + PubMed:16565085 + RESID:AA0557 + + + + + (2R)-2-amino-3-[(phosphonooxy)sulfinyl]propanoic acid + + + + + + L-cysteine sulfinyl phosphate + + + + + + cysteine sulfinic phosphoryl ester + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-(spermidinoglutathion-S-yl)-L-cysteine. + 432.54 + C 17 H 32 N 6 O 5 S 1 + 432.21548 + C 20 H 37 N 7 O 6 S 2 + 535.68 + 535.2247 + C + natural + (2R)-2-amino-3-([(2R)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)-2-([2-([3-([4-aminobutyl]amino)propyl]carbamoyl)methyl]carbamoyl)ethyl]disulfanyl)propanoic acid + L-gamma-glutamyl-[S-(L-cystein-S-yl)]-L-cysteinyl-N-{3-[(4-aminobutyl)amino]propyl}glycinamide + S-(spermidinoglutathion-S-yl)-L-cysteine + cysteine glutathionylspermidine disulfide + PSI-MOD + MOD:01848 + S-(spermidinoglutathion-S-yl)-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-(spermidinoglutathion-S-yl)-L-cysteine. + ChEBI:16613 + PubMed:20530482 + RESID:AA0558 + + + + + (2R)-2-amino-3-([(2R)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)-2-([2-([3-([4-aminobutyl]amino)propyl]carbamoyl)methyl]carbamoyl)ethyl]disulfanyl)propanoic acid + + + + + + L-gamma-glutamyl-[S-(L-cystein-S-yl)]-L-cysteinyl-N-{3-[(4-aminobutyl)amino]propyl}glycinamide + + + + + + S-(spermidinoglutathion-S-yl)-L-cysteine + + + + + + cysteine glutathionylspermidine disulfide + + + + + + + + + + A protein modification that effectively cross-links two L-cysteine residues by a thioether bond to form S-(2-aminovinyl)-D-cysteine. + -80.1 + C -1 H -4 N 0 O -2 S -1 + -79.9932 + C 5 H 7 N 2 O 1 S 1 + 143.18 + 143.02791 + C, C + natural + C-term + uniprot.ptm:PTM-0446 + (2S)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid + (S,Z)-S-(2-aminovinyl)cysteine + CROSSLNK S-(2-aminovinyl)-D-cysteine (Cys-Cys) + S-(2-aminovinyl)-D-cysteine + PSI-MOD + MOD:01849 + Cross-link 2. + S-(2-aminovinyl)-D-cysteine (Cys-Cys) + + + + + A protein modification that effectively cross-links two L-cysteine residues by a thioether bond to form S-(2-aminovinyl)-D-cysteine. + PubMed:20805503 + RESID:AA0204#CYS2 + + + + + (2S)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid + + + + + + (S,Z)-S-(2-aminovinyl)cysteine + + + + + + CROSSLNK S-(2-aminovinyl)-D-cysteine (Cys-Cys) + + + + + + S-(2-aminovinyl)-D-cysteine + + + + + + + + + + A protein modification that effectively cross-links either two L-cysteine residues, or an L-cysteine residue and an L-serine residue by a thioether bond to form S-(2-aminovinyl)-D-cysteine. + C 5 H 7 N 2 O 1 S 1 + 143.18 + 143.02791 + C, X + natural + C-term + (2S)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid + (S,Z)-S-(2-aminovinyl)cysteine + S-(2-aminovinyl)-D-cysteine + PSI-MOD + MOD:01850 + Cross-link 2. + S-(2-aminovinyl)-D-cysteine + + + + + A protein modification that effectively cross-links either two L-cysteine residues, or an L-cysteine residue and an L-serine residue by a thioether bond to form S-(2-aminovinyl)-D-cysteine. + RESID:AA0204 + + + + + (2S)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid + + + + + + (S,Z)-S-(2-aminovinyl)cysteine + + + + + + S-(2-aminovinyl)-D-cysteine + + + + + + + + + + + A protein modification that effectively cross-links either two L-cysteine residues, or an L-cysteine residue and an L-serine residue by a thioether bond to form S-(2-aminovinyl)-cysteine. + C 5 H 7 N 2 O 1 S 1 + 143.18 + 143.02791 + C, X + natural + C-term + 2-amino-3-([2-aminoethenyl]sulfanyl)propanoic acid + PSI-MOD + MOD:01851 + Cross-link 2. + S-(2-aminovinyl)-cysteine + + + + + A protein modification that effectively cross-links either two L-cysteine residues, or an L-cysteine residue and an L-serine residue by a thioether bond to form S-(2-aminovinyl)-cysteine. + PubMed:18688235 + + + + + 2-amino-3-([2-aminoethenyl]sulfanyl)propanoic acid + + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-lysine residue to release hydrogen sulfide and form 2-amino-6-(2-amino-2-carboxyethylamino)hexanoic acid. + -34.08 + C 0 H -2 N 0 O 0 S -1 + -33.98772 + C 9 H 15 N 3 O 2 + 197.24 + 197.11642 + C, K + hypothetical + Lysinoalanine (from Cysteine) + PSI-MOD + MOD:01852 + Cross-link 2. This entry is for a crosslink of peptidyl cysteine and peptidyl lysine. For the modification of peptidyl lysine by a free serine see MOD:01838. From DeltaMass: Average Mass: -34 with no citation or formula. [JSG] + L-lysinoalanine (Lys-Cys) + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-lysine residue to release hydrogen sulfide and form 2-amino-6-(2-amino-2-carboxyethylamino)hexanoic acid. + DeltaMass:0 + + + + + Lysinoalanine (from Cysteine) + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to L-lysinoalanine either by forming a cross-link with peptidyl-cysteine or peptidyl-serine, or by condensation with free serine. + K + natural + PSI-MOD + MOD:01853 + L-lysinoalanine + + + + + A protein modification that effectively converts an L-lysine residue to L-lysinoalanine either by forming a cross-link with peptidyl-cysteine or peptidyl-serine, or by condensation with free serine. + PubMed:18688235 + + + + + + + + + A protein modification that effectively adds one oxygen atom to a sulfur atom of a residue without removing hydrogen atoms. + PSI-MOD + MOD:01854 + + sulfur monooxygenated residue + + + + + A protein modification that effectively adds one oxygen atom to a sulfur atom of a residue without removing hydrogen atoms. + PubMed:18688235 + + + + + + + + + A protein modification that effectively adds two oxygen atoms to a sulfur atom of a residue without removing hydrogen atoms. + PSI-MOD + MOD:01855 + + sulfur dioxygenated residue + + + + + A protein modification that effectively adds two oxygen atoms to a sulfur atom of a residue without removing hydrogen atoms. + PubMed:18688235 + + + + + + + + + A protein modification that crosslinks two residues by rearrangement and condensation of a cysteine with the carbonyl of the preceding residue to form a 1,3-oxazole-4-carbothionic acid. + PSI-MOD + MOD:01856 + oxazole/oxazoline ring crosslinked residues (Cys) + + + + + A protein modification that crosslinks two residues by rearrangement and condensation of a cysteine with the carbonyl of the preceding residue to form a 1,3-oxazole-4-carbothionic acid. + PubMed:18688235 + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-methionine residue by a thioether bond to form 2-(L-cystein-S-yl)-methionine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 8 H 12 N 2 O 2 S 2 + 232.32 + 232.03403 + C, M + natural + uniprot.ptm:PTM-0495 + (2R)-2-amino-2-([2-amino-2-carboxyethyl]sulfanyl)-4-(methylsulfanyl)butanoic acid + 2-(L-cystein-S-yl)-methionine + CROSSLNK 2-(S-cysteinyl)-methionine (Cys-Met) + PSI-MOD + MOD:01857 + Cross-link 2. The chirality around the methionine alpha-carbon has not been determined. + 2-(L-cystein-S-yl)-methionine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-methionine residue by a thioether bond to form 2-(L-cystein-S-yl)-methionine. + PubMed:20805502 + RESID:AA0559 + + + + + (2R)-2-amino-2-([2-amino-2-carboxyethyl]sulfanyl)-4-(methylsulfanyl)butanoic acid + + + + + + 2-(L-cystein-S-yl)-methionine + + + + + + CROSSLNK 2-(S-cysteinyl)-methionine (Cys-Met) + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-(N-acetylamino)glucosyl-L-cysteine. + 203.19 + C 8 H 13 N 1 O 5 S 0 + 203.07938 + C 11 H 18 N 2 O 6 S 1 + 306.33 + 306.08856 + C + natural + uniprot.ptm:PTM-0628 + (2R)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosylsulfanyl)propanoic acid + CARBOHYD S-linked (GlcNAc) cysteine + S-(N-acetylamino)glucosyl-L-cysteine + S-[(N-acetylamino)glycosyl]cysteine + S-[beta-D-(N-acetylamino)glucopyranosyl]cysteine + PSI-MOD + MOD:01858 + S-(N-acetylamino)glucosyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-(N-acetylamino)glucosyl-L-cysteine. + ChEBI:61631 + PubMed:21251913 + PubMed:21395300 + RESID:AA0560 + + + + + (2R)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosylsulfanyl)propanoic acid + + + + + + CARBOHYD S-linked (GlcNAc) cysteine + + + + + + S-(N-acetylamino)glucosyl-L-cysteine + + + + + + S-[(N-acetylamino)glycosyl]cysteine + + + + + + S-[beta-D-(N-acetylamino)glucopyranosyl]cysteine + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form 4-amino-3-isothiazolidinone-L-phenylalanine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 12 H 12 N 2 O 2 S 1 + 248.3 + 248.06195 + C, F + hypothetical + uniprot.ptm:PTM-0451 + (2S)-2-[(4R)-4-amino-3-oxo-1,2-thiazolidin-2-yl]-3-phenylpropanoic acid + 2-(4-amino-3-oxo-isothiazolidin-2-yl)-3-phenylpropanoic acid + 4-amino-3-isothiazolidinone-L-phenylalanine + CROSSLNK N,N-(cysteine-1,S-diyl)phenylalanine (Cys-Phe) + N,N-(L-cysteine-1,S-diyl)-L-phenylalanine + cysteinyl phenylalanine sulfenamide + phenylalanine-cysteine sulfenyl amide cross-link + phenylalanine-cysteine sulphenyl amide cross-link + PSI-MOD + MOD:01859 + Cross-link 2. + 4-amino-3-isothiazolidinone-L-phenylalanine + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form 4-amino-3-isothiazolidinone-L-phenylalanine. + PubMed:17502599 + RESID:AA0562 + + + + + (2S)-2-[(4R)-4-amino-3-oxo-1,2-thiazolidin-2-yl]-3-phenylpropanoic acid + + + + + + 2-(4-amino-3-oxo-isothiazolidin-2-yl)-3-phenylpropanoic acid + + + + + + 4-amino-3-isothiazolidinone-L-phenylalanine + + + + + + CROSSLNK N,N-(cysteine-1,S-diyl)phenylalanine (Cys-Phe) + + + + + + N,N-(L-cysteine-1,S-diyl)-L-phenylalanine + + + + + + cysteinyl phenylalanine sulfenamide + + + + + + phenylalanine-cysteine sulfenyl amide cross-link + + + + + + phenylalanine-cysteine sulphenyl amide cross-link + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteine bacillithiol disulfide. + 396.37 + C 13 H 20 N 2 O 10 S 1 + 396.08386 + C 16 H 25 N 3 O 11 S 2 + 499.51 + 499.09305 + C + natural + uniprot.ptm:PTM-0452 + (2S)-(2-[S-(L-cystein-S-yl)-L-cysteinyl]amino-2-deoxy-alpha-D-glucopyranosyloxy)-butanedioic acid + BSH + L-cysteine bacillithiol disulfide + MOD_RES S-bacillithiol cysteine disulfide + PSI-MOD + MOD:01860 + L-cysteine bacillithiol disulfide + + + + + A protein modification that effectively converts an L-cysteine residue to L-cysteine bacillithiol disulfide. + ChEBI:61338 + PubMed:19578333 + RESID:AA0563 + + + + + (2S)-(2-[S-(L-cystein-S-yl)-L-cysteinyl]amino-2-deoxy-alpha-D-glucopyranosyloxy)-butanedioic acid + + + + + + BSH + + + + + + L-cysteine bacillithiol disulfide + + + + + + MOD_RES S-bacillithiol cysteine disulfide + + + + + + + + + + A protein modification that crosslinks two residues by condensation of a cysteine thiol with the amido nitrogen of the following residue to form an isothiazolidinone ring. + PSI-MOD + MOD:01861 + The isothiazolidinone ring is usually formed by the reaction of a cysteine sulfenic acid with the amido nitrogen releasing water. + isothiazolidinone ring crosslinked residues + + + + + A protein modification that crosslinks two residues by condensation of a cysteine thiol with the amido nitrogen of the following residue to form an isothiazolidinone ring. + PubMed:18688235 + + + + + + + + + A protein modification that effectively replaces the hydrogen atom of a cysteine sulfanyl group with a substituted sulfanyl group, forming a disulfide bond that does not cross-link two encoded peptide chains. + C + S-thiolation + PSI-MOD + MOD:01862 + + disulfide conjugated residue + + + + + A protein modification that effectively replaces the hydrogen atom of a cysteine sulfanyl group with a substituted sulfanyl group, forming a disulfide bond that does not cross-link two encoded peptide chains. + PubMed:18688235 + + + + + S-thiolation + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems mTRAQ reagent reporter+balance groups. + X + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems mTRAQ(TM) reagent + MOD:01863 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + mTRAQ reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems mTRAQ reagent reporter+balance groups. + PubMed:18688235 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems mTRAQ(TM) reagent + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems mTRAQ light reporter+balance group. + 140.09 + (12)C 7 H 12 (14)N 2 (16)O 1 + 140.09496 + X + artifact + Unimod:888 + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + Applied Biosystems mTRAQ(TM) reagent + mTRAQ heavy + MOD:01864 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + mTRAQ light reporter+balance reagent acylated residue + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems mTRAQ light reporter+balance group. + Unimod:888 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + Applied Biosystems mTRAQ(TM) reagent + + + + + + mTRAQ heavy + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems mTRAQ light reporter+balance group. + 140.09 + (12)C 7 H 12 (14)N 2 (16)O 1 + 140.09496 + X + artifact + N-term + Unimod:888 + (4-methylpiperazin-1-yl)acetyl + mTRAQ light on nterm + PSI-MOD + Applied Biosystems mTRAQ(TM) reagent + mTRAQ light + MOD:01865 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + mTRAQ light reporter+balance reagent acylated N-terminal + + + + + A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems mTRAQ light reporter+balance group. + OMSSA:208 + Unimod:888#N-term + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + mTRAQ light on nterm + + + + + + Applied Biosystems mTRAQ(TM) reagent + + + + + + mTRAQ light + + + + + + + + + + + A protein modification that effectively replaces the N6-amino hydrogen atom of a lysine residue with the Applied Biosystems mTRAQ light reporter+balance group. + 140.09 + (12)C 7 H 12 (14)N 2 (16)O 1 + 140.09496 + (12)C 13 H 24 N 2 (14)N 2 O 1 (16)O 1 + 268.19 + 268.1899 + K + artifact + Unimod:888 + (4-methylpiperazin-1-yl)acetyl + mTRAQ light on K + PSI-MOD + Applied Biosystems mTRAQ(TM) reagent + mTRAQ light + MOD:01866 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + mTRAQ light reporter+balance reagent N6-acylated lysine + + + + + A protein modification that effectively replaces the N6-amino hydrogen atom of a lysine residue with the Applied Biosystems mTRAQ light reporter+balance group. + OMSSA:209 + Unimod:888#K + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + mTRAQ light on K + + + + + + Applied Biosystems mTRAQ(TM) reagent + + + + + + mTRAQ light + + + + + + + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems mTRAQ light reporter+balance group. + 140.09 + (12)C 7 H 12 (14)N 2 (16)O 1 + 140.09496 + (12)C 16 H 21 (14)N 3 O 2 (16)O 1 + 303.16 + 303.1583 + Y + artifact + Unimod:888 + (4-methylpiperazin-1-yl)acetyl + mTRAQ light on Y + PSI-MOD + Applied Biosystems mTRAQ(TM) reagent + mTRAQ light + MOD:01867 + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. + mTRAQ light reporter+balance reagent O4'-acylated tyrosine + + + + + A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems mTRAQ light reporter+balance group. + OMSSA:210 + Unimod:888#Y + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + mTRAQ light on Y + + + + + + Applied Biosystems mTRAQ(TM) reagent + + + + + + mTRAQ light + + + + + + + + + + Modifications that have monoisotopic mass differences from their respective origins of 140.094963 Da. + PSI-MOD + MOD:01868 + + modifications with monoisotopic mass differences that are nominally equal at 140.094963 Da + + + + + Modifications that have monoisotopic mass differences from their respective origins of 140.094963 Da. + PubMed:18688235 + + + + + + + + + + + + + + + The protein modification reporter fragment produced by an Applied Biosystems mTRAQ light reagent derivatized residue. + 1+ + (12)C 6 H 13 (14)N 2 + 113.11 + 113.10732 + X + artifact + 4-methyl-1-methylidenepiperazin-1-ium + PSI-MOD + MOD:01869 + + mTRAQ light reporter fragment + + + + + The protein modification reporter fragment produced by an Applied Biosystems mTRAQ light reagent derivatized residue. + PubMed:18688235 + + + + + 4-methyl-1-methylidenepiperazin-1-ium + + + + + + + + + + A protein modification reporter fragment produced by an Applied Biosystems mTRAQ reagent derivatized residue. + PSI-MOD + MOD:01870 + + mTRAQ reporter fragment + + + + + A protein modification reporter fragment produced by an Applied Biosystems mTRAQ reagent derivatized residue. + PubMed:18688235 + + + + + + + + + + + + + + + + + + + + + A protein modification that effectively cyclizes an S-carboxamidomethyl-L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid with the loss of ammonia. + -17.03 + C 0 H -3 N -1 O 0 S 0 + -17.026548 + C 5 H 6 N 1 O 2 S 1 + 144.17 + 144.01192 + MOD:01060 + artifact + N-term + Unimod:26 + (R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid + 5-oxothiomorpholine-3-carboxylic acid + Otc + PSI-MOD + Pyro-carbamidomethyl + S-carbamoylmethylcysteine cyclization (N-terminus) + MOD:01871 + + cyclized N-terminal S-carboxamidomethyl-L-cysteine + + + + + A protein modification that effectively cyclizes an S-carboxamidomethyl-L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid with the loss of ammonia. + DeltaMass:336 + PubMed:12643538 + Unimod:26 + + + + + (R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid + + + + + + 5-oxothiomorpholine-3-carboxylic acid + + + + + + Otc + + + + + + Pyro-carbamidomethyl + + + + + + S-carbamoylmethylcysteine cyclization (N-terminus) + + + + + + + + + + + + + + + + + + + + + + A protein modification that effectively cyclizes an S-carboxymethyl-L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid with the loss of water. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 5 H 6 N 1 O 2 S 1 + 144.17 + 144.01192 + MOD:01061 + artifact + N-term + Unimod:26 + (R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid + 5-oxothiomorpholine-3-carboxylic acid + Otc + PSI-MOD + Pyro-carbamidomethyl + S-carbamoylmethylcysteine cyclization (N-terminus) + MOD:01872 + + Contrary to the impression given in Unimod entry 26, the cyclization of N-terminal S-carboxymethyl-L-cysteine is not reported in PubMed:1263538. The cyclization would be expected to proceed under strongly acidic conditions [JSG]. + cyclized N-terminal S-carboxymethyl-L-cysteine + + + + + A protein modification that effectively cyclizes an S-carboxymethyl-L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid with the loss of water. + PubMed:12643538 + Unimod:26 + + + + + (R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid + + + + + + 5-oxothiomorpholine-3-carboxylic acid + + + + + + Otc + + + + + + Pyro-carbamidomethyl + + + + + + S-carbamoylmethylcysteine cyclization (N-terminus) + + + + + + + + + + + A protein modification that effectively converts an L-alanine residue to N-carboxy-L-alanine. + 44.01 + C 1 H 0 N 0 O 2 + 43.98983 + C 4 H 6 N 1 O 3 + 116.1 + 116.03477 + A + natural + N-term + (S)-2-carboxyamino-propanoic acid + 2-carbamic-propanoic acid + N-carboxymethionine + PSI-MOD + MOD:01873 + This metastable modification can be formed by a protein N-terminal in solutions with a high concentration of dissolved carbon dioxide [JSG]. + N-carboxy-L-alanine + + + + + A protein modification that effectively converts an L-alanine residue to N-carboxy-L-alanine. + PubMed:18688235 + PubMed:4593770 + PubMed:4647257 + PubMed:8312270 + + + + + (S)-2-carboxyamino-propanoic acid + + + + + + 2-carbamic-propanoic acid + + + + + + N-carboxymethionine + + + + + + + + + + + A protein modification that effectively converts an L-alanine residue to N-carboxy-L-valine. + 44.01 + C 1 H 0 N 0 O 2 + 43.98983 + C 6 H 10 N 1 O 3 + 144.15 + 144.06607 + V + natural + N-term + (S)-2-carboxyamino-propanoic acid + 2-carbamic-propanoic acid + N-carboxymethionine + PSI-MOD + MOD:01874 + This metastable modification can be formed by a protein N-terminal in solutions with a high concentration of dissolved carbon dioxide [JSG]. + N-carboxy-L-valine + + + + + A protein modification that effectively converts an L-alanine residue to N-carboxy-L-valine. + PubMed:18688235 + PubMed:4593770 + PubMed:4647257 + PubMed:8312270 + + + + + (S)-2-carboxyamino-propanoic acid + + + + + + 2-carbamic-propanoic acid + + + + + + N-carboxymethionine + + + + + + + + + + + A protein modification that effectively replaces an N6-amino hydrogen atom of L-lysine with an acyl group. + K + natural + N6AcylLys + PSI-MOD + MOD:01875 + + N6-acylated L-lysine + + + + + A protein modification that effectively replaces an N6-amino hydrogen atom of L-lysine with an acyl group. + PubMed:18688235 + + + + + N6AcylLys + + + + + + + + + OBSOLETE because identical to MOD:00457 + MOD:00457 + 100.02 + (12)C 4 (1)H 4 O 3 + 100.016045 + X + artifact + N-term + PSI-MOD + MOD:01876 + 4x(1)H,4x(12)C-labeled alpha-amino succinylated residue + true + + + + + OBSOLETE because identical to MOD:00457 + PubMed:18688235 + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue and an L-arginine residue to 2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid. + -6.05 + C 0 H -6 N 0 O 0 S 0 + -6.04695 + C 9 H 12 N 5 O 2 S 1 + 254.29 + 254.07117 + C, R + natural + N-term + uniprot.ptm:PTM-0457 + (4Z)-2-(4-guanidinobutanoyl)-5-oxo-4-(sulfanylmethylidene)-4,5-dihydro-1H-imidazole + 2-(4-guanidinobutanoyl)-5-hydroxy-1H-imidazole-4-carbothioic O-acid + 2-(4-guanidinobutanoyl)-5-hydroxy-4-thioformyl-1H-imidazole [tautomer] + 2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid + CROSSLNK 2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid (Arg-Cys) + PSI-MOD + MOD:01877 + Cross-link 2. + 2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid + + + + + A protein modification that effectively converts an L-cysteine residue and an L-arginine residue to 2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid. + PubMed:20961038 + RESID:AA0553 + + + + + (4Z)-2-(4-guanidinobutanoyl)-5-oxo-4-(sulfanylmethylidene)-4,5-dihydro-1H-imidazole + + + + + + 2-(4-guanidinobutanoyl)-5-hydroxy-1H-imidazole-4-carbothioic O-acid + + + + + + 2-(4-guanidinobutanoyl)-5-hydroxy-4-thioformyl-1H-imidazole [tautomer] + + + + + + 2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid + + + + + + CROSSLNK 2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid (Arg-Cys) + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue and an L-threonine residue to L-threonine 5-hydroxyoxazole-4-carbothionic acid. + -4.03 + C 0 H -4 N 0 O 0 S 0 + -4.0313 + C 7 H 8 N 2 O 3 S 1 + 200.21 + 200.02556 + C, T + natural + uniprot.ptm:PTM-0458 + (4Z)-2-[(1S,2R)-1-amino-2-hydroxypropyl]-4-(sulfanylmethylidene)-1,3-oxazol-5(4H)-one [tautomer] + 2-[(1S,2R)-1-amino-2-hydroxypropyl]-5-hydroxy-1,3-oxazole-4-carbothioic O-acid + CROSSLNK Threonine 5-hydroxy-oxazole-4-carbonthionic acid (Thr-Cys) + L-threonine 5-hydroxy-oxazole-4-carbonthionic acid + PSI-MOD + MOD:01878 + Cross-link 2. + L-threonine 5-hydroxyoxazole-4-carbonthionic acid + + + + + A protein modification that effectively converts an L-cysteine residue and an L-threonine residue to L-threonine 5-hydroxyoxazole-4-carbothionic acid. + PubMed:20961038 + RESID:AA0554 + + + + + (4Z)-2-[(1S,2R)-1-amino-2-hydroxypropyl]-4-(sulfanylmethylidene)-1,3-oxazol-5(4H)-one [tautomer] + + + + + + 2-[(1S,2R)-1-amino-2-hydroxypropyl]-5-hydroxy-1,3-oxazole-4-carbothioic O-acid + + + + + + CROSSLNK Threonine 5-hydroxy-oxazole-4-carbonthionic acid (Thr-Cys) + + + + + + L-threonine 5-hydroxy-oxazole-4-carbonthionic acid + + + + + + + + + + + A protein modification that effectively converts two L-cysteine residues, an L-arginine residue, an L-threonine residue and a copper atom to the methanobactin SB2 copper complex. + 84.48 + C 0 Cu 1 H -9 N 1 O 1 S 0 + 83.85716 + C 6 Cu 1 H 1 N 3 O 3 S 2 + 290.76 + 289.87552 + C, C, R, T + natural + N-term + METAL copper [Cu-methanobactin SB2 complex] + [5-(hydroxy[sulfanyl-kappaS]methylene)-3,5-dihydro-4H-imidazol-4-onato-kappaN1][4-(hydroxy[sulfanyl-kappaS]methylene)-1,3-oxazol-5(4H)-onato-kappaN]copper + methanobactin SB2 copper complex + PSI-MOD + MOD:01879 + Cross-link 2. + methanobactin SB2 copper complex + + + + + A protein modification that effectively converts two L-cysteine residues, an L-arginine residue, an L-threonine residue and a copper atom to the methanobactin SB2 copper complex. + PubMed:20961038 + RESID:AA0555 + + + + + METAL copper [Cu-methanobactin SB2 complex] + + + + + + [5-(hydroxy[sulfanyl-kappaS]methylene)-3,5-dihydro-4H-imidazol-4-onato-kappaN1][4-(hydroxy[sulfanyl-kappaS]methylene)-1,3-oxazol-5(4H)-onato-kappaN]copper + + + + + + methanobactin SB2 copper complex + + + + + + + + + + + modification from RESID + 71.12 + C 4 H 9 N 1 O 0 + 71.0735 + C 10 H 21 N 3 O 1 + 199.3 + 199.16846 + K + natural + uniprot.ptm:PTM-0684 + (2S)-2-amino-6-[(4-aminobutyl)amino]hexanoic acid + L-deoxyhypusine + MOD_RES Deoxyhypusine + N6-(4-aminobutyl)lysine + deoxyhypusine + PSI-MOD + MOD:01880 + L-deoxyhypusine + + + + + modification from RESID + ChEBI:50038 + PubMed:16452303 + RESID:AA0564 + + + + + (2S)-2-amino-6-[(4-aminobutyl)amino]hexanoic acid + + + + + + L-deoxyhypusine + + + + + + MOD_RES Deoxyhypusine + + + + + + N6-(4-aminobutyl)lysine + + + + + + deoxyhypusine + + + + + + + + + + + + A protein modification that effectively crosslinks an L-phenylalanine residue and an L-valine residue by a free radical process effectively releasing a hydrogen molecule and forming 3-(L-phenylalan-2'-yl)-L-valine. + -2.02 + C 0 H -2 N 0 O 0 + -2.01565 + C 14 H 16 N 2 O 2 + 244.29 + 244.12119 + F, V + natural + (2S)-2-amino-4-(2-[(2S)-2-amino-2-carboxyethyl]phenyl)-3-methylbutanoic acid + 3-(L-phenylalan-2'-yl)-L-valine + symerythrin valine-phenylalanine cross-link + PSI-MOD + MOD:01881 + Cross-link 2. + 3-(L-phenylalan-2'-yl)-L-valine + + + + + A protein modification that effectively crosslinks an L-phenylalanine residue and an L-valine residue by a free radical process effectively releasing a hydrogen molecule and forming 3-(L-phenylalan-2'-yl)-L-valine. + PubMed:21596985 + RESID:AA0565 + + + + + (2S)-2-amino-4-(2-[(2S)-2-amino-2-carboxyethyl]phenyl)-3-methylbutanoic acid + + + + + + 3-(L-phenylalan-2'-yl)-L-valine + + + + + + symerythrin valine-phenylalanine cross-link + + + + + + + + + + A protein modification that effectively crosslinks the carbonyl of an amino acid residue at position n with the alpha amino of a glycine residue at position n+2 to form a 5-imidazolinone ring. + PSI-MOD + MOD:01882 + 5-imidazolinone ring crosslinked residues (Gly) + + + + + A protein modification that effectively crosslinks the carbonyl of an amino acid residue at position n with the alpha amino of a glycine residue at position n+2 to form a 5-imidazolinone ring. + PubMed:18688235 + + + + + + + + + A protein modification that crosslinks two residues by rearrangement and condensation of a cysteine with the carbonyl of the preceding residue to form a 5-imidazolinone ring. + PSI-MOD + MOD:01883 + 5-imidazolinone ring crosslinked residues (Cys) + + + + + A protein modification that crosslinks two residues by rearrangement and condensation of a cysteine with the carbonyl of the preceding residue to form a 5-imidazolinone ring. + PubMed:18688235 + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a 4-aminobutyl group, usually derived from spermidine. + X + PSI-MOD + MOD:01884 + + 4-aminobutylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with a 4-aminobutyl group, usually derived from spermidine. + PubMed:18688235 + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a biotinyl group. + 226.29 + C 10 H 14 N 2 O 2 S 1 + 226.0776 + X + natural + 5-((3aS,4S,6aR)-hexahydro-2-oxo-1H-thieno[3,4-d]imidazol-4-yl)-1-oxopentyl + Biotinylation + BtnRes + PSI-MOD + MOD:01885 + + biotinylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with a biotinyl group. + PubMed:18688235 + + + + + 5-((3aS,4S,6aR)-hexahydro-2-oxo-1H-thieno[3,4-d]imidazol-4-yl)-1-oxopentyl + + + + + + Biotinylation + + + + + + BtnRes + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an sulfanyl or substituted sulfanyl group. + X + PSI-MOD + MOD:01886 + + thiolated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an sulfanyl or substituted sulfanyl group. + PubMed:18688235 + + + + + + + + + + A protein modification that is produced by reaction with 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate, Uniblue A, to form Uniblue A lysine adduct. + 484.5 + C 22 H 16 N 2 O 7 S 2 + 484.0399 + C 28 H 28 N 4 O 8 S 2 + 612.67 + 612.1348 + K + artifact + 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate + 1-amino-9,10-dioxo-4-{[3-(vinylsulfonyl)phenyl]amino}-9,10-dihydroanthracene-2-sulfonate + N6UniblueALys + Uniblue A + PSI-MOD + MOD:01887 + + Uniblue A derivatized lysine + + + + + A protein modification that is produced by reaction with 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate, Uniblue A, to form Uniblue A lysine adduct. + PubMed:18688235 + + + + + 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate + + + + + + 1-amino-9,10-dioxo-4-{[3-(vinylsulfonyl)phenyl]amino}-9,10-dihydroanthracene-2-sulfonate + + + + + + N6UniblueALys + + + + + + Uniblue A + + + + + + + + + + A protein modification that effectively removes two neutral hydrogen atoms (proton and electron) from a residue. + -2.02 + C 0 H -2 N 0 O 0 + -2.01565 + X + Unimod:401 + 2dHRes + PSI-MOD + MOD:01888 + + didehydrogenated residue + + + + + A protein modification that effectively removes two neutral hydrogen atoms (proton and electron) from a residue. + Unimod:401 + + + + + 2dHRes + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-(2-succinyl)-L-cysteine, by addition of either fumaric acid or maleic acid. + 116.07 + C 4 H 4 N 0 O 4 S 0 + 116.010956 + C 7 H 9 N 1 O 5 S 1 + 219.21 + 219.02014 + C + natural + Unimod:957 + uniprot.ptm:PTM-0674 + (2R)-2-amino-3-([(1R)-1,2-dicarboxyethyl]sulfanyl)propanoic acid + (2R)-2-{[(2R)-2-amino-2-carboxyethyl]sulfanyl}butanedioic acid + 2-((2-amino-2-carboxyethyl)thio)butanedioic acid + 2-amino-3-(1,2-dicarboxyethylthio)propanoic acid + MOD_RES S-(2-succinyl)cysteine + S-(1,2-dicarboxyethyl)cysteine + S-(2-succinyl)-L-cysteine + S-(2-succinyl)cysteine + S-[(2R)-2-succinyl]-L-cysteine + PSI-MOD + MOD:01889 + S-(2-succinyl)-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-(2-succinyl)-L-cysteine, by addition of either fumaric acid or maleic acid. + PubMed:16624247 + PubMed:18448829 + PubMed:20677745 + RESID:AA0561 + Unimod:957 + + + + + (2R)-2-amino-3-([(1R)-1,2-dicarboxyethyl]sulfanyl)propanoic acid + + + + + + (2R)-2-{[(2R)-2-amino-2-carboxyethyl]sulfanyl}butanedioic acid + + + + + + 2-((2-amino-2-carboxyethyl)thio)butanedioic acid + + + + + + 2-amino-3-(1,2-dicarboxyethylthio)propanoic acid + + + + + + MOD_RES S-(2-succinyl)cysteine + + + + + + S-(1,2-dicarboxyethyl)cysteine + + + + + + S-(2-succinyl)-L-cysteine + + + + + + S-(2-succinyl)cysteine + + + + + + S-[(2R)-2-succinyl]-L-cysteine + + + + + + + + + + + A protein modification that effectively crosslinks an N-formyl-L-methionine residue and an L-histidine residue to form N-[(L-histidin-1'-yl)methyl]-L-methionine. + -16.0 + C 0 H 0 N 0 O -1 S 0 + -15.994915 + C 12 H 17 N 4 O 2 S 1 + 281.35 + 281.1072 + H, MOD:00030 + hypothetical + N-term + (2S)-2-([(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl)methyl]amino)-4-(methylsulfanyl)butanoic acid + N-[(L-histidin-1'-yl)methyl]-L-methionine + PSI-MOD + MOD:01890 + Cross-link 2. + N-[(L-histidin-1'-yl)methyl]-L-methionine (fMet) + + + + + A protein modification that effectively crosslinks an N-formyl-L-methionine residue and an L-histidine residue to form N-[(L-histidin-1'-yl)methyl]-L-methionine. + PubMed:19622680 + RESID:AA0566#FMET + + + + + (2S)-2-([(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl)methyl]amino)-4-(methylsulfanyl)butanoic acid + + + + + + N-[(L-histidin-1'-yl)methyl]-L-methionine + + + + + + + + + + + A protein modification that effectively crosslinks an L-methionine residue and an L-histidine residue to form N-[(L-histidin-1'-yl)methyl]-L-methionine. + 12.01 + C 1 H 0 N 0 O 0 S 0 + 12.0 + C 12 H 17 N 4 O 2 S 1 + 281.35 + 281.1072 + H, M + hypothetical + N-term + (2S)-2-([(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl)methyl]amino)-4-(methylsulfanyl)butanoic acid + N-[(L-histidin-1'-yl)methyl]-L-methionine + PSI-MOD + MOD:01891 + Cross-link 2. + N-[(L-histidin-1'-yl)methyl]-L-methionine (Met) + + + + + A protein modification that effectively crosslinks an L-methionine residue and an L-histidine residue to form N-[(L-histidin-1'-yl)methyl]-L-methionine. + PubMed:19622680 + RESID:AA0566#MET + + + + + (2S)-2-([(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl)methyl]amino)-4-(methylsulfanyl)butanoic acid + + + + + + N-[(L-histidin-1'-yl)methyl]-L-methionine + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-crotonyl-L-lysine. + 68.07 + C 4 H 4 N 0 O 1 + 68.026215 + C 10 H 16 N 2 O 2 + 196.25 + 196.12119 + K + hypothetical + uniprot.ptm:PTM-0475 + (2S)-2-amino-6-[(2E)-but-2-enamido]hexanoic acid + (2S)-2-amino-6-[(2E)-but-2-enoylamino]hexanoic acid + (2S)-2-azanyl-6-[(2E)-but-2-enoylazanyl]hexanoic acid + MOD_RES N6-crotonyl-L-lysine + N(epsilon)-crotonyllysine + N6-(E)-crotonyllysine + N6-[(2E)-2-butenoyl]-L-lysine + N6-crotonyl-L-lysine + N6-crotonyllysine + N6-trans-crotonyllysine + PSI-MOD + MOD:01892 + N6-crotonyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-crotonyl-L-lysine. + PubMed:21925322 + RESID:AA0567 + + + + + (2S)-2-amino-6-[(2E)-but-2-enamido]hexanoic acid + + + + + + (2S)-2-amino-6-[(2E)-but-2-enoylamino]hexanoic acid + + + + + + (2S)-2-azanyl-6-[(2E)-but-2-enoylazanyl]hexanoic acid + + + + + + MOD_RES N6-crotonyl-L-lysine + + + + + + N(epsilon)-crotonyllysine + + + + + + N6-(E)-crotonyllysine + + + + + + N6-[(2E)-2-butenoyl]-L-lysine + + + + + + N6-crotonyl-L-lysine + + + + + + N6-crotonyllysine + + + + + + N6-trans-crotonyllysine + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-malonyl-L-lysine. + 86.05 + C 3 H 2 N 0 O 3 + 86.0004 + C 9 H 14 N 2 O 4 + 214.22 + 214.09535 + K + hypothetical + uniprot.ptm:PTM-0467 + (2S)-2-amino-6-[(carboxyacetyl)amino]hexanoic acid + 2-azanyl-6-[(carboxyacetyl)azanyl]hexanoic acid + MOD_RES N6-malonyllysine + N(epsilon)-(malonyl)lysine + N6-(carboxyacetyl)lysine + N6-malonyl-L-lysine + N6-malonyllysine + malonyllysine + PSI-MOD + MOD:01893 + N6-malonyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-malonyl-L-lysine. + PubMed:21908771 + PubMed:8349414 + RESID:AA0568 + + + + + (2S)-2-amino-6-[(carboxyacetyl)amino]hexanoic acid + + + + + + 2-azanyl-6-[(carboxyacetyl)azanyl]hexanoic acid + + + + + + MOD_RES N6-malonyllysine + + + + + + N(epsilon)-(malonyl)lysine + + + + + + N6-(carboxyacetyl)lysine + + + + + + N6-malonyl-L-lysine + + + + + + N6-malonyllysine + + + + + + malonyllysine + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an propanoyl group. + 56.06 + C 3 H 4 O 1 + 56.026215 + X + artifact + Unimod:58 + PSI-MOD + Propionate labeling reagent light form (N-term & K) + Propionyl + MOD:01894 + propanoylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an propanoyl group. + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + Unimod:58 + + + + + Propionate labeling reagent light form (N-term & K) + + + + + + Propionyl + + + + + + + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 3x(12)C-labeled propanoyl group. + 56.03 + (12)C 3 H 4 O 1 + 56.026215 + X + artifact + Unimod:58 + PSI-MOD + Propionate labeling reagent light form (N-term & K) + Propionyl + MOD:01895 + alpha-amino 3x(12)C-labeled propanoylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 3x(12)C-labeled propanoyl group. + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + Unimod:58#N-term + + + + + Propionate labeling reagent light form (N-term & K) + + + + + + Propionyl + + + + + + + + + + + A protein modification produced by trifluoroacetic acid forming an adduct, either a salt or a hydrogen bonded carboxylic acid dimer, with an amino acid residue. + 114.02 + C 2 F 3 H 1 O 2 + 113.99287 + X + artifact + TFA + PSI-MOD + MOD:01896 + Trifluoroacetic acid has been observed to form adducts in both negative and positive mode analysis (Mark Collins, private communication) [JSG]. + trifluoroacetic acid adduct + + + + + A protein modification produced by trifluoroacetic acid forming an adduct, either a salt or a hydrogen bonded carboxylic acid dimer, with an amino acid residue. + PubMed:18688235 + + + + + TFA + + + + + + + + + + + + + A protein modification that effectively converts an L-isoleucine residue to 5-hydroxy-3-methyl-L-proline. + 13.98 + C 0 H -2 N 0 O 1 + 13.979265 + C 6 H 9 N 1 O 2 + 127.14 + 127.06333 + I + natural + uniprot.ptm:PTM-0466 + (2S,3S,5Xi)-5-hydroxy-3-methylpyrrolidine-2-carboxylic acid + 5-hydroxy-3-methyl-L-proline + 5-hydroxy-3-methylproline + 5Hy3MePro(Ile) + MOD_RES 5-hydroxy-3-methylproline (Ile) + beta-methyl-delta-hydroxyproline + PSI-MOD + MOD:01897 + 5-hydroxy-3-methyl-L-proline (Ile) + + + + + A protein modification that effectively converts an L-isoleucine residue to 5-hydroxy-3-methyl-L-proline. + PubMed:21788474 + PubMed:7592021 + PubMed:8557573 + RESID:AA0473 + + + + + (2S,3S,5Xi)-5-hydroxy-3-methylpyrrolidine-2-carboxylic acid + + + + + + 5-hydroxy-3-methyl-L-proline + + + + + + 5-hydroxy-3-methylproline + + + + + + 5Hy3MePro(Ile) + + + + + + MOD_RES 5-hydroxy-3-methylproline (Ile) + + + + + + beta-methyl-delta-hydroxyproline + + + + + + + + + + modification from RESID + 28.05 + C 2 H 4 N 0 O 0 + 28.0313 + C 8 H 17 N 4 O 1 + 185.25 + 185.14024 + R + natural + N-term + uniprot.ptm:PTM-0459 + (2S)-5-[(diaminomethylidene)amino]-2-(dimethylamino)pentanoic acid + (2S)-5-carbamimidamido-2-(dimethylamino)pentanoic acid [tautomer] + MOD_RES N2,N2-dimethylarginine + N(alpha),N(alpha)-dimethylarginine + N2,N2-dimethyl-L-arginine + N2,N2-dimethylarginine + PSI-MOD + MOD:01898 + N2,N2-dimethyl-L-arginine + + + + + modification from RESID + PubMed:21568297 + PubMed:21950656 + RESID:AA0569 + + + + + (2S)-5-[(diaminomethylidene)amino]-2-(dimethylamino)pentanoic acid + + + + + + (2S)-5-carbamimidamido-2-(dimethylamino)pentanoic acid [tautomer] + + + + + + MOD_RES N2,N2-dimethylarginine + + + + + + N(alpha),N(alpha)-dimethylarginine + + + + + + N2,N2-dimethyl-L-arginine + + + + + + N2,N2-dimethylarginine + + + + + + + + + + + + A protein modification that effectively crosslinks an L-arginine residue and an L-cysteine residue to form arginine thiazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 S 0 + -20.026215 + C 9 H 13 N 5 O 1 S 1 + 239.3 + 239.08408 + C, R + natural + uniprot.ptm:PTM-0460 + 2-[(1S)-1-amino-4-([diaminomethylidene]amino)butyl]-1,3-thiazole-4-carboxylic acid + CROSSLNK Thiazole-4-carboxylic acid (Arg-Cys) + L-arginine thiazole-4-carboxylic acid + PSI-MOD + MOD:01899 + Cross-link 2. + L-arginine thiazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-arginine residue and an L-cysteine residue to form arginine thiazole-4-carboxylic acid. + PubMed:21568297 + PubMed:21950656 + RESID:AA0570 + + + + + 2-[(1S)-1-amino-4-([diaminomethylidene]amino)butyl]-1,3-thiazole-4-carboxylic acid + + + + + + CROSSLNK Thiazole-4-carboxylic acid (Arg-Cys) + + + + + + L-arginine thiazole-4-carboxylic acid + + + + + + + + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-cysteine 5-methyloxazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 S 0 + -20.026215 + C 7 H 8 N 2 O 2 S 1 + 184.21 + 184.03065 + C, T + natural + uniprot.ptm:PTM-0461 + 2-[(1R)-1-amino-2-sulfanylethyl]-5-methyl-1,3-oxazole-4-carboxylic acid + 2-[(1R)-1-azanyl-2-sulfanylethyl]-5-methyl-1,3-oxazole-4-carboxylic acid + CROSSLNK 5-methyloxazole-4-carboxylic acid (Cys-Thr) + L-cysteine 5-methyloxazole-4-carboxylic acid + PSI-MOD + MOD:01900 + Cross-link 2. + L-cysteine 5-methyloxazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-cysteine 5-methyloxazole-4-carboxylic acid. + PubMed:21568297 + PubMed:21950656 + RESID:AA0571 + + + + + 2-[(1R)-1-amino-2-sulfanylethyl]-5-methyl-1,3-oxazole-4-carboxylic acid + + + + + + 2-[(1R)-1-azanyl-2-sulfanylethyl]-5-methyl-1,3-oxazole-4-carboxylic acid + + + + + + CROSSLNK 5-methyloxazole-4-carboxylic acid (Cys-Thr) + + + + + + L-cysteine 5-methyloxazole-4-carboxylic acid + + + + + + + + + + + A protein modification that effectively crosslinks two L-threonine residues to form L-threonine 5-methyloxazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 + -20.026215 + C 8 H 10 N 2 O 3 + 182.18 + 182.06914 + T, T + natural + uniprot.ptm:PTM-0462 + 2-[(1S,2R)-1-amino-2-hydroxypropyl]-5-methyl-1,3-oxazole-4-carboxylic acid + 2-[(1S,2R)-1-azanyl-2-hydroxypropyl]-5-methyl-1,3-oxazole-4-carboxylic acid + CROSSLNK 5-methyloxazole-4-carboxylic acid (Thr-Thr) + L-threonine 5-methyloxazole-4-carboxylic acid + PSI-MOD + MOD:01901 + Cross-link 2. + L-threonine 5-methyloxazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks two L-threonine residues to form L-threonine 5-methyloxazole-4-carboxylic acid. + PubMed:21568297 + PubMed:21950656 + RESID:AA0572 + + + + + 2-[(1S,2R)-1-amino-2-hydroxypropyl]-5-methyl-1,3-oxazole-4-carboxylic acid + + + + + + 2-[(1S,2R)-1-azanyl-2-hydroxypropyl]-5-methyl-1,3-oxazole-4-carboxylic acid + + + + + + CROSSLNK 5-methyloxazole-4-carboxylic acid (Thr-Thr) + + + + + + L-threonine 5-methyloxazole-4-carboxylic acid + + + + + + + + + + + + A protein modification that effectively crosslinks an L-isoleucine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 + -20.026215 + C 9 H 12 N 2 O 2 + 180.21 + 180.08987 + I, S + natural + uniprot.ptm:PTM-0463 + 2-[(1S,2S)-1-amino-2-methylbutyl]-1,3-oxazole-4-carboxylic acid + 2-[(1S,2S)-1-azanyl-2-methylbutyl]-1,3-oxazole-4-carboxylic acid + CROSSLNK Oxazole-4-carboxylic acid (Ile-Ser) + L-isoleucine oxazole-4-carboxylic acid + PSI-MOD + MOD:01902 + Cross-link 2. + L-isoleucine oxazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-isoleucine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid. + PubMed:21568297 + PubMed:21950656 + RESID:AA0573 + + + + + 2-[(1S,2S)-1-amino-2-methylbutyl]-1,3-oxazole-4-carboxylic acid + + + + + + 2-[(1S,2S)-1-azanyl-2-methylbutyl]-1,3-oxazole-4-carboxylic acid + + + + + + CROSSLNK Oxazole-4-carboxylic acid (Ile-Ser) + + + + + + L-isoleucine oxazole-4-carboxylic acid + + + + + + + + + + + A protein modification that effectively crosslinks two L-serine residues to form serine oxazole-4-carboxylic acid. + -20.03 + C 0 H -4 N 0 O -1 + -20.026215 + C 6 H 6 N 2 O 3 + 154.13 + 154.03784 + S, S + natural + uniprot.ptm:PTM-0464 + 2-[(1S)-1-amino-2-hydroxyethyl]-1,3-oxazole-4-carboxylic acid + 2-[(1S)-1-azanyl-2-hydroxyethyl]-1,3-oxazole-4-carboxylic acid + CROSSLNK Oxazole-4-carboxylic acid (Ser-Ser) + L-serine oxazole-4-carboxylic acid + PSI-MOD + MOD:01903 + Cross-link 2. + L-serine oxazole-4-carboxylic acid + + + + + A protein modification that effectively crosslinks two L-serine residues to form serine oxazole-4-carboxylic acid. + PubMed:21568297 + PubMed:21950656 + RESID:AA0574 + + + + + 2-[(1S)-1-amino-2-hydroxyethyl]-1,3-oxazole-4-carboxylic acid + + + + + + 2-[(1S)-1-azanyl-2-hydroxyethyl]-1,3-oxazole-4-carboxylic acid + + + + + + CROSSLNK Oxazole-4-carboxylic acid (Ser-Ser) + + + + + + L-serine oxazole-4-carboxylic acid + + + + + + + + + + + + A protein modification that effectively crosslinks an L-serine residue and an L-threonine residue to form L-serine 5-methyloxazoline-4-carboxylic acid. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 7 H 10 N 2 O 3 + 170.17 + 170.06914 + S, T + natural + uniprot.ptm:PTM-0465 + 2-[(1S)-1-amino-2-hydroxyethyl]-5-methyl-1,3-oxazoline-4-carboxylic acid + 2-[(1S)-1-amino-2-hydroxyethyl]-5-methyl-4,5-dihydro-1,3-oxazole-4-carboxylic acid + 2-[(1S)-1-azanyl-2-hydroxyethyl]-5-methyl-4,5-dihydro-1,3-oxazole-4-carboxylic acid + CROSSLNK 5-methyloxazoline-4-carboxylic acid (Ser-Thr) + L-serine 5-methyloxazoline-4-carboxylic acid + PSI-MOD + MOD:01904 + Cross-link 2. + L-serine 5-methyloxazoline-4-carboxylic acid + + + + + A protein modification that effectively crosslinks an L-serine residue and an L-threonine residue to form L-serine 5-methyloxazoline-4-carboxylic acid. + PubMed:21568297 + PubMed:21950656 + RESID:AA0575 + + + + + 2-[(1S)-1-amino-2-hydroxyethyl]-5-methyl-1,3-oxazoline-4-carboxylic acid + + + + + + 2-[(1S)-1-amino-2-hydroxyethyl]-5-methyl-4,5-dihydro-1,3-oxazole-4-carboxylic acid + + + + + + 2-[(1S)-1-azanyl-2-hydroxyethyl]-5-methyl-4,5-dihydro-1,3-oxazole-4-carboxylic acid + + + + + + CROSSLNK 5-methyloxazoline-4-carboxylic acid (Ser-Thr) + + + + + + L-serine 5-methyloxazoline-4-carboxylic acid + + + + + + + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to 5-hydroxy-3-methyl-L-proline. + C 6 H 9 N 1 O 2 + 127.14 + 127.06333 + X + natural + (2S,3S,5Xi)-5-hydroxy-3-methylpyrrolidine-2-carboxylic acid + 5-hydroxy-3-methyl-L-proline + 5-hydroxy-3-methylproline + 5Hy3MePro + MOD_RES 5-hydroxy-3-methylproline (Ile) + beta-methyl-delta-hydroxyproline + PSI-MOD + MOD:01905 + 5-hydroxy-3-methyl-L-proline + + + + + A protein modification that effectively converts a source amino acid residue to 5-hydroxy-3-methyl-L-proline. + PubMed:7592021 + PubMed:8557573 + RESID:AA0473 + + + + + (2S,3S,5Xi)-5-hydroxy-3-methylpyrrolidine-2-carboxylic acid + + + + + + 5-hydroxy-3-methyl-L-proline + + + + + + 5-hydroxy-3-methylproline + + + + + + 5Hy3MePro + + + + + + MOD_RES 5-hydroxy-3-methylproline (Ile) + + + + + + beta-methyl-delta-hydroxyproline + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to dehydromethionine. + -1.01 + C 0 H -1 N 0 O 0 S 0 + -1.008374 + 1+ + C 5 H 9 N 1 O 1 S 1 + 131.19 + 131.03993 + M + artifact + N-term + (3S)-3-carboxy-1-methylisothiazolidin-1-ium + L-dehydromethionine + PSI-MOD + MOD:01906 + dehydromethionine + + + + + A protein modification that effectively converts an L-methionine residue to dehydromethionine. + PubMed:18688235 + PubMed:19775156 + + + + + (3S)-3-carboxy-1-methylisothiazolidin-1-ium + + + + + + L-dehydromethionine + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-methioninium (protonated L-methionine) residue to dehydromethionine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.016199 + 1+ + C 5 H 9 N 1 O 1 S 1 + 131.19 + 131.03993 + MOD:001464 + artifact + N-term + (3S)-3-carboxy-1-methylisothiazolidin-1-ium + L-dehydromethionine + PSI-MOD + MOD:01907 + This process accounts only for cyclizaation and not protonation. The alternative process (MOD:01906) accounts for both protonation and cyclization. + dehydromethionine (from L-methioninium) + + + + + A protein modification that effectively converts an L-methioninium (protonated L-methionine) residue to dehydromethionine. + PubMed:18688235 + PubMed:19775156 + + + + + (3S)-3-carboxy-1-methylisothiazolidin-1-ium + + + + + + L-dehydromethionine + + + + + + + + + + A protein modification that effectively converts a residue to the 4-sulfophenyl isothiocyanate adduct, alpha-amino-[(4-sulfophenyl)carbamothioyl] residue. + 215.24 + C 7 H 5 N 1 O 3 S 2 + 214.97108 + X + artifact + Unimod:261 + alpha-amino-[(4-sulfophenyl)carbamothioyl] residue + PSI-MOD + 4-sulfophenyl isothiocyanate + SPITC + MOD:01908 + 4-sulfophenyl isothiocyanate alpha-amino derivatized residue + + + + + A protein modification that effectively converts a residue to the 4-sulfophenyl isothiocyanate adduct, alpha-amino-[(4-sulfophenyl)carbamothioyl] residue. + PubMed:14689565 + PubMed:14745769 + PubMed:15549660 + PubMed:16526082 + Unimod:261#N-term + + + + + alpha-amino-[(4-sulfophenyl)carbamothioyl] residue + + + + + + 4-sulfophenyl isothiocyanate + + + + + + SPITC + + + + + + + + + + A protein modification that effectively converts a residue to the 6x(13)C labeled 4-sulfophenyl isothiocyanate adduct, alpha-amino-[(4-sulfophenyl)carbamothioyl] residue. + 220.99 + (12)C 1 (13)C 6 H 5 N 1 O 3 S 2 + 220.99121 + X + artifact + Unimod:464 + PSI-MOD + 4-sulfophenyl isothiocyanate (Heavy C13) + SPITC:13C(6) + MOD:01909 + 6x(13)C labeled 4-sulfophenyl isothiocyanate alpha-amino derivatized residue + + + + + A protein modification that effectively converts a residue to the 6x(13)C labeled 4-sulfophenyl isothiocyanate adduct, alpha-amino-[(4-sulfophenyl)carbamothioyl] residue. + PubMed:11467524 + PubMed:16526082 + Unimod:464#N-term + + + + + 4-sulfophenyl isothiocyanate (Heavy C13) + + + + + + SPITC:13C(6) + + + + + + + + + + A protein modification that effectively substitutes one hydrogen atom of a residue with one fluorine atom. + 17.99 + C 0 F 1 H -1 N 0 O 0 + 17.990578 + X + artifact + Unimod:127 + F1Res + PSI-MOD + MOD:01910 + monofluorinated residue + + + + + A protein modification that effectively substitutes one hydrogen atom of a residue with one fluorine atom. + Unimod:127 + + + + + F1Res + + + + + + + + + + A protein modification that effectively substitutes one hydrogen atom of a residue with one chlorine atom. + 34.44 + C 0 Cl 1 H -1 N 0 O 0 + 33.96103 + X + artifact + Unimod:936 + Cl1Res + PSI-MOD + MOD:01911 + monochlorinated residue + + + + + A protein modification that effectively substitutes one hydrogen atom of a residue with one chlorine atom. + Unimod:936 + + + + + Cl1Res + + + + + + + + + + A protein modification that effectively substitutes one hydrogen atom of a residue with one bromine atom. + 78.9 + Br 1 C 0 H -1 N 0 O 0 + 77.910515 + X + artifact + Unimod:340 + Br1Res + PSI-MOD + MOD:01912 + monobrominated residue + + + + + A protein modification that effectively substitutes one hydrogen atom of a residue with one bromine atom. + Unimod:340 + + + + + Br1Res + + + + + + + + + + + A protein modification that effectively substitutes one hydrogen atom of an L-tryptophan residue with one chlorine atom. + 34.44 + C 0 Cl 1 H -1 N 0 O 0 + 33.96103 + C 11 Cl 1 H 9 N 2 O 1 + 220.66 + 220.04034 + W + artifact + Cl1Trp + PSI-MOD + MOD:01913 + monochlorinated L-tryptophan + + + + + A protein modification that effectively substitutes one hydrogen atom of an L-tryptophan residue with one chlorine atom. + PubMed:18688235 + + + + + Cl1Trp + + + + + + + + + + + A protein modification that effectively converts a 5-hydroxy-L-lysine residue to O5-galactosyl-L-hydroxylysine. + 162.14 + C 6 H 10 O 5 + 162.05283 + C 16 H 22 N 2 O 7 + 354.36 + 354.1427 + MOD:00037 + natural + Unimod:907 + uniprot.ptm:PTM-0556 + CARBOHYD O-linked (Gal) hydroxylysine + OGal5HyLys + PSI-MOD + Galactosyl hydroxylysine + MOD:01914 + + Secondary to RESID:AA0028. This intermediate is rarely observed [JSG]. + O5-galactosyl-L-hydroxylysine + + + + + A protein modification that effectively converts a 5-hydroxy-L-lysine residue to O5-galactosyl-L-hydroxylysine. + PMID:743239 + PubMed:17516569 + Unimod:907 + + + + + CARBOHYD O-linked (Gal) hydroxylysine + + + + + + OGal5HyLys + + + + + + Galactosyl hydroxylysine + + + + + + + + + + + A protein modification that effectively converts an L-alanine residue to N-formyl-L-alanine. + 28.01 + C 1 H 0 N 0 O 1 + 27.994915 + C 4 H 6 N 1 O 2 + 100.1 + 100.039856 + A + hypothetical + N-term + (2S)-2-(formylamino)propanoic acid + 2-formamidopropanoic acid + 2-formamidopropionic acid + N-formyl-L-alanine + PSI-MOD + MOD:01915 + N-formyl-L-alanine + + + + + A protein modification that effectively converts an L-alanine residue to N-formyl-L-alanine. + PubMed:9334739 + RESID:AA0576 + + + + + (2S)-2-(formylamino)propanoic acid + + + + + + 2-formamidopropanoic acid + + + + + + 2-formamidopropionic acid + + + + + + N-formyl-L-alanine + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to O4'-(N-acetylamino)galactosyl-L-tyrosine. + 203.19 + C 8 H 13 N 1 O 5 + 203.07938 + C 17 H 22 N 2 O 7 + 366.37 + 366.1427 + Y + natural + uniprot.ptm:PTM-0570 + (2S)-2-amino-3-(D-2-acetamido-2-deoxygalactopyranosyloxy)phenylpropanoic acid + CARBOHYD O-linked (GalNAc) tyrosine + O4'-(N-acetylamino)galactosyl-L-tyrosine + O4'-(N-acetylgalactosaminyl)tyrosine + O4'-glycosyl-L-tyrosine + mucin type O-glycosyltyrosine + PSI-MOD + MOD:01916 + O4'-(N-acetylamino)galactosyl-L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to O4'-(N-acetylamino)galactosyl-L-tyrosine. + PubMed:21712440 + PubMed:21983924 + RESID:AA0577 + + + + + (2S)-2-amino-3-(D-2-acetamido-2-deoxygalactopyranosyloxy)phenylpropanoic acid + + + + + + CARBOHYD O-linked (GalNAc) tyrosine + + + + + + O4'-(N-acetylamino)galactosyl-L-tyrosine + + + + + + O4'-(N-acetylgalactosaminyl)tyrosine + + + + + + O4'-glycosyl-L-tyrosine + + + + + + mucin type O-glycosyltyrosine + + + + + + + + + + + + A protein modification that effectively crosslinks an L-aspartic acid residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoaspartyl)-L-lysine and the release of water. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 10 H 15 N 3 O 3 + 225.25 + 225.11134 + D, K + natural + uniprot.ptm:PTM-0486 + (2S)-2-amino-6-([(3S)-3-amino-3-carboxypropanoyl]amino)hexanoic acid + CROSSLNK Isoaspartyl lysine isopeptide (Lys-Asn) + N(epsilon)-(beta-aspartyl)lysine + N6-(L-isoaspartyl)-L-lysine + XLNK-4Asp-N6Lys(Asp) + beta-(N6-lysyl)aspartyl acid + isoaspartyl N6-lysine + PSI-MOD + MOD:01917 + Cross-link 2. + N6-(L-isoaspartyl)-L-lysine (Asp) + + + + + A protein modification that effectively crosslinks an L-aspartic acid residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoaspartyl)-L-lysine and the release of water. + ChEBI:21862 + PubMed:11000116 + PubMed:15044436 + PubMed:18063798 + PubMed:6503713 + RESID:AA0294#ASP + + + + + (2S)-2-amino-6-([(3S)-3-amino-3-carboxypropanoyl]amino)hexanoic acid + + + + + + CROSSLNK Isoaspartyl lysine isopeptide (Lys-Asn) + + + + + + N(epsilon)-(beta-aspartyl)lysine + + + + + + N6-(L-isoaspartyl)-L-lysine + + + + + + XLNK-4Asp-N6Lys(Asp) + + + + + + beta-(N6-lysyl)aspartyl acid + + + + + + isoaspartyl N6-lysine + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to (2S,5S)-5-hydroxylysine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 6 H 12 N 2 O 2 + 144.17 + 144.08987 + K + natural + uniprot.ptm:PTM-0472 + (2S,5S)-2,6-diamino-5-hydroxyhexanoic acid + (2S,5S)-5-hydroxylysine + 2,6-bisazanyl-5-hydroxyhexanoic acid + 2,6-diamino-2,3,4,6-tetradeoxyhexonic acid + L-allo-delta-hydroxylysine + L-threo-delta-hydroxylysine + MOD_RES (5S)-5-hydroxylysine + alpha,epsilon-diamino-delta-hydroxycaproic acid + PSI-MOD + MOD:01918 + + (2S,5S)-5-hydroxylysine + + + + + A protein modification that effectively converts an L-lysine residue to (2S,5S)-5-hydroxylysine. + PubMed:19574390 + PubMed:22238144 + RESID:AA0578 + + + + + (2S,5S)-2,6-diamino-5-hydroxyhexanoic acid + + + + + + (2S,5S)-5-hydroxylysine + + + + + + 2,6-bisazanyl-5-hydroxyhexanoic acid + + + + + + 2,6-diamino-2,3,4,6-tetradeoxyhexonic acid + + + + + + L-allo-delta-hydroxylysine + + + + + + L-threo-delta-hydroxylysine + + + + + + MOD_RES (5S)-5-hydroxylysine + + + + + + alpha,epsilon-diamino-delta-hydroxycaproic acid + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to (2S,3S)-3-hydroxyaspartic acid. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 4 H 5 N 1 O 4 + 131.09 + 131.02185 + D + natural + uniprot.ptm:PTM-0473 + (2S,3S)-2-amino-3-hydroxybutanedioic acid + (2S,3S)-3-hydroxyaspartic acid + (3S)-3-hydroxy-L-aspartic acid + 2-amino-3-hydroxysuccinic acid + 2-azanyl-3-hydroxybutanedioic acid + 3-hydroxyaspartic acid + L-threo-3-hydroxyaspartic acid + L-threo-beta-hydroxyaspartic acid + MOD_RES (3S)-3-hydroxyaspartate + PSI-MOD + MOD:01919 + + (2S,3S)-3-hydroxyaspartic acid + + + + + A protein modification that effectively converts an L-aspartic acid residue to (2S,3S)-3-hydroxyaspartic acid. + ChEBI:10696 + ChEBI:138111 + PubMed:21177872 + RESID:AA0579 + + + + + (2S,3S)-2-amino-3-hydroxybutanedioic acid + + + + + + (2S,3S)-3-hydroxyaspartic acid + + + + + + (3S)-3-hydroxy-L-aspartic acid + + + + + + 2-amino-3-hydroxysuccinic acid + + + + + + 2-azanyl-3-hydroxybutanedioic acid + + + + + + 3-hydroxyaspartic acid + + + + + + L-threo-3-hydroxyaspartic acid + + + + + + L-threo-beta-hydroxyaspartic acid + + + + + + MOD_RES (3S)-3-hydroxyaspartate + + + + + + + + + + + A protein modification that effectively converts an L-histidine residue to 3-hydroxy-L-histidine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 6 H 7 N 3 O 2 + 153.14 + 153.05383 + H + natural + uniprot.ptm:PTM-0477 + (2S)-2-amino-3-hydroxy-3-(1H-imidazol-4-yl)propanoic acid + 3-hydroxy-L-histidine + MOD_RES (3S)-3-hydroxyhistidine + PSI-MOD + MOD:01920 + 3-hydroxy-L-histidine + + + + + A protein modification that effectively converts an L-histidine residue to 3-hydroxy-L-histidine. + ChEBI:138021 + PubMed:21251231 + RESID:AA0580 + + + + + (2S)-2-amino-3-hydroxy-3-(1H-imidazol-4-yl)propanoic acid + + + + + + 3-hydroxy-L-histidine + + + + + + MOD_RES (3S)-3-hydroxyhistidine + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to D-aspartic acid. + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + C 4 H 5 N 1 O 3 + 115.09 + 115.02694 + D + artifactual + (2R)-2-aminobutanedioic acid + 2-azanylbutanedioic acid + D-aspartic acid + aminosuccinic acid + PSI-MOD + MOD:01921 + D-aspartic acid (Asp) + + + + + A protein modification that effectively converts an L-aspartic acid residue to D-aspartic acid. + ChEBI:48094 + PubMed:9384562 + RESID:AA0190#ASP + + + + + (2R)-2-aminobutanedioic acid + + + + + + 2-azanylbutanedioic acid + + + + + + D-aspartic acid + + + + + + aminosuccinic acid + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to 3-methoxydehydroalanine. + 12.01 + C 1 H 0 N 0 O 0 + 12.0 + C 4 H 5 N 1 O 2 + 99.09 + 99.03203 + S + natural + 2-amino-3-methoxyprop-2-enoic acid + 3-methoxydehydroalanine + 3-methoxydidehydroalanine + PSI-MOD + MOD:01922 + 3-methoxydehydroalanine + + + + + A protein modification that effectively converts an L-serine residue to 3-methoxydehydroalanine. + PubMed:19745839 + RESID:AA0582 + + + + + 2-amino-3-methoxyprop-2-enoic acid + + + + + + 3-methoxydehydroalanine + + + + + + 3-methoxydidehydroalanine + + + + + + + + + + + + + A protein modification that effectively crosslinks an L-aspartic acid residue and an L-lysine residue by an isopeptide bond to form N6-(L-aspartyl)-L-lysine and the release of water. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 10 H 16 N 3 O 4 + 242.26 + 242.11407 + D, K + natural + C-term + (2S)-2-amino-6-([(2S)-2-amino-3-carboxypropanoyl]amino)hexanoic acid + N(epsilon)-(alpha-aspartyl)lysine + N6-(L-aspartyl)-L-lysine + XLNK-4Asp-N6Lys(Asp) + alpha-(N6-lysyl)aspartyl acid + aspartyl N6-lysine + PSI-MOD + MOD:01923 + Cross-link 2. + N6-(L-aspartyl)-L-lysine + + + + + A protein modification that effectively crosslinks an L-aspartic acid residue and an L-lysine residue by an isopeptide bond to form N6-(L-aspartyl)-L-lysine and the release of water. + PubMed:15044436 + RESID:AA0583 + + + + + (2S)-2-amino-6-([(2S)-2-amino-3-carboxypropanoyl]amino)hexanoic acid + + + + + + N(epsilon)-(alpha-aspartyl)lysine + + + + + + N6-(L-aspartyl)-L-lysine + + + + + + XLNK-4Asp-N6Lys(Asp) + + + + + + alpha-(N6-lysyl)aspartyl acid + + + + + + aspartyl N6-lysine + + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-octanoyl-L-cysteine. + 126.2 + C 8 H 14 N 0 O 1 S 0 + 126.10446 + C 11 H 19 N 1 O 2 S 1 + 229.34 + 229.11365 + C + natural + (2S)-2-amino-3-(octanoylsulfanyl)propanoic acid + 2-amino-3-(octanoylthio)propanoic acid + ACT_SITE Acyl-thioester intermediate + S-octanoyl-L-cysteine + cysteine octanoate thioester + PSI-MOD + MOD:01924 + S-octanoyl-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-octanoyl-L-cysteine. + PubMed:12591875 + PubMed:16342964 + RESID:AA0584 + + + + + (2S)-2-amino-3-(octanoylsulfanyl)propanoic acid + + + + + + 2-amino-3-(octanoylthio)propanoic acid + + + + + + ACT_SITE Acyl-thioester intermediate + + + + + + S-octanoyl-L-cysteine + + + + + + cysteine octanoate thioester + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to (2S,5R)-5-hydroxylysine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 6 H 12 N 2 O 2 + 144.17 + 144.08987 + K + natural + uniprot.ptm:PTM-0471 + (2S,5R)-2,6-diamino-5-hydroxyhexanoic acid + (2S,5R)-5-hydroxylysine + 2,6-bisazanyl-5-hydroxyhexanoic acid + 2,6-diamino-2,3,4,6-tetradeoxyhexonic acid + 5-hydroxylated L-lysine + 5HyLys + L-erythro-delta-hydroxylysine + MOD_RES (2S,5R)-5-hydroxylysine + alpha,epsilon-diamino-delta-hydroxycaproic acid + PSI-MOD + MOD:01925 + + (2S,5R)-5-hydroxylysine + + + + + A protein modification that effectively converts an L-lysine residue to (2S,5R)-5-hydroxylysine. + ChEBI:18040 + PubMed:13375629 + PubMed:15504407 + PubMed:16101297 + PubMed:2857489 + RESID:AA0028 + + + + + (2S,5R)-2,6-diamino-5-hydroxyhexanoic acid + + + + + + (2S,5R)-5-hydroxylysine + + + + + + 2,6-bisazanyl-5-hydroxyhexanoic acid + + + + + + 2,6-diamino-2,3,4,6-tetradeoxyhexonic acid + + + + + + 5-hydroxylated L-lysine + + + + + + 5HyLys + + + + + + L-erythro-delta-hydroxylysine + + + + + + MOD_RES (2S,5R)-5-hydroxylysine + + + + + + alpha,epsilon-diamino-delta-hydroxycaproic acid + + + + + + + + + + + A protein modification that effectively converts an L-aspartic acid residue to one of the diastereomeric 3-hydroxy-L-aspartic acid residues. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 4 H 5 N 1 O 4 + 131.09 + 131.02185 + D + natural + Unimod:35 + (2S)-2-amino-3-hydroxybutanedioic acid + (2S)-3-hydroxyaspartic acid + 3HyAsp + erythro-beta-hydroxylated L-aspartic acid + hydroxylationd + monohydroxylated aspartic acid + PSI-MOD + Oxidation + MOD:01926 + + 3-hydroxy-L-aspartic acid + + + + + A protein modification that effectively converts an L-aspartic acid residue to one of the diastereomeric 3-hydroxy-L-aspartic acid residues. + OMSSA:59 + Unimod:35#D + + + + + (2S)-2-amino-3-hydroxybutanedioic acid + + + + + + (2S)-3-hydroxyaspartic acid + + + + + + 3HyAsp + + + + + + erythro-beta-hydroxylated L-aspartic acid + + + + + + hydroxylationd + + + + + + monohydroxylated aspartic acid + + + + + + Oxidation + + + + + + + + + + + A protein modification that effectively converts an L-tyrosine residue to O4'-glycosyltyrosine. + Y + natural + OGlycoTyr + PSI-MOD + MOD:01927 + + O-glycosyl-L-tyrosine + + + + + A protein modification that effectively converts an L-tyrosine residue to O4'-glycosyltyrosine. + PubMed:18688235 + + + + + OGlycoTyr + + + + + + + + + + + A protein modification that effectively crosslinks either an L-asparagine residue or an L-aspartic acid residue with a glycine residue by an isopeptide bond with formation of N-(L-isoaspartyl)glycine. + C 6 H 7 N 2 O 3 + 155.13 + 155.04567 + G + natural + N-term + (2S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid + 2-amino-N4-(carboxymethyl)-butanediamic acid + N-(L-isoaspartyl)-glycine + N-beta-aspartylglycine + N4-(carboxymethyl)-asparagine + XLNK-4Asp-NGly + isoaspartyl glycine + PSI-MOD + MOD:01928 + Cross-link 2. + N-(L-isoaspartyl)-glycine + + + + + A protein modification that effectively crosslinks either an L-asparagine residue or an L-aspartic acid residue with a glycine residue by an isopeptide bond with formation of N-(L-isoaspartyl)glycine. + ChEBI:21479 + PubMed:1826288 + RESID:AA0126 + + + + + (2S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid + + + + + + 2-amino-N4-(carboxymethyl)-butanediamic acid + + + + + + N-(L-isoaspartyl)-glycine + + + + + + N-beta-aspartylglycine + + + + + + N4-(carboxymethyl)-asparagine + + + + + + XLNK-4Asp-NGly + + + + + + isoaspartyl glycine + + + + + + + + + + + A protein modification that effectively crosslinks an either an L-asparagine residue or an L-aspartic acid residue with an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoaspartyl)-L-lysine. + C 10 H 15 N 3 O 3 + 225.25 + 225.11134 + K + natural + (2S)-2-amino-6-([(3S)-3-amino-3-carboxypropanoyl]amino)hexanoic acid + CROSSLNK Isoaspartyl lysine isopeptide (Lys-Asn) + N(epsilon)-(beta-aspartyl)lysine + N-(beta-Aspartyl)-Lysine (Crosslink) + N6-(L-isoaspartyl)-L-lysine + XLNK-4Asp-N6Lys + beta-(N6-lysyl)aspartyl acid + isoaspartyl N6-lysine + PSI-MOD + MOD:01929 + Cross-link 2. + N6-(L-isoaspartyl)-L-lysine + + + + + A protein modification that effectively crosslinks an either an L-asparagine residue or an L-aspartic acid residue with an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoaspartyl)-L-lysine. + ChEBI:21862 + DeltaMass:0 + PubMed:11000116 + PubMed:6503713 + RESID:AA0294 + + + + + (2S)-2-amino-6-([(3S)-3-amino-3-carboxypropanoyl]amino)hexanoic acid + + + + + + CROSSLNK Isoaspartyl lysine isopeptide (Lys-Asn) + + + + + + N(epsilon)-(beta-aspartyl)lysine + + + + + + N-(beta-Aspartyl)-Lysine (Crosslink) + + + + + + N6-(L-isoaspartyl)-L-lysine + + + + + + XLNK-4Asp-N6Lys + + + + + + beta-(N6-lysyl)aspartyl acid + + + + + + isoaspartyl N6-lysine + + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to D-aspartic acid. + 0.98 + C 0 H -1 N -1 O 1 + 0.984016 + C 4 H 5 N 1 O 3 + 115.09 + 115.02694 + N + artifactual + (2R)-2-aminobutanedioic acid + 2-azanylbutanedioic acid + D-aspartic acid + aminosuccinic acid + PSI-MOD + MOD:01930 + D-aspartic acid (Asn) + + + + + A protein modification that effectively converts an L-asparagine residue to D-aspartic acid. + ChEBI:48094 + PubMed:9384562 + RESID:AA0190#ASN + + + + + (2R)-2-aminobutanedioic acid + + + + + + 2-azanylbutanedioic acid + + + + + + D-aspartic acid + + + + + + aminosuccinic acid + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-phospho-L-lysine. + 79.98 + C 0 H 1 N 0 O 3 P 1 + 79.96633 + C 6 H 13 N 2 O 4 P 1 + 208.15 + 208.0613 + K + hypothetical + (2S)-2-amino-6-(phosphonoamino)hexanoic acid + (2S)-2-azanyl-6-(phosphonoamino)hexanoic acid + 6-phospholysine + N(6)-phosphonolysine + N(epsilon)-phospholysine + N(epsilon)-phosphonolysine + N(epsilon)-phosphonyllysine + N(epsilon)-phosphoryllysine + N6-phospho-L-lysine + PSI-MOD + MOD:01931 + N6-phospho-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-phospho-L-lysine. + PubMed:20144148 + RESID:AA0585 + + + + + (2S)-2-amino-6-(phosphonoamino)hexanoic acid + + + + + + (2S)-2-azanyl-6-(phosphonoamino)hexanoic acid + + + + + + 6-phospholysine + + + + + + N(6)-phosphonolysine + + + + + + N(epsilon)-phospholysine + + + + + + N(epsilon)-phosphonolysine + + + + + + N(epsilon)-phosphonyllysine + + + + + + N(epsilon)-phosphoryllysine + + + + + + N6-phospho-L-lysine + + + + + + + + + + + A protein modification that effectively cross-links two lysine residues with a carbon-nitrogen bond to form L-lysinonorleucine.. + -17.03 + C 0 H -3 N -1 O 0 + -17.026548 + C 12 H 21 N 3 O 2 + 239.32 + 239.16338 + K, K + natural + (2S)-2-amino-6-([(5S)-5-amino-5-carboxypentyl]amino)hexanoic acid + (2S,2'S)-6,6'-iminobis(2-aminohexanoic acid) + 6-(N6-L-lysino)-L-norleucine + L-lysinonorleucine + N6-[(5S)-5-amino-5-carboxypentyl]-L-lysine + lysinonorleucine + lysinorleucine [misspelling] + lysylnorleucine + PSI-MOD + MOD:01932 + Cross-link 2. + L-lysinonorleucine + + + + + A protein modification that effectively cross-links two lysine residues with a carbon-nitrogen bond to form L-lysinonorleucine.. + PubMed:5117030 + PubMed:5817620 + PubMed:5879466 + PubMed:6030254 + RESID:AA0586 + + + + + (2S)-2-amino-6-([(5S)-5-amino-5-carboxypentyl]amino)hexanoic acid + + + + + + (2S,2'S)-6,6'-iminobis(2-aminohexanoic acid) + + + + + + 6-(N6-L-lysino)-L-norleucine + + + + + + L-lysinonorleucine + + + + + + N6-[(5S)-5-amino-5-carboxypentyl]-L-lysine + + + + + + lysinonorleucine + + + + + + lysinorleucine [misspelling] + + + + + + lysylnorleucine + + + + + + + + + + + A protein modification that effectively cross-links four L-lysine residues to form desmosine. + -58.15 + C 0 H -16 N -3 O 0 + -58.13497 + 1+ + C 24 H 32 N 5 O 4 + 454.55 + 454.24487 + K, K, K, K + natural + 4-[(4S)-4-amino-4-carboxybutyl]-1-[(5S)-5-amino-5-carboxypentyl]-3,5-bis[(3S)-3-amino-3-carboxypropyl]pyridinium + 6-[4-(4-amino-4-carboxybutyl)-3,5-bis(3-amino-3-carboxypropyl)pyridinio]norleucine + desmosine + PSI-MOD + MOD:01933 + Cross-link 4. + desmosine + + + + + A protein modification that effectively cross-links four L-lysine residues to form desmosine. + ChEBI:37629 + PubMed:13941623 + PubMed:14109938 + PubMed:14109939 + PubMed:5839176 + RESID:AA0587 + + + + + 4-[(4S)-4-amino-4-carboxybutyl]-1-[(5S)-5-amino-5-carboxypentyl]-3,5-bis[(3S)-3-amino-3-carboxypropyl]pyridinium + + + + + + 6-[4-(4-amino-4-carboxybutyl)-3,5-bis(3-amino-3-carboxypropyl)pyridinio]norleucine + + + + + + desmosine + + + + + + + + + + + A protein modification that effectively cross-links four L-lysine residues to form isodesmosine. + -58.15 + C 0 H -16 N -3 O 0 + -58.13497 + 1+ + C 24 H 32 N 5 O 4 + 454.55 + 454.24487 + K, K, K, K + natural + 2-[(4S)-4-amino-4-carboxybutyl]-1-[(5S)-5-amino-5-carboxypentyl]-3,5-bis[(3S)-3-amino-3-carboxypropyl]pyridinium + 6-[2-(4-amino-4-carboxybutyl)-3,5-bis(3-amino-3-carboxypropyl)pyridinio]norleucine + isodesmosine + PSI-MOD + MOD:01934 + Cross-link 4. + isodesmosine + + + + + A protein modification that effectively cross-links four L-lysine residues to form isodesmosine. + ChEBI:37629 + PubMed:13941623 + PubMed:14109938 + PubMed:14109939 + PubMed:5839176 + RESID:AA0588 + + + + + 2-[(4S)-4-amino-4-carboxybutyl]-1-[(5S)-5-amino-5-carboxypentyl]-3,5-bis[(3S)-3-amino-3-carboxypropyl]pyridinium + + + + + + 6-[2-(4-amino-4-carboxybutyl)-3,5-bis(3-amino-3-carboxypropyl)pyridinio]norleucine + + + + + + isodesmosine + + + + + + + + + + + + + + + + + modification from RESID + 178.14 + C 6 H 10 N 0 O 6 + 178.04774 + C 12 H 22 N 2 O 7 + 306.32 + 306.1427 + K + natural + uniprot.ptm:PTM-0572 + (D-glucopyranosyl)oxy-L-lysine + CARBOHYD O-linked (Glc) hydroxylysine + O-glucosyl-L-hydroxylysine + PSI-MOD + MOD:01935 + O-glucosyl-L-hydroxylysine + + + + + modification from RESID + PubMed:22045808 + RESID:AA0589 + + + + + (D-glucopyranosyl)oxy-L-lysine + + + + + + CARBOHYD O-linked (Glc) hydroxylysine + + + + + + O-glucosyl-L-hydroxylysine + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-oleoyl-L-lysine. + 264.45 + C 18 H 32 N 0 O 1 + 264.24533 + C 24 H 44 N 2 O 2 + 392.63 + 392.34027 + K + natural + (2S)-2-amino-6-([(9Z)-octadec-9-enoyl]amino)hexanoic acid + N6-[(9Z)-1-oxo-9-octadecenyl]lysine + N6-oleoyl-L-lysine + PSI-MOD + MOD:01936 + N6-oleoyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-oleoyl-L-lysine. + PubMed:20942504 + RESID:AA0590 + + + + + (2S)-2-amino-6-([(9Z)-octadec-9-enoyl]amino)hexanoic acid + + + + + + N6-[(9Z)-1-oxo-9-octadecenyl]lysine + + + + + + N6-oleoyl-L-lysine + + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to N-palmitoyl-L-methionine. + 238.41 + C 16 H 30 N 0 O 1 S 0 + 238.22966 + C 21 H 40 N 1 O 2 S 1 + 370.62 + 370.27798 + M + natural + N-term + (2S)-2-(hexadecanoylamino)-4-(methylsulfanyl)butanoic acid + 2-(hexadecanamido)-4-(methylsulfanyl)butanoic acid + LIPID N-palmitoyl methionine + N-(1-oxohexadecyl)methionine + N-palmitoyl-L-methionine + PSI-MOD + MOD:01937 + N-palmitoyl-L-methionine + + + + + A protein modification that effectively converts an L-methionine residue to N-palmitoyl-L-methionine. + PubMed:20942504 + RESID:AA0591 + + + + + (2S)-2-(hexadecanoylamino)-4-(methylsulfanyl)butanoic acid + + + + + + 2-(hexadecanamido)-4-(methylsulfanyl)butanoic acid + + + + + + LIPID N-palmitoyl methionine + + + + + + N-(1-oxohexadecyl)methionine + + + + + + N-palmitoyl-L-methionine + + + + + + + + + + + + A protein modification that crosslinks an asparagine and the following cysteine residue with the formation of (2-aminosuccinimidyl)-3-sulfanylpropanoic acid and the release of ammonia. + -17.03 + C 0 H -3 N -1 O 0 S 0 + -17.026548 + C 7 H 8 N 2 O 3 S 1 + 200.21 + 200.02556 + C, N + natural + (2R)-2-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-3-sulfanylpropanoic acid + 2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid + aspartimide cysteine + PSI-MOD + MOD:01938 + Cross-link 2. + 2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid (Asn) + + + + + A protein modification that crosslinks an asparagine and the following cysteine residue with the formation of (2-aminosuccinimidyl)-3-sulfanylpropanoic acid and the release of ammonia. + RESID:AA0592#ASN + + + + + (2R)-2-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-3-sulfanylpropanoic acid + + + + + + 2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid + + + + + + aspartimide cysteine + + + + + + + + + + + + A protein modification that crosslinks an aspartic acid and the following cysteine residue with the formation of (2-aminosuccinimidyl)-3-sulfanylpropanoic acid and the loss of a water molecule. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 7 H 8 N 2 O 3 S 1 + 200.21 + 200.02556 + C, D + natural + (2R)-2-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-3-sulfanylpropanoic acid + 2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid + aspartimide cysteine + PSI-MOD + MOD:01939 + Cross-link 2. + 2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid (Asp) + + + + + A protein modification that crosslinks an aspartic acid and the following cysteine residue with the formation of (2-aminosuccinimidyl)-3-sulfanylpropanoic acid and the loss of a water molecule. + RESID:AA0592#ASP + + + + + (2R)-2-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-3-sulfanylpropanoic acid + + + + + + 2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid + + + + + + aspartimide cysteine + + + + + + + + + + + + A protein modification that crosslinks an asparagine and the following glutamic acid residue with the formation of (2-aminosuccinimidyl)pentanedioic acid and the release of ammonia. + -17.03 + C 0 H -3 N -1 O 0 + -17.026548 + C 9 H 10 N 2 O 5 + 226.19 + 226.05898 + E, N + natural + (4S)-4-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-5-oxopentanoic acid + 2-(2-aminosuccinimidyl)pentanedioic acid + aspartimide glutamic acid + PSI-MOD + MOD:01940 + Cross-link 2. + 2-(2-aminosuccinimidyl)pentanedioic acid (Asn) + + + + + A protein modification that crosslinks an asparagine and the following glutamic acid residue with the formation of (2-aminosuccinimidyl)pentanedioic acid and the release of ammonia. + RESID:AA0593#ASN + + + + + (4S)-4-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-5-oxopentanoic acid + + + + + + 2-(2-aminosuccinimidyl)pentanedioic acid + + + + + + aspartimide glutamic acid + + + + + + + + + + + + A protein modification that crosslinks an aspartic acid and the following glycine residue with the formation of (2-aminosuccinimidyl)pentanedioic acid and the loss of a water molecule. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 9 H 10 N 2 O 5 + 226.19 + 226.05898 + D, E + natural + (4S)-4-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-5-oxopentanoic acid + 2-(2-aminosuccinimidyl)pentanedioic acid + aspartimide glutamic acid + PSI-MOD + MOD:01941 + Cross-link 2. + 2-(2-aminosuccinimidyl)pentanedioic acid (Asp) + + + + + A protein modification that crosslinks an aspartic acid and the following glycine residue with the formation of (2-aminosuccinimidyl)pentanedioic acid and the loss of a water molecule. + RESID:AA0593#ASP + + + + + (4S)-4-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-5-oxopentanoic acid + + + + + + 2-(2-aminosuccinimidyl)pentanedioic acid + + + + + + aspartimide glutamic acid + + + + + + + + + + + A protein modification that effectively converts a source amino acid residue to D-aspartic acid. + C 4 H 5 N 1 O 3 + 115.09 + 115.02694 + X + artifactual + (2R)-2-aminobutanedioic acid + 2-azanylbutanedioic acid + D-aspartic acid + aminosuccinic acid + PSI-MOD + MOD:01942 + D-aspartic acid + + + + + A protein modification that effectively converts a source amino acid residue to D-aspartic acid. + ChEBI:48094 + PubMed:9384562 + RESID:AA0190 + + + + + (2R)-2-aminobutanedioic acid + + + + + + 2-azanylbutanedioic acid + + + + + + D-aspartic acid + + + + + + aminosuccinic acid + + + + + + + + + + A protein modification that crosslinks two adjacent residues by formation of a pyrrolidione ring. + PSI-MOD + MOD:01943 + pyrrolidione ring crosslinked residues + + + + + A protein modification that crosslinks two adjacent residues by formation of a pyrrolidione ring. + PubMed:18688235 + + + + + + + + + + A protein modification that forms (2-aminosuccinimidyl)acetic acid by crosslinking either an aspartic acid residue or an asparagine residue with the following residue. + X + hypothetical + PSI-MOD + MOD:01944 + + Cross-link 2; this cross-link is formed by the condensation of an aspartic acid residue or an asparagine residue with the alpha-amido of the following residue. + 2-aminosuccinimide ring crosslinked residues + + + + + A protein modification that forms (2-aminosuccinimidyl)acetic acid by crosslinking either an aspartic acid residue or an asparagine residue with the following residue. + PubMed:18688235 + + + + + + + + + + A protein modification that forms (2-aminosuccinimidyl)-3-sulfanylpropanoic acid by crosslinking either an aspartic acid residue or an asparagine residue with the following cysteine residue. + C 6 H 6 N 2 O 3 + 154.13 + 154.03784 + C, X + hypothetical + PSI-MOD + MOD:01945 + Cross-link 2; this cross-link is formed by the condensation of an aspartic acid residue or an asparagine residue with the alpha-amido of the following residue. + 2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid + + + + + A protein modification that forms (2-aminosuccinimidyl)-3-sulfanylpropanoic acid by crosslinking either an aspartic acid residue or an asparagine residue with the following cysteine residue. + PubMed:18688235 + + + + + + + + + + A protein modification that forms (2-aminosuccinimidyl)pentanedioicacid by crosslinking either an aspartic acid residue or an asparagine residue with the following glutamic acid + residue. + C 6 H 6 N 2 O 3 + 154.13 + 154.03784 + E, X + hypothetical + PSI-MOD + MOD:01946 + Cross-link 2; this cross-link is formed by the condensation of an aspartic acid residue or an asparagine residue with the alpha-amido of the following residue. + 2-(2-aminosuccinimidyl)pentanedioic acid + + + + + A protein modification that forms (2-aminosuccinimidyl)pentanedioicacid by crosslinking either an aspartic acid residue or an asparagine residue with the following glutamic acid + residue. + PubMed:18688235 + + + + + + + + + + + + A protein modification that effectively cross-links an L-threonine residue and an L-aspartic acid residue with an ester bond to form O-(L-isoaspartyl)-L-threonine. + -18.02 + C 0 H -2 N 0 O -1 + -18.010565 + C 8 H 10 N 2 O 4 + 198.18 + 198.06406 + D, T + natural + (2S)-2-amino-4-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-4-oxobutanoic acid + (2S,3R)-2-amino-3-([(4S)-3-amino-3-carboxypropanoyl]oxy)propanoic acid + CROSSLNK isoaspartyl threonine ester (Thr-Asp) + O(beta)-(beta-aspartyl)threonine + O-(L-isoaspartyl)-L-threonine + O3-(isoaspartyl)-threonine + PSI-MOD + MOD:01947 + Cross-link 2. + O-(L-isoaspartyl)-L-threonine (cross-link) + + + + + A protein modification that effectively cross-links an L-threonine residue and an L-aspartic acid residue with an ester bond to form O-(L-isoaspartyl)-L-threonine. + PubMed:17157318 + PubMed:8706862 + RESID:AA0525#TDX + + + + + (2S)-2-amino-4-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-4-oxobutanoic acid + + + + + + (2S,3R)-2-amino-3-([(4S)-3-amino-3-carboxypropanoyl]oxy)propanoic acid + + + + + + CROSSLNK isoaspartyl threonine ester (Thr-Asp) + + + + + + O(beta)-(beta-aspartyl)threonine + + + + + + O-(L-isoaspartyl)-L-threonine + + + + + + O3-(isoaspartyl)-threonine + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and two L-serine residues by a thioether bond and a carbon-carbon bond to form labionin. + -36.03 + C 0 H -4 N 0 O -2 S 0 + -36.02113 + C 9 H 11 N 3 O 3 S 1 + 241.26 + 241.05211 + C, S, S + natural + (2S,4S)-2,4-diamino-2-[([(2R)-2-amino-2-carboxyethyl]sulfanyl)methyl]pentanedioic acid + (2S,4S,8R)-2,4,8-triamino-4-carboxy-6-thianonanedioic acid + (2S,4S,8R)-labionin + labionin + PSI-MOD + MOD:01948 + Cross-link 3. + labionin + + + + + A protein modification that effectively cross-links an L-cysteine residue and two L-serine residues by a thioether bond and a carbon-carbon bond to form labionin. + PubMed:20082397 + RESID:AA0594 + + + + + (2S,4S)-2,4-diamino-2-[([(2R)-2-amino-2-carboxyethyl]sulfanyl)methyl]pentanedioic acid + + + + + + (2S,4S,8R)-2,4,8-triamino-4-carboxy-6-thianonanedioic acid + + + + + + (2S,4S,8R)-labionin + + + + + + labionin + + + + + + + + + + + + A protein modification that effectively cross-links a phenylalanine and two tyrosine residues to form coelenterazine. + -50.06 + C -1 H -6 N 0 O -2 + -50.036777 + C 26 H 21 N 3 O 3 + 423.47 + 423.1583 + F, Y, Y + hypothetical + N-term + 8-benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one + Oplophorus luciferin + coelenterazine + PSI-MOD + MOD:01949 + Cross-link 3. + coelenterazine + + + + + A protein modification that effectively cross-links a phenylalanine and two tyrosine residues to form coelenterazine. + ChEBI:2311 + PubMed:10830969 + PubMed:11572972 + PubMed:19833098 + RESID:AA0595 + + + + + 8-benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one + + + + + + Oplophorus luciferin + + + + + + coelenterazine + + + + + + + + + + A protein modification that effectively converts an L-glutamine residue to L-isoglutamyl histamine. + 94.12 + C 5 H 6 N 2 O 0 + 94.0531 + C 10 H 14 N 4 O 2 + 222.25 + 222.11168 + Q + natural + uniprot.ptm:PTM-0488 + (2S)-2-amino-5-([2-(1H-imidazol-5-yl)ethyl]amino)-5-oxopentanoic acid + (gamma-glutamyl)histamine + L-isoglutamyl histamine + PSI-MOD + MOD:01950 + L-isoglutamyl histamine + + + + + A protein modification that effectively converts an L-glutamine residue to L-isoglutamyl histamine. + PubMed:23022564 + RESID:AA0596 + + + + + (2S)-2-amino-5-([2-(1H-imidazol-5-yl)ethyl]amino)-5-oxopentanoic acid + + + + + + (gamma-glutamyl)histamine + + + + + + L-isoglutamyl histamine + + + + + + + + + + + + A protein modification that effectively crosslinks an L-glutamine residue and an L-serine residue by an ester bond and releasing ammonia to form O-(L-isoglutamyl)-L-serine. + -17.03 + C 0 H -3 N -1 O 0 + -17.026548 + C 8 H 10 N 2 O 4 + 198.18 + 198.06406 + Q, S + natural + (2S)-2-amino-5-[(2S)-2-amino-2-carboxyethoxy]-5-oxopentanoic acid + O(beta)-(gamma-glutamyl)serine + O-(L-isoglutamyl)-L-serine + O3-(isoglutamyl)-serine + PSI-MOD + MOD:01951 + Cross-link 2. + O-(L-isoglutamyl)-L-serine (Gln-Ser) + + + + + A protein modification that effectively crosslinks an L-glutamine residue and an L-serine residue by an ester bond and releasing ammonia to form O-(L-isoglutamyl)-L-serine. + PubMed:17051152 + RESID:AA0597#QSX + + + + + (2S)-2-amino-5-[(2S)-2-amino-2-carboxyethoxy]-5-oxopentanoic acid + + + + + + O(beta)-(gamma-glutamyl)serine + + + + + + O-(L-isoglutamyl)-L-serine + + + + + + O3-(isoglutamyl)-serine + + + + + + + + + + + + + + A protein modification that effectively cross-links an L-threonine residue and an L-glutamine residue with an ester bond releasing ammonia to form O-(L-isoglutamyl)-L-threonine. + -17.03 + C 0 H -3 N -1 O 0 + -17.026548 + C 9 H 12 N 2 O 4 + 212.2 + 212.07971 + Q, T + natural + (2S)-2-amino-5-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-5-oxopentanoic acid + (2S,3R)-2-amino-3-([(4S)-4-amino-4-carboxybutanoyl]oxy)-propanoic acid + 5-(threon-O3-yl)glutamate + O(beta)-(gamma-glutamyl)threonine + O-(L-isoglutamyl)-L-threonine + O3-(isoglutamyl)threonine + PSI-MOD + MOD:01952 + Cross-link 2. + O-(L-isoglutamyl)-L-threonine (Gln-Thr) + + + + + A protein modification that effectively cross-links an L-threonine residue and an L-glutamine residue with an ester bond releasing ammonia to form O-(L-isoglutamyl)-L-threonine. + PubMed:17051152 + RESID:AA0536#TQX + + + + + (2S)-2-amino-5-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-5-oxopentanoic acid + + + + + + (2S,3R)-2-amino-3-([(4S)-4-amino-4-carboxybutanoyl]oxy)-propanoic acid + + + + + + 5-(threon-O3-yl)glutamate + + + + + + O(beta)-(gamma-glutamyl)threonine + + + + + + O-(L-isoglutamyl)-L-threonine + + + + + + O3-(isoglutamyl)threonine + + + + + + + + + + + A protein modification that effectively converts four L-cysteine residues and a four-iron cluster to tetrakis-L-cysteinyl tetrairon octanitrosyl. + 459.4 + C 0 Fe 4 H -4 N 8 O 8 S 0 + 459.69235 + C 12 Fe 4 H 16 N 12 O 12 S 4 + 871.95 + 871.7291 + C, C, C, C + hypothetical + PSI-MOD + MOD:01953 + Cross-link 4. + tetrakis-L-cysteinyl tetrairon octanitrosyl + + + + + A protein modification that effectively converts four L-cysteine residues and a four-iron cluster to tetrakis-L-cysteinyl tetrairon octanitrosyl. + PubMed:21182249 + RESID:AA0599 + + + + + + + + + + A protein modification that effectively converts an L-selenocysteine residue to dehydroalanine. + -80.99 + C 0 H -2 N 0 O 0 Se -1 + -81.932175 + C 3 H 3 N 1 O 1 + 69.06 + 69.02146 + U + natural + 2,3-didehydroalanine + 2-aminoacrylic acid + 2-aminopropenoic acid + 4-methylidene-imidazole-5-one (MIO) active site + Dha + anhydroserine + dehydroalanine + PSI-MOD + MOD:01954 + dehydroalanine (Sec) + + + + + A protein modification that effectively converts an L-selenocysteine residue to dehydroalanine. + ChEBI:17123 + PubMed:10220322 + PubMed:12781460 + PubMed:1547888 + PubMed:1815586 + PubMed:20805503 + PubMed:21420488 + PubMed:22031445 + PubMed:2914619 + PubMed:7947813 + PubMed:8239649 + RESID:AA0181 + + + + + 2,3-didehydroalanine + + + + + + 2-aminoacrylic acid + + + + + + 2-aminopropenoic acid + + + + + + 4-methylidene-imidazole-5-one (MIO) active site + + + + + + Dha + + + + + + anhydroserine + + + + + + dehydroalanine + + + + + + + + + + + + + + + modification from RESID + 333.78 + C 0 Ca 1 H -6 Mn 4 N 0 O 5 + 333.6424 + C 32 Ca 1 H 38 Mn 4 N 9 O 23 + 1176.53 + 1175.9229 + A, D, D, E, E, E, H + natural + C-term + 4Mn-Ca-5O cluster + L-alaninato bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese pentoxide + mu2-alaninato-1kappaO(1),3kappaO(1')-mu2-aspartato-1kappaO(4),5kappaO(4')-mu2-aspartato-2kappaO(4),3kappaO(4')-mu2-glutamato-3kappaO(5),4kappaO(5')-mu2-glutamato-4kappaO(5),5kappaO(5')-mu-glutamato-2kappaO(5)-mu-histidino-2kappaN(tau)-mu4-oxido-1:2:4:5kappa(4)O-tri-mu3-oxido-1:2:3kappa(3)O;1:3:4kappa(3)O;2:3:4kappa(3)O;mu-oxido-4:5kappa(2)O-calciumtetramanganese + photosystem II catalytic cluster + PSI-MOD + MOD:01955 + Cross-link 7. + L-alaninato bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese pentoxide + + + + + modification from RESID + PubMed:21499260 + RESID:AA0600 + + + + + 4Mn-Ca-5O cluster + + + + + + L-alaninato bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese pentoxide + + + + + + mu2-alaninato-1kappaO(1),3kappaO(1')-mu2-aspartato-1kappaO(4),5kappaO(4')-mu2-aspartato-2kappaO(4),3kappaO(4')-mu2-glutamato-3kappaO(5),4kappaO(5')-mu2-glutamato-4kappaO(5),5kappaO(5')-mu-glutamato-2kappaO(5)-mu-histidino-2kappaN(tau)-mu4-oxido-1:2:4:5kappa(4)O-tri-mu3-oxido-1:2:3kappa(3)O;1:3:4kappa(3)O;2:3:4kappa(3)O;mu-oxido-4:5kappa(2)O-calciumtetramanganese + + + + + + photosystem II catalytic cluster + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to (3R)-3-hydroxy-L-arginine. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 6 H 12 N 4 O 2 + 172.19 + 172.09602 + R + natural + uniprot.ptm:PTM-0476 + (2S,3R)-2-amino-5-[(diaminomethylidene)amino]-3-hydroxypentanoic acid + (3R)-3-hydroxy-L-arginine + 2-amino-5-(carbamimidamido)-3-hydroxypentanoic acid [tautomer] + 2-amino-5-[(aminoiminomethyl)amino]-3-hydroxypentanoic acid [tautomer] + 2-amino-5-guanidino-3-hydroxypentanoic acid + C(beta)-hydroxyarginine + MOD_RES (3R)-3-hydroxyarginine + beta-hydroxyarginine + PSI-MOD + MOD:01956 + (3R)-3-hydroxy-L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to (3R)-3-hydroxy-L-arginine. + PubMed:10094780 + PubMed:23103944 + PubMed:786730 + RESID:AA0601 + + + + + (2S,3R)-2-amino-5-[(diaminomethylidene)amino]-3-hydroxypentanoic acid + + + + + + (3R)-3-hydroxy-L-arginine + + + + + + 2-amino-5-(carbamimidamido)-3-hydroxypentanoic acid [tautomer] + + + + + + 2-amino-5-[(aminoiminomethyl)amino]-3-hydroxypentanoic acid [tautomer] + + + + + + 2-amino-5-guanidino-3-hydroxypentanoic acid + + + + + + C(beta)-hydroxyarginine + + + + + + MOD_RES (3R)-3-hydroxyarginine + + + + + + beta-hydroxyarginine + + + + + + + + + + A protein modification that effectively converts an L-proline residue to 2-hydroxyproline. + 16.0 + C 0 H 0 N 0 O 1 + 15.994915 + C 5 H 7 N 1 O 2 + 113.12 + 113.047676 + P + hypothetical + uniprot.ptm:PTM-0668 + (2R)-2-hydroxypyrrolidine-2-carboxylic acid + 2-hydroxyproline + 2-oxidanylpyrrolidine-2-carboxylic acid + MOD_RES 2-hydroxyproline + alpha-hydroxyproline + PSI-MOD + MOD:01957 + 2-hydroxyproline + + + + + A protein modification that effectively converts an L-proline residue to 2-hydroxyproline. + ChEBI:141809 + PubMed:23385463 + RESID:AA0602 + + + + + (2R)-2-hydroxypyrrolidine-2-carboxylic acid + + + + + + 2-hydroxyproline + + + + + + 2-oxidanylpyrrolidine-2-carboxylic acid + + + + + + MOD_RES 2-hydroxyproline + + + + + + alpha-hydroxyproline + + + + + + + + + + + A protein modification that effectively converts four L-cysteine residues and a two-iron two-sulfur cluster to bis-L-cysteinyl bisglutathion-S-yl diiron disulfide. + 786.42 + C 20 Fe 2 H 30 N 6 O 12 S 4 + 785.9503 + C 26 Fe 2 H 40 N 8 O 14 S 6 + 992.7 + 991.9687 + C, C + natural + bis-L-cysteinyl bisglutathion-S-yl diiron disulfide + di-mu-sulfido-bis(cysteinato)-1kappaS,2kappaS-bis(glutathionato)-1kappaS,2kappaS-diiron + mitochondrial glutaredoxin 2 dimer iron-sulfur cluster + plant glutaredoxin C1 dimer iron-sulfur cluster + PSI-MOD + MOD:01958 + Cross-link 2. + bis-L-cysteinyl bisglutathion-S-yl diiron disulfide + + + + + A protein modification that effectively converts four L-cysteine residues and a two-iron two-sulfur cluster to bis-L-cysteinyl bisglutathion-S-yl diiron disulfide. + PubMed:17121859 + RESID:AA0603 + + + + + bis-L-cysteinyl bisglutathion-S-yl diiron disulfide + + + + + + di-mu-sulfido-bis(cysteinato)-1kappaS,2kappaS-bis(glutathionato)-1kappaS,2kappaS-diiron + + + + + + mitochondrial glutaredoxin 2 dimer iron-sulfur cluster + + + + + + plant glutaredoxin C1 dimer iron-sulfur cluster + + + + + + + + + + + + A protein modification that effectively converts three L-cysteine residues, an L-glutamic acid and a four-iron four-sulfur cluster to tris-L-cysteinyl L-glutamato tetrairon tetrasulfide. + 347.59 + C 0 Fe 4 H -4 N 0 O 0 S 4 + 347.59674 + C 14 Fe 4 H 18 N 4 O 6 S 7 + 786.12 + 785.6669 + C, C, C, E + natural + tris-L-cysteinyl L-glutamato tetrairon tetrasulfide + tris-mu3-sulfido-tris(cysteinato)-1kappaS,2kappaS,3kappaS-glutamato-4kappaO(5),4kappaO(5')-tetrairon + PSI-MOD + MOD:01959 + Cross-link 4. + tris-L-cysteinyl L-glutamato tetrairon tetrasulfide + + + + + A protein modification that effectively converts three L-cysteine residues, an L-glutamic acid and a four-iron four-sulfur cluster to tris-L-cysteinyl L-glutamato tetrairon tetrasulfide. + PubMed:21167158 + RESID:AA0604 + + + + + tris-L-cysteinyl L-glutamato tetrairon tetrasulfide + + + + + + tris-mu3-sulfido-tris(cysteinato)-1kappaS,2kappaS,3kappaS-glutamato-4kappaO(5),4kappaO(5')-tetrairon + + + + + + + + + + + + A protein modification that effectively converts three L-cysteine residues, an L-glutamine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-glutamin-O6-yl tetrairon tetrasulfide. + 347.59 + C 0 Fe 4 H -4 N 0 O 0 S 4 + 347.59674 + C 14 Fe 4 H 19 N 5 O 5 S 7 + 785.14 + 784.68286 + C, C, C, Q + natural + METAL Iron-sulfur (4Fe-4S) + tris-L-cysteinyl L-glutamin-O6-yl tetrairon tetrasulfide + tris-mu3-sulfido-tris(cysteinato)-1kappaS,2kappaS,3kappaS-glutaminato-4kappaN(5)-tetrairon + PSI-MOD + MOD:01960 + Cross-link 4. + tris-L-cysteinyl L-glutamin-O6-yl tetrairon tetrasulfide + + + + + A protein modification that effectively converts three L-cysteine residues, an L-glutamine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-glutamin-O6-yl tetrairon tetrasulfide. + PubMed:11796730 + RESID:AA0605 + + + + + METAL Iron-sulfur (4Fe-4S) + + + + + + tris-L-cysteinyl L-glutamin-O6-yl tetrairon tetrasulfide + + + + + + tris-mu3-sulfido-tris(cysteinato)-1kappaS,2kappaS,3kappaS-glutaminato-4kappaN(5)-tetrairon + + + + + + + + + OBSOLETE because redundant and identical to MOD:01785. Remap to MOD:01785. + MOD:01785 + 129.12 + C 5 H 7 N 1 O 3 + 129.04259 + C 9 H 14 N 2 O 5 + 230.22 + 230.09027 + T + natural + (2S)-2-amino-5-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-5-oxopentanoic acid + (2S,3R)-2-amino-3-([(4S)-4-amino-4-carboxybutanoyl]oxy)-propanoic acid + 5-(threon-O3-yl)glutamate + O(beta)-(gamma-glutamyl)threonine + O-(L-isoglutamyl)-L-threonine + O3-(isoglutamyl)threonine + PSI-MOD + MOD:01961 + O-(L-isoglutamyl)-L-threonine (THR) + true + + + + + OBSOLETE because redundant and identical to MOD:01785. Remap to MOD:01785. + PubMed:16618936 + PubMed:17051152 + PubMed:17687277 + PubMed:18555071 + RESID:AA0536#THR + + + + + (2S)-2-amino-5-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-5-oxopentanoic acid + + + + + + (2S,3R)-2-amino-3-([(4S)-4-amino-4-carboxybutanoyl]oxy)-propanoic acid + + + + + + 5-(threon-O3-yl)glutamate + + + + + + O(beta)-(gamma-glutamyl)threonine + + + + + + O-(L-isoglutamyl)-L-threonine + + + + + + O3-(isoglutamyl)threonine + + + + + + + + + + A protein modification that effectively converts an L-asparagine residue to N4-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-asparagine. + 228.25 + C 10 H 16 N 2 O 4 + 228.11101 + C 14 H 22 N 4 O 6 + 342.35 + 342.15393 + N + natural + uniprot.ptm:PTM-0506 + (2S)-2-amino-4-[(2,4-diacetylamino-2,4,6-trideoxy-beta-D-glucopyranosyl)amino]-4-oxobutanoic acid + CARBOHYD N-linked (DATDGlc) asparagine + DABA + DATDH + DiNAcBac + N4-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-asparagine + N4-[2,4-bis(acetylamino)-2,4,6-trideoxy-beta-D-glucopyranosyl]-L-asparagine + N4-[N,N-diacetylbacillosaminyl]asparagine + N4-[N2,N4-diacetylbacillosaminyl]asparagine + PSI-MOD + MOD:01962 + N4-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-asparagine + + + + + A protein modification that effectively converts an L-asparagine residue to N4-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-asparagine. + PubMed:12186869 + PubMed:19236052 + RESID:AA0606 + + + + + (2S)-2-amino-4-[(2,4-diacetylamino-2,4,6-trideoxy-beta-D-glucopyranosyl)amino]-4-oxobutanoic acid + + + + + + CARBOHYD N-linked (DATDGlc) asparagine + + + + + + DABA + + + + + + DATDH + + + + + + DiNAcBac + + + + + + N4-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-asparagine + + + + + + N4-[2,4-bis(acetylamino)-2,4,6-trideoxy-beta-D-glucopyranosyl]-L-asparagine + + + + + + N4-[N,N-diacetylbacillosaminyl]asparagine + + + + + + N4-[N2,N4-diacetylbacillosaminyl]asparagine + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-serine. + 228.25 + C 10 H 16 N 2 O 4 + 228.11101 + C 13 H 21 N 3 O 6 + 315.33 + 315.14304 + S + natural + uniprot.ptm:PTM-0548 + (2S)-2-amino-4-[(2,4-diacetamido-2,4,6-trideoxy-beta-D-glucopyranosyl)oxy]propanoic acid + CARBOHYD O-linked (DATDGlc) serine + DABA + DATDH + DiNAcBac + O-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-serine + O-[2,4-bis(acetylamino)-2,4,6-trideoxy-beta-D-glucopyranosyl]-L-serine + O-[N,N-diacetylbacillosaminyl]serine + O-[N2,N4-diacetylbacillosaminyl]serine + PSI-MOD + MOD:01963 + O-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-serine. + PubMed:23030644 + RESID:AA0607 + + + + + (2S)-2-amino-4-[(2,4-diacetamido-2,4,6-trideoxy-beta-D-glucopyranosyl)oxy]propanoic acid + + + + + + CARBOHYD O-linked (DATDGlc) serine + + + + + + DABA + + + + + + DATDH + + + + + + DiNAcBac + + + + + + O-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-serine + + + + + + O-[2,4-bis(acetylamino)-2,4,6-trideoxy-beta-D-glucopyranosyl]-L-serine + + + + + + O-[N,N-diacetylbacillosaminyl]serine + + + + + + O-[N2,N4-diacetylbacillosaminyl]serine + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucosyl)-L-serine. + 274.27 + C 11 H 18 N 2 O 6 + 274.1165 + C 14 H 23 N 3 O 8 + 361.35 + 361.14853 + S + natural + uniprot.ptm:PTM-0549 + (2S)-2-amino-3-[(2-acetamido-4-glycerylamino-2,4,6-trideoxy-D-glucopyranosyl)oxy]propanoic acid + CARBOHYD O-linked (GATDGlc) serine + GATDH + O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucopyranosyl)-L-serine + O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucosyl)-L-serine + O-(N2-acetyl-N4-glycerylbacillosaminyl)-L-serine + PSI-MOD + MOD:01964 + O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucosyl)-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucosyl)-L-serine. + PubMed:17804791 + RESID:AA0608 + + + + + (2S)-2-amino-3-[(2-acetamido-4-glycerylamino-2,4,6-trideoxy-D-glucopyranosyl)oxy]propanoic acid + + + + + + CARBOHYD O-linked (GATDGlc) serine + + + + + + GATDH + + + + + + O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucopyranosyl)-L-serine + + + + + + O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucosyl)-L-serine + + + + + + O-(N2-acetyl-N4-glycerylbacillosaminyl)-L-serine + + + + + + + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to 2xC(13),3x(2)H labeled N6-acetyl-L-lysine. + 47.04 + (13)C 2 (1)H -1 (2)H 3 O 1 + 47.036106 + (12)C 6 (13)C 2 (1)H 11 (2)H 3 N 2 O 2 + 175.13 + 175.13107 + K + artifact + Acetate labeling reagent (K) (heavy form, +5amu) + COFRADIC heavy acetyl 13C2 2H3 + PSI-MOD + MOD:01965 + 2xC(13),3x(2)H labeled N6-acetyl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to 2xC(13),3x(2)H labeled N6-acetyl-L-lysine. + PubMed:18688235 + + + + + Acetate labeling reagent (K) (heavy form, +5amu) + + + + + + COFRADIC heavy acetyl 13C2 2H3 + + + + + + + + + OBSOLETE because redundant and identical to MOD:00720. Remap to MOD:00720. + MOD:00720 + 16.0 + C 0 H 0 N 0 O 1 S 0 + 15.994915 + C 5 H 9 N 1 O 2 S 1 + 147.19 + 147.0354 + M + natural + (2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid + L-methionine (R)-S-oxide + L-methionine (R)-sulfoxide + MOD_RES Methionine (R)-sulfoxide + PSI-MOD + MOD:01966 + L-methionine (R)-sulfoxide + true + + + + + OBSOLETE because redundant and identical to MOD:00720. Remap to MOD:00720. + ChEBI:45764 + PubMed:21406390 + PubMed:22116028 + PubMed:23911929 + RESID:AA0581 + + + + + (2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid + + + + + + L-methionine (R)-S-oxide + + + + + + L-methionine (R)-sulfoxide + + + + + + MOD_RES Methionine (R)-sulfoxide + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to omega-N-(N-acetylamino)glucosyl-L-arginine. + 203.19 + C 8 H 13 N 1 O 5 + 203.07938 + C 14 H 25 N 5 O 6 + 359.38 + 359.18048 + R + natural + uniprot.ptm:PTM-0518 + (2S)-2-amino-5-[(amino[(2-N-acetylamino-2-deoxy-D-glucopyranosyl)amino]methylidene)amino]pentanoic acid + CARBOHYD N-linked (GlcNAc) arginine + N(omega)-(2-N-acetylaminoglucosyl)arginine + N(omega)-(2-acetamido-2-deoxy-D-glucopyranosyl)-L-arginine + N(omega)-(2-acetylamino-2-deoxy-D-glucopyranosyl)-L-arginine + NG-(2-N-acetylaminoglucosyl)arginine + NG-(2-acetamido-2-deoxy-D-glucopyranosyl)-L-arginine + NG-(2-acetylamino-2-deoxy-D-glucopyranosyl)-L-arginine + omega-N-(2-N-acetylaminoglucosyl)arginine + omega-N-(2-acetamido-2-deoxy-D-glucopyranosyl)-L-arginine + omega-N-(2-acetylamino-2-deoxy-D-glucopyranosyl)-L-arginine + omega-N-(N-acetylamino)glucosyl-L-arginine + PSI-MOD + MOD:01967 + omega-N-(N-acetylamino)glucosyl-L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to omega-N-(N-acetylamino)glucosyl-L-arginine. + PubMed:23955153 + RESID:AA0609 + + + + + (2S)-2-amino-5-[(amino[(2-N-acetylamino-2-deoxy-D-glucopyranosyl)amino]methylidene)amino]pentanoic acid + + + + + + CARBOHYD N-linked (GlcNAc) arginine + + + + + + N(omega)-(2-N-acetylaminoglucosyl)arginine + + + + + + N(omega)-(2-acetamido-2-deoxy-D-glucopyranosyl)-L-arginine + + + + + + N(omega)-(2-acetylamino-2-deoxy-D-glucopyranosyl)-L-arginine + + + + + + NG-(2-N-acetylaminoglucosyl)arginine + + + + + + NG-(2-acetamido-2-deoxy-D-glucopyranosyl)-L-arginine + + + + + + NG-(2-acetylamino-2-deoxy-D-glucopyranosyl)-L-arginine + + + + + + omega-N-(2-N-acetylaminoglucosyl)arginine + + + + + + omega-N-(2-acetamido-2-deoxy-D-glucopyranosyl)-L-arginine + + + + + + omega-N-(2-acetylamino-2-deoxy-D-glucopyranosyl)-L-arginine + + + + + + omega-N-(N-acetylamino)glucosyl-L-arginine + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form (2R,3R,2'R)-3-methyllanthionine. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 7 H 10 N 2 O 2 S 1 + 186.23 + 186.0463 + C, T + natural + (2R,3R)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)butanoic acid + (2R,3R,2'R)-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid + (2R,3R,2'R)-3-methyllanthionine + (2R,3R,6R)-2,6-diamino-3-methyl-4-thiaheptanedioic acid + (2R,3R,6R)-3-methyllanthionine + 2-azanyl-3-[(2-azanyl-2-carboxyethyl)sulfanyl]butanoic acid + 3-methyl-L,L-lanthionine + cysteine-3-L-butyrine thioether + PSI-MOD + MOD:01968 + Cross-link 2. + (2R,3R,2'R)-3-methyllanthionine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form (2R,3R,2'R)-3-methyllanthionine. + PubMed:23314913 + RESID:AA0610 + + + + + (2R,3R)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)butanoic acid + + + + + + (2R,3R,2'R)-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid + + + + + + (2R,3R,2'R)-3-methyllanthionine + + + + + + (2R,3R,6R)-2,6-diamino-3-methyl-4-thiaheptanedioic acid + + + + + + (2R,3R,6R)-3-methyllanthionine + + + + + + 2-azanyl-3-[(2-azanyl-2-carboxyethyl)sulfanyl]butanoic acid + + + + + + 3-methyl-L,L-lanthionine + + + + + + cysteine-3-L-butyrine thioether + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine. + 289.31 + C 10 H 15 N 3 O 5 S 1 + 289.07324 + C 13 H 20 N 4 O 6 S 2 + 392.44 + 392.08243 + C + natural + (2S)-2-amino-5-([(2R)-1-([2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-2-oxoethyl]amino)-1-oxo-3-sulfanylpropan-2-yl]amino)-5-oxopentanoic acid + ACT_SITE S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine intermediate + S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine + S-(glutathion-1-yl)-L-cysteine + PSI-MOD + MOD:01969 + S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine. + PubMed:9398217 + RESID:AA0611 + + + + + (2S)-2-amino-5-([(2R)-1-([2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-2-oxoethyl]amino)-1-oxo-3-sulfanylpropan-2-yl]amino)-5-oxopentanoic acid + + + + + + ACT_SITE S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine intermediate + + + + + + S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine + + + + + + S-(glutathion-1-yl)-L-cysteine + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl glutamic acid, forming an isopeptide bond with a free glutamic acid. + 129.12 + C 5 H 7 N 1 O 3 + 129.04259 + C 10 H 14 N 2 O 6 + 258.23 + 258.08517 + E + natural + Unimod:450 + uniprot.ptm:PTM-0479 + (2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)pentanedioic acid + (2S)-2-[(4S)-4-amino-4-carboxybutanamido]pentanedioic acid + 2-([4-azanyl-4-carboxybutanoyl]azanyl)pentanedioic acid + 5-glutamyl glutamic acid + MOD_RES 5-glutamyl glutamate + N alpha -(gamma-Glutamyl)-Glu + N-(gamma-L-glutamyl)-L-glutamic acid + gamma-glutamylglutamate + isoglutamyl glutamic acid + isoglutamyl monoglutamic acid + PSI-MOD + Glu + monoglutamyl + MOD:01970 + 5-glutamyl glutamic acid + + + + + A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl glutamic acid, forming an isopeptide bond with a free glutamic acid. + PubMed:10747868 + PubMed:15525938 + PubMed:1680872 + PubMed:23434852 + RESID:AA0612 + Unimod:450 + + + + + (2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)pentanedioic acid + + + + + + (2S)-2-[(4S)-4-amino-4-carboxybutanamido]pentanedioic acid + + + + + + 2-([4-azanyl-4-carboxybutanoyl]azanyl)pentanedioic acid + + + + + + 5-glutamyl glutamic acid + + + + + + MOD_RES 5-glutamyl glutamate + + + + + + N alpha -(gamma-Glutamyl)-Glu + + + + + + N-(gamma-L-glutamyl)-L-glutamic acid + + + + + + gamma-glutamylglutamate + + + + + + isoglutamyl glutamic acid + + + + + + isoglutamyl monoglutamic acid + + + + + + Glu + + + + + + monoglutamyl + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to N2-ornithine. + 114.15 + C 5 H 10 N 2 O 1 + 114.079315 + C 10 H 17 N 3 O 4 + 243.26 + 243.1219 + E + hypothetical + uniprot.ptm:PTM-0478 + (2S)-5-amino-2-([(4S)-4-amino-4-carboxybutanoyl]amino)pentanoic acid + (2S)-5-amino-2-[(4S)-4-amino-4-carboxybutanamido]pentanoic acid + 4-amino-5-[(4-amino-1-carboxy-butyl)amino]-5-ketovaleric acid + 4-amino-5-[(4-amino-1-carboxy-butyl)amino]-5-oxopentanoic acid + 5-glutamyl N2-ornithine + MOD_RES 5-glutamyl N2-ornithine + N2-(L-isoglutamyl)-L-ornithine + N2-(gamma-glutamyl)ornithine + gamma-glutamylornithine + PSI-MOD + MOD:01971 + 5-glutamyl N2-ornithine + + + + + A protein modification that effectively converts an L-glutamic acid residue to N2-ornithine. + ChEBI:136763 + PubMed:23434852 + RESID:AA0613 + + + + + (2S)-5-amino-2-([(4S)-4-amino-4-carboxybutanoyl]amino)pentanoic acid + + + + + + (2S)-5-amino-2-[(4S)-4-amino-4-carboxybutanamido]pentanoic acid + + + + + + 4-amino-5-[(4-amino-1-carboxy-butyl)amino]-5-ketovaleric acid + + + + + + 4-amino-5-[(4-amino-1-carboxy-butyl)amino]-5-oxopentanoic acid + + + + + + 5-glutamyl N2-ornithine + + + + + + MOD_RES 5-glutamyl N2-ornithine + + + + + + N2-(L-isoglutamyl)-L-ornithine + + + + + + N2-(gamma-glutamyl)ornithine + + + + + + gamma-glutamylornithine + + + + + + + + + + + + A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl coenzyme A thioester. + 749.52 + C 21 H 34 N 7 O 15 P 3 S 1 + 749.1046 + C 26 H 41 N 8 O 18 P 3 S 1 + 878.63 + 878.1472 + E + natural + (2S)-2-amino-5-(2-[([3-([(2R)-2-hydroxy-3,3-dimethyl-4-([3'-phospho-adenosyl-5'-diphosphoryl]-oxy)-butanoyl]-amino)-propanoyl]-amino)-ethyl]-sulfanyl)-5-oxopentanoic acid + (2S)-2-amino-5-([2-(3-[(2R)-2-hydroxy-3,3-dimethyl-4-([3'-phospho-adenosyl-5'-diphosphoryl]-oxy)-butanamido]-propanamido)-ethyl]-sulfanyl)-5-oxopentanoic acid + 5-glutamyl 4-[(3'-phospho-adenosyl-5'-diphosphoryl)oxy]pantetheine thioester + 5-glutamyl coenzyme A thioester + 5-glutamyl coenzyme A thioester intermediate + PSI-MOD + MOD:01972 + 5-glutamyl coenzyme A thioester + + + + + A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl coenzyme A thioester. + PubMed:16253988 + PubMed:20977214 + PubMed:7915164 + RESID:AA0614 + + + + + (2S)-2-amino-5-(2-[([3-([(2R)-2-hydroxy-3,3-dimethyl-4-([3'-phospho-adenosyl-5'-diphosphoryl]-oxy)-butanoyl]-amino)-propanoyl]-amino)-ethyl]-sulfanyl)-5-oxopentanoic acid + + + + + + (2S)-2-amino-5-([2-(3-[(2R)-2-hydroxy-3,3-dimethyl-4-([3'-phospho-adenosyl-5'-diphosphoryl]-oxy)-butanamido]-propanamido)-ethyl]-sulfanyl)-5-oxopentanoic acid + + + + + + 5-glutamyl 4-[(3'-phospho-adenosyl-5'-diphosphoryl)oxy]pantetheine thioester + + + + + + 5-glutamyl coenzyme A thioester + + + + + + 5-glutamyl coenzyme A thioester intermediate + + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-(3-phosphoglyceryl)-L-lysine. + 168.04 + C 3 H 5 N 0 O 6 P 1 + 167.98238 + C 9 H 17 N 2 O 7 P 1 + 296.22 + 296.07733 + K + natural + (2S)-2-amino-6-([(2R)-2-hydroxy-3-(phosphonooxy)propanoyl]amino)hexanoic acid + (2S)-2-amino-6-[(2R)-2-hydroxy-3-(phosphonooxy)propanamido]hexanoic acid + 3-phosphoglyceryl-lysine + N6-(3-phosphoglyceryl)-L-lysine + PSI-MOD + MOD:01973 + N6-(3-phosphoglyceryl)-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-(3-phosphoglyceryl)-L-lysine. + PubMed:23908237 + RESID:AA0615 + + + + + (2S)-2-amino-6-([(2R)-2-hydroxy-3-(phosphonooxy)propanoyl]amino)hexanoic acid + + + + + + (2S)-2-amino-6-[(2R)-2-hydroxy-3-(phosphonooxy)propanamido]hexanoic acid + + + + + + 3-phosphoglyceryl-lysine + + + + + + N6-(3-phosphoglyceryl)-L-lysine + + + + + + + + + + A protein modification that effectively converts an L-methionine residue to S-methyl-L-methionine. + 15.03 + C 1 H 3 N 0 O 0 S 0 + 15.022927 + 1+ + C 6 H 12 N 1 O 1 S 1 + 146.23 + 146.06342 + M + natural + uniprot.ptm:PTM-0636 + (2S)-2-amino-4-(dimethylsulfonio)butanoate + (3S)-(3-amino-3-carboxypropyl)dimethylsulfanium + S-methyl-L-methionine + S-methylmethionine + S-methylmethioninium + [(3S)-3-amino-3-carboxypropyl](dimethyl)sulfonium + vitamin U + PSI-MOD + MOD:01974 + S-methyl-L-methionine + + + + + A protein modification that effectively converts an L-methionine residue to S-methyl-L-methionine. + ChEBI:17728 + PubMed:23532849 + RESID:AA0616 + + + + + (2S)-2-amino-4-(dimethylsulfonio)butanoate + + + + + + (3S)-(3-amino-3-carboxypropyl)dimethylsulfanium + + + + + + S-methyl-L-methionine + + + + + + S-methylmethionine + + + + + + S-methylmethioninium + + + + + + [(3S)-3-amino-3-carboxypropyl](dimethyl)sulfonium + + + + + + vitamin U + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to S-(poly-3-hydroxybutyrate)-L-cysteine. + C + natural + uniprot.ptm:PTM-0641 + (alpha)-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-(omega)-[(3R)-3-hydroxybutanoyl]-poly([(3R)-3-methyl-1-oxopropane-1,3-diyl]oxy) + MOD_RES S-poly(beta-hydroxybutyryl)lysine + S-poly(3-hydroxybutanoate)cysteine + S-poly(3-hydroxybutanoic acid)cysteine + S-poly(3-hydroxybutyrate)-L-cysteine + S-poly(3-hydroxybutyrate)cysteine + S-poly(3-hydroxybutyric acid)cysteine + S-poly(beta-hydroxybutyrate)cysteine + S-poly[(R)-3-hydroxybutyrate]cysteine + PSI-MOD + MOD:01975 + S-poly(3-hydroxybutyrate)-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to S-(poly-3-hydroxybutyrate)-L-cysteine. + PubMed:19711985 + PubMed:9888824 + RESID:AA0617 + + + + + (alpha)-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-(omega)-[(3R)-3-hydroxybutanoyl]-poly([(3R)-3-methyl-1-oxopropane-1,3-diyl]oxy) + + + + + + MOD_RES S-poly(beta-hydroxybutyryl)lysine + + + + + + S-poly(3-hydroxybutanoate)cysteine + + + + + + S-poly(3-hydroxybutanoic acid)cysteine + + + + + + S-poly(3-hydroxybutyrate)-L-cysteine + + + + + + S-poly(3-hydroxybutyrate)cysteine + + + + + + S-poly(3-hydroxybutyric acid)cysteine + + + + + + S-poly(beta-hydroxybutyrate)cysteine + + + + + + S-poly[(R)-3-hydroxybutyrate]cysteine + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to O3-(poly-3-hydroxybutyrate)-L-serine. + S + natural + uniprot.ptm:PTM-0640 + (2S)-2-amino-3-[([(3R)-3-hydroxybutanoyl]oxy)-poly([(3R)-3-methyl-1-oxopropane-1,3-diyl]oxy)]propanoic acid + MOD_RES O3-poly(beta-hydroxybutyryl)lysine + O3-(poly-3-hydroxybutyrate)-L-serine + O3-poly(3-hydroxybutanoate)serine + O3-poly(3-hydroxybutanoic acid)serine + O3-poly(3-hydroxybutyrate)serine + O3-poly(3-hydroxybutyric acid)serine + O3-poly(beta-hydroxybutyrate)serine + O3-poly[(R)-3-hydroxybutyrate]serine + PSI-MOD + MOD:01976 + + O3-(poly-3-hydroxybutyrate)-L-serine + + + + + A protein modification that effectively converts an L-serine residue to O3-(poly-3-hydroxybutyrate)-L-serine. + PubMed:17659252 + PubMed:20004640 + RESID:AA0618 + + + + + (2S)-2-amino-3-[([(3R)-3-hydroxybutanoyl]oxy)-poly([(3R)-3-methyl-1-oxopropane-1,3-diyl]oxy)]propanoic acid + + + + + + MOD_RES O3-poly(beta-hydroxybutyryl)lysine + + + + + + O3-(poly-3-hydroxybutyrate)-L-serine + + + + + + O3-poly(3-hydroxybutanoate)serine + + + + + + O3-poly(3-hydroxybutanoic acid)serine + + + + + + O3-poly(3-hydroxybutyrate)serine + + + + + + O3-poly(3-hydroxybutyric acid)serine + + + + + + O3-poly(beta-hydroxybutyrate)serine + + + + + + O3-poly[(R)-3-hydroxybutyrate]serine + + + + + + + + + + + + A protein modification that effectively crosslinks either an L-glutamine residue or an L-glutamic acid residue with an L-serine residue by an ester bond to form O-(L-isoglutamyl)-L-serine. + C 8 H 10 N 2 O 4 + 198.18 + 198.06406 + S, X + natural + (2S)-2-amino-5-[(2S)-2-amino-2-carboxyethoxy]-5-oxopentanoic acid + O(beta)-(gamma-glutamyl)serine + O-(L-isoglutamyl)-L-serine + O3-(isoglutamyl)-serine + PSI-MOD + MOD:01977 + Cross-link 2. + O-(L-isoglutamyl)-L-serine + + + + + A protein modification that effectively crosslinks either an L-glutamine residue or an L-glutamic acid residue with an L-serine residue by an ester bond to form O-(L-isoglutamyl)-L-serine. + PubMed:17051152 + RESID:AA0597 + + + + + (2S)-2-amino-5-[(2S)-2-amino-2-carboxyethoxy]-5-oxopentanoic acid + + + + + + O(beta)-(gamma-glutamyl)serine + + + + + + O-(L-isoglutamyl)-L-serine + + + + + + O3-(isoglutamyl)-serine + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-(L-isoaspartyl)-L-threonine, using either free L-asparagine and releasing ammonia or using a peptidyl L-aspartic acid residue and releasing water. + C 8 H 12 N 2 O 5 + 216.19 + 216.07462 + T, X + natural + (2S)-2-amino-4-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-4-oxobutanoic acid + (2S,3R)-2-amino-3-([(4S)-3-amino-3-carboxypropanoyl]oxy)propanoic acid + O(beta)-(beta-aspartyl)threonine + O-(L-isoaspartyl)-L-threonine + O3-(isoaspartyl)-threonine + PSI-MOD + MOD:01978 + This is a threonine active intermediate and not an ester cross-link of peptides [JSG]. + O-(L-isoaspartyl)-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-(L-isoaspartyl)-L-threonine, using either free L-asparagine and releasing ammonia or using a peptidyl L-aspartic acid residue and releasing water. + PubMed:8706862 + RESID:AA0525 + + + + + (2S)-2-amino-4-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-4-oxobutanoic acid + + + + + + (2S,3R)-2-amino-3-([(4S)-3-amino-3-carboxypropanoyl]oxy)propanoic acid + + + + + + O(beta)-(beta-aspartyl)threonine + + + + + + O-(L-isoaspartyl)-L-threonine + + + + + + O3-(isoaspartyl)-threonine + + + + + + + + + + + A protein modification that effectively converts an L-threonine residue to O-(L-isoglutamyl)-L-threonine, using free L-glutamine and releasing ammonia, or using a peptidyl L-glutamine and releasing ammonia. + C 9 H 14 N 2 O 5 + 230.22 + 230.09027 + T, X + hypothetical + (2S)-2-amino-5-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-5-oxopentanoic acid + (2S,3R)-2-amino-3-([(4S)-4-amino-4-carboxybutanoyl]oxy)-propanoic acid + 5-(threon-O3-yl)glutamate + O(beta)-(gamma-glutamyl)threonine + O-(L-isoglutamyl)-L-threonine + O3-(isoglutamyl)threonine + PSI-MOD + MOD:01979 + This is not an ester cross-link of peptides [JSG]. + O-(L-isoglutamyl)-L-threonine + + + + + A protein modification that effectively converts an L-threonine residue to O-(L-isoglutamyl)-L-threonine, using free L-glutamine and releasing ammonia, or using a peptidyl L-glutamine and releasing ammonia. + PubMed:8706862 + RESID:AA0536 + + + + + (2S)-2-amino-5-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-5-oxopentanoic acid + + + + + + (2S,3R)-2-amino-3-([(4S)-4-amino-4-carboxybutanoyl]oxy)-propanoic acid + + + + + + 5-(threon-O3-yl)glutamate + + + + + + O(beta)-(gamma-glutamyl)threonine + + + + + + O-(L-isoglutamyl)-L-threonine + + + + + + O3-(isoglutamyl)threonine + + + + + + + + + + + A protein modification that effectively converts an L-arginine residue to N4-glycosyl-arginine. + R + natural + Unimod:41 + (2S)-2-amino-5-(beta-D-glucopyranosyl[imino(methylamino)methyl]amino)pentanoic acid + NG-beta-D-glucosylarginine + omega-N-(beta-D-glucosyl)-L-arginine + omega-N-glucosyl-L-arginine + omega-N-glycosyl-L-arginine + PSI-MOD + Hex + Hexose + MOD:01980 + omega-N-glycosyl-L-arginine + + + + + A protein modification that effectively converts an L-arginine residue to N4-glycosyl-arginine. + PubMed:15279557 + PubMed:8521968 + PubMed:9536051 + RESID:AA0327 + Unimod:41#R + + + + + (2S)-2-amino-5-(beta-D-glucopyranosyl[imino(methylamino)methyl]amino)pentanoic acid + + + + + + NG-beta-D-glucosylarginine + + + + + + omega-N-(beta-D-glucosyl)-L-arginine + + + + + + omega-N-glucosyl-L-arginine + + + + + + omega-N-glycosyl-L-arginine + + + + + + Hex + + + + + + Hexose + + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 3-methyllanthionine with unresolved stereospecificity. + -18.02 + C 0 H -2 N 0 O -1 S 0 + -18.010565 + C 7 H 10 N 2 O 2 S 1 + 186.23 + 186.0463 + C, T + natural + 2,6-diamino-3-methyl-4-thiaheptanedioic acid + 2-amino-3-([2-amino-2-carboxyethyl]sulfanyl)butanoic acid + 2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid + 2-azanyl-3-[(2-azanyl-2-carboxyethyl)sulfanyl]butanoic acid + 3-methyllanthionine + cysteine-3-L-butyrine thioether + PSI-MOD + MOD:01981 + Cross-link 2. + 3-methyllanthionine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 3-methyllanthionine with unresolved stereospecificity. + PubMed:18688235 + + + + + 2,6-diamino-3-methyl-4-thiaheptanedioic acid + + + + + + 2-amino-3-([2-amino-2-carboxyethyl]sulfanyl)butanoic acid + + + + + + 2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid + + + + + + 2-azanyl-3-[(2-azanyl-2-carboxyethyl)sulfanyl]butanoic acid + + + + + + 3-methyllanthionine + + + + + + cysteine-3-L-butyrine thioether + + + + + + + + + + + modification from RESID + 43.09 + C 3 H 7 N 0 O 0 + 43.054775 + 1+ + C 5 H 11 N 1 O 1 + 101.15 + 101.08406 + G + natural + N-term + uniprot.ptm:PTM-0485 + (trimethylammonio)ethanoic acid + 1-carboxy-N,N,N-trimethylmethanazanium + 2-trimethylammonioacetate + MOD_RES N,N,N-trimethylglycine + N,N,N-trimethylglycine cation + N,N,N-trimethylglycinium + N2Me3+Gly + betaine + carboxy-N,N,N-trimethylmethanaminium + carboxymethyl-trimethylazanium + glycine betaine + PSI-MOD + MOD:01982 + + N,N,N-trimethylglycine + + + + + modification from RESID + ChEBI:17750 + PubMed:23818633 + PubMed:23978223 + RESID:AA0619 + + + + + (trimethylammonio)ethanoic acid + + + + + + 1-carboxy-N,N,N-trimethylmethanazanium + + + + + + 2-trimethylammonioacetate + + + + + + MOD_RES N,N,N-trimethylglycine + + + + + + N,N,N-trimethylglycine cation + + + + + + N,N,N-trimethylglycinium + + + + + + N2Me3+Gly + + + + + + betaine + + + + + + carboxy-N,N,N-trimethylmethanaminium + + + + + + carboxymethyl-trimethylazanium + + + + + + glycine betaine + + + + + + + + + + + A protein modification that effectively converts a glycine residue to N,N-dimethyllglycine. + 28.05 + C 2 H 4 N 0 O 0 + 28.0313 + C 4 H 8 N 1 O 1 + 86.11 + 86.06059 + G + natural + N-term + uniprot.ptm:PTM-0484 + (dimethylamino)ethanoic acid + 1-carboxy-N,N-dimethylaminomethane + 2-(dimethylamino)acetic acid + MOD_RES N,N-dimethylglycine + vitamin B16 + PSI-MOD + MOD:01983 + N,N-dimethylglycine + + + + + A protein modification that effectively converts a glycine residue to N,N-dimethyllglycine. + ChEBI:17724 + PubMed:23818633 + PubMed:23978223 + RESID:AA0620 + + + + + (dimethylamino)ethanoic acid + + + + + + 1-carboxy-N,N-dimethylaminomethane + + + + + + 2-(dimethylamino)acetic acid + + + + + + MOD_RES N,N-dimethylglycine + + + + + + vitamin B16 + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-alanine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-alanine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 6 H 8 N 2 O 2 S 1 + 172.2 + 172.03065 + A, C + natural + (2R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid + (2R,5R)-2,5-diamino-5-methyl-4-thiahexanedioic acid + alpha-(L-cystein-S-yl)-L-alanine + PSI-MOD + MOD:01984 + Cross-link 2. + 2-(L-cystein-S-yl)-L-alanine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-alanine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-alanine. + PubMed:21526839 + RESID:AA0621 + + + + + (2R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid + + + + + + (2R,5R)-2,5-diamino-5-methyl-4-thiahexanedioic acid + + + + + + alpha-(L-cystein-S-yl)-L-alanine + + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-asparagine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-asparagine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 7 H 9 N 3 O 3 S 1 + 215.23 + 215.03647 + C, N + natural + (2S)-2,4-diamino-2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-4-oxobutanoic acid + alpha-(L-cystein-S-yl)-D-asparagine + PSI-MOD + MOD:01985 + Cross-link 2. + 2-(L-cystein-S-yl)-D-asparagine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-asparagine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-asparagine. + PubMed:21786372 + RESID:AA0622 + + + + + (2S)-2,4-diamino-2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-4-oxobutanoic acid + + + + + + alpha-(L-cystein-S-yl)-D-asparagine + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-serine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 6 H 8 N 2 O 3 S 1 + 188.2 + 188.02556 + C, S + natural + (2R)-2-amino-2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-hydroxypropanoic acid + (2R,5R)-2,5-diamino-5-carboxy-6-hydroxy-4-thiahexanoic acid + PSI-MOD + MOD:01986 + Cross-link 2. + 2-(L-cystein-S-yl)-L-serine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-serine. + PubMed:21526839 + RESID:AA0623 + + + + + (2R)-2-amino-2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-hydroxypropanoic acid + + + + + + (2R,5R)-2,5-diamino-5-carboxy-6-hydroxy-4-thiahexanoic acid + + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-serine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 6 H 8 N 2 O 3 S 1 + 188.2 + 188.02556 + C, S + natural + (2R,5S)-2,5-diamino-5-carboxy-6-hydroxy-4-thiahexanoic acid + (2S)-2-amino-2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-hydroxypropanoic acid + PSI-MOD + MOD:01987 + Cross-link 2. + 2-(L-cystein-S-yl)-D-serine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-serine. + PubMed:21786372 + RESID:AA0624 + + + + + (2R,5S)-2,5-diamino-5-carboxy-6-hydroxy-4-thiahexanoic acid + + + + + + (2S)-2-amino-2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-hydroxypropanoic acid + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-threonine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 7 H 10 N 2 O 3 S 1 + 202.23 + 202.04121 + C, T + natural + (2R,3R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid + (2R,5R,6R)-2,5-diamino-5-carboxy-6-hydroxy-4-thiaheptanoic acid + alpha-(L-cystein-S-yl)-L-threonine + PSI-MOD + MOD:01988 + Cross-link 2. + 2-(L-cystein-S-yl)-L-threonine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-threonine. + PubMed:21526839 + RESID:AA0625 + + + + + (2R,3R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid + + + + + + (2R,5R,6R)-2,5-diamino-5-carboxy-6-hydroxy-4-thiaheptanoic acid + + + + + + alpha-(L-cystein-S-yl)-L-threonine + + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-tyrosine. + -2.02 + C 0 H -2 N 0 O 0 S 0 + -2.01565 + C 12 H 12 N 2 O 3 S 1 + 264.3 + 264.05685 + C, Y + natural + (2R,5S)-2,5-diamino-5-carboxyl-6-(hydroxyphenyl)-4-thiahexanoic acid + (2S)-2-amino-2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-(4-hydroxyphenyl)propanoic acid + alpha-(L-cystein-S-yl)-D-tyrosine + PSI-MOD + MOD:01989 + Cross-link 2. + 2-(L-cystein-S-yl)-D-tyrosine + + + + + A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-tyrosine. + PubMed:21526839 + RESID:AA0626 + + + + + (2R,5S)-2,5-diamino-5-carboxyl-6-(hydroxyphenyl)-4-thiahexanoic acid + + + + + + (2S)-2-amino-2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-(4-hydroxyphenyl)propanoic acid + + + + + + alpha-(L-cystein-S-yl)-D-tyrosine + + + + + + + + + + + A protein modification that effectively converts a glycine residue to a glycinium (protonated glycine). + 1.01 + C 0 H 1 N 0 O 0 + 1.007276 + 1+ + C 2 H 5 N 1 O 1 + 59.07 + 59.036564 + G + natural + N-term + PSI-MOD + MOD:01990 + + protonated glycine (glycinium) residue + + + + + A protein modification that effectively converts a glycine residue to a glycinium (protonated