Annotation note 01 - "[PSI-MOD:ref]" has been replaced by PubMed:18688235.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Annotation note 07 - The synonym cross-reference "MOD:old name" has been replaced by "MOD:alternate name".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).
Misnomer tagged alternate name from RESID
Protein feature description from UniProtKB
'Entity A' contains 'Entity B' implies that 'Entity B' is a part of the structure of 'Entity A'.
'Entity A' derives_from 'Entity B' implies that 'Entity A' is chemically derived from 'Entity B'.
'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.
This relationship indicates that the formula and mass of the child are not inherited from the mass of the parent.
'Entity A' part_of 'Entity B' implies that 'Entity A' is a part of the structure of 'Entity B'.
Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue.
A protein modification that effectively replaces a hydrogen atom with an alkyl group.
A protein modification that effectively converts an L-serine residue to O3-glycosylserine.
This term is for organizational use only and should not be assigned. [JSG]
Artifact entry from Unimod - OBSOLETE because organizational use is no longer required.
A protein modification that effectively converts an L-threonine residue to O3-glycosylthreonine.
A protein modification that effectively replaces a residue hydrogen atom on a nitrogen with a carbohydrate-like group through a glycosidic bond.
A protein modification that effectively substitutes a selenium atom for a sulfur atom.
Entry from Unimod representing one or more entries in RESID. OBSOLETE because organizational use is no longer required.
A protein modification that removes a residue, or inserts or replaces a residue with a natural, standard or nonstandard, encoded residue.
A protein modification that effectively converts a source amino acid residue to an L-alanine.
A protein modification that effectively converts a source amino acid residue to an L-arginine.
(2S)-2-amino-5-[(diaminomethylidene)amino]pentanoic acid
2-amino-5-(carbamimidamido)pentanoic acid [tautomer]
2-amino-5-[(aminoiminomethyl)amino]pentanoic acid [tautomer]
2-azanyl-5-[bis(azanyl)methylideneazanyl]pentanoic acid
A protein modification that effectively converts a source amino acid residue to an L-asparagine.
A protein modification that effectively converts a source amino acid residue to an L-aspartic acid.
A protein modification that effectively converts a source amino acid residue to an L-cysteine.
A protein modification that effectively converts a source amino acid residue to an L-glutamic acid.
A protein modification that effectively converts a source amino acid residue to an L-glutamine.
A protein modification that effectively converts a source amino acid residue to a glycine.
A protein modification that effectively converts a source amino acid residue to an L-histidine.
(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]
alpha-amino-beta-(4-imidazole)propionic acid
A protein modification that effectively converts a source amino acid residue to an L-isoleucine.
A protein modification that effectively converts a source amino acid residue to an L-leucine.
A protein modification that effectively converts a source amino acid residue to L-lysine.
ACT_SITE Schiff-base intermediate with substrate
A protein modification that effectively converts a source amino acid residue to L-methionine.
(2S)-2-amino-4-(methylsulfanyl)butanoic acid
2-azanyl-4-(methylsulfanyl)butanoic acid
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.
A protein modification that effectively converts a source amino acid residue to L-proline.
A protein modification that effectively converts a source amino acid residue to L-serine.
A protein modification that effectively converts a source amino acid residue to L-threonine.
A protein modification that effectively converts a source amino acid residue to L-tryptophan.
(2S)-2-amino-3-(1H-indol-3-yl)propanoic acid
2-azanyl-3-(1H-indol-3-yl)propanoic acid
alpha-amino-beta-(3-indolyl)propionoic acid
A protein modification that effectively converts a source amino acid residue to L-tyrosine.
(2S)-2-amino-3-(4-hydoxyphenyl)propanoic acid
2-azanyl-3-(4-hydoxyphenyl)propanoic acid
alpha-amino-beta-(para-hydroxyphenyl)propionic acid
A protein modification that effectively converts a source amino acid residue to an L-valine.
A protein modification that effectively converts a source amino acid residue to an N-formyl-L-methionine, a natural pretranslational modification.
(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
A protein modification that effectively converts a source amino acid residue to an L-selenocysteine, a natural pretranslational modification.
A protein modification that is not chemically categorized.
A protein modification that crosslinks two or more amino acid residues with covalent bonds.
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.
A protein modification that effectively cross-links two L-cysteine residues to form L-cystine.
(2R,2'R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid)
3,3'-disulfane-1,2-diylbis(2-azanylpropanoic acid)
bis(alpha-aminopropionic acid)-beta-disulfide
2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid
Cross-link 2; for formation of a disulfide bond between a peptide cysteine and a free cysteine, see MOD:00765.
A protein modification that effectively converts an L-asparagine residue to (2S,3R)-3-hydroxyasparagine.
(2S,3R)-2,4-diamino-3-hydroxy-4-oxobutanoic acid
(2S,3R)-2-amino-3-hydroxy-4-butanediamic acid
A protein modification that effectively converts an L-aspartic acid residue to (2S,3R)-3-hydroxyaspartic acid.
(2S,3R)-2-amino-3-hydroxybutanedioic acid
erythro-beta-hydroxylated L-aspartic acid
A protein modification that effectively converts an L-lysine residue to one of the diastereomeric 5-hydroxy-L-lysine residues.
A protein modification that effectively converts an L-proline residue to 3-hydroxy-L-proline.
(2S,3S)-3-hydroxypyrrolidine-2-carboxylic acid
beta-hydroxypyrrolidine-alpha-carboxylic acid
A protein modification that effectively converts an L-proline residue to 4-hydroxy-L-proline
(2S,4R)-4-hydroxypyrrolidine-2-carboxylic acid
gamma-hydroxypyrrolidine-alpha-carboxylic acid
A protein modification that effectively converts an L-glutamine residue to 2-pyrrolidone-5-carboxylic acid.
DeltaMass gives a formula C 5 H 5 N 1 O 2 with mass 111.1
A protein modification that effectively converts an L-glutamic acid residue to L-gamma-carboxyglutamic acid.
(3S)-3-aminopropane-1,1,3-tricarboxylic acid
(3S)-3-azanylpropane-1,1,3-tricarboxylic acid
3-azanylpropane-1,1,3-tricarboxylic acid
DeltaMass has an incorrect formula C 6 H 7 N 5 O 1 (N and O reversed) with mass 173.
A protein modification that effectively converts an L-aspartic acid residue to L-aspartic 4-phosphoric anhydride.
(2S)-2-amino-4-oxo-4-(phosphonooxy)butanoic acid
2-aminobutanedioic 4-phosphoric anhydride
2-azanyl-4-oxo-4-(phosphonooxy)butanoic acid
ACT_SITE 4-aspartylphosphate intermediate
A protein modification that effectively converts an L-cysteine residue to S-phospho-L-cysteine.
(2R)-2-amino-3-(phosphonosulfanyl)propanoic acid
2-azanyl-3-(phosphonosulfanyl)propanoic acid
A protein modification that effectively converts an L-histidine residue to tele-phospho-L-histidine (N-tau-phospho-L-histidine, 1'-phospho-L-histidine).
(2S)-2-amino-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid
2-azanyl-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid
ACT_SITE Tele-phosphohistidine intermediate
A protein modification that effectively converts an L-histidine residue to pros-phospho-L-histidine (N-pi-phospho-L-histidine, 3'-phospho-L-histidine).
(2S)-2-amino-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid
2-azanyl-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid
ACT_SITE Pros-phosphohistidine intermediate
A protein modification that effectively converts an L-serine residue to O-phospho-L-serine.
(2S)-2-amino-3-(phosphonooxy)propanoic acid
2-amino-3-hydroxypropanoic acid 3-phosphate
A protein modification that effectively converts an L-threonine residue to O-phospho-L-threonine.
(2S,3R)-2-amino-3-(phosphonooxy)butanoic acid
2-amino-3-hydroxybutanoic acid 3-phosphate
A protein modification that effectively converts an L-tyrosine residue to O4'-phospho-L-tyrosine.
(2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid
2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate
2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid
A protein modification that effectively converts an L-histidine residue to diphthamide.
2-amino-3-2-(3-amino-3-carbamoyl-prop-1-enyl)-1,1,3-trimethyl-2,3-dihydroimidazol-5-ylpropanoic acid
A protein modification that effectively converts an L-alanine residue to N-acetyl-L-alanine.
A protein modification that effectively converts an L-aspartic acid residue to N-acetyl-L-aspartic acid.
A protein modification that effectively converts an L-cysteine residue to N-acetyl-L-cysteine.
(2R)-2-acetamido-3-sulfanylpropanoic acid
A protein modification that effectively converts an L-glutamic acid residue to N-acetyl-L-glutamic acid.
A protein modification that effectively converts an L-glutamine residue to N-acetyl-L-glutamine.
2-acetylamino-5-amino-5-oxopentanoic acid
2-acetylazanyl-5-azanyl-5-oxopentanoic acid
This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
A protein modification that effectively converts a glycine residue to N-acetylglycine.
A protein modification that effectively converts an L-isoleucine residue to N-acetyl-L-isoleucine.
(2S,3S)-2-acetamido-3-methylpentanoic acid
A protein modification that effectively converts an L-lysine residue to N2-acetyl-L-lysine.
A protein modification that effectively converts an L-methionine to N-acetyl-L-methionine.
(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
A protein modification that effectively converts an L-proline residue to N-acetyl-L-proline.
(2S)-1-acetyl-2-pyrrolidinecarboxylic acid
A protein modification that effectively converts an L-serine residue to N-acetyl-L-serine.
(2S)-2-acetamido-3-hydroxypropanoic acid
A protein modification that effectively converts an L-threonine residue to N-acetyl-L-threonine.
(2S,3R)-2-acetamido-3-hydroxybutanoic acid
A protein modification that effectively converts an L-tyrosine residue to N-acetyl-L-tyrosine.
(2S)-2-acetamido-3-(4-hydoxyphenyl)propanoic acid
2-acetylamino-3-(4-hydoxyphenyl)propanoic acid
2-acetylazanyl-3-(4-hydoxyphenyl)propanoic acid
A protein modification that effectively converts an L-valine residue to N-acetyl-L-valine.
A protein modification that effectively converts an L-lysine residue to N6-acetyl-L-lysine.
A protein modification that effectively converts an L-cysteine residue to S-acetyl-L-cysteine.
(2R)-3-acetylsulfanyl-2-aminopropanoic acid
2-azanyl-3-(acetylsulfanyl)propanoic acid
A protein modification that effectively converts a glycine residue to N-formylglycine.
A protein modification that effectively converts a glycine residue to N-D-glucuronoylglycine.
A protein modification that effectively converts a glycine residue to N-myristoylglycine.
A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-L-cysteine.
(2R)-2-hexadecanoylamino-3-sulfanylpropanoic acid
2-hexadecanamido-3-sulfanylpropanoic acid
2-hexadecanoylamino-3-mercaptopropanoic acid
incidental to RESID:AA0107 incidental to RESID:AA0309
A protein modification that effectively converts an L-alanine residue to N-methyl-L-alanine.
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].
A protein modification that effectively converts an L-alanine residue to N,N,N-trimethyl-L-alanine.
A protein modification that effectively converts a glycine residue to N-methylglycine.
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].
A protein modification that effectively converts an L-methionine residue to N-methyl-L-methionine.
(2S)-2-methylamino-4-(methylsulfanyl)butanoic acid
2-methylamino-4-(methylthio)butanoic acid
A protein modification that effectively converts an L-phenylalanine residue to N-methyl-L-phenylalanine.
(2S)-2-methylamino-3-phenylpropanoic acid
A protein modification that effectively converts an L-proline residue to N,N-dimethyl-L-proline.
Unimod terminal specification corrected [JSG].
A protein modification that effectively converts an L-arginine residue to symmetric dimethylarginine, N(omega),N'(omega)-dimethyl-L-arginine.
(2S)-2-amino-5-[((methylamino)(methylimino)methyl)amino]pentanoic acid
omega-N,omega-N'-dimethylated L-arginine
A protein modification that effectively converts an L-arginine residue to asymmetric dimethylarginine, N(omega),N(omega)-dimethyl-L-arginine.
(2S)-2-amino-5-([(dimethylamino)(imino)methyl]amino)pentanoic acid
A protein modification that effectively converts an L-arginine residue to N(omega)-methyl-L-arginine.
(2S)-2-amino-5-[(imino(methylamino)methyl)amino]pentanoic acid
A protein modification that effectively converts an L-asparagine residue to N4-methyl-L-asparagine.
A protein modification that effectively converts an L-glutamine residue to N5-methyl-L-glutamine.
(2S)-2-amino-5-methylamino-5-oxopentanoic acid
A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-methyl ester.
(2S)-2-amino-5-methoxy-5-oxopentanoic acid
DeltaMass gives the formula "C 6 H 9 O 1 N 3" with mass 143 (formula incorrect, N and O reversed) [JSG].
A protein modification that effectively converts an L-histidine residue to pros-methyl-L-histidine (N-pi-methyl-L-histidine, 3'-methyl-L-histidine).
(2S)-2-amino-3-(3-methyl-3H-imidazol-4-yl)propanoic acid
A protein modification that effectively converts an L-lysine residue to N6,N6,N6-trimethyl-L-lysine.
2-amino-6-(trimethylammonio)hexanoic acid
DeltaMass calculates the mass difference from protonated lysine rather than neutral lysine; for trimethylated lysine starting from protonated lysine see MOD:00855
A protein modification that effectively converts an L-lysine residue to N6,N6-dimethyl-L-lysine.
(2S)-2-amino-6-(dimethylamino)hexanoic acid
A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine.
A protein modification that effectively converts an L-lysine residue to N6-palmitoyl-L-lysine.
(2S)-2-amino-6-(hexadecanoylamino)hexanoic acid
A protein modification that effectively converts an L-lysine residue to N6-myristoyl-L-lysine.
(2S)-2-amino-6-(tetradecanoylamino)hexanoic acid
2-amino-6-(tetradecanamido)hexanoic acid
A protein modification that effectively converts an L-threonine residue to O-palmitoyl-L-threonine.
(2S,3R)-2-amino-3-(hexadecanoyloxy)butanoic acid
A protein modification that effectively converts an L-serine residue to O-palmitoyl-L-serine.
(2S)-2-amino-3-(hexadecanoyloxy)propanoic acid
ACT_SITE O-palmitoyl serine intermediate
A protein modification that effectively converts an L-alanine residue to L-alanine amide.
A protein modification that effectively converts an L-arginine residue to L-arginine amide.
A protein modification that effectively converts an L-asparagine residue to L-asparagine amide.
A protein modification that effectively converts an L-aspartic acid residue to L-aspartic acid 1-amide.
A protein modification that effectively converts an L-cysteine residue to L-cysteine amide.
A protein modification that effectively converts an L-glutamine residue to L-glutamine amide.
A protein modification that effectively converts an L-glutamic acid residue to L-glutamic acid 1-amide.
A protein modification that effectively converts a glycine residue to glycine amide.
A protein modification that effectively converts an L-histidine residue to L-histidine amide.
A protein modification that effectively converts an L-isoleucine residue to L-isoleucine amide.
A protein modification that effectively converts an L-leucine residue to L-leucine amide.
A protein modification that effectively converts an L-lysine residue to L-lysine amide.
A protein modification that effectively converts an L-methionine residue to L-methionine amide.
A protein modification that effectively converts an L-phenylalanine residue to L-phenylalanine amide.
A protein modification that effectively converts an L-proline residue to L-proline amide.
A protein modification that effectively converts an L-serine residue to L-serine amide.
A protein modification that effectively converts an L-threonine residue to L-threonine amide.
A protein modification that effectively converts an L-tryptophan residue to L-tryptophan amide.
A protein modification that effectively converts an L-tyrosine residue to L-tyrosine amide.
A protein modification that effectively converts an L-valine residue to L-valine amide.
A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl disulfide.
(2R)-2-amino-3-(methyldisulfanediyl)propanoic acid
2-amino-3-(methyldisulfanediyl)propanoic acid
2-amino-3-methyldisulfanylpropanoic acid
2-azanyl-3-(methyldisulfanediyl)-propanoic acid
methyl methanethiolsulfonate derivatized cysteine
methyl methanethiosulfonate derivatized cysteine
Produced artifactually by reaction of cysteine residues with methyl methanethiosulfonate (MMTS) [JSG], but also naturally in bacteria [PMT].
A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine.
(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
From DeltaMass: (name misspelled "S-farnesyl cystenyl")
A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine.
(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
A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine.
2-amino-3-(3,7,11,15-tetramethyl-2,6,10,14-hexadecatetraenylthio)propanoic acid
DeltaMass calculates the mass with two double bonds rather than four
A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl ester.
2-amino-3-mercaptopropanoic methyl ester
2-amino-3-sulfanylpropanoic methyl ester
methyl (2R)-2-amino-3-sulfanylpropanoate
Secondary to RESID:AA0102; secondary to RESID:AA0103; secondary to RESID:AA0104.
A protein modification that effectively converts an L-cysteine residue to S-palmitoyl-L-cysteine.
(2R)-2-amino-3-(hexadecanoylsulfanyl)propanoic acid
2-amino-3-(hexadecanoylthio)propanoic acid
ACT_SITE S-palmitoyl cysteine intermediate
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
A protein modification that effectively converts an L-cysteine residue to S-diacylglycerol-L-cysteine.
(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
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.
(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-gamma-glutamyl (crosslinked to cysteine)
Cross-link 2; DeltaMass calculates the mass difference from glutamic acid rather than glutamine.
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.
(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
CROSSLNK 2'-(S-cysteinyl)-histidine (Cys-His)
S-(2-histidyl)- (crosslinked to cysteine)
A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form L-lanthionine.
(2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid)
(R,R)-2,6-diamino-4-thiaheptanedioic acid
(R,R)-3,3'-thiobis-(2-aminopropanoic acid)
2-amino-3-(2-amino-2-carboxyethyl)sulfanylpropanoic acid
Cross-link 2. The natural occurrence of this modification is rare. For the more common modification see MOD:00120 meso-lanthionine [JSG].
A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form meso-lanthionine.
(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
(2S)-2-amino-3-[[(2R)-2-amino-2-carboxyethyl]sulfanyl]propanoic acid
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.
(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,6R)-2,6-diamino-3-methyl-4-thiaheptanedioic acid
(2S-[2R*,3R*(S*)])-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid
CROSSLNK Beta-methyllanthionine (Cys-Thr)
CROSSLNK Beta-methyllanthionine (Thr-Cys)
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.
(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
CROSSLNK 3'-(S-cysteinyl)-tyrosine (Cys-Tyr)
CROSSLNK 3'-(S-cysteinyl)-tyrosine (Tyr-Cys)
A protein modification that effectively converts an L-lysine residue to N6-carboxy-L-lysine.
(2S)-2-amino-6-(carboxyamino)hexanoic acid
A protein modification that effectively converts an L-lysine residue to N6-1-carboxyethyl-L-lysine.
(2S)-2-amino-6-([(1S)-1-carboxyethyl]amino)hexanoic acid
A protein modification that effectively converts an L-lysine residue to hypusine, N6-(4-amino-2-hydroxybutyl)-L-lysine.
(2S)-2-amino-6-([(2R)-4-amino-2-hydroxybutyl]amino)hexanoic acid
(2S,9R)-2,11-diazanyl-9-hydroxy-7-azaundecanoic acid
2-azanyl-6-[(4-azanyl-2-hydroxybutyl)azanyl]hexanoic acid
This modification occurs uniquely in translation initiation factor eIF-5A [JSG].
A protein modification that effectively converts an L-lysine residue to N6-biotinyl-L-lysine.
(2S)-2-amino-6-(5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoylamino)hexanoic acid
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.
A protein modification that effectively converts an L-lysine residue to N6-lipoyl-L-lysine.
(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
A protein modification that effectively converts an L-lysine residue to N6-pyridoxal phosphate-L-lysine.
(2S)-2-amino-6-[([3-hydroxy-2-methyl-5-phosphonooxymethylpyridin-4-yl]methylidene)amino]hexanoic acid
Pyridoxal phosphate (Schiff Base formed to lysine)
A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine, the adduct of retinal.
(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
A protein modification that effectively converts an L-lysine residue to L-allysine.
Oxidation of lysine (to aminoadipic semialdehyde)
alpha-amino-adipic acid delta-semialdahyde
Lysine oxidation to aminoadipic semialdehyde
A protein modification that effectively converts an L-lysine residue to L-2-aminoadipic acid.
Oxidation of lysine (to aminoadipic acid)
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]
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.
(2S)-2-amino-6-([(2R)-2-amino-2-carboxyethyl]amino)hexanoic acid
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.
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.
(2S)-2-amino-6-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid
2-azanyl-6-([4-azanyl-4-carboxybutanoyl]azanyl)hexanoic acid
CROSSLNK Isoglutamyl lysine isopeptide (Lys-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.
(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-...)
Cross-link 2; this is the common crosslink structure formed by ubiquitin, SUMO, and similar proteins.
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.
(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)
A protein modification that effectively converts an L-cysteine residue to pyruvic acid.
A protein modification that effectively converts an L-phenylalanine residue into L-3-phenyllactic acid.
This modification is not the result of deamidation, instead the alpha amino group is replaced with an hydroxyl group.
A protein modification that effectively converts an L-threonine residue into 2-oxobutanoic acid.
A protein modification that effectively converts an L-tryptophan residue to N2-succinyl-L-tryptophan.
(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
Succinic anhydride labeling reagent light form (N-term)
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycocyanobilin.
(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
BINDING Phycocyanobilin chromophore (covalent; via 1 link)
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoerythrobilin.
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)
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phytochromobilin.
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)
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.
2,4-bis[1-(S-cysteinyl)ethyl]protoporphyrin IX
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.
4-[1-(S-cysteinyl)ethyl]protoporphyrin IX
A protein modification that effectively converts four L-cysteine residues iron atom to 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.
METAL Iron-sulfur (2Fe-2S); shared with dimeric partner
A protein modification that effectively converts six L-cysteine residues and a three-iron three-sulfur cluster to hexakis-L-cysteinyl triiron trisulfide.
Cross-link 6. This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
A protein modification that effectively converts three L-cysteine residues and a three-iron four-sulfur cluster to tris-L-cysteinyl triiron tetrasulfide.
mu3-sulfido tri-mu-sulfido tris-S-L-cysteinyl triiron
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.
METAL Iron-sulfur (4Fe-4S); shared with dimeric partner
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.
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
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 to L-cysteinyl molybdopterin.
(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
A protein modification that effectively converts an L-cysteine residue to S'-(8alpha-FAD)-L-cystine.
(2R)-2-amino-3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]sulfanylpropanoic acid
A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FAD)-L-histidine.
(2S)-2-amino-3-(3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid
A protein modification that effectively converts an L-tyrosine residue to O4'-(8alpha-FAD)-L-tyrosine.
(2S)-2-amino-3-(4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxyphenyl)propanoic acid
A protein modification that effectively converts an L-tyrosine residue to L-3',4'-dihydroxyphenylalanine.
(2S)-2-amino-3-(3,4-dihydroxyphenyl)propanoic acid
3,4-Dihydroxy-Phenylalanine (from Tyrosine) (DOPA)
incidental to RESID:AA0368 From DeltaMass: Average Mass: 16
A protein modification that effectively converts an L-tyrosine residue to an L-2',4',5'-topaquinone.
(2S)-2-amino-3-(5-hydroxy-2,5-cyclohexadien-1,4-dion-2-yl)propanoic acid
A protein modification that effectively converts an L-tryptophan residue to an L-tryptophan quinone.
(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
incidental to RESID:AA0149; incidental to RESID:AA0313; From DeltaMass: Average Mass: 30.
A protein modification that effectively cross-links two L-tryptophan residues by a carbon-carbon bond to form 4'-(L-tryptophan)-L-tryptophyl quinone.
2-amino-3-[2-[2-amino-3-(2-carboxyethyl)-6,7-dioxo-1H-indol-4-yl]-1H-indol-3-yl]propanoic acid
4-(L-tryptophan-2-yl)-L-tryptophyl quinone
CROSSLNK Tryptophan tryptophylquinone (Trp-Trp)
alpha,alpha'-diamino-6',7'-dihydro-6',7'-dioxo-(2,4'-bi-1H-indole)-3,3'-dipropanoic acid
Cross-link 2; secondary to RESID:AA0148; From DeltaMass: Average Mass: 28.
A protein modification that effectively converts an L-serine residue to O-phosphopantetheine-L-serine.
MOD_RES O-(pantetheine 4'-phosphoryl)serine
Unimod has DiffFormula C 11 H 20 N 2 O 6 P 1 S 1 From DeltaMass: Average Mass: 339
A protein modification that effectively converts an L-asparagine residue to an N4-glycosyl-L-asparagine.
A protein modification that effectively converts an L-cysteine residue to S-glucosylated L-cysteine.
(2R)-2-amino-3-[(beta-D-glucopyranosyl)sulfanyl]propanoic acid
A protein modification that effectively converts an L-lysine residue to O5-glucosylgalactosyl-L-hydroxylysine.
(2S,5R)-2,6-diamino-5-[2-O-(alpha-D-glucopyranosyl)-beta-D-galactopyranosyloxy]hexanoic acid
A protein modification that effectively converts an L-serine residue to O-(N-acetylaminogalactosyl)-L-serine.
(2S)-2-amino-3-(2-acetamido-2-deoxy-alpha-D-galactopyranosyloxy)propanoic acid
A protein modification that effectively converts an L-asparagine residue to O-(N-acetylaminogalactosyl)-L-threonine.
(2S,3R)-2-amino-3-(2-acetamido-2-deoxy-alpha-D-galactopyranosyloxy)butanoic acid
A protein modification that effectively converts an L-tryptophan residue to 1'-mannosyl-L-tryptophan.
(2S)-2-amino-3-(1-D-mannopyranosyloxy-1H-indol-3-yl)propanoic acid
A protein modification that effectively converts an L-tyrosine residue to O4'-glucosyl-tyrosine.
(2S)-2-amino-3-(4-alpha-D-glucopyranosyloxy)phenylpropanoic acid
A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylphosphatidylinositolethanolamine.
A protein modification that effectively converts an L-aspartic acid residue to N-(aspart-1-yl)-glycosylphosphatidylinositolethanolamine.
A protein modification that effectively converts an L-cysteine residue to N-cysteinyl-glycosylphosphatidylinositolethanolamine.
A protein modification that effectively converts a glycine residue to N-glycyl-glycosylphosphatidylinositolethanolamine.
A protein modification that effectively converts an L-serine residue to N-seryl-glycosylphosphatidylinositolethanolamine.
A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylphosphatidylinositolethanolamine.
A protein modification that effectively converts an L-threonine residue to N-threonyl-glycosylphosphatidylinositolethanolamine.
A protein modification that effectively converts a glycine residue to N-glycyl-glycosylsphingolipidinositolethanolamine.
A protein modification that effectively converts an L-serine residue to N-seryl-glycosylsphingolipidinositolethanolamine.
A protein modification that effectively converts an L-serine residue to O-(phosphoribosyl dephospho-coenzyme A)-L-serine.
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
A protein modification that effectively converts an L-argininine residue to omega-N-(ADP-ribosyl)-L-arginine.
(S)-2-amino-5-([imino([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)methyl]amino)pentanoic acid
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)
A protein modification that effectively converts an L-cysteine residue to S-(ADP-ribosyl)-L-cysteine.
(R)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]sulfanyl)propanoic acid
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)
A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-glycerylphosphorylethanolamine.
(S)-2-amino-5-[2-([([2,3-dihydroxypropyl]oxy)(hydroxy)phosphoryl]oxy)ethyl]amino-5-oxopentanoic acid
5-L-glutamyl glycerylphosphorylethanolamine
L-glutamyl 5-glycerophosphorylethanolamine
L-glutamyl 5-glycerylphosphorylethanolamine
MOD_RES 5-glutamyl glycerylphosphorylethanolamine
A protein modification that effectively converts an L-cysteine residue to S-sulfo-L-cysteine.
(2R)-2-amino-3-(sulfosulfanyl)propanoic acid
A protein modification that effectively converts an L-tyrosine residue to O4'-sulfo-L-tyrosine.
(S)-2-amino-3-(4-sulfooxyphenyl)propanoic acid
2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-sulfate
From DeltaMass: Average Mass: 80 Average Mass Change:80 PubMed:9624161.
A protein modification that effectively converts an L-histidine residue to L-bromohistidine.
A protein modification that effectively converts an L-phenylalanine residue to L-2'-bromophenylalanine.
(S)-2-amino-3-(2-bromophenyl)propanoic acid
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.
A protein modification that effectively converts an L-phenylalanine residue to L-3'-bromophenylalanine.
(S)-2-amino-3-(3-bromophenyl)propanoic acid
A protein modification that effectively converts an L-phenylalanine residue to L-4'-bromophenylalanine.
(2S)-2-amino-3-(4-bromophenyl)propanoic acid
A protein modification that effectively substitutes an L-tyrosine residue with 3,3',5-triiodo-L-thyronine.
(S)-2-amino-3-[4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl]propanoic acid
A protein modification that effectively substitutes an L-tyrosine residue with L-thyroxine.
(S)-2-amino-3-[4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodophenyl]propanoic acid
A protein modification that effectively converts an L-tryptophan residue to 6'-bromo-L-tryptophan.
(2S)-2-amino-3-(6-bromo-1H-indol-3-yl)propanoic acid
A protein modification that effectively converts an L-serine residue to dehydroalanine.
4-methylidene-imidazole-5-one (MIO) active site
A protein modification that effectively converts an L-threonine residue to dehydrobutyrine.
A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine.
(2Z)-2-amino-3-(4-hydroxyphenyl)prop-2-enoic acid
amino-(para-hydroxybenzylidenyl)acetic acid
para-hydroxybenzylidene-imidazolidinone chromophore
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
A protein modification that effectively crosslinks an L-serine residue and a glycine residue to form L-serine 5-imidazolinone glycine.
(2-[(1R)-1-amino-2-hydroxyethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365.
A protein modification that effectively converts an L-cysteine residue to L-oxoalanine.
A protein modification that effectively converts an L-serine residue to an amino-terminal lactic acid.
A protein modification that effectively crosslinks an L-alanine residue and a glycine residue to form L-alanine 5-imidazolinone glycine.
(2-[(1S)-1-aminoethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
4-methylidene-imidazole-5-one active site
Cross-link 2; carboxamidine; incidental to RESID:AA0181; incidental to RESID:AA0183; incidental to RESID:AA0365.
A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form L-cysteine 5-imidazolinone glycine.
(2-[(1R)-1-amino-2-sulfanylethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
A protein modification that effectively crosslinks an L-glutamine residue and a glycine residue to form 2-imino-glutamine 5-imidazolinone glycine.
2,N-didehydroglutaminyl-5-imidazolinone glycine
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
A protein modification that effectively converts an L-alanine residue to D-alanine.
A protein modification that effectively converts an L-isoleucine residue to a D-allo-isoleucine.
A protein modification that effectively converts an L-methionine residue to D-methionine.
(2R)-2-amino-4-(methylsulfanyl)butanoic acid
A protein modification that effectively converts an L-phenylalanine residue to D-phenylalanine.
A protein modification that effectively converts an L-serine residue to D-serine.
A protein modification that effectively converts an L-asparagine residue to D-asparagine.
A protein modification that effectively converts an L-leucine residue to D-leucine.
A protein modification that effectively converts an L-tryptophan residue to D-tryptophan.
(R)-2-amino-3-(1H-indol-3-yl)propanoic acid
A protein modification that effectively converts an L-glutamic acid residue to L-isoglutamyl-polyglycine.
A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl-polyglutamic acid, forming an isopeptide bond with a polyglutamic 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.
(2S)-2-amino-3-[4-(5'-adenosine phosphonoxy)phenyl]propanoic acid
O4'-L-tyrosine 5'-adenosine phosphodiester
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.
(2S)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid
CROSSLNK S-(2-aminovinyl)-D-cysteine (Ser-Cys)
A protein modification that effectively monooxygenates an L-cysteine residue to L-cysteine sulfenic acid.
(2R)-2-amino-3-(hydroxysulfanyl)propanoic acid
(2R)-2-amino-3-(oxido-lambda(4)-sulfanyl)propanoic acid [tautomer]
2-amino-3-sulfinylpropanoic acid [tautomer]
ACT_SITE Cysteine sulfenic acid (-SOH) intermediate
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).
A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a thioester bond to form S-glycyl-L-cysteine.
(2R)-2-amino-3-[(aminoacetyl)sulfanyl]propanoic acid
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].
A protein modification that effectively converts an L-cysteine residue to S-4-hydroxycinnamyl-L-cysteine.
(2R)-2-amino-3-([(2E)-3-(4-hydroxyphenyl)prop-2-enoyl]sulfanyl)propanoic acid
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.
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.
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.
heparan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine
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.
(2S)-2-amino-6-(formylamino)hexanoic acid
A protein modification that effectively converts an L-proline residue to O4-arabinosyl-L-hydroxyproline.
(2S,4R)-4-(beta-L-arabinofuranosyloxy)pyrrolidine-2-carboxylic acid
4-Glycosyloxy- (pentosyl,C5) (of Proline)
secondary to RESID:AA0030; From DeltaMass: Average Mass: 147.
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)-2-amino-3-(5'-ribonucleic acid phosphonoxy)propanoic acid
A protein modification that effectively converts an L-arginine residue to L-citrulline.
(S)-2-amino-5-(carbamoylamino)pentanoic acid
2-amino-5-(aminocarbonyl)aminopentanoic acid
This modification is not the result of deamidation, instead the guanidino group is replaced with an ureido group.
A protein modification that effectively converts an L-arginine residue to a 4-hydroxy-L-arginine.
(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
A protein modification that effectively crosslinks L-aspartic acid and L-cysteine residues via an isopeptide bond to form N-(L-isoaspartyl)-L-cysteine.
(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)
A protein modification that effectively converts an L-tryptophan residue to 2'-alpha-mannosyl-L-tryptophan.
(2S)-2-amino-3-(2-beta-D-mannopyranosyl-1H-indol-3-yl)propanoic acid
A protein modification that effectively converts an L-lysine residue to N6-mureinyl-L-lysine.
A protein modification that effectively converts an L-aspartic acid residue to 1-chondroitin sulfate-L-aspartic acid ester
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.
(R)-2-amino-3-[6-riboflavin 5'-dihydrogen phosphate]sulfanylpropanoic acid
A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FAD)-L-histidine.
(S)-2-amino-3-(1-[8alpha riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid
N theta and N pi-(8alpha-Flavin) (on Histidine)
A protein modification that effectively converts an L-arginine residue to omega-N-phospho-L-arginine.
(2S)-2-amino-5-(N'-phosphonocarbamimidamido)pentanoic acid
(2S)-2-amino-5-([amino(phosphonoamino)methylidene]amino)pentanoic acid
alpha-amino-delta-phosphonoguanidinovaleric acid
A protein modification that effectively converts an L-cysteine residue to S-diphytanylglycerol diether-L-cysteine.
(2R)-2-amino-3-([(2S)-2,3-bis(3,7,11,15-tetramethylhexadecanyloxy)propyl]sulfanyl)propanoic acid
A protein modification that effectively converts two L-cysteine residues to form alpha-1-microglobulin-Ig alpha complex chromophore.
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.
METAL Iron-sulfur (2Fe-2S); via pros nitrogen
bis-L-cysteinyl bis-L-histidino diiron disulfide
A protein modification that effectively converts six L-cysteine residues and a six-iron six-sulfur cluster to hexakis-L-cysteinyl hexairon hexasulfide.
hexakis-L-cysteinyl hexairon hexasulfide
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.
(2S)-2-amino-6-(5'-adenosine phosphonamino)hexanoic acid
L-lysine monoanhydride with 5'-adenylic acid
N6-L-lysine 5'-adenosine phosphoramidester
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.
(2S)-2-amino-6-(5'-guanosine phosphonamino)hexanoic acid
L-lysine monoanhydride with 5'-guanylic acid
N6-L-lysine 5'-guanosine phosphoramidester
From DeltaMass: Average Mass: 345 Formula:C10H12O5N7P1 Monoisotopic Mass Change:345.047 Average Mass Change:345.209 References:PE Sciex
A protein modification that effectively converts an L-cysteine residue to S-glutathionyl-L-cysteine.
(2S)-2-amino-3-((2S)-2-((4R)-4-amino-4-carboxyl-1-oxobutyl)amino-3-(carboxylmethyl)amino-3-oxo-propyl)dithio-propanoic acid
L-gamma-glutamyl-L-cysteinyl-glycine (2-1')-disulfide with L-cysteine
Glutamyl-transpeptidase cleaves glutathione into cysteinylglycine (Cys-Gly) and a Glu residue. [PubMed: 28537416]
A protein modification that effectively converts an L-cysteine residue to S-nitrosyl-L-cysteine.
(2R)-2-amino-3-nitrososulfanyl-propanoic acid
A protein modification that effectively converts an L-asparagine residue to N4-(ADP-ribosyl)-L-asparagine.
(S)-2-amino-4-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)-4-oxobutanoic acid
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)
A protein modification that effectively converts an L-aspartic acid residue to L-beta-methylthioaspartic acid.
(2R,3Xi)-2-amino-3-(methylsulfanyl)butanedioic acid
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.
CROSSLNK Lysine tyrosylquinone (Lys-Tyr)
CROSSLNK Lysine tyrosylquinone (Tyr-Lys)
Cross-link 2; secondary to RESID:AA0147.
A protein modification that effectively converts an L-cysteine residue to S-methyl-L-cysteine.
(R)-2-amino-3-(methylsulfanyl)propanoic acid
A protein modification that effectively converts an L-lysine residue to 4-hydroxy-L-lysine.
(2S,4R)-2,6-diamino-4-hydroxyhexanoic acid
alpha,epsilon-diamino-gamma-hydroxycaproic acid
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].
A protein modification that effectively converts an L-asparagine residue to N4-hydroxymethyl-L-asparagine.
(2S)-2-amino-4-[(hydroxymethyl)amino]-4-oxobutanoic acid
2-amino-N4-hydroxymethylbutanediamic acid
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].
A protein modification that effectively converts an L-serine residue to O-(ADP-ribosyl)-L-serine.
(S)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]oxy)-propanoic acid
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)
A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid.
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)
A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazoline-4-carboxylic acid.
(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)
A protein modification that effectively crosslinks a glycine residue and an L-serine residue to form glycine oxazole-4-carboxylic acid.
2-aminomethyl-1,3-oxazole-4-carboxylic acid
2-azanylmethyl-1,3-oxazole-4-carboxylic acid
CROSSLNK Oxazole-4-carboxylic acid (Gly-Ser)
A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form glycine thiazole-4-carboxylic acid.
2-(aminomethyl)-1,3-thiazole-4-carboxylic acid
2-(azanylmethyl)-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Gly-Cys)
A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-serine thiazole-4-carboxylic acid.
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)
A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazole-4-carboxylic acid.
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.
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)
A protein modification that effectively crosslinks an L-cysteine residue and an L-lysine residue to form L-lysine thiazole-4-carboxylic acid.
2-[(1S)-1,5-diaminopentyl]-1,3-thiazole-4-carboxylic acid
2-[1,5-bis(azanyl)pentyl]-1,3-thiazole-4-carboxylic acid
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].
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)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)propanoic acid
ACT_SITE O-(5'-phospho-DNA)-serine intermediate
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.
keratan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-threonine
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).
L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) (Sec)
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.
(S)-2-amino-3-[4-(5'-ribonucleic acid phosphonoxy)phenyl]propanoic acid
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.
(2S,3R)-2-amino-3-(5-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl)-3-(4-hydroxyphenyl)propanoic acid
CROSSLNK 3'-histidyl-3-tyrosine (His-Tyr)
A protein modification that dioxygenates an L-methionine residue to L-methionine sulfone.
(2S)-2-amino-4-(methylsulfonyl)butanoic acid
DeltaMass gives the formula C 5 H 9 N 3 O 1 S 1 with mass 163
A protein modification that effectively converts an L-cysteine residue to dipyrrolylmethanemethyl-L-cysteine.
(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
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.
(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)
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.
(S)-2-amino-3-[4-(5'-deoxyribonucleic acid phosphonoxy)phenyl]propanoic acid
ACT_SITE O-(5'-phospho-DNA)-tyrosine intermediate
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.
(S)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)butanoic acid
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.
(S)-2-amino-3-[4-(5'-uridine phosphonoxy)phenyl]propanoic acid
O4'-L-tyrosine 5'-uridine phosphodiester
A protein modification that effectively forms a peptide bond between a C-terminal L-glutamic acid residue and a free L-tyrosine.
(S,S)-2-(2-aminopentanedio-1-yl)amino-3-(4-hydoxyphenyl)propanoic acid
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoviolobilin.
BINDING Phycoviolobilin chromophore (covalent; via 1 link)
A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycoerythrobilin.
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)
A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycourobilin.
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
BINDING Phycourobilin chromophore (covalent; via 2 links)
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.
A protein modification that effectively dioxygenates an L-cysteine residue to L-cysteine sulfinic acid.
2-amino-3-(dioxido-lambda(6)-sulfanyl)propanoic acid [tautomer]
2-amino-3-sulfonylpropanoic acid [tautomer]
A protein modification that effectively converts an L-tyrosine residue to L-3',4',5'-trihydroxyphenylalanine.
(S)-2-amino-3-(3,4,5-trihydroxyphenyl)propanoic acid
3,4,6-Trihydroxy-Phenylalanine (from Tyrosine) (TOPA)
MOD_RES 3',4',5'-trihydroxyphenylalanine
A protein modification that effectively converts an L-serine residue to O-(sn-1-glycerophosphoryl)-L-serine.
(2S)-2-amino-3-[(2Xi)-2,3-dihydroxypropyl]phosphonoxypropanoic acid
MOD_RES O-(sn-1-glycerophosphoryl)serine
O3-2,3-dihydroxypropyl hydrogen phosphate-L-serine ester
A protein modification that effectively converts a glycine residue to an internal 1-thioglycine.
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).
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.
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.
(2S,3R)-2-amino-3-(5'-adenosine phosphonoxy)butanoic acid
L-threonine monoanhydride with 5'-adenylic acid
O3-L-threonine 5'-adenosine phosphodiester
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.
METAL Iron-oxo-sulfur (4Fe-2O-2S); via persulfide group
METAL Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogen
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
Cross-link 7; secondary to RESID:AA0269.
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.
ACT_SITE Cysteine persulfide intermediate
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.
(2S)-2-amino-3-[1-(5-[(2S)-2-amino-2-carboxyethyl]-2-hydroxyphenyl)-1H-imidazol-4-yl]propanoic acid
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.
A protein modification that effectively converts an L-arginine residue to 5-methyl-L-arginine.
(2S,5S)-2-amino-5-carbamimidamidohexanoic acid
A protein modification that effectively converts an L-glutamine residue to 2-methyl-L-glutamine.
A protein modification that effectively converts an L-cysteine residue to N-pyruvic acid 2-iminyl-L-cysteine.
(R)-2-(1-carboxy-2-sulfanylethanimino)propanoic acid
A protein modification that effectively converts an L-valine residue to N-pyruvic acid 2-iminyl-L-valine.
(S)-2-(1-carboxy-2-methylpropanimino)propanoic acid
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.
2-[1-(N3'-histidyl)ethyl]protoporphyrin IX
BINDING Heme (covalent; via pros nitrogen)
A protein modification that effectively converts an L-cysteine residue to S-selenyl-L-cysteine.
(R)-2-amino-3-(selanylsulfanyl)propanoic acid
2-amino-3-hydroselenosulfidopropanoic acid
2-amino-3-hydroselenylsulfidopropanoic acid
2-amino-3-hydroselenylthiopropanoic acid
A protein modification that effectively converts an L-lysine residue to an N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine.
(alpha)- ([([(5S)-5-amino-5-carboxypentyl]amino)propyl][(methyl)amino])-(omega)-methyl poly[propane-1,3-diyl(methylimino)]
MOD_RES N6-poly(methylaminopropyl)lysine
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.
1,5-bishydroxymethyl protoporphyrin IX 1-glutamate ester 5-aspartate ester
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, 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.
1,5-bishydroxymethyl protoporphyrin IX 1-glutamate ester 5-aspartate ester 2-methionine sulfonium
dihydroxyheme-L-aspartate ester-L-glutamate ester-L-methionine sulfonium
A protein modification that effectively converts an L-cysteine residue to L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide).
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
molybdenum bis(molybdopterin guanine dinucleotide)
A protein modification that effectively converts an L-proline residue to a (2S,3R,4S)-3,4-dihydroxyproline.