glycine). + ChEBI:64723 + PubMed:18688235 + + + + + + + + + + + + + + + A protein modification that effectively converts a glycinium (protonated glycine) residue to an N,N,N-trimethylglycine. + 42.08 + C 3 H 6 N 0 O 0 + 42.046402 + 1+ + C 5 H 11 N 1 O 1 + 101.15 + 101.08351 + MOD:01990 + natural + N-term + N2Me3Gly + PSI-MOD + MOD:01991 + + For amino acids residues, amine trimethylation can effectively only be accomplished with an aminium, protonated primary amino, group. This process accounts only for trimethylation and not protonation. The alternative N2Me3+Gly process (MOD:01982) accounts for both protonation and trimethylation. + N,N,N-trimethylglycine (from glycinium) + + + + + A protein modification that effectively converts a glycinium (protonated glycine) residue to an N,N,N-trimethylglycine. + ChEBI:17750 + PubMed:23818633 + PubMed:23978223 + RESID:AA0619 + + + + + N2Me3Gly + + + + + + + + + + A protein modification that crosslinks two residues by formation of a thioether bond between a cysteine thiol and the alpha-carbon of another amino acid residue. + PSI-MOD + MOD:01992 + alpha-carbon thioether crosslinked residues + + + + + A protein modification that crosslinks two residues by formation of a thioether bond between a cysteine thiol and the alpha-carbon of another amino acid residue. + PubMed:18688235 + + + + + + + + + A protein modification that crosslinks two residues by formation of a thioether bond between a cysteine thiol and the beta-carbon of another amino acid residue. + PSI-MOD + MOD:01993 + These are typical lanthionine-like crosslinks. + beta-carbon thioether crosslinked residues + + + + + A protein modification that crosslinks two residues by formation of a thioether bond between a cysteine thiol and the beta-carbon of another amino acid residue. + PubMed:18688235 + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to N1'-formyl-L-tryptophan. + 28.01 + C 1 H 0 N 0 O 1 + 27.994915 + C 12 H 10 N 2 O 2 + 214.22 + 214.07423 + W + hypothetical + N1'FoTrp + PSI-MOD + MOD:01994 + This modifications has not been reported as commonly encountered [JSG]. + N1'-formyl-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to N1'-formyl-L-tryptophan. + PubMed:18688235 + + + + + N1'FoTrp + + + + + + + + + + A protein modification that effectively converts an L-tryptophan residue to N2-formyl-L-tryptophan. + 28.01 + C 1 H 0 N 0 O 1 + 27.994915 + C 12 H 11 N 2 O 2 + 215.23 + 215.08205 + W + hypothetical + N-term + N2FoTrp + PSI-MOD + MOD:01995 + This modifications has not been reported as commonly encountered [JSG]. + N2-formyl-L-tryptophan + + + + + A protein modification that effectively converts an L-tryptophan residue to N2-formyl-L-tryptophan. + PubMed:18688235 + + + + + N2FoTrp + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an butanoyl group. + 70.09 + C 4 H 6 O 1 + 70.04186 + X + ButRes + butyrylation + PSI-MOD + Butyryl + MOD:01996 + Amino hydrogens are replaced to produce amides; hydroxyl hydrogens are replaced to produce esters; and hydrosulfanyl (thiol) hydrogens are replaced to produce sulfanyl esters (thiol esters). + butanoylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an butanoyl group. + PubMed:18688235 + + + + + ButRes + + + + + + butyrylation + + + + + + Butyryl + + + + + + + + + + A protein modification that effectively replaces a residue amino or imino hydrogen with a butanoyl group. + 70.09 + C 4 H 6 N 0 O 1 + 70.04186 + X + N-butanoyl + N-butanoylation + N-butyryl + N-butyrylation + NButRes + PSI-MOD + MOD:01997 + N-butanoylated residue + + + + + A protein modification that effectively replaces a residue amino or imino hydrogen with a butanoyl group. + PubMed:18688235 + + + + + N-butanoyl + + + + + + N-butanoylation + + + + + + N-butyryl + + + + + + N-butyrylation + + + + + + NButRes + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a butanoyl group. + 70.09 + C 4 H 6 N 0 O 1 + 70.04186 + X + artifact + N-term + N2ButRes + PSI-MOD + MOD:01998 + alpha-amino butanoylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a butanoyl group. + PubMed:18688235 + + + + + N2ButRes + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-retinylidene-(11-cis)-L-lysine. + 266.43 + C 20 H 26 N 0 O 0 + 266.20346 + C 26 H 38 N 2 O 1 + 394.6 + 394.2984 + K + natural + (2S)-2-amino-6-[(2E,4Z,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid + PSI-MOD + MOD:01999 + N6-(11-cis)-retinylidene-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-retinylidene-(11-cis)-L-lysine. + PubMed:18688235 + + + + + (2S)-2-amino-6-[(2E,4Z,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine (unspecified geometric isomer). + 266.43 + C 20 H 26 N 0 O 0 + 266.20346 + C 26 H 38 N 2 O 1 + 394.6 + 394.2984 + K + natural + (2S)-2-amino-6-[3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid + PSI-MOD + MOD:02000 + N6-retinylidene-L-lysine (unspecified geometric isomer) + + + + + A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine (unspecified geometric isomer). + PubMed:18688235 + + + + + (2S)-2-amino-6-[3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a stearoyl group. + 266.47 + C 18 H 34 O 1 + 266.26096 + X + natural + PSI-MOD + MOD:02001 + + stearoylated residue + + + + + + + + + + A protein modification that effectively replaces a residue sulfanyl group with a palmitoleylsulfanyl group. + 236.4 + C 16 H 28 N 0 O 1 + 236.21402 + X + natural + PSI-MOD + MOD:02002 + + S-palmitoleylated residue + + + + + + + + + + A protein modification that effectively replaces an O3-hydroxy hydrogen atom of L-serine with an acyl group. + S + natural + PSI-MOD + MOD:02003 + + O3-acylated L-serine + + + + + + + + + + A protein modification that effectively replaces an O3-hydroxy hydrogen atom of L-threonine with an acyl group. + T + natural + PSI-MOD + MOD:02004 + + O3-acylated L-threonine + + + + + + + + + + A protein modification that effectively replaces an sulfanyl hydrogen atom of L-cysteine with an acyl group. + C + natural + PSI-MOD + MOD:02005 + + S-acylated L-cysteine + + + + + + + + + + A protein modification that effectively replaces a residue sulfanyl group with a stearoylsulfanyl group. + 266.47 + C 18 H 34 O 1 + 266.26096 + X + natural + PSI-MOD + MOD:02006 + + S-stearoylated residue + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-palmitoleyl-L-lysine. + 236.4 + C 16 H 28 N 0 O 1 + 236.21402 + C 22 H 40 N 2 O 2 + 364.58 + 364.309 + K + natural + PSI-MOD + MOD:02007 + + N6-palmitoleyl-L-lysine + + + + + + + + + + A protein modification that effectively replaces a residue amino group with a palmitoleylamino group. + 236.4 + C 16 H 28 N 0 O 1 + 236.21402 + X + natural + PSI-MOD + MOD:02008 + + N-palmitoleylated residue + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-stearoyl-L-lysine. + 266.47 + C 18 H 34 O 1 + 266.26096 + C 24 H 46 N 2 O 2 + 394.65 + 394.35593 + K + natural + PSI-MOD + MOD:02009 + + N6-stearoyl-L-lysine + + + + + + + + + + A protein modification that effectively replaces a residue amino group with a stearoylamino group. + 266.47 + C 18 H 34 O 1 + 266.26096 + X + natural + PSI-MOD + MOD:02010 + + N-stearoylated residue + + + + + + + + + + A protein modification that effectively replaces a residue amino group with a oleoylamino group. + 264.45 + C 18 H 32 N 0 O 1 + 264.24533 + X + natural + PSI-MOD + MOD:02011 + + N-oleoylated residue + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a oleoyl group. + 264.45 + C 18 H 32 N 0 O 1 + 264.24533 + X + natural + PSI-MOD + MOD:02012 + + oleoylated residue + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-linoloyl-L-lysine. + 262.45 + C 18 H 30 N 0 O 1 + 262.22968 + C 24 H 42 N 2 O 2 + 390.63 + 390.32462 + K + natural + PSI-MOD + MOD:02013 + + N6-linoloyl-L-lysine + + + + + + + + + + A protein modification that effectively replaces a residue amino group with a linoloylamino group. + 262.45 + C 18 H 30 N 0 O 1 + 262.22968 + X + natural + PSI-MOD + MOD:02014 + + N-linoloylated residue + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a linoloyl group. + 262.45 + C 18 H 30 N 0 O 1 + 262.22968 + X + natural + PSI-MOD + MOD:02015 + + linoloylated residue + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-arachidonoyl-L-lysine. + 286.49 + C 20 H 30 N 0 O 1 + 286.22968 + C 26 H 42 N 2 O 2 + 414.67 + 414.32462 + K + natural + PSI-MOD + MOD:02016 + + N6-arachidonoyl-L-lysine + + + + + + + + + + A protein modification that effectively replaces a residue amino group with an arachidonoylamino group. + 286.49 + C 20 H 30 N 0 O 1 + 286.22968 + X + natural + PSI-MOD + MOD:02017 + + N-arachidonoylated residue + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an arachidonoyl group. + 286.49 + C 20 H 30 N 0 O 1 + 286.22968 + X + natural + PSI-MOD + MOD:02018 + + arachidonoylated residue + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-timnodonoyl-L-lysine. + 284.48 + C 20 H 28 N 0 O 1 + 284.21402 + C 26 H 40 N 2 O 2 + 412.66 + 412.309 + K + natural + PSI-MOD + MOD:02019 + + N6-timnodonoyl-L-lysine + + + + + + + + + + A protein modification that effectively replaces a residue amino group with a timnodonoylamino group. + 284.48 + C 20 H 28 N 0 O 1 + 284.21402 + X + natural + PSI-MOD + MOD:02020 + + N-timnodonoylated residue + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a timnodonoyl group. + 284.48 + C 20 H 28 N 0 O 1 + 284.21402 + X + natural + PSI-MOD + MOD:02021 + + timnodonoylated residue + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-cervonoyl-L-lysine. + 310.53 + C 22 H 30 N 0 O 1 + 310.22968 + C 28 H 42 N 2 O 2 + 438.71 + 438.32462 + K + natural + PSI-MOD + MOD:02022 + + N6-cervonoyl-L-lysine + + + + + + + + + + A protein modification that effectively replaces a residue amino group with a cervonoylamino group. + 310.53 + C 22 H 30 N 0 O 1 + 310.22968 + X + natural + PSI-MOD + MOD:02023 + + N-cervonoylated residue + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with a cervonoyl group. + 310.53 + C 22 H 30 N 0 O 1 + 310.22968 + X + natural + PSI-MOD + MOD:02024 + + cervonoylated residue + + + + + + + + + A protein modification that effectively converts the alpha amino group of a glutamine residue to glutaminyl glutamic acid by forming an isopeptide bond with the side chain carboxyl group of a free glutamic acid. + 128.13 + C 5 H 8 N 2 O 2 + 128.05858 + C 10 H 15 N 3 O 5 + 257.24 + 257.10117 + E + natural + PSI-MOD + MOD:02025 + 5-glutaminyl glutamic acid + + + + + A protein modification that effectively converts the alpha amino group of a glutamine residue to glutaminyl glutamic acid by forming an isopeptide bond with the side chain carboxyl group of a free glutamic acid. + PubMed:28801462 + + + + + + + + + + + + + + + + A protein modification that effectively cross-links an L-cysteinyl-L-glycine dipeptide and an L-cysteine residue by a disulfide bond to form S-(cysteinyl-glycyl)-L-cysteine. + 176.17 + C 5 H 8 N 2 O 3 S 1 + 176.02556 + C 8 H 13 N 3 O 4 S 2 + 279.33 + 279.03476 + C + natural + PSI-MOD + MOD:02026 + Glutamyl-transpeptidase cleaves glutathione into cysteinylglycine (Cys-Gly) and a Glu residue. [PubMed:28537416] + S-(cysteinyl-glycyl)-L-cysteine + + + + + A protein modification that effectively cross-links an L-cysteinyl-L-glycine dipeptide and an L-cysteine residue by a disulfide bond to form S-(cysteinyl-glycyl)-L-cysteine. + PubMed:20594348 + PubMed:27936627 + PubMed:29627744 + + + + + + + + + + + + + + + + + A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a URM1 protein. + K + natural + PSI-MOD + MOD:02027 + + urmylated lysine + + + + + A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a URM1 protein. + PubMed:10713047 + PubMed:21209336 + + + + + + + + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups. + 144.1 + 144.10242 + X + artifact + (4-methylpiperazin-1-yl)acetyl + PSI-MOD + iTRAQ + MOD:02028 + + The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. Four versions of chemically identical iTRAQ4plex moyeties, but with different isotope distribution. This modification is calculated as the average of the four species. It has no isotopic distribution reality, the exact mass does not correspond to any real isotopic distribution. + iTRAQ4plex reporter+balance reagent acylated residue, average mass modification + + + + + A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups. + Unimod:214 + + + + + (4-methylpiperazin-1-yl)acetyl + + + + + + iTRAQ + + + + + + + + + + A protein modification that effectively specifies the boundary conformation of two adjacent source amino acid residues, the second (C-term side) being a L-proline, where the carbonyl group of the amide bond of the N-side of the L-proline is positioned such that the organodiyl group is in the cis orientation (omega=0) + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + X, P + natural + PSI-MOD + MOD:02029 + cis-peptidyl-L-proline + + + + + A protein modification that effectively specifies the boundary conformation of two adjacent source amino acid residues, the second (C-term side) being a L-proline, where the carbonyl group of the amide bond of the N-side of the L-proline is positioned such that the organodiyl group is in the cis orientation (omega=0) + ChEBI:83833 + PubMed:15311922 + PubMed:15735342 + PubMed:24116866 + PubMed:5485910 + + + + + + + + + A protein modification that effectively specifies the boundary conformation of two adjacent source amino acid residues, the second (C-term side) being a L-proline, where the carbonyl group of the amide bond of the N-side of the L-proline is positioned such that the organodiyl group is in the trans orientation (omega=180) + 0.0 + C 0 H 0 N 0 O 0 + 0.0 + X, P + natural + PSI-MOD + MOD:02030 + trans-peptidyl-L-proline + + + + + A protein modification that effectively specifies the boundary conformation of two adjacent source amino acid residues, the second (C-term side) being a L-proline, where the carbonyl group of the amide bond of the N-side of the L-proline is positioned such that the organodiyl group is in the trans orientation (omega=180) + ChEBI:83834 + PubMed:15311922 + PubMed:15735342 + PubMed:24116866 + PubMed:5485910 + + + + + + + + + + modification from Unimod N-linked glycosylation, dHex Hex(4) HexNAc(5) + 1810.68 + C 70 H 115 N 5 O 49 + 1809.666 + C 74 H 121 N 7 O 51 + 1924.78 + 1923.709 + N + natural + GNO:G03382KH + Unimod:1519 + PSI-MOD + dHex Hex(4) HexNAc(5) + MOD:02031 + dHex1Hex4HexNAc5 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation, dHex Hex(4) HexNAc(5) + PubMed:33135055 + Unimod:1519 + + + + + dHex Hex(4) HexNAc(5) + + + + + + + + + + + modification from Unimod N-linked glycosylation, dHex(2) Hex(4) HexNAc(5) + 1956.82 + C 76 H 125 N 5 O 53 + 1955.724 + C 80 H 131 N 7 O 55 + 2070.92 + 2069.7668 + N + natural + GNO:G70418MS + Unimod:1785 + PSI-MOD + dHex(2) Hex(4) HexNAc(5) + MOD:02032 + dHex2Hex4HexNAc5 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation, dHex(2) Hex(4) HexNAc(5) + PubMed:33135055 + Unimod:1785 + + + + + dHex(2) Hex(4) HexNAc(5) + + + + + + + + + + + modification from Unimod N-linked glycosylation, dHex Hex(5) HexNAc(3) + 1566.43 + C 60 H 99 N 3 O 44 + 1565.5602 + C 64 H 105 N 5 O 46 + 1680.53 + 1679.603 + N + natural + GNO:G82119TF + Unimod:1484 + PSI-MOD + dHex Hex(5) HexNAc(3) + MOD:02033 + dHex1Hex5HexNAc3 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation, dHex Hex(5) HexNAc(3) + PubMed:33135055 + Unimod:1484 + + + + + dHex Hex(5) HexNAc(3) + + + + + + + + + + + modification from Unimod N-linked glycosylation, dHex Hex(3) HexNAc(6) + 1851.73 + C 72 H 118 N 6 O 49 + 1850.6926 + C 76 H 124 N 8 O 51 + 1965.83 + 1964.7356 + N + natural + GNO:G50757KG + Unimod:1781 + PSI-MOD + dHex Hex(3) HexNAc(6) + MOD:02034 + dHex1Hex3HexNAc6 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation, dHex Hex(3) HexNAc(6) + PubMed:33135055 + Unimod:1781 + + + + + dHex Hex(3) HexNAc(6) + + + + + + + + + + + modification from Unimod N-linked glycosylation, dHex Hex(6) HexNAc(3) + 1728.57 + C 66 H 109 N 3 O 49 + 1727.6129 + C 70 H 115 N 5 O 51 + 1842.67 + 1841.6559 + N + natural + GNO:G84820NF + Unimod:1509 + PSI-MOD + dHex Hex(6) HexNAc(3) + MOD:02035 + dHex1Hex6HexNAc3 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation, dHex Hex(6) HexNAc(3) + PubMed:33135055 + Unimod:1509 + + + + + dHex Hex(6) HexNAc(3) + + + + + + + + + + + modification from Unimod N-linked glycosylation, Hex(9)HexNAc(2) + 1865.66 + C 70 H 116 N 2 O 55 + 1864.6342 + C 74 H 122 N 4 O 57 + 1979.76 + 1978.6771 + N + natural + GNO:G70101JE + Unimod:1531 + PSI-MOD + M9/Man9 + MOD:02036 + Hex9HexNAc2 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation, Hex(9)HexNAc(2) + PubMed:33135055 + Unimod:1531 + + + + + M9/Man9 + + + + + + + + + + + modification from Unimod N-linked glycosylation, Hex(7) HexNAc(2) + 1541.38 + C 58 H 96 N 2 O 45 + 1540.5286 + C 62 H 102 N 4 O 47 + 1655.48 + 1654.5714 + N + natural + GNO:G05724UK + Unimod:1480 + PSI-MOD + M7/Man7 + MOD:02037 + Hex7HexNAc2 N4-glycosylated asparagine + + + + + modification from Unimod N-linked glycosylation, Hex(7) HexNAc(2) + PubMed:33135055 + Unimod:1480 + + + + + M7/Man7 + + + + + + + + + + + A protein modification that effectively replaces one hydrogen atom of an L-histidine residue with one methyl group. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 7 H 9 N 3 O 1 + 151.17 + 151.07455 + H + natural + Unimod:34 + uniprot.ptm:PTM-0176 + MOD_RES Methylhistidine + Me1His + methylh + PSI-MOD + Methyl + MOD:02038 + + monomethylated L-histidine + + + + + A protein modification that effectively replaces one hydrogen atom of an L-histidine residue with one methyl group. + DeltaMass:215 + OMSSA:77 + Unimod:34#H + + + + + MOD_RES Methylhistidine + + + + + + Me1His + + + + + + methylh + + + + + + Methyl + + + + + + + + + + A protein modification that effectively replaces a hydrogen group with a amino group + X + AmRes + PSI-MOD + MOD:02039 + aminated residue + + + + + AmRes + + + + + + + + + + A protein modification that contains an L-alanine residue crosslinked to one or more amino acid residues. + A + XlnkAla + PSI-MOD + MOD:02040 + + crosslinked L-alanine residue + + + + + A protein modification that contains an L-alanine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkAla + + + + + + + + + + A protein modification that contains an L-arginine residue crosslinked to one or more amino acid residues. + R + XlnkArg + PSI-MOD + MOD:02041 + + crosslinked L-arginine residue + + + + + A protein modification that contains an L-arginine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkArg + + + + + + + + + + A protein modification that contains an L-asparagine residue crosslinked to one or more amino acid residues. + N + XlnkAsn + PSI-MOD + MOD:02042 + + crosslinked L-asparagine residue + + + + + A protein modification that contains an L-asparagine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkAsn + + + + + + + + + + A protein modification that contains an L-aspartic acid residue crosslinked to one or more amino acid residues. + D + XlnkAsp + PSI-MOD + MOD:02043 + + crosslinked L-aspartic acid residue + + + + + A protein modification that contains an L-aspartic acid residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkAsp + + + + + + + + + + A protein modification that contains an L-cysteine residue crosslinked to one or more amino acid residues. + C + XlnkCys + PSI-MOD + MOD:02044 + + crosslinked L-cysteine residue + + + + + A protein modification that contains an L-cysteine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkCys + + + + + + + + + + A protein modification that contains an L-glutamic acid residue crosslinked to one or more amino acid residues. + E + XlnkGlu + PSI-MOD + MOD:02045 + + crosslinked L-glutamic acid residue + + + + + A protein modification that contains an L-glutamic acid residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkGlu + + + + + + + + + + A protein modification that contains an L-glutamine residue crosslinked to one or more amino acid residues. + Q + XlnkGln + PSI-MOD + MOD:02046 + + crosslinked L-glutamine residue + + + + + A protein modification that contains an L-glutamine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkGln + + + + + + + + + + A protein modification that contains a glycine residue crosslinked to one or more amino acid residues. + G + XlnkGly + PSI-MOD + MOD:02047 + + crosslinked glycine residue + + + + + A protein modification that contains a glycine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkGly + + + + + + + + + + A protein modification that contains an L-histidine residue crosslinked to one or more amino acid residues. + H + XlnkHis + PSI-MOD + MOD:02048 + + crosslinked L-histidine residue + + + + + A protein modification that contains an L-histidine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkHis + + + + + + + + + + A protein modification that contains an L-isoleucine residue crosslinked to one or more amino acid residues. + I + XlnkIle + PSI-MOD + MOD:02049 + + crosslinked L-isoleucine residue + + + + + A protein modification that contains an L-isoleucine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkIle + + + + + + + + + + A protein modification that contains an L-leucine residue crosslinked to one or more amino acid residues. + L + XlnkLeu + PSI-MOD + MOD:02050 + + crosslinked L-leucine residue + + + + + A protein modification that contains an L-leucine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkLeu + + + + + + + + + + A protein modification that contains an L-lysine residue crosslinked to one or more amino acid residues. + K + XlnkLys + PSI-MOD + MOD:02051 + + crosslinked L-lysine residue + + + + + A protein modification that contains an L-lysine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkLys + + + + + + + + + + A protein modification that contains an L-methionine residue crosslinked to one or more amino acid residues. + M + XlnkMet + PSI-MOD + MOD:02052 + + crosslinked L-methionine residue + + + + + A protein modification that contains an L-methionine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkMet + + + + + + + + + + A protein modification that contains an L-phenylalanine residue crosslinked to one or more amino acid residues. + F + XlnkPhe + PSI-MOD + MOD:02053 + + crosslinked L-phenylalanine residue + + + + + A protein modification that contains an L-phenylalanine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkPhe + + + + + + + + + + A protein modification that contains an L-proline residue crosslinked to one or more amino acid residues. + P + XlnkPro + PSI-MOD + MOD:02054 + + crosslinked L-proline residue + + + + + A protein modification that contains an L-proline residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkPro + + + + + + + + + + A protein modification that contains an L-serine residue crosslinked to one or more amino acid residues. + S + XlnkSer + PSI-MOD + MOD:02055 + + crosslinked L-serine residue + + + + + A protein modification that contains an L-serine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkSer + + + + + + + + + + A protein modification that contains an L-threonine residue crosslinked to one or more amino acid residues. + T + XlnkThr + PSI-MOD + MOD:02056 + + crosslinked L-threonine residue + + + + + A protein modification that contains an L-threonine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkThr + + + + + + + + + + A protein modification that contains an L-tryptophan residue crosslinked to one or more amino acid residues. + W + XlnkTrp + PSI-MOD + MOD:02057 + + crosslinked L-tryptophan residue + + + + + A protein modification that contains an L-tryptophan residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkTrp + + + + + + + + + + A protein modification that contains an L-tyrosine residue crosslinked to one or more amino acid residues. + Y + XlnkTyr + PSI-MOD + MOD:02058 + + crosslinked L-tyrosine residue + + + + + A protein modification that contains an L-tyrosine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkTyr + + + + + + + + + + A protein modification that contains an L-valine residue crosslinked to one or more amino acid residues. + V + XlnkVal + PSI-MOD + MOD:02059 + + crosslinked L-valine residue + + + + + A protein modification that contains an L-valine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkVal + + + + + + + + + + A protein modification that contains an D-asparagine residue crosslinked to one or more amino acid residues. + MOD:00203 + XlnkDAsn + PSI-MOD + MOD:02060 + + crosslinked D-asparagine residue + + + + + A protein modification that contains an D-asparagine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkDAsn + + + + + + + + + + A protein modification that contains an L-selenocysteine residue crosslinked to one or more amino acid residues. + U + PSI-MOD + MOD:02061 + + crosslinked L-selenocysteine residue + + + + + A protein modification that contains an L-selenocysteine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + + + + + A protein modification that contains an N-formyl-L-methionine residue crosslinked to one or more amino acid residues. + MOD:00030 + PSI-MOD + MOD:02062 + + crosslinked N-formyl-L-methionine residue + + + + + A protein modification that contains an N-formyl-L-methionine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + + + + + A protein modification that contains an D-phenylalanine residue crosslinked to one or more amino acid residues. + F + XlnkDPhe + PSI-MOD + MOD:02063 + + crosslinked D-phenylalanine residue + + + + + A protein modification that contains an D-phenylalanine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkDPhe + + + + + + + + + + A protein modification that contains an D-serine residue crosslinked to one or more amino acid residues. + S + XlnkDSer + PSI-MOD + MOD:02064 + + crosslinked D-serine residue + + + + + A protein modification that contains an D-serine residue crosslinked to one or more amino acid residues. + PubMed:18688235 + + + + + XlnkDSer + + + + + + + + + + A protein modification that contains an L-alanine residue coordinated to one or more metal atoms or metal clusters. + A + PSI-MOD + MOD:02065 + + metal or metal cluster coordinated L-alanine residue + + + + + A protein modification that contains an L-alanine residue coordinated to one or more metal atoms or metal clusters. + PubMed:18688235 + + + + + + + + + A protein modification that contains an L-aspartic acid residue coordinated to one or more metal atoms or metal clusters. + D + PSI-MOD + MOD:02066 + + metal or metal cluster coordinated L-aspartic acid residue + + + + + A protein modification that contains an L-aspartic acid residue coordinated to one or more metal atoms or metal clusters. + PubMed:18688235 + + + + + + + + + A protein modification that contains an L-cysteine residue coordinated to one or more metal atoms or metal clusters. + C + PSI-MOD + MOD:02067 + + metal or metal cluster coordinated L-cysteine residue + + + + + A protein modification that contains an L-cysteine residue coordinated to one or more metal atoms or metal clusters. + PubMed:18688235 + + + + + + + + + A protein modification that contains an L-glutamic acid residue coordinated to one or more metal atoms or metal clusters. + E + PSI-MOD + MOD:02068 + + metal or metal cluster coordinated L-glutamic acid residue + + + + + A protein modification that contains an L-glutamic acid residue coordinated to one or more metal atoms or metal clusters. + PubMed:18688235 + + + + + + + + + A protein modification that contains an L-glutamine residue coordinated to one or more metal atoms or metal clusters. + Q + PSI-MOD + MOD:02069 + + metal or metal cluster coordinated L-glutamine residue + + + + + A protein modification that contains an L-glutamine residue coordinated to one or more metal atoms or metal clusters. + PubMed:18688235 + + + + + + + + + A protein modification that contains an L-histidine residue coordinated to one or more metal atoms or metal clusters. + H + PSI-MOD + MOD:02070 + + metal or metal cluster coordinated L-histidine residue + + + + + A protein modification that contains an L-histidine residue coordinated to one or more metal atoms or metal clusters. + PubMed:18688235 + + + + + + + + + A protein modification that contains an L-methionine residue coordinated to one or more metal atoms or metal clusters. + M + PSI-MOD + MOD:02071 + + metal or metal cluster coordinated L-methionine residue + + + + + A protein modification that contains an L-methionine residue coordinated to one or more metal atoms or metal clusters. + PubMed:18688235 + + + + + + + + + A protein modification that contains an L-serine residue coordinated to one or more metal atoms or metal clusters. + S + PSI-MOD + MOD:02072 + + metal or metal cluster coordinated L-serine residue + + + + + A protein modification that contains an L-serine residue coordinated to one or more metal atoms or metal clusters. + PubMed:18688235 + + + + + + + + + A protein modification that contains an L-selenocysteine residue coordinated to one or more metal atoms or metal clusters. + U + PSI-MOD + MOD:02073 + + metal or metal cluster coordinated L-selenocysteine residue + + + + + A protein modification that contains an L-selenocysteine residue coordinated to one or more metal atoms or metal clusters. + PubMed:18688235 + + + + + + + + + A protein modification that contains an L-lysine residue coordinated to one or more metal atoms or metal clusters. + K + PSI-MOD + MOD:02074 + + metal or metal cluster coordinated L-lysine residue + + + + + A protein modification that contains an L-lysine residue coordinated to one or more metal atoms or metal clusters. + PubMed:18688235 + + + + + + + + + A protein modification that contains an L-tyrosine residue coordinated to one or more metal atoms or metal clusters. + Y + PSI-MOD + MOD:02075 + + metal or metal cluster coordinated L-tyrosine residue + + + + + A protein modification that contains an L-tyrosine residue coordinated to one or more metal atoms or metal clusters. + PubMed:18688235 + + + + + + + + + A protein modification that contains an L-arginine residue coordinated to one or more metal atoms or metal clusters. + R + PSI-MOD + MOD:02076 + + metal or metal cluster coordinated L-arginine residue + + + + + A protein modification that contains an L-arginine residue coordinated to one or more metal atoms or metal clusters. + PubMed:18688235 + + + + + + + + + A protein modification that effectively replaces a hydrogen atom with an nitrosyl (NO) group. + 29.0 + C 0 H -1 N 1 O 1 S 0 + 28.990164 + X + natural + Unimod:275 + PSI-MOD + Nitrosyl + MOD:02077 + + nitrosylated residue + + + + + A protein modification that effectively replaces a hydrogen atom with an nitrosyl (NO) group. + PubMed:10442087 + PubMed:11562475 + PubMed:15688001 + PubMed:8626764 + PubMed:8637569 + Unimod:275 + + + + + Nitrosyl + + + + + + + + + + A protein modification that effectively replaces one or more hydrogen atoms with one or more acetyl groups. + X + artifact + AcRes + PSI-MOD + Acetyl + MOD:02078 + + acetylated residue + + + + + A protein modification that effectively replaces one or more hydrogen atoms with one or more acetyl groups. + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + PubMed:14730666 + PubMed:15350136 + + + + + AcRes + + + + + + Acetyl + + + + + + + + + + A protein modification that effectively replaces one hydrogen atom with one acetyl group. + 84.07 + C 4 H 4 N 0 O 2 + 84.021126 + X + artifact + Ac2Res + PSI-MOD + Diacetyl + MOD:02079 + + Amino hydrogens are replaced to produce amides; hydroxyl hydrogens are replaced to produce esters; and hydrosulfanyl (thiol) hydrogens are replaced to produce sulfanyl esters (thiol esters). From DeltaMass: Average Mass: 42 + diacetylated residue + + + + + A protein modification that effectively replaces one hydrogen atom with one acetyl group. + PubMed:11857757 + PubMed:11999733 + PubMed:12175151 + PubMed:14730666 + PubMed:15350136 + Unimod:1 + + + + + Ac2Res + + + + + + Diacetyl + + + + + + + + + + + A protein modification that effectively converts an L-serine residue to either N-acetyl-L-serine, O-acetyl-L-serine, or N,O-diacetyl-L-serine. + 84.07 + C 4 H 4 N 0 O 2 + 84.021126 + C 7 H 10 N 1 O 4 + 172.16 + 172.06099 + S + natural + Ac2Ser + PSI-MOD + MOD:02080 + + diacetylated L-serine + + + + + A protein modification that effectively converts an L-serine residue to either N-acetyl-L-serine, O-acetyl-L-serine, or N,O-diacetyl-L-serine. + PubMed:18688235 + + + + + Ac2Ser + + + + + + + + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a succinyl group. + 100.07 + C 4 H 4 O 3 + 100.016045 + X + natural + N-term + Unimod:64 + PSI-MOD + Succinyl + MOD:02081 + alpha-amino succinylated residue + + + + + A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a succinyl group. + PubMed:11857757 + PubMed:12175151 + Unimod:64#N-term + + + + + Succinyl + + + + + + + + + + A protein modification that effectively removes two neutral hydrogen atoms (proton and electron) and a water moiety from a residue. + -20.03 + C 0 H -4 N 0 O -1 + -20.026215 + X + 2dHdH2ORes + PSI-MOD + MOD:02082 + + didehydrogenated and dehydrated residue + + + + + A protein modification that effectively removes two neutral hydrogen atoms (proton and electron) and a water moiety from a residue. + Unimod:401 + + + + + 2dHdH2ORes + + + + + + + + + + A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through the 4-alpha position of FMN. + 456.35 + C 17 H 21 N 4 O 9 P 1 + 456.1046 + X + natural + 4aFMNRes + PSI-MOD + MOD:02083 + + 4alpha-FMN modified residue + + + + + A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through the 4-alpha position of FMN. + PubMed:18688235 + + + + + 4aFMNRes + + + + + + + + + + A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through the 6 position of FMN. + 454.33 + C 17 H 19 N 4 O 9 P 1 + 454.08896 + X + natural + 6-FMNRes + PSI-MOD + MOD:02084 + + 6-FMN modified residue + + + + + A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through the 6 position of FMN. + PubMed:18688235 + + + + + 6-FMNRes + + + + + + + + + + A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through the 8-alpha position of FMN. + 454.33 + C 17 H 19 N 4 O 9 P 1 + 454.08896 + X + natural + 8a-FMNRes + PSI-MOD + MOD:02085 + + 8alpha-FMN modified residue + + + + + A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through the 8-alpha position of FMN. + PubMed:18688235 + + + + + 8a-FMNRes + + + + + + + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-phenylalanine residue with a bromine atom. + F + BrPhe + PSI-MOD + MOD:02086 + brominated phenylalanine + + + + + A protein modification that effectively substitutes a hydrogen atom of an L-phenylalanine residue with a bromine atom. + PubMed:18688235 + + + + + BrPhe + + + + + + + + + + A protein modification that effectively results from forming an adduct with one or more ADP-ribose moieties or to modified residues through formation of a glycosidic bond. + X + natural + ADPRibRes + PSI-MOD + MOD:02087 + + adenosine diphosphoribosyl (ADP-ribosyl) modified residue + + + + + A protein modification that effectively results from forming an adduct with one or more ADP-ribose moieties or to modified residues through formation of a glycosidic bond. + DeltaMass:0 + + + + + ADPRibRes + + + + + + + + + + + A protein modification that effectively replaces a natural, standard, encoded residue. + X + natural + PSI-MOD + MOD:02088 + + This represents the replacement of an encoded residue in a polypeptide, and must be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution. + natural, standard, encoded residue substitution + + + + + A protein modification that effectively replaces a natural, standard, encoded residue. + PubMed:18688235 + + + + + + + + + + A protein modification that effectively crosslinks an L-serine residue and 5'-phosphouridine through a phosphodiester bond to form O-(phospho-5'-uridine)-L-serine. + 306.17 + C 9 H 11 N 2 O 8 P 1 + 306.0253 + C 12 H 16 N 3 O 9 P 1 + 377.24 + 377.0624 + S + natural + Unimod:417 + uniprot.ptm:PTM-0501 + MOD_RES O-UMP-serine + OUMPSer + PSI-MOD + PhosphoUridine + MOD:02089 + + O-(phospho-5'-uridine)-L-serine + + + + + A protein modification that effectively crosslinks an L-serine residue and 5'-phosphouridine through a phosphodiester bond to form O-(phospho-5'-uridine)-L-serine. + ChEBI:156051 + DeltaMass:0 + PubMed:22504181 + Unimod:417#S + + + + + MOD_RES O-UMP-serine + + + + + + OUMPSer + + + + + + PhosphoUridine + + + + + + + + + + + A protein modification that effectively modifies an L-threonine residue with 5'-phosphouridine through a phosphodiester bond to form O-(phospho-5'-uridine)-L-threonine. + 306.17 + C 9 H 11 N 2 O 8 P 1 + 306.0253 + C 13 H 18 N 3 O 9 P 1 + 391.27 + 391.07806 + T + natural + Unimod:417 + uniprot.ptm:PTM-0502 + MOD_RES O-UMP-threonine + OUMPThr + PSI-MOD + PhosphoUridine + MOD:02090 + + O-(phospho-5'-uridine)-L-threonine + + + + + A protein modification that effectively modifies an L-threonine residue with 5'-phosphouridine through a phosphodiester bond to form O-(phospho-5'-uridine)-L-threonine. + ChEBI:156052 + DeltaMass:0 + PubMed:22504181 + Unimod:417#T + + + + + MOD_RES O-UMP-threonine + + + + + + OUMPThr + + + + + + PhosphoUridine + + + + + + + + + + + A protein modification that effectively modifies an L-serine residue with 5'-phosphoadenosine through a phosphodiester bond to form O-(phospho-5'-adenosine)-L-serine. + 329.21 + C 10 H 12 N 5 O 6 P 1 + 329.05252 + C 13 H 17 N 6 O 8 P 1 + 416.28 + 416.08456 + S + natural + Unimod:405 + uniprot.ptm:PTM-0651 + MOD_RES O-AMP-serine + PSI-MOD + Phosphoadenosine + MOD:02091 + + O-(phospho-5'-adenosine)-L-serine + + + + + A protein modification that effectively modifies an L-serine residue with 5'-phosphoadenosine through a phosphodiester bond to form O-(phospho-5'-adenosine)-L-serine. + PubMed:21472612 + Unimod:405#S + + + + + MOD_RES O-AMP-serine + + + + + + Phosphoadenosine + + + + + + + + + + + A protein modification that effectively converts an L-cysteine residue to form S-methylbutanedioic acid-L-cysteine by alkylation with itaconate through a thioether bond. + 130.1 + C 5 H 6 N 0 O 4 P 0 S 0 + 130.02661 + C 8 H 11 N 1 O 5 P 0 S 1 + 233.24 + 233.0358 + C + natural + uniprot.ptm:PTM-0676 + MOD_RES S-(2,3-dicarboxypropyl)cysteine + PSI-MOD + MOD:02092 + + S-methylbutanedioic acid-L-cysteine + + + + + A protein modification that effectively converts an L-cysteine residue to form S-methylbutanedioic acid-L-cysteine by alkylation with itaconate through a thioether bond. + PubMed:29590092 + + + + + MOD_RES S-(2,3-dicarboxypropyl)cysteine + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-(2-hydroxyisobutanoyl)-L-lysine. + 86.09 + C 4 H 6 N 0 O 2 + 86.03678 + C 10 H 18 N 2 O 3 + 214.27 + 214.13174 + K + natural + Unimod:1849 + uniprot.ptm:PTM-0638 + MOD_RES N6-(2-hydroxyisobutyryl)lysine + PSI-MOD + MOD:02093 + N6-(2-hydroxyisobutanoyl)-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-(2-hydroxyisobutanoyl)-L-lysine. + ChEBI:144968 + PubMed:24681537 + PubMed:29775581 + Unimod:1849 + + + + + MOD_RES N6-(2-hydroxyisobutyryl)lysine + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-((3R)-3-hydroxybutanoyl)-L-lysine. + 86.09 + C 4 H 6 N 0 O 2 + 86.03678 + C 10 H 18 N 2 O 3 + 214.27 + 214.13174 + K + natural + uniprot.ptm:PTM-0499 + MOD_RES N6-(beta-hydroxybutyryl)lysine + PSI-MOD + MOD:02094 + N6-((3R)-3-hydroxybutanoyl)-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-((3R)-3-hydroxybutanoyl)-L-lysine. + ChEBI:149490 + PubMed:27105115 + + + + + MOD_RES N6-(beta-hydroxybutyryl)lysine + + + + + + + + + + A protein modification that effectively converts an L-lysine residue to N6-glutaryl-L-lysine. + 114.1 + C 5 H 6 N 0 O 3 + 114.03169 + C 11 H 18 N 2 O 4 + 242.28 + 242.12666 + K + natural + uniprot.ptm:PTM-0487 + MOD_RES N6-glutaryllysine + PSI-MOD + MOD:02095 + N6-glutaryl-L-lysine + + + + + A protein modification that effectively converts an L-lysine residue to N6-glutaryl-L-lysine. + ChEBI:87828 + PubMed:24703693 + + + + + MOD_RES N6-glutaryllysine + + + + + + + + + + + + + + A protein modification that effectively converts a D-asparagine residue to N4-methyl-D-asparagine. + 14.03 + C 1 H 2 N 0 O 0 + 14.01565 + C 5 H 8 N 2 O 2 + 128.13 + 128.05858 + N + natural + uniprot.ptm:PTM-0691 + MOD_RES N4-methyl-D-asparagine + N4-methylated D-asparagine + PSI-MOD + MOD:02096 + + N4-methyl-D-asparagine + + + + + A protein modification that effectively converts a D-asparagine residue to N4-methyl-D-asparagine. + ChEBI:149514 + PubMed:22983711 + + + + + MOD_RES N4-methyl-D-asparagine + + + + + + N4-methylated D-asparagine + + + + + + + + + + A protein modification that modifies a D-asparagine residue. + ModDAsn + PSI-MOD + MOD:02097 + + modified D-asparagine residue + + + + + A protein modification that modifies a D-asparagine residue. + PubMed:18688235 + + + + + ModDAsn + + + + + + + +