(2S,3R,4S)-3,4-dihydroxypyrrolidine-2-carboxylic acid
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.
2,4,6-tricarboxylic-pyrrolo[2,3-5,6]quinoline 8,9-quinone
4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-5,6]quinoline-2,7,9-tricarboxylic acid
CROSSLNK Pyrroloquinoline quinone (Glu-Tyr)
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.
METAL Iron-sulfur (4Fe-4S); via tele nitrogen
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.
METAL Iron-sulfur (4Fe-4S); via pros nitrogen
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.
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.
(2S)-2-amino-6-([1-carboxyethylidene]amino)hexanoic acid
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.
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.
bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide
A protein modification that effectively converts an L-serine residue to O-octanoyl-L-serine.
(2S)-2-amino-3-(octanoyloxy)propanoic acid
A protein modification that effectively converts an L-serine residue to O-D-glucuronosyl-L-serine.
(2S)-2-amino-3-(beta-D-glucopyranuronosyl)propanoic acid
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.
carbon monoxide dehydrogenase nickel-iron cofactor
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
Cross-link 7; secondary to RESID:AA0269. This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
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.
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.
(2S)-2-amino-6-([(3S)-3-amino-3-carboxypropanoyl]amino)hexanoic acid
CROSSLNK Isoaspartyl lysine isopeptide (Lys-Asn)
A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl-5-poly(ADP-ribose).
(S)-2-amino-5-poly[2'-adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with 1alpha-D-ribofuranosyl]oxy-5-oxopentanoic acid
O-ADP-ribosylation (on Glutamate or C terminus)
A protein modification that effectively converts an L-serine residue to O-(N-acetylglucosamine-1-phosphoryl)-L-serine.
(2S)-2-amino-3-[([(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)oxy][hydroxy]phosphoryl)oxy]propanoic acid
O3-L-serine 2-(acetylamino)-2-deoxy-D-glucopyranose 1-phosphodiester
A protein modification that effectively converts an L-serine residue to O-(phosphoglycosyl-D-mannose-1-phosphoryl)-L-serine.
O3-L-serine alpha-D-mannopyranose 1-phosphodiester
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.
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.
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.
hexakis-L-cysteinyl L-serinyl octairon heptasulfide
Cross-link 7; incidental to RESID:AA0141.
Natural or modified residues with a mass of 113.084064 Da.
A protein modification that effectively cyclizes an L-asparagine residue to form a carboxyl-terminal L-aspartimide.
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.
A protein modification that effectively cyclizes an L-glutamine residue to form a carboxyl-terminal L-glutamimide.
A protein modification that effectively converts an L-aspartic acid residue to L-beta-carboxyaspartic acid.
(2S)-2-aminoethane-1,1,2-tricarboxylic acid
References to this modification as a gamma-carboxylation are in error [JSG].
A protein modification that effectively converts an L-arginine residue to N5-methyl-L-arginine.
(2S)-2-amino-5-(N-methylcarbamimidamido)pentanoic acid
A protein modification that effectively converts an L-cysteine residue to L-cysteine coenzyme A disulfide.
(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)
DeltaMass gives no formula with mass as 454.
A protein modification that effectively converts an L-cysteine residue to S-myristoyl-L-cysteine.
(R)-2-amino-3-(tetradecanoylsulfanyl)propanoic acid
A protein modification that effectively converts an L-cysteine residue to S-palmitoleyl-L-cysteine.
(R)-2-amino-3-((Z)-9-hexadecenoylsulfanyl)propanoic acid
A protein modification that effectively converts a glycine residue to glycine cholesterol ester.
Incidental to RESID:AA0060. Unimod origin corrected [JSG].
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.
METAL Nickel-iron-sulfur (Ni-4Fe-5S); via tele nitrogen
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.
(2S)-2-amino-4-(dimethylamino)-4-oxobutanoic acid
A protein modification that effectively converts an L-lysine residue to N6-3,4-didehydroretinylidene-L-lysine.
(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
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.
(2R)-2-amino-3-[(3-[(2S)-2-amino-2-carboxyethyl]-6,7-dioxo-6,7-dihydro-1H-indol-4-yl)sulfanyl]propanoic acid
4'-(L-cystein-S-yl)-L-tryptophyl quinone
CROSSLNK 4'-cysteinyl-tryptophylquinone (Cys-Trp)
Cross-link 2; secondary to RESID:AA0148.
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.
(2R,3S)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)butanedioic acid
(2R,3S,6R)-2,6-diamino-3-carboxy-4-thiaheptanedioic acid
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.
(2S,3S,7R)-2,7-diamino-4-carboxy-5-thiaoctanedioic acid
(2S,4S)-2-amino-4-[(R)-2-amino-2-carboxyethyl]sulfanylpentanedioic 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.
(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
cis-14-hydroxy-10,13-dioxo-7-heptadecenoic ester
A protein modification that effectively converts an L-histidine residue to tele-methyl-L-histidine.
(S)-2-amino-3-(1-methyl-1H-imidazol-4-yl)propanoic acid
A protein modification that effectively converts an L-lysine residue to L-lysine methyl ester.
alpha,epsilon-diaminocaproic methyl ester
A protein modification that effectively converts an L-serine residue to L-serinyl molybdenum bis(molybdopterin guanine 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.
(2R,3Xi)-2-amino-3-(methylsulfanyl)-4-butanediamic acid
2,4-diamino-3-(methylsulfanyl)-4-oxobutanoic acid
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].
A protein modification that effectively converts an L-lysine residue to L-pyrrolysine (not known as a natural, post-translational modification process).
(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
monomethylamine methyltransferase cofactor lysine adduct
This entry is for the artifactual formation of L-pyrrolysine from lysine. For encoded L-pyrrolysine, use MOD:01187 [JSG].
A protein modification that effectively converts an L-tryptophan residue to a 3-hydroxy-L-tryptophan.
(2S,3S)-2-amino-3-hydroxy-3-(1H-indol-3-yl)propanoic acid
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.
(S)-2-amino-3-[4-(3'-deoxyribonucleic acid phosphonoxy)phenyl]propanoic acid
ACT_SITE O-(3'-phospho-DNA)-tyrosine intermediate
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.
5-hydroxymethyl protoporphyrin IX 5-glutamate ester
cytochrome P450 CYP4A family heme cofactor
A protein modification that effectively converts an L-histidine residue to a (phospho-5'-guanosine)-L-histidine.
(2S)-2-amino-3-(1-(5'-adenosine phosphono)imidazol-4-yl)propanoic acid
L-histidine 5'-guanosine phosphoramidester
L-histidine monoanhydride with 5'-guanylic acid
A protein modification that effectively converts four L-cysteine residues and a three-iron four-sulfur cluster to tetrakis-L-cysteinyl triiron tetrasulfide.
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.
(2S)-2-amino-5-(beta-D-glucopyranosyl[imino(methylamino)methyl]amino)pentanoic acid
A protein modification that effectively converts an L-asparagine residue to (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine.
MOD_RES Aspartic acid 1-[(3-aminopropyl)(5'-adenosyl)phosphono]amide
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.
2-[1-(N1'-histidyl)ethyl]protoporphyrin IX
BINDING Heme (covalent; via tele nitrogen)
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.
(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
CROSSLNK Beta-methyllanthionine sulfoxide (Thr-Cys)
(2S,3S,2'R)-3-methyllanthionine sulfoxide
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.
tris-L-cysteinyl L-aspartato diiron disulfide
A protein modification that effectively converts an L-cysteine residue to S-carbamoyl-L-cysteine.
(R)-2-amino-3-(carbamoylsulfanyl)propanoic acid
2-amino-3-(aminocarbonyl)sulfanylpropanoic acid
2-amino-3-(aminocarbonyl)thiopropanoic acid
alpha-amino-beta-carbamylthiopropionic acid
A protein modification that effectively converts an L-cysteine residue to S-cyano-L-cysteine.
(2R)-2-amino-3-thiocyanatopropanoic acid
alpha-amino-beta-thiocyanatopropionic acid
A protein modification that effectively converts an L-cysteine residue to L-cysteinyl hydrogenase diiron subcluster.
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
A protein modification that effectively converts an L-cysteine residue to S-amidino-L-cysteine.
(2R)-2-amino-3-(carbamimidoylsulfanyl)propanoic acid
alpha-amino-beta-amidinothiopropionic acid
A protein modification that effectively converts an L-isoleucine residue to N-methyl-L-isoleucine.
(2S,3S)-2-methylamino-3-methylpentanoic acid
A protein modification that effectively converts an L-leucine residue to N-methyl-L-leucine.
(S)-2-methylamino-4-methylpentanoic acid
A protein modification that effectively converts an L-tyrosine residue to N-methyl-L-tyrosine.
(2S)-3-(4-hydroxyphenyl)-2-(methylamino)propanoic acid
A protein modification that effectively converts a glycine residue to N-palmitoylglycine.
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.
(2R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylpropanoic acid
(2R,5R)-2,5-diamino-3-thia-2-phenylmethylhexanedioic acid
CROSSLNK 2-cysteinyl-L-phenylalanine (Cys-Phe)
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.
(2S)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylpropanoic acid
(2S,5R)-2,5-diamino-3-thia-2-phenylmethylhexanedioic acid
CROSSLNK 2-cysteinyl-D-phenylalanine (Cys-Phe)
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.
(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
CROSSLNK 2-cysteinyl-D-allo-threonine (Cys-Thr)
A protein modification that effectively converts an L-alanine residue to N-carbamoyl-L-alanine.
A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form 4-amino-3-isothiazolidinone-L-serine.
(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
CROSSLNK N,N-(cysteine-1,S-diyl)serine (Cys-Ser)
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.
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.
LIPID Phosphatidylethanolamine amidated glycine
A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-omega-hydroxyceramide ester.
(S)-2-amino-5-[30-((2S,3R,4E)-1,3-dihydroxyicos-4-en-2-ylamino)-30-oxotriacontan-1-yloxy]-5-oxopentanoic acid
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.
A protein modification that effectively converts an L-threonine residue to O-(riboflavin phosphoryl)-L-threonine.
(2S,3R)-2-amino-3-(riboflavin 5'-hydrogen phosphonoxy)butanoic acid
A protein modification that effectively converts an L-serine residue to O-(riboflavin phosphoryl)-L-serine.
(R)-2-amino-3-(riboflavin 5'-hydrogen phosphonoxy)propanoic acid
A protein modification that effectively converts an L-cysteine residue to S-(4a-FMN)-L-cysteine.
(R)-2-amino-3-(4a-riboflavin 5'-dihydrogen phosphate)sulfanylpropanoic acid
A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FMN)-L-histidine.
(S)-2-amino-3-(1-[8alpha riboflavin 5'-dihydrogen phosphate]imidazol-4-yl)propanoic acid
A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FMN)-L-histidine.
(S)-2-amino-3-(3-[8alpha riboflavin 5'-dihydrogen phosphate]imidazol-4-yl)propanoic acid
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].
A protein modification that effectively converts an L-arginine residue to N2-acetyl-L-arginine.
(S)-2-acetamido-5-carbamimidamidopentanoic acid
alpha-acetylamino-delta-guanidinovaleric acid
A protein modification that effectively converts an L-cysteine residue to L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide.
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
copper sulfido molybdopterin cytosine dinuncleotide
L-cysteinyl 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.
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.
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.
(R,R)-2-amino-3-[3-(2-aminopropanoic acid)sulfanyl]selanylpropanoic acid
CROSSLNK Cysteinyl-selenocysteine (Cys-Sec)
CROSSLNK Cysteinyl-selenocysteine (Sec-Cys)
A protein modification that effectively converts an L-lysine residue to 5-hydroxy-N6,N6,N6-trimethyl-L-lysine.
5-hydroxy-N6,N6,N6-trimethyllysine cation
5-hydroxylated N6,N6,N6-trimethylated L-lysine
MOD_RES N6,N6,N6-trimethyl-5-hydroxylysine
alpha-amino-epsilon-dimethylamino-delta-hydroxycaproic acid
Incidental to RESID:AA0278; secondary to RESID:AA0028; secondary to RESID:AA0074.
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.
(S)-2-amino-5-(carboxymethyl)amino-5-oxopentanoic acid
2-amino-N5-(carboxymethyl)-pentanediamic acid
CROSSLNK Isoglutamyl glycine isopeptide (Gly-Glu)
A protein modification that effectively converts an L-serine residue to O-sulfo-L-serine.
2-amino-3-hydroxypropanoic acid 3-sulfate
A protein modification that effectively converts an L-threonine residue to O-sulfo-L-threonine.
(2S,3R)-2-amino-3-(sulfooxy)butanoic acid
2-amino-3-hydroxybutanoic acid 3-sulfate
A protein modification that effectively converts an L-methionine residue to N-carboxy-L-methionine.
(S)-2-carboxyamino-4-(methylsulfanyl)butanoic acid
2-carbamic-4-(methylsulfanyl)butanoic acid
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].
A protein modification that effectively converts an L-serine residue to O-acetyl-L-serine.
(2S)-3-(acetyloxy)-2-aminopropanoic acid
A protein modification that effectively converts an L-tyrosine residue to (E)-2,3-didehydrotyrosine.
(2E)-2-amino-3-(4-hydroxyphenyl)prop-2-enoic acid
blue non-fluorescent pocilloporin chromophore
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.
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
A protein modification that effectively cross-links two L-tyrosine residues with a carbon-carbon bond to form 3'-(3'-L-tyrosinyl)-L-tyrosine.
(2S,2'S)-3,3'-(6,6'-dihydroxybiphenyl-3,3'-diyl)bis(2-aminopropanoic acid)
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
Cross-link 2; From DeltaMass: Average Mass: -2.
A protein modification that effectively cross-links L-tyrosine residues with an ether bond to form 3'-(O4'-L-tyrosinyl)-L-tyrosine.
(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
Cross-link 2; secondary to RESID:AA0146; From DeltaMass: Average Mass: -2.
A protein modification that effectively converts an L-arginine residue to 3,4-dihydroxy-L-arginine.
(2S,3Xi,4Xi)-2-amino-5-carbamimidamido-3,4-dihydroxypentanoic acid
2-amino-5-guanidino-3,4-dihydroxypentanoic acid
A protein modification that effectively converts an L-lysine residue to 4,5-dihydroxy-L-lysine.
(2S,4Xi,5Xi)-2,6-diamino-4,5-dihydroxyhexanoic acid
alpha,epsilon-diamino-delta,gamma-dihydroxycaproic acid
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.
(2S)-2-amino-3-[1-(5'-adenosine phosphono)imidazol-4-yl]propanoic acid
ACT_SITE Tele-AMP-histidine intermediate
L-histidine 5'-adenosine phosphoramidester
L-histidine monoanhydride with 5'-adenylic acid
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.
(S)-2-amino-3-[1-(5'-uridine phosphono)imidazol-4-yl]propanoic acid
ACT_SITE Tele-UMP-histidine intermediate
L-histidine 5'-uridine phosphoramidester
L-histidine monoanhydride with 5'-uridylic acid
A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl semialdehyde.
A protein modification that effectively converts an L-serine residue to L-serine microcin E492 siderophore ester.
L-serine microcin E492 siderophore ester
MOD_RES Serine microcin E492 siderophore ester
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).
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
A protein modification that effectively converts an L-selenocysteine residue to L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide).
L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide) (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.
GFP-like chromoprotein asFP595 chromophore
carboxamidine; cross-link 1. This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue to form 2-imino-glutamic acid 5-imidazolinone glycine.
2,N-didehydroglutamyl-5-imidazolinone glycine
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
Cross-link 2; carboxamidine; cross-link 1; incidental to RESID:AA0183; incidental to RESID:AA0365.
A protein modification that effectively crosslinks an L-methionine residue and a glycine residue to form 2-imino-methionine 5-imidazolinone glycine.
(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-imino-methionine 5-imidazolinone glycine
2-imino-methionyl-5-imidazolinone glycine
CROSSLNK 2-iminomethyl-5-imidazolinone (Met-Gly)
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.
(2-[(1S)-1,3-diamino-3-oxopropyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
Zoanthus sp. fluorescent protein FP506 chromophore
[2-(1,3-diamino-3-oxopropyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form L-lysine 5-imidazolinone glycine.
(2-[(1S)-1,5-diaminopentyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
Anemonia majano fluorescent protein FP486 chromophore
[2-(1,5-diaminopentanyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form 2-tetrahydropyridinyl-5-imidazolinone glycine.
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
A protein modification that effectively attaches an L-alanine residue to murein peptidoglycan by a pentaglycine linker peptide.
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.
(2S)-1-formylpyrrolidine-2-carboxylic acid
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].
A protein modification that effectively converts an L-serine residue to O-decanoyl-L-serine.
(2S)-2-amino-3-(decanoyloxy)propanoic acid
A protein modification that effectively converts an L-threonine residue to O-octanoyl-L-threonine.
(2S)-2-amino-3-(octanoyloxy)butanoic acid
A protein modification that effectively converts an L-threonine residue to O-decanoyl-L-threonine.
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.
A protein modification that effectively replaces one hydrogen atom with one acetyl group.
Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac)
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
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.
A protein modification that effectively replaces a residue hydrogen atom on an oxygen with a carbohydrate-like group through a glycosidic bond.
A protein modification that is produced by reaction with iodoacetamide, usually replacement of a reactive hydrogen with a methylcarboxamido group.
A protein modification that effectively replaces a hydrogen atom with a carbamoyl (carboxamido) group. Replacement of an amino hydrogen produces a ureido group.
This modification can be produced by hydrogen cyanate, either used as a reagent or as released by urea degradation in solution [JSG].
A protein modification that is produced by reaction with iodoacetic acid, usually replacement of a reactive hydrogen with a methylcarboxy group.
From DeltaMass: Average Mass: 58 Abbreviation:CmC Average Mass Change:58 Notes:Cysteine reacts with iodoacetic acid to produce carboxymethyl cysteine.
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.
Deamidation of Asparagine and Glutamine to Aspartate and Glutamate
A protein modification that is produced by formation of an adduct of a cysteine residue with the Gygi isotope-coded affinity tag d0 reagent.
A protein modification that is produced by formation of an adduct of a cysteine residue with the Gygi isotope-coded affinity tag d8 reagent.
A protein modification that effectively converts an L-methionine residue to homoserine.
Homoserine formed from Met by CNBr treatment
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.
A protein modification that effectively converts an L-methionine residue to homoserine lactone.
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.
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.
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 d0 reagent.
Applied Biosystems original ICAT(TM) d0 modified cysteine
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.
A protein modification that effectively replaces a residue amino or imino hydrogen with an acetyl group.
A protein modification that effectively replaces a residue amino group with a formamido group.
A protein modification that effectively converts an L-cysteine residue to S-(N-isopropylcarboxamidomethyl)-L-cysteine.
modification from Unimod Isotopic label. OBSOLETE because Unimod:18 is now merged with entry 258 remap to MOD:00581 'single 018 label'
modification from Unimod artifact. OBSOLETE because Unimod entry 19 is now merged with Unimod 35 remap to MOD:00425 'monohydroxylated residue'.
A protein modification that is produced by reaction of a cysteine residue with biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine.
biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine derivatized cysteine
A protein modification that effectively replaces one hydrogen atom of an L-arginine residue with one methyl group.
From DeltaMass: formula incorrect, N and O reversed
modification from Unimod - OBSOLETE because Unimod entry 22 is now merged with entry 21 remap to MOD:00696 'phosphorylated residue'.
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.
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 protein modification that effectively converts an L-cysteine residue to S-carboxamidoethyl-L-cysteine.
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)
A protein modification that effectively replaces a hydrogen atom with an (pyridin-3-yl)acetyl group.
Produced by reaction with N-[(pyrid-3-yl)acetyl]oxy-succinimide [JSG].
A protein modification that effectively converts an L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid.
(R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid
S-carbamoylmethylcysteine cyclization (N-terminus)
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-glutamic acid residue to 2-pyrrolidone-5-carboxylic acid.
MOD_RES Pyrrolidone carboxylic acid (Glu)
Pyroglutamic Acid formed from Glutamic Acid
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].
A protein modification that effectively replaces a residue hydrogen atom on a carbon with a carbohydrate-like group through a glycosidic bond.
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a morpholine-2-acetyl group.
N-succinimidylmorpholine-2-acetate alpha-amino derivative
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 substitutes one sodium atom for one hydrogen atom.
A protein modification that effectively converts an L-cysteine residue to S-pyridylethyl-L-cysteine.
vinylpyridine derivatized cysteine residue
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
A protein modification that effectively replaces one hydrogen atom with a hydroxyl group.
A protein modification that effectively replaces a residue hydrogen atom on a sulfur with a carbohydrate-like group through a glycosidic bond.
A protein modification that effectively replaces a hydrogen atom with a methyl group.
Methylation (N terminus, N epsilon of Lysine, O of Serine, Threonine or C terminus, N of Asparagine)
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
A protein modification that effectively replaces two hydrogen atoms with two hydroxyl groups.
A protein modification that effectively replaces two hydrogen atoms with two methyl groups.
N,N dimethylation (of Arginine or Lysine)
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].
A protein modification that effectively replaces three hydrogen atoms with three methyl groups.
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.
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.
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 trihydrogen phosphate molecular fragment.
modified residue with neutral loss of phosphate
A protein modification that effectively replaces a hydrogen atom with an glucose group through a glycosidic bond.
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.
From DeltaMass: Average Mass: 162 Formula:C6 H10 05 Monoisotopic Mass Change:162.053 Average Mass Change:162.143 References:PE Sciex.
Covalent modification of a peptide or protein amino acid phosphorylated serine with a secondary loss of a neutral trihydrogen phosphate molecular fragment.
O-phospho-L-serine with neutral loss of phosphate
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.
A protein modification that effectively replaces a hydrogen atom with a farnesyl group.
A protein modification that effectively replaces a hydrogen atom with a myristoyl group.
Covalent modification of a peptide or protein amino acid phosphorylated threonine with a secondary loss of a neutral trihydrogen phosphate molecular fragment.
O-phospho-L-threonine with neutral loss of phosphate
A protein modification that effectively replaces a hydrogen atom with a palmitoyl group.
A protein modification that effectively replaces a hydrogen atom with a geranylgeranyl group.
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.
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-dimethlyated L-arginine with secondary neutral loss of an N,N-dimethylamine molecular fragment.
protonated omega-N,omega-N-dimethlyated L-arginine with secondary neutral loss of N,N-dimethylamine
A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine.
A protein modification that effectively converts an L-lysine residue to L-homoarginine, such as reaction with O-methylisourea.
A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal.
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].
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.
A protein modification that effectively replaces a hydrogen atom with an N-acetylaminoglucose group through a glycosidic bond.
Acetate labeling reagent (N-term & K) (heavy form, +3amu)
acetate labeling reagent (N-term) (heavy form, +3amu)
OBSOLETE because this isotopic label from Unimod entry 57 is deprecated
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a propanoyl group.
Propionate labeling reagent light form (N-term & K)
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 3x(13)C-labeled propanoyl group.
Propionate labeling reagent heavy form (+3amu), N-term & K
alpha-amino 3x(13)C-labeled propanoylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent light form group.
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.
Quaternary amine labeling reagent heavy (+3amu) form, N-term & K
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 (+6amu) form group.
Quaternary amine labeling reagent heavy form (+6amu), N-term & K
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.
Quaternary amine labeling reagent heavy form (+9amu), N-term & K
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.
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 4x(2)H labeled succinyl group.
Succinic anhydride labeling reagent, heavy form (+4amu, 4H2), N-term
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(13)C labeled succinyl group.
Succinic anhydride labeling reagent, heavy form (+4amu, 4C13), N-term & K
4x(13)C labeled alpha-amino succinylated residue
A protein modification that effectively trioxygenates an L-cysteine residue to L-cysteine sulfonic acid.
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 substitutes a nitrite (NO2) group for a hydrogen atom.
Note, this is often misrepresented as the introduction of a nitrate (NO3) group [JSG].
A protein modification that effectively converts an L-tryptophan residue to L-kynurenine.
(2S)-2-amino-4-(2-aminophenyl)-4-oxo-butanoic acid
A protein modification that effectively converts an L-tryptophan residue to 3'-hydroxy-L-kynurenine.
tryptophan oxidation to hydroxykynurenin
A protein modification that effectively converts an L-tryptophan residue to N'-formyl-L-kynurenine.
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.
A protein modification that effectively converts an L-phenylalanine residue to a dihydroxyphenylalanine.
Dihydroxyphenyalanines with a 4'-hydroxyl orginate naturally by a monohydroxylation of tyrosine, and not by dihydroxylation of phenylalanine [JSG].
A protein modification that effectively converts a residue to a glycosylsphingolipidinositolethanolamidated.
glycosylsphingolipidinositolated residue
A protein modification that effectively substitutes an iminobiotinyl group for a hydrogen atom.
modification from Unimod Chemical derivative
A protein modification that effectively converts an L-cysteine residue to S-(1,1,2-(2)H3)-propanamide-L-cysteine.
A protein modification that effectively converts an L-tyrosine residue to 2-amino-L-tyrosine.
A protein modification that effectively replaces a hydrogen atom with an galactose group through a glycosidic bond.
A protein modification that effectively converts, by oxidative decarboxylation, an L-proline residue to 2-pyrrolidone with breakage of the peptide chain.
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.
A protein modification that effectively converts an L-proline residue to L-glutamyl semialdehyde.
Oxidation of proline to gamma-glutamyl semialdehyde
A protein modification that effectively converts an L-arginine residue to L-glutamyl semialdehyde.
Oxidation of arginine (to glutamic acid)
Arginine oxidation to glutamic semialdehyde
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.
Applied Biosystems cleavable ICAT(TM) light
Applied Biosystems cleavable ICAT(TM) heavy
A protein modification that effectively converts an L-methionine residue to N-formyl-L-methionine (not known as a natural, post-translational modification process).
This entry is for the artifactual formation of N-formyl-L-methionine from methionine. For encoded N-formyl-L-methionine, use MOD:00030 [JSG].
A protein modification that is produced by reaction with N-ethylmaleimide.
Oxidized lysine biotinylated with biotin-LC-hydrazide, reduced
Oxidized lysine biotinylated with biotin-LC-hydrazide
Oxidized proline biotinylated with biotin-LC-hydrazide, reduced
Oxidized Proline biotinylated with biotin-LC-hydrazide
Oxidized arginine biotinylated with biotin-LC-hydrazide
Oxidized arginine biotinylated with biotin-LC-hydrazide, reduced
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.
ubiquitination signature dipeptidyl lysine
A protein modification that effectively replaces a hydrogen atom with a formyl group.
N-iodoacetyl, p-chlorobenzyl-12C6-glucamine
N-iodoacetyl, p-chlorobenzyl-13C6-glucamine
OBSOLETE because Unimod entry 125 is merged with entry 199, remap to id: MOD:00552
modification from Unimod [(35)S]dithiobis(succinimidyl propionate) crosslinking
The name "thioacylation of primary amines" in Unimod was a misdescription [JSG].
A protein modification that effectively substitutes a hydrogen of a residue with a fluorine atom.
fluorophenylalanine replacement of phenylalanine
5-Iodoacetamidofluorescein (Molecular Probe, Eugene, OR)
A protein modification that effectively substitutes one hydrogen atom of a residue with one iodine atom.
Iodination (of Histidine[C4] or Tyrosine[C3])
A protein modification that effectively substitutes two hydrogen atoms of a residue with two iodine atoms.
A protein modification that effectively substitutes three hydrogen atoms of a residue with three iodine atoms.
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].
A protein modification that effectively converts a glycine residue to N-(cis-delta 5)-tetradecaenoylglycine.
A protein modification that effectively converts a glycine residue to N-(cis,cis-delta 5,delta 8)-tetradecadienoylglycine.
(cis,cis-delta 5, delta 8)-tetradecadienoyl
N-(cis,cis-delta 5,delta 8)-tetradecadienoylglycine
labeling reagent light form (N-term & K)
benzoyl labeling reagent light form (N-term and K)
modification from Unimod N-linked glycosylation, Hex(5) HexNAc(2)
N-linked glycan core N4-glycosylated asparagine
OBSOLETE because redundant, replaced by MOD:01653. Remap to MOD:01653.
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
Virtual Modification for MS/MS of a-type ions, by decarboxylation of C-terminus as reaction inside the mass spectrometer.
amidination of lysines or N-terminal amines with methyl acetimidate
modification from Unimod N-linked glycosylation, dHex HexNAc
modification from Unimod N-linked glycosylation, HexNAc(2)
modification from Unimod N-linked glycosylation, Hex3
modification from Unimod N-linked glycosylation, dHex(2) HexNAc
modification from Unimod N-linked glycosylation, dHex Hex HexNAc
Hex1HexNAc1dHex1 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, dHex HexNAc(2)
modification from Unimod N-linked 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 composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond.
Hex1HexNAc2Pent1 N4-glycosylated asparagine
Hex1HexNAc2dHex1 N4-glycosylated asparagine
Hex3HexNAc1Pent1 N4-glycosylated asparagine
Hex1HexNAc2dHex1Pent1 N4-glycosylated asparagine
Hex1HexNAc2dHex2 N4-glycosylated asparagine
Hex2HexNAc2Pent1 N4-glycosylated asparagine
Hex2HexNAc2dHex1 N4-glycosylated asparagine
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.
Hex3HexNAc2P1 N4-glycosylated asparagine
A protein modification that effectively converts an L-methionine residue to L-selenomethionine.
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.
modification from Unimod Post-translational
Michael addition of BHT quinone methide to Cysteine and Lysine
DAET = 2-(dimethylamino)ethanethiol. The phosphorylation to amine is the beta elimination of phosphate and Michael addition of 2-(dimethylamino)ethanethiol to the site.
OBSOLETE because Unimod 179 merged with Unimod 447 remap to ??? a protein modification that replaces an L-serine residue with an L-alanine residue
A protein modification that effectively converts an L-threonine residue to L-alanine.
This could represent either an engineered replacement or a chemical modification.
Modified amino acid residues groups into isobaric sets at particular mass resolution cut-offs.
protein modification categorized by isobaric sets
OBSOLETE because Unimod 179 merged wth Unimod 447 remap to ??? modification from Unimod O-linked glycosylation
A protein modification that effectively converts a residue containing common isotopes to a 9x(13)C labeled residue.
A protein modification that effectively converts an L-tyrosine residue to 9x(13)C labeled L-phosphotyrosine.
OH-PGO and PGO react with arginine at a stoichiometry of 2:1 [Unimod].
A protein modification that effectively converts a residue containing common isotopes to a 6x(13)C labeled residue.
OBSOLETE because redundant with MOD:00927. Remap to MOD:00927.
A protein modification that effectively substitutes two (18)O atom for the two (16)O atoms of an alpha-carboxyl (1-carboxyl) group.
modification from Unimod Chemical derivative used for amino acid analysis
6-aminoquinolyl-N-hydroxysuccinimidyl carbamate
Derivatization of cysteine with 3-acrylamidopropyl)trimethylammonium chloride [JSG].
Derivatization of cysteine with 3-acrylamidopropyl)trimethylammonium chloride (difference formula correct) [JSG].
A protein modification that effectively converts a residue containing common isotopes to a 4x(2)H labeled dimethylated residue.
Supposed to be alpha-amino and Lys-N6 derivatized by C(2)H2O and reduction.
A protein modification that effectively substitutes a (2-sulfanylethyl)sulfanyl (or thioethylthiol) group for a hydroxy group.
From DeltaMass: Average Mass: 93; supposed to be derivatization of serine and threonine.
OBSOLETE because Unimod entry 202 was merged with entry 195, remap to MOD:00548. modification from Unimod Chemical derivative
OBSOLETE because this modification not supported by any literature that I can find[PMT]
OBSOLETE because this modification not supported by the papers listed or any other that I can find[PMT]
A protein modification that effectively replaces a hydrogen atom with an N-acetylaminogalactose group through a glycosidic bond.
mono-N-acetylaminogalactosylated residue
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.
Representative mass and accurate mass for 116 & 117
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
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].
"IDBEST tag for quantitation, http://www.targetdiscovery.com/index.php?topic=prod.idbe"
OBSOLETE because Unimod entry 244 is redundant with Unimod 348. Remap to MOD:00775.
OBSOLETE because Unimod entry 245 is redundant with Unimod 349. Remap to MOD:00776
Natural or modified residues that are isobaric at a resolution below 0.000001 Da.
residues isobaric at a resolution below 0.000001 Da
Natural or modified residues with a mass of 71.037114 Da.
A modification that effectively oxygenates C5 of an L-proline residue to form a 2-pyrrolidone-5-carboxylic acid, pyroglutamic acid.
The review article PubMed:9252331 does not provide an original citation for this modification [JSG].
oxidized Arginine biotinylated with biotin hydrazide
oxidized Lysine biotinylated with biotin hydrazide
oxidized proline biotinylated with biotin hydrazide
oxidized Threonine biotinylated with biotin hydrazide
modification occurs as a Schiff base in the presence of pentalysine
OBSOLETE because this modification not supported by any literature that I can find [PMT]
OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other
OBSOLETE because entry removed from Unimod. Remap potentially to MOD:00579 propionaldehyde +40
A protein modification that effectively substitutes one (18)O atom for one (16)O atom.
A protein modification that effectively converts an L-lysine residue to 6x(13)C,2x(15)N labeled L-lysine.
A protein modification that effectively replaces a hydrogen atom with a thiophosphono group (H2PO2S, 'thiophosphate').
A protein modification produced by formation of an adduct with 4-sulfophenyl isothiocyanate.
4-sulfophenyl isothiocyanate derivatized residue
A protein modification that effectively substitutes three (2)H deuterium atoms for three (1)H protium atoms.
A protein modification that effectively converts an L-arginine residue to 6x(13)C, 4x(15)N labeled L-arginine.
A protein modification that effectively converts an L-valine residue to 5x(13)C,1x(15)N labeled L-valine.
A protein modification that effectively converts an L-phenylalanine residue to (13)C,(15)N labeled L-phenylalanine.
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
nucleophilic addition to cytopiloyne+H2O
OBSOLETE because removed from Unimod. modification from Unimod Chemical derivative
covalent modification of lysine by cross-linking reagent
covalent modification of lysine by omega-maleimido alkanoyl N-hydroxysuccinimido esters
Natural or modified resiues with a mass of 113.047678 Da.
A protein modification that effectively replaces a hydrogen atom with an manose group through a glycosidic bond
A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS.
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
OBSOLETE because Unimod entry 277 redundant with Unimod 39. Remap to MOD:00110.
A protein modification that effectively converts an L-cysteine residue to S-(2-hydroxyethyl)cysteine
This modification of cysteine is produced by the reagent iodoethanol with triethylphosphine [JSG].
A protein modification that effectively replaces one hydrogen atom with one methyl group.
A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-ethyl ester.
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].
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.
A protein modification that effectively replaces a hydrogen atom of a residue amino or imino group with an methyl group.
OBSOLETE because Unimod entry 283 is redundant with Unimod 280. Remap to MOD:00600
A protein modification that effectively converts an L-lysine residue to 2x(2)H labeled monomethylated L-lysine.
modification from Unimod Chemical derivative, C-Terminal/Glutamate/Aspartate sulfonation
Unimod name, formula, and terminal specification corrected. Formula corresponded to uncleaved intermediate [JSG].
Pierce EZ-Link Biotin-HPDP modified L-cysteine
A protein modification that is produced by reaction of iodouridine monophosphate with a residue.
Cross-link of (Iodo)-uracil MP with W,F,Y
iodouridine monophosphate derivatized 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.
3-(carboxamidomethylthio)propanoylated 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.
OBSOLETE because entry Unimod:261 site N-term R was abandoned. Remap to MOD:00584
4-sulfophenyl isothiocyante modification to N-term R
Natural or modified residues that are isobaric at a resolution below 0.1 Da.
residues isobaric at a resolution below 0.1 Da
A protein modification that effectively converts a residue containing common isotopes to a 3x(2)H labeled residue methyl ester.
There is no literature citation for this Unimod entry [JSG].
OBSOLETE because entry 300 is redundant with Unimod 6 remap to MOD:01328
1-(bromomethyl)-2,6,7-trimethylpyrazolo[1,2-a]pyrazole-3,5-dione, C 10 H 11 Br 1 N 2 O 2.
From DeltaMass: Average Mass: 76 Average Mass Change:76 PubMed:8019414.
fucosylated biantennary (-2 galactose) N4-glycosylated asparagine
Natural or modified residues with a mass of 113.0-113.1 Da.
fluorescein-5-thiosemicarbazide modified residue
(2S)-2-amino-6-(2,5-dimethylpyrrolidin-1-yl)hexanoic acid
There is no citation for this Unimod entry. Add PubMed:7981420, correct spelling [JSG].
2,5-dimethylpyrrole lysine from 2,5-hexanedione adduct
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
Usually major adduct formed from malondialdehyde (MDA) with the amino group of lysine residues [UniProt].
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.
N-ethylmaeimide adduct + H20 (a mixture of isobaric products) [JSG].
OBSOLETE because this chemical derivative modification from Unimod 321 is deprecated.
Invitrogen B-10621, a red fluorescent cross-linking reagent (only link to Cys is indicated) [Unimod].
Pierce reagent, needs sites for N, Q, R, K, and N-term [JSG].
A protein modification that effectively converts an L-serine residue to S-ethylcysteine.
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.
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.
1x(13)C,3x(2)H labeled monomethylated 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.
2x(13)C,6x(2)H labeled dimethylated L-arginine
6-N-biotinylaminohexyl isopropyl phosphate
6-N-biotinylaminohexyl isopropyl phosphorofluoridate
OBSOLETE because Unimod entry 334 is merged with Unimod 293. Remap to MOD:00612
A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4.
methylamine Michael addition derivatized residue
A protein modification that effectively replaces a residue hydroxyl group with an acetoxy group.
A protein modification that effectively replaces a residue sulfanyl group with an acetylsulfanyl group.
A protein modification that effectively converts an L-cysteine residue to either N-acetyl-L-cysteine or S-acetyl-L-cysteine.
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.
A protein modification that effectively converts an L-serine residue to N,O-diacetyl-L-serine.
(S)-2-acetamido-3-acetyloxypropanoic acid
In one paper, the samples were prepared using glacial acetic acid, and were probably artifactual [JSG].
A protein modification that effectively replaces a hydrogen atom with an acyl group.
A protein modification that effectively replaces a residue amino group with a myristoylamino group.
A protein modification that effectively replaces a residue amino group with a palmitoylamino group.
A protein modification that effectively replaces a residue hydroxyl group with a palmitoyloxy group.
A protein modification that effectively replaces a residue sulfanyl group with an palmitoylsulfanyl group.
a protein modification that effectively replaces a sulfanyl group with a methylsulfanyl group
A protein modification that effectively replaces a residue sulfanyl group with an myristoylsulfanyl group.
A protein modification that effectively replaces a residue hydrocarbyl hydrogen with an methyl group.
A protein modification that effectively converts an L-glutamine residue to L-glutamate 5-methyl ester.
deamidated 5-methyl esterified glutamine
This is known to be a natural modification of glutamine in prokaryotes.
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.
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.
A protein modification that effectively converts an L-cysteine residue to a methylated cysteine, either S-methylcysteine, or cysteine methyl ester.
A protein modification that effectively converts an L-histidine residue to a methylated histidine, such as pros-methylhistidine, or tele-methylhistidine.
A protein modification that effectively converts an L-leucine residue to a methylated leucine, either N-methylleucine, or leucine methyl ester.
A protein modification that effectively converts an L-lysine residue to a methylated lysine.
A protein modification that effectively replaces a residue L-enantiomer (stereoisomer) with a D-enantiomer or with a different diastereomeric isomer.
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 protein modification that effectively replaces a hydrogen atom with an octanoyl group.
A protein modification that effectively replaces a hydrogen atom with a decanoyl group.
A protein modification that effectively replaces a residue hydroxyl group with a decanoyloxy group.
A protein modification that effectively replaces a residue hydroxyl group with a octanoyloxy group.
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acyl group.
A protein modification that effectively replaces a residue hydroxyl group with a acyloxy group.
A protein modification that effectively replaces a residue sulfanyl group with an acylsulfanyl group.
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.
A protein modification that effectively replaces a carboxyl group with a carboxamido group.
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.
A protein modification that effectively adds oxygen atoms to a residue with or without the removal of hydrogen atoms.
A protein modification that effectively replaces a hydrogen atom with an hydroxyl group.
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.
A protein modification that effectively adds oxygen atoms to a carbon atom of a residue and removes hydrogen atoms.
A protein modification that effectively adds oxygen atoms to a sulfur atom of a residue without removing hydrogen atoms.
A protein modification that effectively converts an L-lysine residue to a hydroxylated L-lysine.
A protein modification that effectively converts an L-arginine residue to a hydroxylated L-arginine.
A protein modification that effectively removes neutral hydrogen atoms (proton and electron) from a residue.
A protein modification that effectively converts an L-asparagine residue to L-aspartic acid.
A protein modification that effectively converts an L-glutamine residue to L-glutamic acid.
A protein modification that effectively converts an L-cysteine residue to L-selenocysteine (not known as a natural, post-translational modification process).
This entry is for the artifactual formation of L-selenocysteine from cysteine. For encoded L-selenocysteine, use MOD:00031 [JSG].
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.
A protein modification that crosslinks two residues with an amide bond where either the donor amino or carboxyl is not an alpha group.
A protein modification that crosslinks two cysteine residues by formation of a disulfide bond.
A protein modification that crosslinks two residues by formation of an oxazole or thiazole ring.
oxazole/thiazole ring crosslinked residues
A protein modification that crosslinks two residues by formation of an 5-imidazolinone ring.
5-imidazolinone ring crosslinked residues
A protein crosslink modification that is not chemically categorized.
A protein modification that effectively replaces a hydrogen atom with an carbohydrate-like group through a glycosidic bond.
A protein modification that effectively substitutes a halogen atom for a hydrogen atom.
A protein modification that effectively substitutes a sulfonyl group for the hydrogen atom of a hydroxyl or sulfanyl group.
A protein modification that effectively replaces a hydrogen atom with a phosphono group (H2PO3 or 'phosphate').
Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine)
A protein modification that effectively results from forming an adduct with a compound containing a flavin group.
A protein modification that effectively substitutes a metal atom or a metal cluster for hydrogen atoms, or coordinates a metal ion.
metal or metal cluster containing modified residue
A protein modification that effectively results from forming an adduct with a compound containing a porphyrin group.
A protein modification that effectively results from forming an adduct with a compound containing a tetrapyrrole group.
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.
nucleotide or nucleic acid modified residue
A protein modification that effectively substitutes atoms of particular common isotopes with atoms or groups containing isotopes that are not the most common.
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.
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.
A protein modification that effectively forms a double bond by removing a molecule of water from a residue.
A protein modification that effectively converts an L-valine residue to D-valine.
A protein modification that effectively converts L-tyrosine to 2,3-didehydrotyrosine.
a protein modification that effectively converts an L-tyrosine residue to a multihydroxylated L-phenylalanine
A protein modification that effectively adds oxygen atoms to a sulfur atom of L-cysteine residue without removing hydrogen atoms.
A protein modification that effectively adds oxygen atoms to a sulfur atom of L-methionine residue without removing hydrogen atoms.
A protein modification that effectively adds a proton and replaces two hydrogen atoms with two methyl groups.
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.
A protein modification that effectively replaces three hydrogen atoms with three methyl groups, after a proton has been added to form an aminium group.
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.
A protein modification that effectively converts an L-proline residue to a methylated proline, such as N,N-dimethylproline.
A protein modification that effectively converts an L-glutamic acid residue to a methylated glutamic acid, such as L-glutamate 5-methyl ester.
A protein modification that effectively converts a glycine residue to a methylated glycine, such as N-methylglycine.
A protein modification that effectively converts an L-isoleucine residue to a methylated isoleucine residue, such as N-methyl-L-isoleucine.
A protein modification that effectively converts an L-methionine residue to a methylated methionine, such as N-methyl-L-methionine.
A protein modification that effectively converts an L-phenylalanine residue to a methylated phenylalanine, such as N-methyl-L-phenylalanine.
A protein modification that effectively converts an L-tyrosine residue to a methylated tyrosine, such as N-methyl-L-tyrosine.
A protein modification that oxygenates an L-methionine residue to one of the diastereomeric L-methionine sulfoxide residues.
(2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid
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.
A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide R-diastereomer.
A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide S-diastereomer.
A protein modification that effectively replaces one hydrogen atom of an L-glutamine residue with one methyl group.
A protein modification that effectively converts an L-lysine residue to either N2-acetyl-L-lysine, or N6-acetyl-L-lysine.
A protein modification that effectively replaces one hydrogen atom on a nitrogen of an L-histidine residue with one methyl group.
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.
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.
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,
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.
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
for Pentoses DeltaMass gives mass 132, for Pentosyl DeltaMass gives formula C 6 H 10 N4 with mass 146
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
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
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
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.
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.
From DeltaMass: Average Mass: 203 Formula:C8H13O5N1 Monoisotopic Mass Change:203.079 Average Mass Change:203.196 References:PE Sciex
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.
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
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.
N-acetylneuraminic acid (Sialic acid, NeuAc, NANA, SA)
A protein modification that effectively substitutes an iron atom or a cluster containing iron for hydrogen atoms, or that coordinates an iron ion.
A protein modification that effectively substitutes a cluster of iron and sulfur atoms for hydrogen atoms.
iron-sulfur cluster containing modification
A protein modification that effectively substitutes a manganese atom or a cluster containing manganese for hydrogen atoms, or that coordinates a manganese ion.
A protein modification that effectively substitutes a nickel atom or a cluster containing nickel for hydrogen atoms, or that coordinates a nickel ion.
A protein modification that effectively substitutes a copper atom or a cluster containing copper for hydrogen atoms, or that coordinates a copper ion.
A protein modification that effectively substitutes a molybdenum atom or a cluster containing molybdenum for hydrogen atoms, or that coordinates a molybdenum ion.
A protein modification containing a molybdenum atom in a pterin ring system.
molybdenum pterin containing modification
A protein modification that effectively substitutes a selenium atom or a cluster containing selenium for hydrogen atoms.
A protein modification that effectively substitutes a tungsten atom or a cluster containing tungsten for hydrogen atoms, or that coordinates a tungsten ion.
A protein modification that effectively substitutes a sodium atom for a hydrogen atom.
A protein modification that effectively results from forming an adduct with a compound containing a pterin group.
A protein modification that effectively substitutes a sulfur atom for an oxygen atom.
A protein modification that effectively crosslinks an amino acid residue and the 3'- or 5'-end of DNA through a phosphodiester bond.
A protein modification that effectively results from forming an adduct with one ADP-ribose through formation of a glycosidic bond.
monoadenosine diphosphoribosyl (ADP-ribosyl) modified residue
A protein modification that effectively substitutes a chlorine atom for a hydrogen atom.
A protein modification that effectively substitutes a bromine atom for a hydrogen atom.
A protein modification that effectively substitutes an iodine atom of a residue for a hydrogen atom.
A protein modification that effectively converts an L-valine residue to 4-hydroxy-D-valine.
(2R,3Xi)-2-amino-4-hydroxy-3-methylbutanoic acid
A protein modification that effectively converts an L-proline residue to O4-galactosyl-L-hydroxyproline.
(2S,4R)-4-(beta-D-galactopyranosyloxy)pyrrolidine-2-carboxylic acid
A protein modification that effectively converts an L-proline residue to O4-(N-acetylamino)glucosyl-L-hydroxyproline.
(2S,4R)-4-[2-acetamido-2-deoxy-alpha-D-glucopyranosyloxy]pyrrolidine-2-carboxylic acid
CARBOHYD O-linked (GlcNAc) hydroxyproline
fucosylated biantennary (-1 galactose) N4-glycosylated asparagine
modification from Unimod N-linked glycosylation - missing ref
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.
biantennary (-2 galactose) N4-glycosylated asparagine
biantennary (-1 galactose) N4-glycosylated asparagine
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.
A protein modification that effectively converts an L-cysteine residue to S-(L-cysteinyl)-L-cysteine, forming a disulfide bond with free cysteine.
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)
modification from Unimod Post-translational - C-terminal loss of lysine OBSOLETE because the idenical to MOD:01642. Remap to MOD:01642
Loss of C-terminal K from Heavy Chain of MAb
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.
Oxidation of methionine to methionine sulfone with neutral loss of CH3SO2H.
Originally created from Unimod:508 that was later deleted.
methionine oxidation with neutral loss of 80 Da
Natural or modified residues with a mass of 71.0-71.1 Da.
Natural or modified residues that are isobaric at a resolution below 0.01 Da.
residues isobaric at a resolution below 0.01 Da
Natural or modified residues with a mass of 166.98-167.00 Da.
A protein modification that effectively substitutes a vanadium atom or a cluster containing vanadium for hydrogen atoms, or that coordinates a vanadium ion.
Natural or modified residues with a mass of 181.00-181.02 Da.
Natural or modified residues with a mass of 243.02-243.03 Da.
An artifactual protein modification that converts an L-histidine residue to L-asparagine by oxidative degradation.
An artifactual protein modification that converts an L-histidine residue to L-aspartic acid by oxidative degradation.
From OMSSA: desc="oxidation of H to D" monomass= -23.015984 (this is the same mass difference as OMSSA:54, his2asnh) [JSG].
Natural or modified residues with a mass of 182.96-182.98 Da.
Natural or modified residues with a mass of 182.9-183.0 Da.
OBSOLETE because redundant with MOD:00130. Remap to MOD:00130.
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.
A protein modification that effectively converts an L-asparagine residue to N-acetyl-L-asparagine.
This modification has not been observed to occur naturally.
A protein modification that effectively converts an L-histidine residue to N2-acetyl-L-histidine.
A protein modification that effectively converts an L-leucine residue to N-acetyl-L-leucine.
A protein modification that effectively replaces two hydrogen atoms of an L-arginine residue with two methyl groups.
A protein modification that effectively converts an L-phenylalanine residue to N-acetyl-L-phenylalanine.
A protein modification that effectively converts an L-tryptophan residue to N2-acetyl-L-tryptophan.
A protein modification that effectively substitutes one or more (2)H deuterium atoms for (1)H protium atoms.
modification from Unimod - label for the active site serine of the serine esterase/protease family also shown to label tyrosine in serum albumin
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.
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form
A protein modification that effectively converts an L-glutamine residue to L-glutamic acid with one (18)O.
A protein modification that effectively substitutes one (2)H deuterium atom for one (1)H protium atom.
A protein modification that effectively converts an L-cysteine residue to dehydroalanine.
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].
OBSOLETE because redundant and identical to MOD:00477. Remap to MOD:00477.
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.
Michael addition of hydroxymethylvinyl ketone to cysteine
A protein modification that effectively converts an L-arginine residue to L-ornithine.
a protein modification that effectively converts an L-cysteine residue to the PEP adduct, 2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal
(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
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.
A protein modification that effectively converts an L-cysteine residue to S-galactosyl-L-cysteine.
(2R)-2-amino-3-(D-galactopyranosylsulfanyl)propanoic acid
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].
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.
L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide carbide
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 an eight-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl octairon nonasulfide.
L-cysteinyl-L-histidino-homocitryl octairon nonasulfide carbide
L-cysteinyl-L-histidino-homocitryl octairon nonasulfide
a protein modification that effectively converts an L-histidine residue to L-histidino vanadium tetraoxide
(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (dihydroxy)dioxovanadium
dihydrogen (4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (tetraoxido)vanadate
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.
(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
CROSSLNK 3-(S-cysteinyl)-tyrosine (Cys-Tyr)
A protein modification that effectively converts an L-serine residue to O3-beta-glucosylated L-serine.
(2S)-2-amino-3-(beta-D-glucopyranosyloxy)propanoic acid
A protein modification that effectively converts an L-serine residue to O3-(N-acetylaminoglucosyl)-L-serine.
(2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)propanoic acid
A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminoglucosyl)-L-threonine.
(2S,3R)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)butanoic acid
A protein modification that effectively converts an L-serine residue to pyruvic acid.
DeltaMass gives mass 70 and difference mass -16 with no formula
A protein modification that effectively converts an L-serine residue to O3-galactosylserine.
(2S)-2-amino-3-(alpha-D-galactopyranosyloxy)propanoic acid
A protein modification that effectively converts an L-threonine residue to O3-galactosylthreonine.
(2S,3R)-2-amino-3-(alpha-D-galactopyranosyloxy)butanoic acid
A protein modification that effectively converts an L-serine residue to O3-mannosylserine.
(2S)-2-amino-3-(alpha-D-mannopyranosyloxy)propanoic acid
a protein modification that effectively forms a O3-mannosylthreonine
(2S,3R)-2-amino-3-(alpha-D-mannopyranosyloxy)butanoic acid
A protein modification that effectively converts an L-serine residue to an O-fucosylserine.
(2S)-2-amino-3-(6-deoxy-alpha-D-galactopyranosyloxy)propanoic acid
A protein modification that effectively converts an threonine residue to an O-fucosylthreonine.
(2S,3R)-2-amino-3-(6-deoxy-alpha-D-galactopyranosyloxy)butanoic acid
A protein modification that effectively converts an L-serine residue to O3-xylosylserine.
(2S)-2-amino-3-(alpha-D-xylopyranosyloxy)propanoic acid
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].
OBSOLETE because redundant with MOD:00151. Remap to MOD:00151.
A protein modification that effectively converts an L-cysteine residue to S-stearoyl-L-cysteine.
(R)-2-amino-3-(octadecanoylsulfanyl)propanoic acid
2-amino-3-(octadecanoylthio)propanoic acid
A protein modification that effectively converts an L-tryptophan residue to 3'-geranyl-2',3'-dihydro-2',N2-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
A protein modification that effectively converts a residue to a glycosylphosphatidylinositolethanolamidated.
glycosylphosphatidylinositolated residue
A protein modification that effectively converts an L-glutamic acid residue to L-2-aminobutanoic acid.
A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue to form 2-imino-alanine 5-imidazolinone glycine.
(2-ethanimidoyl-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
2,N-didehydroalanyl-5-imidazolinone glycine
[2-(1-iminoethyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
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.
(2R)-2-amino-3-([(2S)-2-aminopropanoyl]sulfanyl)propanoic acid
CROSSLNK Alanyl cysteine thioester (Cys-Ala)
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.
(2R)-2-amino-3-([(2S)-2-amino-4-methylpentanoyl]sulfanyl)propanoic acid
CROSSLNK Leucyl cysteine thioester (Cys-Leu)
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.
(2R)-2-amino-3-([(2S)-2-amino-4-(methylsulfanyl)butanoyl]sulfanyl)propanoic acid
CROSSLNK Methionyl cysteine thioester (Cys-Met)
A protein modification that effectively converts an L-tyrosine residue to 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.
(2R)-2-amino-3-([(2S)-2-amino-3-phenylpropanoyl]sulfanyl)propanoic acid
CROSSLNK Phenylalanyl cysteine thioester (Cys-Phe)
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.
(2R)-2-amino-3-([(2S,3R)-2-amino-3-hydroxybutanoyl]sulfanyl)propanoic acid
CROSSLNK Threonyl cysteine thioester (Cys-Thr)
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.
(2R)-2-amino-3-([(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]sulfanyl)propanoic acid
CROSSLNK Tyrosyl cysteine thioester (Cys-Tyr)
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.
(2R)-2-amino-3-([(2S)-2-amino-3-(1H-indol-3-yl)propanoyl]sulfanyl)propanoic acid
CROSSLNK Tryptophanyl cysteine thioester (Cys-Trp)
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.
(2S)-2-amino-3-([(2S)-2-amino-3-phenylpropanoyl]oxy)propanoic acid
CROSSLNK Phenylalanyl serine ester (Ser-Phe)
A protein modification that effectively converts an L-proline residue to an N-methyl-L-proline.
(S)-1-methylpyrrolidine-2-carboxylic acid
A protein modification that effectively converts an L-asparagine residue to N4-(N-acetylaminoglucosyl)-L-asparagine.
A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminogalactosyl)-L-asparagine.
(2S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)amino-4-oxobutanoic acid
A protein modification that effectively converts an L-asparagine residue to N4-glucosyl-asparagine.
(2S)-2-amino-4-(D-glucopyranosyl)amino-4-oxobutanoic acid
A protein modification that effectively converts an L-serine residue to O3-(N-acetamino)fucosylserine.
(2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-fucopyranosyloxy)propanoic acid
A protein modification that effectively converts an L-serine residue to L-oxoalanine.
A protein modification that effectively substitutes two (2)H deuterium atoms for two (1)H protium atoms.
A protein modification that effectively substitutes four (2)H deuterium atoms for four (1)H protium atoms.
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.
A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing deuteriumm, (2)H.
A protein modification produced by formation of an adduct with an isocyanate compound.
A protein modification produced by formation of an adduct with an isothiocyanate compound.
isothiocyanate reagent derivatized residue
A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (13)C.
A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (15)N.
A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (18)O.
A protein modification that effectively substitutes one or more (18)O atoms for (16)O atoms.
A protein modification that effectively substitutes two (18)O atom for two (16)O atoms.
A protein modification that is produced by formation of an adduct with a particular compound used as a reagent.
A protein modification that effectively substitutes a potassium atom for a hydrogen atom.
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.
A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with (18)O.
A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with one (18)O.
A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with two (18)O.
A protein modification that effectively converts an L-lysine to L-lysinium (protonated L-lysine).
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-lysinium (N6-protonated L-lysine) residue to an N6,N6,N6-trimethyl-L-lysine.
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-alanine residue to an L-alaninium (protonated L-alanine).
protonated L-alanine (L-alaninium) residue
A protein modification that effectively converts an L-alaninium (protonated L-alanine) residue to an N,N,N-trimethyl-L-alanine.
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-serine residue to D-alanine.
A protein modification that can be derived from different natural residues by different chemical processes.
modified residue that can arise from different natural residues
A protein modification that produces an amino acid residue containing an exogenous sulfur atom.
A protein modification that produces an amino acid residue containing a phosphorus atom.
A protein modification that effectively converts a source amino acid residue to D-alanine.
A protein modification that effectively converts an L-threonine residue to D-allo-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.
tris-L-cysteinyl L-histidino diiron disulfide
A protein modification that effectively converts an L-aspartic acid residue to N-aspartyl-glycosylsphingolipidinositolethanolamine.
LIPID GPI-like-anchor amidated aspartate
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.
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.
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.
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.
A protein modification that effectively converts an L-aspartic acid residue to L-alanine.
This has been reported to occur by a natural process of beta-decarboxylation.
A protein modification produced by formation of an adduct with phenyl isocyanate.
A protein modification produced by formation of an adduct with (2)H5-phenyl isocyanate.
(2)H5-phenyl isocyanate derivatized residue
OBSOLETE because redundant and identical to MOD:01970. Remap to MOD:01970.
A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamic acid, forming an isopeptide bond with a diglutamic 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.
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.
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.
dimethyl pimelimidate modification from Unimod
One end of crosslink attached, one end free
imidoester crosslink dimethyl pimelimidate singly attached
dimethyl pimelimidate modification from Unimod - Mechanism of the reaction of imidoesters with amines
Both ends of crosslink attached to same peptide
imidoester crosslink dimethyl pimelimidate doubly attached
A protein modification produced by formation of an adduct with 6x(13)C labeled 4-sulfophenyl isothiocyanate.
4-sulfophenyl isothiocyanate (Heavy C13)
6x(13)C labeled 4-sulfophenyl isothiocyanate derivatized residue
OBSOLETE because Unimod entry 465 megerd with 199. Remap to MOD:00552 DiMethyl-CH2D.
A protein modification that effectively converts an L-serine residue to S-(2-aminoethyl)cysteine.
From DeltaMass: Average Mass: 146 Abbreviation:-AECys_ Formula:C5H10O2N1S1 Monoisotopic Mass Change:146.051 Average Mass Change:146.214 References:PE Sciex.
A protein modification that effectively replaces a 1-carboxyl group (usually referred to as the alpha-carboxyl) with a carboxamido group.
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].
A protein modification that effectively converts an L-cysteine residue to S-2-aminoethylcysteine.
This modified residue is a chemical isolog of L-lysine for trypsin hydolysis produced from L-cysteine by aziridine.
A protein modification that crosslinks two residues by formation of an ester bond.
A protein modification that effectively converts an L-tryptophan residue to 6'-chloro-L-tryptophan.
(2S)-2-amino-3-(6-chloro-1H-indol-3-yl)propanoic acid
The Unimod:340 cross-reference to RESID:AA0180 is incorrect. RESID:AA0180 should be cross-referenced by Unimod:936 [JSG].
A protein modification that effectively converts an L-aspartic acid residue to a methylated aspartic acid, such as aspartic acid 4-methyl ester.
A protein modification that effectively converts an L-proline to an L-prolinium (protonated L-proline).
protonated L-proline (L-prolinium) residue
A protein modification that effectively converts an L-prolinium (charged L-proline) residue to N,N-dimethyl-L-proline.
N,N-dimethyl-L-proline (from L-prolinium)
A protein modification that effectively converts an L-histidine residue to a phosphorylated L-histidine, such as pros-phosphohistidine, or tele-phosphohistidine.
A protein modification that effectively converts a source amino acid residue to D-serine.
A protein modification that effectively converts an L-cysteine residue to D-serine.
Natural or modified residues with a mass of 128.0-128.1 Da.
Natural or modified resiues with a mass of 128.058578 Da.
A protein modification that effectively results from forming an adduct with a compound containing a flavin adenine dinucleotide (FAD) group.
A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group.
A protein modification that effectively converts an L-cysteine residue to N-acetyl-S-archeol-L-cysteine.
A protein modification that effectively converts an L-cysteine residue to S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine.
A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-diacylglycerol-L-cysteine.
A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine.
(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 protein modification that modifies an L-arginine residue.
A protein modification that modifies an L-asparagine residue.
A protein modification that modifies an L-aspartic acid residue.
A protein modification that modifies an L-cysteine residue.
A protein modification that modifies an L-glutamic acid residue.
A protein modification that modifies an L-glutamine residue.
A protein modification that modifies a glycine residue.
A protein modification that modifies an L-histidine residue.
A protein modification that modifies an L-isoleucine residue.
A protein modification that modifies an L-leucine residue.
A protein modification that modifies an L-lysine residue.
A protein modification that modifies an L-methionine residue.
A protein modification that modifies an L-phenylalanine residue.
A protein modification that modifies an L-proline residue.
A protein modification that modifies an L-serine residue.
A protein modification that modifies an L-threonine residue.
A protein modification that modifies an L-tryptophan residue.
A protein modification that modifies an L-tyrosine residue.
A protein modification that modifies an L-valine residue.
New uncategorized Unimod. OBSOLETE because organizational use is no longer required.
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.
(2S)-2-amino-6-([(2S,3R)-2-amino-3-hydroxybutanoyl]amino)hexanoic acid
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.
Modification from Unimod Non-standard residue. OBSOLETE because not an amino acid modification. From Unimod not an approved entry.
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.
2x(13)C,4x(2)H labeled dimethylated residue
Should have children for K and X-N-term [JSG].
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.
CARBOHYD N-linked (Lac) (glycation) lysine
The term lactosylation used with this meaning is a misnomer [JSG].
tyrosine adduct with substrate analog inhibitor 1,2-dideoxy-2'-methyl-alpha-D-glucopyranoso-[2,1-d]-Delta2'-thiazoline.
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
Michael addition of t-butyl hydroxylated BHT (BHTOH) to C, H or K
modification from Unimod Chemical derivative - 5-hydro-5-methylimidazol-4-one, arginine methylglyoxal arginine adduct (+54 amu)
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.
Levuglandinyl - arginine hydroxylactam adduct
Oxidation of methionine to methionine sulfoxide with neutral loss of CH3SOH.
Originally created from Unimod:507 that was later deleted.
methionine oxidation with neutral loss of 64 Da
Levuglandinyl - lysine hydroxylactam adduct
Levuglandinyl - hydroxylactam adduct, K and N-term
Levuglandinyl - lactam adduct, K and N-term
hydrolyzed N-methylmaleimide cysteine adduct
A protein modification produced by formation of an adduct with 3-methyl-2-pyridyl isocyanate.
3-methyl-2-pyridyl isocyanate derivatized residue
Dehydropyrrolizidine alkaloid (dehydroretronecine) on cysteines
dehydropyrrolizidine alkaloid (dehydroretronecine) derivatized cysteine
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-trimethylammoniumbutanoyl derivatized residue
d9-4-trimethylammoniumbutanoyl derivatized residue
OBSOLETE because redundant and identical to MOD:00626. Remap to MOD:00626.
A protein modification that crosslinks two residues with a covalent bond and the loss of ammonia.
crosslinked residues with loss of ammonia
Entries from DeltaMass see http://www.abrf.org/index.cfm/dm.home?AvgMass=all.
OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
OBSOLETE because redundant and identical to MOD:01933. Remap to MOD:01933.
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
From DeltaMass: Average Mass: -48 Average Mass Change:-48 References:Anal. Biochem. Vol 216 No.1 p141
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.
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
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.
(3-amino-2,5-dioxo-1-pyrrolidinyl)acetic acid
CROSSLNK (2-aminosuccinimidyl)acetic acid (Asp-Gly)
[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]acetic acid
Cross-link 2; this cross-link is formed by the condensation of an aspartic acid residue with the alpha-amido of the following residue.
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.
(2S)-2-amino-5-[(2S)-2-amino-2-carboxyethoxy]-5-oxopentanoic acid
CROSSLNK isoglutamyl serine ester (Ser-Glu)
Cross-link 2; From DeltaMass: with no citation.
A protein modification that crosslinks two residues with a covalent bond and the loss of water.
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.
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)
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
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.
modified residue with neutral loss of carbon dioxide
Cross-link 2; From DeltaMass: Average Mass: -5
crosslink between Arg and His sidechains
Cross-link 4; From DeltaMass: Average Mass: -4
A protein modification that effectively replaces a carboxylic acid group with a hydrogen atom.
A protein modification that effectively reduces the disulfide bond of cystine to form two cysteine residues.
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 by reducing the indole ring system of tryptophan to indoline effectively converts an L-tryptophan residue to 2',3'-dihydrotryptophan.
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].
Modification from DeltaMass. OBSOLETE because redundant and identical to MOD:00462. Remap to MOD:00462.
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.
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.
A protein modification that effectively converts an N-terminal L-cysteine residue by a formadehyde adduct to 4-thiazolidinecarboxylic acid.
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.
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.
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 cross-links two L-lysine residues to form syndesine, hydroxylysinohydroxynorleucine.
Cross-link 2; From DeltaMass: Average Mass: 13 Average Mass Change: 13 (incorrect) [JSG].
OBSOLETE because this isn't a protein modification, but rather the difference between two known modifications. modification from DeltaMass
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.
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.
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.
A protein modification that effectively converts an L-histidine residue to 2-oxohistidine.
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
A protein modification that effectively converts an L-phenylalanine residue to a monobrominated L-phenylalanine, such as L-2'-bromophenylalanine.
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)
modification from DeltaMass - OBSOLETE because redundant and identical to MOD:01072. Remap to MOD:01072.
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.
modification from DeltaMass - OBSOLETE because redundant, the difference component of MOD:01060. Remap to MOD:01060.
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
A protein modification that effectively converts an L-serine residue to L-selenocysteine (not known as a natural post-translational modification process).
[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].
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.
A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a halogen atom.
(35)Cl and (37)Cl labeled 3',5'-dichlorotyrosine
A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a chlorine atom.
A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a bromine atom.
OBSOLETE because redundant, the difference component of MOD:01079. Remap to MOD:01079.
From DeltaMass with no citation or formula.
From DeltaMass: Average Mass: 74 with no citation.
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].
From DeltaMass: Average Mass: 76, on acidic amino acids
A protein modification that effectively converts an L-phenylalanine residue to (81)Br-L-2'-bromophenylalanine.
A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with an iodine atom.
OBSOLETE because redundant and identical to MOD:00404. Remap to MOD:00404.
From DeltaMass: Average Mass: 83 Formula:C4H5O1N1 Monoisotopic Mass Change:83.037 Average Mass Change:83.09
A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one bromine atom.
A protein modification that inserts or replaces a residue with a 2-aminoisobutyric acid.
Modification from DeltaMass: Average Mass: 85.
From DeltaMass: Average Mass: 85 Formula: C 4 H 7 O 1 N 1 Monoisotopic Mass Change: 85.053 Average Mass Change: 85.106
From DeltaMass: Average Mass: 86 Formula: C 3 H 6 O 2 N 1 Monoisotopic Mass Change: 86.048 Average Mass Change: 86.094
A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two bromine atoms.
A protein modification that effectively substitutes an anisyl (methoxyphenyl) group for a hydroxyl group, typically at the 4 or para position.
From DeltaMass with no citation or formula: Average Mass: 90.
A protein modification that effectively substitutes a benzyl (phenylmethyl) group for a hydrogen atom.
benzyl (Bzl) and benzyl ester (OBzl) modified residue
A protein modification that effectively substitutes a trifluoroacetyl group for a hydrogen atom.
A protein modification that effectively oxidizes the disulfide bond of a cystine crosslink to form two cysteic acid residues.
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
tetramethylguanidinium termination by-product on amine
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
A protein modification that inserts or replaces a residue with an isovaline.
OBSOLETE because redundant and identical to MOD:00403. Remap to MOD:00403.
From DeltaMass: Average Mass: 101 Abbreviation:-Hse- Formula:C4H7O2N Monoisotopic Mass Change:101.048 Average Mass Change:101.105
A protein modification that effectively converts an L-lysine residue to 2-piperidinecarboxylic acid.
A protein modification that effectively converts an L-tyrosine residue to 3',5'-dibromo-L-tyrosine.
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.
From DeltaMass: Average Mass: 131. This is the mass of the free amino acid [JSG].
A protein modification that effectively converts an L-tyrosine residue to 3'-bromo-L-tyrosine.
A protein modification that inserts or replaces a residue with a norleucine.
A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one chlorine atom.
A protein modification that effectively replaces a hydrogen atom with a succinyl group linked through a carbonyl carbon.
Succinic anhydride labeling reagent light form (N-term & K)
From DeltaMass with no citation or formula, Average Mass: 117 [JSG].
A protein modification that effectively substitutes a benzyloxymethyl group for a hydrogen atom.
A protein modification that effectively substitutes a p-methoxybenzyl group for a hydrogen atom.
A protein modification that effectively substitutes a 4-nitrophenyl group for a hydrogen atom.
OBSOLETE because redundant and identical to MOD:01181. Remap to MOD:01181.
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
A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two chlorine atoms.
OBSOLETE because this represents a free amino acid and the corresponding residue is MOD:01026.
OBSOLETE because redundant and identical to MOD:00036. Remap to MOD:00036.
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
A protein modification that inserts or replaces a residue with a penicillamine.
2-amino-3-mercapto-3-methylbutanoic acid
2-amino-3-methyl-3-sulfanylbutanoic acid
From DeltaMass: Name misspelled 'bb-dimethyl cystenyl'. No citation provided.
A protein modification that effectively substitutes a benzyloxycarbonyl group for a hydrogen atom.
A protein modification that effectively substitutes a adamantyl group for a hydrogen atom.
A protein modification that effectively substitutes a p-nitrobenzyl group for the hydrogen atom of a carboxyl group.
OBSOLETE because redundant and identical to MOD:00080. Remap to MOD:00080.
From DeltaMass with no citation. Formula:C6H10O2N2 (name misspelled, formula for N5-methylglutaminyl, rather than N2-methylglutamyl)
A protein modification that effectively converts an L-tyrosine residue to 3',5'-dichloro-L-tyrosine.
A protein modification that effectively converts an L-tyrosine residue to 3'-chloro-L-tyrosine.
A protein modification that effectively converts an L-lysine residue to a monohydroxylated lysine.
From DeltaMass: Average Mass: 144 Abbreviation:-Hyl- Formula:C6H12N2O2 Monoisotopic Mass Change:144.09 Average Mass Change:144.174.
A protein modification that effectively converts a source amino acid residue to 2-pyrrolidone-5-carboxylic acid.
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.
A protein modification that effectively substitutes a hydrogen atom of an L-histidine residue with a halogen atom.
From DeltaMass: Average Mass: 148 Formula:C8H8O2N1 Monoisotopic Mass Change:148.064 Average Mass Change:148.165
(79)Br and (81)Br labeled 3',5'-dibromotyrosine
A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine.
From DeltaMass: (name misspelled "Carboxyamidomethyl Cystenyl") [JSG].
A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine.
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].
OBSOLETE because duplicate and redundant with MOD:01061. Remap to MOD:01061
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
A protein modification that effectively converts an L-phenylalanine residue to a monomethylated phenylalanine.
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].
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.
A protein modification that effectively substitutes a hydrogen atom of an L-phenylalanine residue with a halogen atom.
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
A protein modification that effectively substitutes a hydrogen atom of an L-tryptophan residue with a halogen atom.
A protein modification that effectively substitutes a 2,4-dinitrophenyl group for a hydrogen atom.
A protein modification that effectively substitutes a pentafluorophenyl group for a hydrogen atom.
From DeltaMass: name mispelled "pentaflourophenyl"
A protein modification that effectively substitutes a diphenylmethyl group for a hydrogen atom.
A protein modification that effectively substitutes one potassium atom for one hydrogen atom.
A protein modification that effectively substitutes a 2-chlorobenzyloxycarbonyl group for a hydrogen atom.
2-chlorobenzyloxycarbonyl modified residue
A protein modification that effectively substitutes a napthylacetyl group for a hydrogen atom.
A protein modification that effectively substitutes a mercury atom or a cluster containing mercury for hydrogen atoms, or that coordinates a mercury ion.
modification from DeltaMass - OBSOLETE because redundant and identical to MOD:00414. Remap to MOD:00414.
From DeltaMass: Average Mass: 170 Formula:C7H14O4N1 Monoisotopic Mass Change:170.117 Average Mass Change:170.215
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)
A protein modification that effectively converts an L-threonine residue to S-(2-aminoethyl)-3-methylcysteine.
2-amino-3-(2-aminoethyl)sulfanyl-3-methylbutanoic acid
A protein modification that effectively converts an L-cysteine residue to S-[(acetylamino)methyl]-L-cysteine.
N-(hydroxymethyl)acetamide derivatized L-cysteine
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].
OBSOLETE because this is identical to MOD:00417. modification from DeltaMass
From DeltaMass: (name misspelled "Acrylamidyl Cystenyl") Average Mass: 174 Formula: C6H10O2N2S1 Monoisotopic Mass Change: 174.046 Average Mass Change: 174.221
From DeltaMass: Average Mass: 177. CAUTION - mass does not match formula.
delta-glycosyloxy- (of lysine) or beta-glycosyloxy- (of phenylalanine or tyrosine)
OBSOLETE because redundant with MOD:00757, remap. modification from DeltaMass
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)
A protein modification that effectively converts an L-serine residue to O-benzyl-L-serine.
A protein modification that by reaction of iodoacetic acid effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a carboxymethyl group.
iodoacetic acid derivatized amino-terminal residue
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
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.
A protein modification that effectively substitutes a 2,4,5-trichlorophenyl group for a hydrogen atom.
A protein modification that effectively substitutes a 2,4,6-trimethyloxybenzyl group for a hydrogen atom.
2,4,6-trimethyloxybenzyl modified residue
A protein modification that by reaction of iodoacetamide effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a carboxamidomethyl group.
iodoacetamide derivatized amino-terminal residue
A protein modification that effectively substitutes one hydrogen atom of an L-phenylalanine residue with one chlorine atom.
From DeltaMass: Average Mass: 182 Formula:C9H8O1N1Cl1 Monoisotopic Mass Change:181.029 Average Mass Change:181.623
From DeltaMass: Average Mass: 184 Formula: C9H16O2N2 Monoisotopic Mass Change: 184.12 Average Mass Change: 184.24 with no citation.
A protein modification that effectively converts an L-lysine residue to N6-carboxymethyl-L-lysine.
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].
Modification from DeltaMass. OBSOLETE because not an amino acid modification.
From DeltaMass with no citation, formula incorrect, N and O reversed: Formula: C10H8O1N3 Monoisotopic Mass Change: 190.05 Average Mass Change: 190.18.
A protein modification that effectively converts an L-threonine residue to O-benzyl-L-threonine.
A protein modification that effectively converts an L-cysteine residue to S-benzyl-L-cysteine.
From DeltaMass: misspelled "Benzyl Cystenyl".
A protein modification that inserts or replaces a residue with a naphthylalanine.
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].
A protein modification that effectively converts an L-aspartic acid residue to succinyl beta-aspartyl anhydride.
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].
From DeltaMass: Average Mass: 201 with no citation.
OBSOLETE because erroneous and apparently redundant to MOD:00111. Remap to MOD:00111.
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.
OBSOLETE because redundant and identical to MOD:00504. Remap to MOD:00504.
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)
OBSOLETE because redundant and identical to MOD:00503. Remap to MOD:00503.
From DeltaMass with no citation or formula: Average Mass: 208.
From DeltaMass: Average Mass: 212 with no citation.
From DeltaMass: Average Mass: 213 with no citation.
A protein modification that effectively converts an L-tryptophan residue to N-formyl-L-tryptophan.
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]
A protein modification that effectively converts an L-glutamic acid residue to O5-benzyl-L-glutamate.
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].
A protein modification that effectively converts an L-glutamic acid residue to 2-amino-5-(4-methoxyphenyl)-5-oxopentanoic acid, glutamtic acid anisole adduct.
2-amino-5-(4-methoxyphenyl)-5-oxopentanoic acid (Glu)
From DeltaMass: Average Mass: 222 with no citation.
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).
A protein modification that effectively substitutes a dimethoxybenzhydryl group for a hydrogen atom.
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].
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
From DeltaMass: Average Mass: 238 with no citation.
From DeltaMass: Average Mass: 242 Average Mass Change: 242.3 Notes: blocking group used in peptide synthesis for C,H,Q,N
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).
A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine methyl ester.
From DeltaMass: Average Mass: 252 with no citation.
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
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 converts an L-cysteine residue to S-geranylgeranyl-L-cysteine methyl ester.
S-geranylgeranyl-L-cysteine methyl ester
A protein modification that is produced by formation of an adduct with 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride, Pmc chloride.
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
From DeltaMass: Average Mass: 272 Average Mass Change: 272
From DeltaMass: Average Mass: 289 with no citation.
OBSOLETE because redundant and identical to MOD:01123. Remap to MOD:01123.
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
From DeltaMass: Average Mass: 304 with no citation.
From DeltaMass: Average Mass: 305 with no citation.
OBSOLETE because redundant and identical to MOD:01166. Remap to MOD:01166.
From DeltaMass: Average Mass: 306 Formula: C9H11O2N8P1 Monoisotopic Mass Change: 306.025 Average Mass Change: 306.17
From DeltaMass: Average Mass: 307 with no citation.
From DeltaMass: Average Mass: 313 Formula: C10H12O5N5P1 Monoisotopic Mass Change: 313.058 Average Mass Change: 313.211
From DeltaMass: Average Mass: 327 Formula: C17H17O3N4 Monoisotopic Mass Change: 327.122 Average Mass Change: 327.342
OBSOLETE because redundant and identical to MOD:01165. Remap to MOD:01165.
A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine methyl ester.
S-12-hydroxyfarnesyl-L-cysteine methyl ester
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
From DeltaMass: Average Mass: 365 with no citation.
OBSOLETE because this is a small molecule contaminant and not a modification to a polypeptide. modification from DeltaMass
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.
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.
From DeltaMass: Average Mass: Formula: C20H30O2N4S1 Monoisotopic Mass Change: 394.192 Average Mass Change: 394.534
OBSOLETE because no evidence has been seen for this protein modification. modification from DeltaMass
[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
OBSOLETE because this is a MS contaminant, not a known modification to a polypeptide. modification from DeltaMass
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.
A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two iodine atoms.
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.
From DeltaMass: Average Mass: Formula: C20H30O4N4S1 Monoisotopic Mass Change: 422.199 Average Mass Change: 422.547
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound 15,16-dihydrobiliverdin.
BINDING 15,16-dihydrobiliverdin (covalent; via 1 link)
A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound 15,16-dihydrobiliverdin.
BINDING 15,16-dihydrobiliverdin (covalent; via 2 links)
A protein modification that effectively converts an L-cysteine residue to S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine.
S-(sn-1-Dipalmitoyl-glyceryl)- (on Cysteine)
A protein modification that effectively converts an L-histidine residue to N-tau-(ADP-ribosyl)diphthamide.
From DeltaMass: (name misspelled "N theta -(ADP-ribosyl) diphthamide (of Histidine)") Average Mass: 648
A protein modification that effectively converts an L-cysteine residue to S-(6-FAD)-L-cystine.
From DeltaMass: Average Mass: 784 with no citation. This modification has not been reported [JSG].
dHex1Hex3HexNAc2 N4-glycosylated asparagine
A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a ubiquitin.
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.
A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a nedd8 protein.
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.
phosphorylated residue with neutral loss of phosphate
A protein modification that effectively replaces a hydrogen atom with a carboxylic acid group.
A protein modification that effectively replaces a hydrogen atom with an methylsulfanyl group (thiomethyl group).
A protein modification that effectively converts a source amino acid to 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.
Modified amino acid residue derived from a natural amino acid by a real or hypothetical chemical process.
protein modification categorized by chemical process
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.
protein modification categorized by amino acid modified
A protein modification that modifies an L-selenocysteine 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.
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.
A protein modification that effectively removes oxygen atoms from a residue without the removal of hydrogen atoms.
A protein modification that effectively crosslinks an amino acid residue and 5'-phosphoguanosine through either a phosphodiester or a phosphoramide bond.
From DeltaMass: (formula incorrect, N and O reversed) Average Mass: 345 Formula: C10H12O5N7P1 Monoisotopic Mass Change: 345.047 Average Mass Change: 345.209.
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.
A protein modification that effectively crosslinks an amino acid residue and 5'-phosphoadenosine through either a phosphodiester or a phosphoramide bond.
From DeltaMass: (name misspelled "5'phos adenosinyl") Average Mass: 329
A protein modification that effectively crosslinks an amino acid residue and 5'-phosphouridine through either a phosphodiester or a phosphoramide bond.
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
A protein modification that effectively converts a source amino acid residue to dehydroalanine.
A protein modification that effectively converts a source amino acid residue to L-oxoalanine.
A protein modification that effectively forms a 2-ketoimine of pyruvicacid with a residue amino group.
A protein modification that effectively converts an L-threonine residue to O-acetyl-L-threonine.
(2S,3R)-3-(acetyloxy)-2-aminobutanoic acid
A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylsphingolipidinositolethanolamine.
A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylsphingolipidinositolethanolamine.
LIPID GPI-like-anchor amidated asparagine
A protein modification that effectively converts an L-cysteine residue to S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)-L-cysteine.
(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
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.
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)
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.
(2S)-2-amino-6-([(5S)-5-amino-5-carboxypentylidene]amino)hexanoic acid
CROSSLNK Dehydrolysinonorleucine (Lys-Lys)
A protein modification that effectively converts an L-histidine residue to 1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine.
(S)-2-amino-3-[1-(1,2,3-trihydroxypropan-2-yl)-1H-imidazol-4-yl]propanoic acid
MOD_RES Tele-(1,2,3-trihydroxypropan-2-yl)histidine
N(epsilon)-histidine dihydroxyacetone adduct
A protein modification that effectively converts an L-aspartic acid residue to S-(aspart-4-yloxy) thiocarbonate.
(2S)-2-amino-4-(carboxysulfanyl)oxy-4-oxobutanoic acid
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].
A protein modification that effectively converts an L-alanine residue to N,N-dimethyl-L-alanine.
A protein modification that effectively converts a glycine residue to 2-hydroxyglycine.
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].
A protein modification that effectively converts an L-aspartic acid residue to L-aspartate 4-methyl ester.
(2S)-2-amino-4-methoxy-4-oxobutanoic acid
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].
A protein modification that crosslinks a cysteine and a histidine residue by forming the adduct 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FAD.
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
BINDING FAD (covalent; via 2 links, pros nitrogen)
CROSSLNK 6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-Cys)
A protein modification that effectively cross-links two L-selenocysteine residues to form L-selenocystine,
(R,R)-3,3'-diselane-1,2-diylbis(2-aminopropanoic acid)
bis(alpha-aminopropionic acid)-beta-diselenide
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 substitutes two selenium atoms for two sulfur atoms in L-cystine to form L-selenocystine.
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 converts an L-aspartic acid residue to L-asparagine.
A protein modification that effectively converts an L-threonine residue to either N-acetyl-L-threonne, or O-acetyl-Lthreonine.
A protein modification that inserts or replaces a residue with an L-pyrrolysine residue, a natural pretranslational modification.
modification from Unimod Isotopic label -
Modification from Unimod Chemical derivative. OBSOLETE because duplicate and redundant with MOD:01006. Remap to MOD:01006.
modification from Unimod Chemical derivative -
benzoyl labeling reagent light form - site K
OBSOLETE because redundant, replaced with MOD:01654. Remap to MOD:01654.
5-dimethylaminonaphthalene-1-sulfonyl - site K
A protein modification that effectively converts an L-glutamine residue to N-heptosyl-L-glutamine.
A protein modification that effectively converts an L-serine residue to O-heptosyl-L-serine.
A protein modification that effectively converts an L-arginine residue to an N-heptosyl-L-arginine.
A protein modification that effectively converts an L-threonine residue to O-heptosyl-L-threonine.
A protein modification that effectively converts an L-lysine residue to N6-heptosyl-L-lysine.
A protein modification that effectively converts an L-asparagine residue to N-heptosyl-L-asparagine.
A protein modification that effectively converts an L-lysine residue to N6-[(pyrid-3-yl)acetyl]lysine.
Prompt loss of side chain from oxidised Met
prompt loss of methanethiol from oxidixed methionine
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.
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.
Hex1HexNAc1NeuAc2 O-glycosylated threonine
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.
Hex1HexNAc1NeuAc2 N4-glycosylated asparagine
A protein modification that effectively converts a C-terminal residue to the copper(1+) carboxylate salt.
copper(1+) carboxylate C-terminal residue
A protein modification that effectively converts an L-aspartic acid residue to the copper(1+) aspartate salt.
A protein modification that effectively converts an L-glutamic acid residue to the copper(1+) glutamate salt.
A protein modification that effectively converts an L-lysine residue to N6-(morpholine-2-acetyl)-lysine.
N-succinimidylmorpholine-2-acetate N6-derivatized lysine
A protein modification that effectively converts an L-lysine residue to N6-(carboxamidomethyl)lysine.
A protein modification that effectively converts an L-histidine residue to an iodoacetamide derivatized histidine, either 1'- or 3'-(carboxamidolmethyl)histidine.
modification from Unimod Chemical derivative - OBSOLETE because redundant, the difference component of MOD:01060. Remap to MOD:01060.
A protein modification that effectively converts an L-aspartic acid residue to O4-(carboxamidomethyl)aspartate.
A protein modification that effectively converts an L-glutamic acid residue to O5-(carboxamidomethyl)glutamate.
Sulfanilic Acid (SA), light C12 - site D
Sulfanilic Acid (SA), light C12 - site E
Sulfanilic Acid (SA), heavy C13 - site D
Sulfanilic Acid (SA), heavy C13 - site E
A protein modification that effectively converts an L-threonine residue to O-formyl-L-threonine.
From Unimod: Can occur under CNBr cleavage conditions (70% HCOOH).
A protein modification that effectively converts an L-serine residue to O-formyl-L-serine.
thioacylation of primary amines (N-term and Lys)
This Unimod entry is misdescribed as "thioacylation" [JSG].
thioacylation of primary amines - site N-term
thioacylation of primary amines - site K
A protein modification that effectively converts an L-tyrosine residue into an L-fluorotyrosine.
From Unimod: the citation appears to be correct, but the PMID is not and has been corrected [JSG].
A protein modification that effectively converts an L-tryptophan residue to an L-fluorotryptophan.
A protein modification that effectively converts an L-phenylalanine residue to an L-fluorophenylalanine.
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].
A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one iodine atom.
From DeltaMass: Average Mass: 289 [name misspelled "monoiodated" - JSG].
A protein modification that effectively converts an L-histidine residue to an L-iodohistidine.
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form - site K
A protein modification that effectively converts an L-lysine residue to 3x(13)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.
A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled N6-acetyl-L-lysine.
modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate
A protein modification produced by formation of an adduct of an L-cysteine residue with 4-hydroxynonenal.
A protein modification produced by formation of an adduct of an L-lysine residue with 4-hydroxynonenal.
A protein modification produced by formation of an adduct of an L-histidine residue with 4-hydroxynonenal.
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.
ubiquitination signature tetrapeptidyl lysine
A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled L-aspartic acid 4-methyl ester.
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-glutamic acid 5-methyl ester.
3x(2)H labeled L-glutamic acid 5-methyl ester
A protein modification that effectively converts a C-terminal residue to the potassium carboxylate salt.
potassium carboxylate C-terminal residue
A protein modification that effectively converts an L-glutamioc acid residue to the potassium glutamate salt.
A protein modification that effectively converts an L-aspartic acid residue to the potassium aspartate salt.
OBSOLETE because redundant and identical to MOD:00812 after formula correction. Remap to MOD:00812.
OBSOLETE because redundant and identical to MOD:00813 after formula correction. Remap to MOD:00813.
A protein modification that is produced by reaction of iodouridine monophosphate with an L-tyrosine residue to form an ether linkage.
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-tryptophan residue.
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-phenylalanine residue.
This has a carbon-carbon linkage and not a phosphodiester linkage with UMP.
iodouridine monophosphate derivatized phenylalanine
A protein modification that effectively converts an L-lysine residue to N6-[3-(carboxamidomethylthio)propanoyl]lysine.
OBSOLETE because redundant and identical to MOD:00933. Remap to MOD:00933.
5-hydro-5-methylimidazol-4-one, methylglyoxal arginine adduct (+54 amu)
modification from Unimod Chemical derivative - Malondialdehyde (MDA) adduct
A protein modification that effectively converts an L-lysine residue to 4x(2)H labeled dimethylated L-lysine.
A protein modification that effectively converts an L-serine residue to S-(2-sulfanylethyl)cysteine.
A protein modification that effectively converts an L-threonine residue to 3-methyl-S-(2-sulfanylethyl)cysteine.
3-methyl-S-(2-sulfanylethyl)cysteine (Thr)
6-aminoquinolyl-N-hydroxysuccinimidyl carbamate - site K
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 -
nucleophilic addtion to cytopiloyne - site Y
nucleophilic addtion to cytopiloyne - site S
nucleophilic addition to cytopiloyne - site R
nucleophilic addtion to cytopiloyne - site K
nucleophilic addtion to cytopiloyne - site C
nucleophilic addtion to cytopiloyne - site P
nucleophilic addition to cytopiloyne+H2O - site C
nucleophilic addition to cytopiloyne+H2O - site K
nucleophilic addition to cytopiloyne+H2O - site T
nucleophilic addition to cytopiloyne+H2O - site R
nucleophilic addition to cytopiloyne+H2O - site S
nucleophilic addition to cytopiloyne+H2O - site Y
A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-serine residue.
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-histidine residue.
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-lysine residue.
A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-tyrosine residue.
OBSOLETE because this modification is not supported by the linked literature [PMT]
A protein modification that effectively converts an L-leucine residue to 6x(13)C,1x(15)N isotope labeled L-leucine.
A protein modification that effectively converts an L-isoleucine residue to 6x(13)C,1x(15)N isotope labeled L-isoleucine.
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form - site K
OBSOLETE because this is not supported by the literature [PMT]
OBSOLETE because redundant and identical to MOD:00465. Remap to MOD:00465.
OBSOLETE because redundant and identical to MOD:00464. Remap to MOD:00464.
OBSOLETE because redundant and identical to MOD:00075. Map to MOD:00075.
A protein modification that effectively converts an L-asparagine residue to L-aspartic acid with one (18)O.
OBSOLETE identical and redundant with MOD:00791. Remap to MOD:00791.
A protein modification that effectively converts an L-aspartic acid residue to monosodium L-aspartate.
A protein modification that effectively converts an L-glutamic acid residue to monosodium L-glutamate.
A protein modification that effectively converts an L-proline residue to 5x(13)C labeled L-proline.
In PubMed:12716131, fully (13)C labeled proline apparently resulted from the catabolic conversion of (13)C labeled L-arginine during SILAC.
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.
reduced cysteine 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.
reduced histidine 4-hydroxynonenal adduct
A protein modification that effectively converts an L-threonine residue to 2-amino-3-(methylamino)butanoic acid.
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-serine residue to 2-amino-3-(methylamino)propanoic acid.
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-asparagine residue to an N4-hexosaminyl-L-asparagine.
The natural modifications are N4-(N-acetylamino)galactosyl-L-asparagine (MOD:00832) or N4-(N-acetylamino)glucosyl-L-asparagine (MOD:00831) [JSG].
A protein modification that effectively converts an L-lysine residue to an N4-hexosaminyl-L-lysine, as a synthetic peptide protectting group.
A protein modification that effectively converts an L-tryptophan residue to N1'-hexosaminyl-L-tryptophan.
The natural modification is N1'-mannosyl-L-tryptophan (MOD:00165) [JSG].
A protein modification that effectively converts an L-threonine residue to O-hexosaminyl-L-threonine.
The natural modifications are O-(N-acetylaminogalactosyl)-L-threonine (MOD:00164) or O-(N-acetylaminoglucosyl)-L-threonine (MOD:00806) [JSG].
thiophosphate labeled with biotin-HPDP -site S
thiophosphate labeled with biotin-HPDP -site T
thiophosphate labeled with biotin-HPDP - site Y
A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent light form group.
quaternary amine labeling reagent light form N6-L-lysine
A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+3amu) form group.
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 (+6amu) form group.
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 (+9amu) form group.
quaternary amine labeling reagent heavy form (+9amu) N6-L-lysine
A protein modification that effectively converts an L-lysine residue to 4x(1)H,4x(12)C-labeled N6-succinyl-L-lysine.
Succinic anhydride labeling reagent light form (K)
4x(1)H,4x(12)C-labeled N6-succinyl-L-lysine
A protein modification that effectively converts an L-lysine residue to 4x(2)H-labeled N6-succinyl-L-lysine.
Succinic anhydride labeling reagent, heavy form (+4amu, 4H2), N-term & K
A protein modification that effectively converts an L-lysine residue to 4x(13)C labeled N6-succinyl-L-lysine.
Succinic anhydride labeling reagent, heavy form (+4amu, 4C13), K
Secondary adduct, much less common than cysteine. [Unimod]
Michael addition of BHT quinone methide to histidine
Michael addition of BHT quinone methide to lysine
Michael addition of BHT quinone methide to cysteine
OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other -
OBSOLETE because this is not supported by the linked literature [PMT]
A protein modification that effectively converts an L-tyrosine residue to 9x(13)C labeled L-tyrosine.
A protein modification that effectively converts an L-phenylalanine residue to 9x(13)C labeled L-phenylalanine.
modification from Unimod Chemical derivative - hydroxylethanone
There is no citation for this Unimod entry. Iodoacetic acid derivatization of tryptophan is not mentioned in the citation [JSG].
Modification from Unimod Chemical derivative, Unimod:6 site C
OBSOLETE because identical with MOD:01094. Remap to MOD:01094
A protein modification that effectively converts an L-arginine residue to 6x(13)C labeled L-arginine.
A protein modification that effectively converts an L-leucine residue to 6x(13)C labeled L-leucine.
A protein modification that effectively converts an L-isoleucine residue to 6x(13)C labeled L-isoleucine.
A protein modification that effectively converts an L-lysine residue to 6x(13)C labeled L-lysine.
6x(13)C labeled 4-sulfophenyl isothiocyanate derivatized lysine
OBSOLETE - identical and redundant with MOD:00657. Remap to MOD:00657.
Modification from Unimod Post-translational - Unimod:528.
deamidation followed by a methylation -site Q
A protein modification that effectively converts an L-asparagine residue to L-aspartate 4-methyl ester.
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-lysine residue to N6-ethyl-L-lysine.
The Unimod citation refers to the formation of glutamate ethyl ester and not to either lysine or N-terminal alkylation [JSG].
A protein modification that effectively replaces a hydrogen atom with an ethyl group.
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].
OBSOLETE because redundant and identical to MOD:00530. Remap to MOD:00530.
selenium substitution for sulfur - site M
OBSOLETE because redundant and identical to MOD:00686. Remap to MOD:00686.
selenium substitution for sulfur - site C
OBSOLETE because redundant and identical with MOD:00835. Remap to MOD:00835.
A protein modification that effectively converts an L-threonine residue to 2-amino-3-oxobutanoic acid.
There is no citation for this modification in the Unimod entry. Although mentioned in PubMed:9252331, there is no citation for it there [JSG].
A protein modification that effectively converts an L-asparagine residue to an N4-hexosyl-L-asparagine.
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.
A protein modification that effectively converts an L-threonine residue to an O-hexosyl-L-threonine.
Hydolyzed N-ethylmaeimide adduct, a mixture of isobaric 2- and 3-(S-cysteinyl)-4-(ethylamino)-4-oxobutanoic acid [JSG].
hydrolyzed N-ethylmaleimide cysteine adduct
Hydolyzed N-ethylmaeimide adduct, a mixture of isobaric 2- and 3-(N6-lysyl)-4-(ethylamino)-4-oxobutanoic acid [JSG].
hydrolyzed N-ethylmaleimide lysine adduct
A protein modification that effectively converts an L-tryptophan residue to a nitrated L-tryptophan.
One or more isobaric isomers are produced by nitration with peroxynitrite reagent [JSG].
A protein modification that effectively converts an L-tyrosine residue to a nitrated L-tyrosine.
amidination of lysines or N-terminal amines with methyl acetimidate - site K
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.
Hex1HexNAc1NeuAc1 N4-glycosylated asparagine
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.
Hex1HexNAc1NeuAc1 O-glycosylated threonine
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.
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.
2x(13)C,4x(2)H labeled dimethylated L-lysine
modification from Unimod Isotopic label - Use when labelling post-digest
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form - site N-term
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form - site K
A protein modification that effectively converts an L-lysine residue to the 4-sulfophenyl isothiocyanate adduct, N6-[(4-sulfophenyl)carbamothioyl]lysine.
4-sulfophenyl isothiocyanate N6-derivatized lysine
A protein modification that effectively converts an L-threonine residue to O-thiophospho-L-threonine.
A protein modification that effectively converts an L-serine residue to O-thiophospho-L-serine.
A protein modification that effectively converts an L-tyrosine residue to O4'-thiophospho-L-tyrosine.
fluorescein-5-thiosemicarbazide - site S
fluorescein-5-thiosemicarbazide - site C
fluorescein-5-thiosemicarbazide - site K
fluorescein-5-thiosemicarbazide - site P
fluorescein-5-thiosemicarbazide - site R
A protein modification that effectively replaces a carboxamido group with a carboxyl methyl ester group.
deamidated and methyl esterified residue
A protein modification that effectively converts a residue containing common isotopes to a 6x(13)C,1x(15)N labeled residue.
OBSOLETE bcecause identical and redundant with MOD:00851. Remap to MOD:00851.
A protein modification that effectively converts an L-leucine residue to a (2S)-4-hydroxyleucine.
(2S)-2-amino-4-hydroxy-4-methylpentanoic acid
A protein modification that effectively converts an L-leucine residue to a (2S,4R)-5-hydroxyleucine.
(2S,4R)-2-amino-5-hydroxy-4-methylpentanoic acid
A modification that effectively oxygenates C5 of an L-leucine residue to form a (2S,4R)-5-oxoleucine.
(2S,4R)-2-amino-4-methyl-5-oxopentanoic acid
A protein modification that effectively converts an L-leucine residue to a (2S,4R)-4,5-dihydroxyleucine.
(2S,4R)-2-amino-4,5-dihydroxy-4-methylpentanoic acid
A protein modification that effectively converts an L-isoleucine residue to a (2S,3S,4R)-3,4-dihydroxyisoleucine.
(2S,3S,4R)-2-amino-3,4-dihydroxy-3-methylpentanoic acid
A protein modification that effectively converts an L-isoleucine residue to a (2S,3R,4S)-4-hydroxyisoleucine.
(2S,3R,4S)-2-amino-3-methyl-4-hydroxyvaleric acid
(2S,3R,4S)-2-amino-4-hydroxy-3-methylpentanoic acid
A protein modification that effectively converts an L-isoleucine residue to a (2S,3R,4R)-4,5-dihydroxyisoleucine.
(2S,3R,4R)-2-amino-4,5-dihydroxy-3-methylpentanoic acid
A protein modification that effectively converts an L-tryptophan residue to 2'-methylsulfonyl-L-tryptophan.
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.
2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide
CROSSLNK 2'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-Cys)
A protein modification that effectively converts an L-serine residue to O-palmitoleyl-L-serine.
(2S)-2-amino-3-((9Z)-9-hexadecenoyloxy)propanoic acid
A protein modification that effectively converts an L-methionine residue to N,N,N-trimethyl-L-methionine.
2-trimethylammonio-4-(methylthio)butanoic acid
A protein modification that effectively cross-links two L-cysteine residues and oxidizes a sulfur to form L-cystine S-oxide.
(2R)-2-amino-3-[([(2R)-2-amino-2-carboxyethyl]sulfanyl)sulfinyl]propanoic acid
CROSSLNK S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)
S-[(2R)-2-amino-3-oxopropyl] (2R)-2-amino-3-oxopropane-1-sulfinothioate
A protein modification that effectively converts an L-serine residue to an aminomalonic acid.
A protein modification that effectively converts an L-phenylalanine residue to 3-hydroxy-L-phenylalanine.
(2S,3S)-2-amino-3-hydroxy-3-phenylpropanoic acid
(S)-2-amino-3-(3-hydroxyphenyl)propanoic acid
A protein modification that effectively converts an L-valine residue to 3-hydroxy-L-valine.
(2S)-2-amino-3-hydroxy-3-methylbutanoic acid
A protein modification that effectively converts an L-threonine residue to O-methyl-L-threonine.
A protein modification that effectively converts an L-threonine residue into 1-amino-2-propanol.
A protein modification that effectively crosslinks an L-cysteine residue and an L-isoleucine residue to form L-isoleucine thiazole-4-carboxylic acid.
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)
A protein modification that effectively crosslinks an L-cysteine residue and an L-valine residue to form L-valine thiazole-4-carboxylic acid.
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)
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.
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.
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.
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.
(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.
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.
(2S,3S,5Xi)-5-hydroxy-3-methylpyrrolidine-2-carboxylic acid
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].
A protein modification that effectively crosslinks an L-serine residue and an L-threonine residue to form L-serine 5-methyloxazole-4-carboxylic acid.
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.
(2S)-2-amino-6-(propanoylamino)hexanoic acid
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].
A protein modification that effectively converts an L-lysine residue to an N6-(ADP-ribosyl)-L-lysine.
(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
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)
A protein modification that effectively converts an L-lysine residue to an L-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.
(2S,3S)-2,4-diamino-3-hydroxy-4-oxobutanoic acid
(2S,3S)-2-amino-3-hydroxy-4-butanediamic acid
A protein modification that effectively converts an L-proline residue to a (2S,3R,4R)-3,4-dihydroxyproline.
(2S,3R,4R)-3,4-dihydroxypyrrolidine-2-carboxylic acid
A protein modification that effectively converts an L-leucine residue to a (2S)-4,5,5'-trihydroxyleucine.
(2S)-2-amino-4,5-dihydroxy-4-(hydroxymethyl)pentanoic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-asparagine residue to form L-asparagine thiazole-4-carboxylic acid.
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)
A protein modification that effectively crosslinks an L-cysteine residue and an L-proline residue to form L-proline thiazole-4-carboxylic acid.
2-[(2S)-pyrrolidin-2-yl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Pro-Cys)
A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-threonine thiazole-4-carboxylic acid.
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)
A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazoline-4-carboxylic acid.
(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.
(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
L-threonine thiazoline-4-carboxylic acid
A protein modification that effectively replaces three hydrogen atoms with three hydroxyl groups.
A protein modification that effectively converts an L-leucine residue to an hydroxylated leucine.
A protein modification that effectively converts an L-leucine residue to a monohydroxylated leucine.
A protein modification that effectively converts an L-leucine residue to a dihydroxylated leucine.
A protein modification that effectively converts an L-leucine residue to a trihydroxylated leucine.
A protein modification that effectively converts an L-isoleucine residue to an hydroxylated isoleucine.
A protein modification that effectively converts an L-isoleucine residue to a monohydroxylated isoleucine.
A protein modification that effectively converts an L-isoleucine residue to a dihydroxylated isoleucine.
A protein modification that effectively converts an L-proline residue to a monomethylated proline.
A protein modification that effectively converts an L-threonine residue to a methylated threonine, such as O-methyl-L-threonine.
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.
oxazole/oxazoline 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.
thiazole/thiazoline ring crosslinked residues
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.
oxazole/oxazoline ring crosslinked residues (Ser)
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.
oxazole/oxazoline ring crosslinked residues (Thr)
A protein modification that effectively replaces a hydrogen atom with a palmitoleyl group.
A protein modification that effectively results from forming an adduct with a compound containing a quinaldate, kynurenate, or xanthurenate group.
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.
A protein modification that forms an adduct with a particular isotope labeled compound used as a reagent.
isotope tagged reagent derivatized residue
OBSOLETE because redundant and identical to MOD:00819. Remap to MOD:00819.
A protein modification that forms an adduct with a (13)C labeled compound used as a reagent.
A protein modification that forms an adduct with a (15)N labeled compound used as a reagent.
A protein modification that forms an adduct with a (2)H labeled compound used as a reagent.
A protein modification that effectively converts an L-leucine residue to a (2S,4S)-4,5-dihydroxyleucine.
(2S,4S)-2-amino-4,5-dihydroxy-4-methylpentanoic acid
A protein modification that effectively converts an L-threonine residue into 1-amino-2-propanone.
A protein modification that effectively converts an L-glutamic acid residue to a 4-hydroxy-L-glutamic acid.
(2S,4Xi)-2-amino-4-hydroxypentanedioic 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.
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.
(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 (Cys)
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.
cyclo[(prolylserin)-O-yl] cysteinate (Cys-Pro-Ser cross-link)
A protein modification that effectively converts an L-cysteine residue to S-[2-(pyridin-2-yl)ethyl]-L-cysteine.
2-vinylpyridine derivatized cysteine residue
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
A protein modification that effectively converts an L-cysteine residue to S-[2-(pyridin-4-yl)ethyl]-L-cysteine.
A protein modification that effectively converts a source amino acid residue to an L-glutamyl semialdehyde.
A protein modification that inserts or replaces a residue with a natural, standard, encoded residue.
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.
(2S)-2-amino-3-(4-[(2S)-2-amino-2-carboxyethyl]phenoxy)-3-methylbutanoic acid
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.
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 an L-cysteine residue to L-3,3-dihydroxyoalanine.
A protein modification that effectively converts an L-serine residue to L-3,3-dihydroxyoalanine.
A protein modification that effectively converts an N-formyl-Lmethionine residue to N-(dihydroxymethyl)-L-methionine.
(2S)-2-[(dihydroxymethyl)amino]-4-(methylsulfanyl)butanoic acid
A protein modification that effectively converts an L-methionine residue to N-(dihydroxymethyl)-L-methionine (not known as a natural, post-translational modification process).
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.
A protein modification that effectively converts a source amino acid residue to L-3,3-dihydroxyoalanine.
A protein modification that effectively converts an L-3-oxoalanine residue to L-3,3-dihydroxyoalanine.
A protein modification that modifies an N-formyl-L-methionine residue.
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.
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
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.
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
A protein modification that effectively converts a source amino acid residue to L-glutamate 5-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.
DNA glycosylase proline Schiff base intermediate
This linkage is not a Schiff-base [JSG].
A protein modification that effectively replaces a residue hydroxyl or carboxyl hydrogen with a phosphono group (H2PO3 or 'phosphate').
A protein modification that effectively replaces a hydrogen atom of a residue amino or imino group with a phosphono group (H2PO3 or 'phosphate').
A protein modification that effectively converts an L-serine residue to L-cysteine (not known as a natural, post-translational modification process).
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acetyl group.
A protein modification that effectively converts an N-terminal residue to an 4x(2)H labeled alpha-dimethylamino N-terminal residue.
4x(2)H labeled alpha-dimethylamino N-terminal residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a methyl group.
A protein modification that effectively replaces an L-alanine alpha amino hydrogen with a methyl group.
A protein modification that effectively replaces an L-proline alpha imino hydrogen with a methyl group.
A protein modification that effectively replaces an L-methionine alpha amino hydrogen with a methyl group.
A protein modification that effectively converts an L-methionine residue to an L-methioninium (protonated L-methionine).
protonated L-methionine (L-methioninium) residue
A protein modification that effectively converts an L-methioninium (protonated L-methionine) residue to an N6,N6,N6-trimethyl-L-methionine.
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-cysteine residue to L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) (not known as a natural, post-translational modification process).
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
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 tungsten bis(molybdopterin guanine dinucleotide) (not known as a natural, post-translational modification process).
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-threonine residue to (E)-dehydrobutyrine.
A protein modification that effectively converts an L-threonine residue to (Z)-dehydrobutyrine.
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.
A protein modification that effectively adds neutral hydrogen atoms (proton and electron) to a residue.
A protein modification that effectively converts an L-serine residue to O-[S-(carboxymethyl)phosphopantetheine]-L-serine.
This modification results from the derivatization of the pantetheine sulfhydryl with iodoacetic acid [JSG].
A protein modification that effectively converts an L-serine residue to O-[S-(carboxamidomethyl)phosphopantetheine]-L-serine.
This modification results from the derivatization of the pantetheine sulfhydryl with iodoacetamide [JSG].
A protein modification that effectively converts an L-phenylalanine residue to an 2'-fluoro-L-fluorophenylalanine.
A protein modification that effectively converts an L-phenylalanine residue to an 3'-fluoro-L-fluorophenylalanine.
A protein modification that effectively converts an L-phenylalanine residue into an 4'-fluoro-L-fluorophenylalanine.
A protein modification that effectively converts an L-tryptophan residue into an 4'-fluoro-L-tryptophan.
A protein modification that effectively converts an L-tryptophan residue into an 5'-fluoro-L-tryptophan.
A protein modification that effectively converts an L-tryptophan residue into an 6'-fluoro-L-tryptophan.
A protein modification that effectively substitutes a calcium atom or a cluster containing calcium for hydrogen atoms, or that coordinates a calcium ion.
A protein modification that effectively replaces a residue hydroxyl group with a formyloxy group.
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.
Cross-link 2. This cross-link is usually made by glutamine and releases ammonia, rather than glutamic acid and requiring the consumption of ATP.
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
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 protein N-terminal with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
iTRAQ4plex-114 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
iTRAQ4plex-114 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
iTRAQ4plex-114 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
iTRAQ4plex-114 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
iTRAQ4plex-114 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
iTRAQ4plex-114 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
iTRAQ4plex-115 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
iTRAQ4plex-115 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
iTRAQ4plex-115 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
iTRAQ4plex-115 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
iTRAQ4plex-115 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
iTRAQ4plex-115 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
iTRAQ4plex-115 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
iTRAQ4plex-116 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
iTRAQ4plex-116 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
iTRAQ4plex-116 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
iTRAQ4plex-116 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
iTRAQ4plex-116 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
iTRAQ4plex-116 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
iTRAQ4plex-116 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
iTRAQ4plex-117 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
iTRAQ4plex-117 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
iTRAQ4plex-117 reporter+balance reagent O3-acylated threonine
Modifications that have monoisotopic mass differences from their respective origins that are nominally equal (sometimes called isobaric) at a resolution below 0.1 Da.
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 0.01 Da.
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 0.000001 Da.
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 of 144.099-144.106 Da.
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 144.102062 Da.
modifications with monoisotopic mass differences that are nominally equal at 144.102062 Da
A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups.
iTRAQ4plex reporter+balance reagent acylated residue
A distinct molecular entity produced from a protein or a protein modification as the result of a fragmentation process.
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.
A distinct molecular entity produced as the result of a fragmentation process performed on a particular modified residue.
A protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex reagent derivatized residue.
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 114 reagent derivatized residue.
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 115 reagent derivatized residue.
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 116 reagent derivatized residue.
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 117 reagent derivatized residue.
iTRAQ4plex-117, mTRAQ heavy, reporter fragment
A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance groups.
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 distinct molecular entity produced from a particular amino acid residue as the result of a fragmentation process.
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex-113 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
iTRAQ8plex-113 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
iTRAQ8plex-113 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
iTRAQ8plex-113 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
iTRAQ8plex-113 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
iTRAQ8plex-113 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
iTRAQ8plex-113 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
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 protein N-terminal with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
iTRAQ8plex-114 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
iTRAQ8plex-114 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
iTRAQ8plex-114 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
iTRAQ8plex-114 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
iTRAQ8plex-114 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
iTRAQ8plex-114 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
iTRAQ8plex-115 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
iTRAQ8plex-115 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
iTRAQ8plex-115 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
iTRAQ8plex-115 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
iTRAQ8plex-115 reporter+balance reagent N'-derivatized histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
iTRAQ8plex-115 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
iTRAQ8plex-115 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
iTRAQ8plex-116 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
iTRAQ8plex-116 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
iTRAQ8plex-116 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
iTRAQ8plex-116 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
iTRAQ8plex-116 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
iTRAQ8plex-116 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
iTRAQ8plex-116 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
iTRAQ8plex-117 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
iTRAQ8plex-117 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
iTRAQ8plex-117 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
iTRAQ8plex-117 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
iTRAQ8plex-117 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
iTRAQ8plex-117 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
iTRAQ8plex-117 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
iTRAQ8plex-118 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
iTRAQ8plex-118 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
iTRAQ8plex-118 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
iTRAQ8plex-118 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
iTRAQ8plex-118 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
iTRAQ8plex-118 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
iTRAQ8plex-118 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
iTRAQ8plex-119 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
iTRAQ8plex-119 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
iTRAQ8plex-119 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
iTRAQ8plex-119 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
iTRAQ8plex-119 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
iTRAQ8plex-119 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
iTRAQ8plex-119 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
iTRAQ8plex-121 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
iTRAQ8plex-121 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
iTRAQ8plex-121 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
iTRAQ8plex-121 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
iTRAQ8plex-121 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
iTRAQ8plex-121 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
iTRAQ8plex-121 reporter+balance reagent O3-acylated threonine
Modifications that have monoisotopic mass differences from their respective origins of 304.199039 Da.
modifications with monoisotopic mass differences that are nominally equal at 304.199039 Da
A protein modification that effectively crosslinks an L-serine residue and a glycine residue by an ester bond to form O-glycyl-L-serine.
(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-...)
A protein modification that effectively crosslinks an L-threonine residue and a glycine residue by an ester bond to form O-glycyl-L-threonine.
(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-...)
A protein modification that effectively converts an L-serine residue to O-(2-aminoethylphosphoryl)-L-serine.
(2S)-2-amino-3-([(2-aminoethoxy)(hydroxy)phosphoryl]oxy)propanoic acid
MOD_RES O-(2-aminoethylphosphoryl)serine
A protein modification that effectively converts an L-serine residue to O-cholinephosphoryl-L-serine.
A protein modification that effectively converts an L-serine residue to O-(2,4-diacetamido-2,4-dideoxyglucosyl)-L-serine.
(2S)-2-amino-3-[(2,4-diacetamido-2,4-dideoxy-beta-D-glucopyranosyl)oxy]propanoic acid
A protein modification that effectively converts an L-tryptophan residue to 3'-farnesyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan.
(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
Modifications that have monoisotopic mass differences from their respective origins of 304.205359 Da.
modifications with monoisotopic mass differences that are nominally equal at 304.205359 Da
Modifications that have monoisotopic mass differences from their respective origins of 304.199-304.206 Da.
modifications with monoisotopic mass differences that are nominally equal at 304.199-304.206 Da
A protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex reagent derivatized residue.
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-113 reagent derivatized residue.
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-114 reagent derivatized residue.
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-115 reagent derivatized residue.
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-116 reagent derivatized residue.
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-117 reagent derivatized residue.
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-118 reagent derivatized residue.
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-119 reagent derivatized residue.
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-121 reagent derivatized residue.
A protein modification that effectively converts an L-lysine residue, and an L-methionine residue to S-(L-lysyl)-L-methionine sulfilimine.
(2S)-2-amino-6-([(E)-[(3S)-3-amino-3-carboxypropyl](methyl)-lambda(4)-sulfanylidene]amino)hexanoic acid
A protein modification that effectively converts an L-lysine residue to 2x(15)N labeled L-lysine.
A protein modification that effectively converts an L-arginine residue to 4x(15)N labeled L-arginine.
A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl 2-aminoadipic acid.
(2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanedioic acid
A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl 2-aminoadipic 6-phosphoric anhydride.
(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.
(2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)-6-oxohexanoic acid
A protein modification that effectively converts an L-glutamic acid residue to N2-(L-isoglutamyl)-L-lysine. This is not an isopeptide cross-link.
(2S)-6-amino-2-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid
A protein modification that effectively converts an L-tryptophan residue to 7'-hydroxy-2'-alpha-mannosyl-L-tryptophan.
(2S)-2-amino-3-[7-hydroxy-2-(alpha-D-mannopyranosyl)-1H-indol-3-yl]propanoic acid
CARBOHYD C-linked (Man) hydroxytryptophan
A protein modification that effectively converts an L-threonine residue to L-threonine methyl ester.
methyl (2S,3R)-2-amino-3-hydroxybutanoate
A protein modification that crosslinks a cysteine and a histidine residue by forming the adduct 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FMN.
6-((R)-2-amino-2-carboxyethyl)sulfanyl-8alpha-[4-((S)-2-amino-2-carboxyethyl)imidazol-3-yl]-riboflavin 5'-trihydrogen phosphate
BINDING FMN (covalent; via 2 links, pros nitrogen)
A protein modification that effectively converts an L-tyrosine residue to 3'-iodo-L-tyrosine.
(2S)-2-amino-3-(4-hydroxy-3-iodophenyl)propanoic acid
A protein modification that effectively converts an L-tyrosine residue to 3',5'-diiodo-L-tyrosine.
(2S)-2-amino-3-(4-hydroxy-3,5-diiodophenyl)propanoic acid
A protein modification that effectively converts a glycine residue to glycyl phospho-5'-adenosine.
(2-aminoacetyl)oxy-([(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy)phosphinic acid
aminoacetyl [5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl hydrogen phosphate
glycine monoanhydride with 5'-adenylic acid
A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a dithioester bond to form glycyl cysteine dithioester.
(2R)-2-amino-3-[(aminoacetyl)disulfanyl]propanoic acid
A protein modification that effectively cross-links two L-cysteine residues and adds three sulfur atoms to form trithiocystine.
(2R,2'R)-3,3'-pentasulfane-1,5-diylbis(2-aminopropanoic acid)
A protein modification that effectively converts an L-threonine residue to O-(6-phosphomannosyl)-L-threonine.
(2S,3R)-2-amino-3-[6-phosphonooxy-alpha-D-mannopyranosyloxy]butanoic acid
A protein modification that effectively converts an L-alaine residue and an L-asparagine residue to L-alanyl-L-isoaspartyl cyclopeptide.
(2S,5S)-2-methyl-3,7-dioxo-1,4-diazepane-5-carboxylic acid
CROSSLNK Alanine isoaspartyl cyclopeptide (Ala-Asn)
A protein modification that crosslinks two cysteine residues by formation of a chain of two or more bonded sulfur atoms.
A protein modification that crosslinks two cysteine residues by formation of a chain of three or more bonded sulfur atoms.
A protein modification that crosslinks two or more amino acid residues by forming an adduct with a compound containing a flavin group.
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.
A protein modification that effectively converts a glycine residue to a C-terminal 1-thioglycine.
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.
CROSSLNK (2-aminosuccinimidyl)acetic acid (Asn-Gly)
A protein modification that effectively converts a glycine residue to 1-thioglycine.
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].
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.
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).
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.
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.
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.
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.
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 .
A protein modification that effectively removes or replaces an L-alanine.
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.
A protein modification that effectively removes or replaces an L-arginine.
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.
A protein modification that effectively removes or replaces an L-asparagine.
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.
A protein modification that effectively removes or replaces an L-aspartic acid.
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.
A protein modification that effectively removes or replaces an L-cysteine.
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.
A protein modification that effectively removes or replaces an L-glutamic acid.
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.
A protein modification that effectively removes or replaces an L-glutamine.
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.
A protein modification that effectively removes or replaces a glycine.
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.
A protein modification that effectively removes or replaces an L-histidine.
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.
A protein modification that effectively removes or replaces an L-isoleucine.
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.
A protein modification that effectively removes or replaces an L-leucine.
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.
A protein modification that effectively removes or replaces an L-lysine.
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.
A protein modification that effectively removes or replaces an L-methionine.
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].
A protein modification that effectively removes or replaces an L-phenylalanine.
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.
A protein modification that effectively removes or replaces an L-proline.
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.
A protein modification that effectively removes or replaces an L-serine.
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.
A protein modification that effectively removes or replaces an L-threonine.
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.
A protein modification that effectively removes or replaces an L-tryptophan.
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.
A protein modification that effectively removes or replaces an L-tyrosine.
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.
A protein modification that effectively removes or replaces an L-valine.
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.
A protein modification that effectively removes a natural, standard, encoded residue.
This represents the loss of an encoded residue in a polypeptide.
natural, standard, encoded residue removal
A protein modification that is produced by formation of an adduct with a sulfonyl halide compound used as a reagent.
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 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride.
A protein modification that is produced by reaction with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride, to form N6-Dansyl-lysine.
A protein modification that is produced by reaction with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride, to form an alpha-amino-Dansyl-derivatized residue.
A protein modification that is produced by formation of an adduct with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, Dabsyl chloride.
A protein modification that is produced by reaction with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, dabsyl chloride, to form N6-Dabsyl-lysine.
A protein modification that is produced by reaction with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, dabsyl chloride, to form an alpha-amino-Dabsyl-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.
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
This reagent has a reactive sulfonyl vinyl and typically reacts with the free thiol group of cysteine residues.
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.
A protein modification that effectively converts an L-tyrosine residue to pyruvic acid.
A protein modification that effectively converts an L-glutamine residue to N5-(ADP-ribosyl)-L-glutamine.
(S)-2-amino-4-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)-5-oxopentanoic acid
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.
(S)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]oxy)-butanoic acid
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.
(2S)-2-amino-3-(7-hydroxy-1H-indol-3-yl)propanoic acid
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.
(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
A protein modification that is produced by formation of an adduct with epicocconone.
A protein modification that effectively converts an L-aspartic acid residue to O4-(8alpha-FAD)-L-aspartate.
(2S)-2-amino-4-oxo-4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxybutanoic acid
A protein modification that effectively converts an L-arginine residue to N(omega),N(omega),N'(omega)-trimethyl-L-arginine.
(2S)-2-amino-5-([(dimethylamino)(methylamino)methylidene]amino)pentanoic acid
(2S)-2-amino-5-([(dimethylamino)(methylimino)methyl]amino)pentanoic acid
(2S)-2-amino-6-(chloroamino)hexanoic acid
A protein modification that effectively converts an L-threonine residue to O-(L-isoaspartyl)-L-threonine, using free L-asparagine and releasing ammonia.
(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
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 substitutes a hydrogen atom of an L-lysine residue with a halogen atom.
A protein modification that effectively replaces a hydrogen atom with an N-acetylaminohexose group through a glycosidic bond.
A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminohexosyl)-L-asparagine.
(S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-hexopyranosyl)amino-4-oxobutanoic acid
A protein modification that effectively converts an L-serine residue to O3-(N-acetylaminohexosyl)-L-serine.
(S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-hexopyranosyloxy)propanoic acid
A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminohexosyl)-L-threonine.
(2S,3R)-2-amino-3-(alpha-D-2-acetamido-2-deoxyhexopyranosyloxy)butanoic acid
A protein modification that effectively converts an L-proline residue to O4-(N-acetylamino)hexosyl-L-hydroxyproline.
(2S,4R)-4-[2-acetamido-2-deoxy-alpha-D-hexopyranosyloxy]pyrrolidine-2-carboxylic acid
A protein modification that effectively coverts L-lysine to N6-carbamoyl-L-lysine.
This modification can be produced by hydrogen cyanate, either as a reagent or as released by urea degradation in solution [JSG].
A protein modification that effectively replaces a residue alpha amino or imino hydrogen with a carbamoyl group.
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].
A protein modification that effectively replaces one residue alpha amino or imino hydrogen with one methyl group.
A protein modification that effectively replaces one hydrogen atom of an L-aspartic acid residue with one methyl group.
A protein modification that effectively replaces one hydrogen atom of an L-cysteine residue with one methyl group.
A protein modification that effectively replaces one hydrogen atom of an L-lysine residue with one methyl group.
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.
A protein modification that effectively replaces a residue alpha-amino group with a alpha-palmitoylamino group.
A protein modification that effectively replaces two alpha amino hydrogen atoms with two methyl group.
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.
A protein modification that effectively replaces an alpha-aminium group with a trimethylaminium group.
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.
A protein modification that effectively converts an L-asparagine residue to one of the diastereomeric 3-hydroxy-L-asparagine residues.
A protein modification that effectively converts a carboxyl-terminal residue to an alpha-carboxyl (1-carboxyl) methyl ester.
A protein modification that effectively converts an L-cysteine residue to N-[(12R)-12-hydroxymyristoyl]-L-cysteine.
2-[(12R)-12-hydroxytetradecanoyl]amino-3-sulfanylpropanoic acid
LIPID N-[(12R)-12-hydroxymyristoyl]cysteine
A protein modification that effectively converts an L-cysteine residue to N-(12-ketomyristoyl)-L-cysteine.
2-(12-oxotetradecanoyl)amino-3-sulfanylpropanoic acid
A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl semialdehyde.
A protein modification that effectively replaces a residue alpha amino or imino hydrogen with a (pyrid-3-yl)acetyl group.
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.
(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
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an 3-(carboxamidomethylthio)propanoyl group.
alpha-amino 3-(carboxamidomethylthio)propanoylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an 4-(2-aminoethyl)benzenesulfonyl group.
alpha-amino 4-(2-aminoethyl)benzenesulfonylated residue
A protein modification that effectively replaces an amino group with a trimethylaminium group.
alpha-amino trimethylated protonated-residue
A protein modification that effectively adds a hydrogen cation, a proton, forming a cationic 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.
A protein modification that effectively removes a hydrogen cation, a proton, forming an anionic 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.
A protein modification that effectively converts a source amino acid residue to dehydrobutyrine.
A protein modification that effectively converts an L-methionine residue to dehydrobutyrine, by neutral loss of methyl sulfide.
It is expected that this neutral loss will produce a mix of (E)- and (Z)-isomers [JSG].
A protein modification that effectively replaces a residue hydrogen with an isotope tagged reagent acyl group.
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an isotope tagged reagent acyl group.
isotope tagged reagent N-acylated residue
A protein modification that effectively replaces a residue hydroxyl group with an isotope tagged reagent acyloxy group.
isotope tagged reagent O-acylated residue
isotope tagged reagent alpha-amino 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.
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 iTRAQ8plex reagent reporter+balance groups.
iTRAQ8plex reporter+balance reagent N-acylated residue
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.
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 iTRAQ8plex reagent reporter+balance groups.
iTRAQ8plex reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a residue hydroxyl with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance acyloxy groups.
iTRAQ4plex 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.
iTRAQ8plex reporter+balance reagent O-acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with a Proteome Sciences TMT6plex reporter+balance group.
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
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-126 reagent acylated residue.
A protein modification that effectively replaces a residue amino- or imino-hydrogen with a Proteome Sciences TMT6plex reporter+balance group.
TMT6plex reporter+balance reagent N-acylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a Proteome Sciences TMT6plex reporter+balance group.
TMT6plex reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a residue hydroxyl with one of the Proteome Sciences TMT6plex reagent reporter+balance acyloxy groups.
TMT6plex reporter+balance reagent O-acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
TMT6plex-126 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-126 reporter+balance group.
TMT6plex-126 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
TMT6plex-126 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
TMT6plex-126 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
TMT6plex-126 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
TMT6plex-126 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
TMT6plex-126 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
TMT6plex-127 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-127 reporter+balance group.
TMT6plex-127 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
TMT6plex-127 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
TMT6plex-127 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
TMT6plex-127 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
TMT6plex-127 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
TMT6plex-127 reporter+balance reagent O3-acylated threonine
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-127 reagent acylated residue.
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
TMT6plex-128 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-128 reporter+balance group.
TMT6plex-128 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
TMT6plex-128 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
TMT6plex-128 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
TMT6plex-128 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
TMT6plex-128 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
TMT6plex-128 reporter+balance reagent O3-acylated threonine
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-128 reagent acylated residue.
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
TMT6plex-129 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-129 reporter+balance group.
TMT6plex-129 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
TMT6plex-129 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
TMT6plex-129 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
TMT6plex-129 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
TMT6plex-129 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
TMT6plex-129 reporter+balance reagent O3-acylated threonine
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-129 reagent acylated residue.
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
TMT6plex-130 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-130 reporter+balance group.
TMT6plex-130 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
TMT6plex-130 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
TMT6plex-130 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
TMT6plex-130 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
TMT6plex-130 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
TMT6plex-130 reporter+balance reagent O3-acylated threonine
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-130 reagent acylated residue.
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
TMT6plex-131 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-131 reporter+balance group.
TMT6plex-131 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
TMT6plex-131 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
TMT6plex-131 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
TMT6plex-131 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
TMT6plex-131 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
TMT6plex-131 reporter+balance reagent O3-acylated threonine
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-131 reagent acylated residue.
A protein modification that effectively replaces a residue hydroxyl group with a palmitoleyloxy group.
A protein modification that effectively converts an L-threonine residue to O-palmitoleyl-L-threonine.
(2S,3R)-2-amino-3-((Z)-9-hexadecenoyloxy)butanoic acid
A protein modification that effectively converts an L-threonine residue to O-palmitoyl-L-threonine amide.
The farnesyl cation protein modification reporter fragment produced by fragmentation of some farnesyl modified residues.
The palmityl cation protein modification reporter fragment produced by fragmentation of some palmitoyl modified residues.
Covalent modification of a trimethyllysine residue with secondary loss of a neutral trimethylamine molecular fragment.
N6,N6,N6-trimethyl-L-lysine with neutral loss of trimethylamine
A protein modification that effectively converts an L-lysine residue to N6-octanoyl-L-lysine.
(2S)-2-amino-6-(octanoylamino)hexanoic acid
A protein modification that effectively converts an L-glutamine residue to 5-glutamyl serotonin.
(2S)-2-amino-5-([2-(5-hydroxy-1H-indol-3-yl)ethyl]amino)-5-oxopentanoic acid
A protein modification that effectively converts an L-cysteine residue to S-methylthiocarbonylaminoethylcysteine.
(2R)-2-amino-3-([2-([(methylsulfanyl)carbonyl]amino)ethyl]sulfanyl)propanoic acid
L-cysteine N-(methylthiocarbonyl)aziridine adduct
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 a C-terminal glycine residue to S-(glycyl)-L-cysteine by forming a thioester bond with a free L-cysteine.
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].
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.
(2R)-2-[(aminoacetyl)amino]-3-sulfanylpropanoic acid
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.
(2S)-2-amino-6-([(2S)-2,6-diaminohexanoyl]amino)hexanoic acid
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].
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.
(2S)-2-amino-6-([(3R)-3,6-diaminohexanoyl]amino)-5-hydroxyhexanoic acid
MOD_RES N6-(3,6-diaminohexanoyl)-5-hydroxylysine
lysyl spermidine derivative [misidentification]
A protein modification that effectively converts an L-lysine residue to N6-butanoyl-L-lysine.
(2S)-2-amino-6-(butanoylamino)hexanoic acid
(2S)-2-azanyl-6-(butanoylamino)hexanoic acid
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].
A protein modification that effectively converts an L-serine residue to N-methyl-L-serine.
(2S)-3-hydroxy-2-(methylamino)propanoic acid
A protein modification that effectively converts an L-serine residue to N,N-dimethyl-L-serine.
A protein modification that effectively converts an L-serine residue to N,N,N-trimethyl-L-serine.
(2S)-2-trimethylammonio-3-hydroxypropanoic acid
A protein modification that effectively converts an L-threonine residue to O-(L-isoglutamyl)-L-threonine, using free L-glutamine and releasing ammonia.
(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
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-tyrosine residue to 3'-nitro-L-tyrosine.
(2S)-2-amino-3-(4-hydroxy-3-nitrophenyl)propanoic acid
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.
(2S,2'S)-3,3'-[iminobis(4-hydroxybenzene-3,1-diyl)]bis(2-aminopropanoic acid)
CROSSLNK 5'-tyrosyl-5'-aminotyrosine (Tyr-Tyr) (interchain)
A protein modification that effectively converts an N-terminal L-histidine residue to histidine immonium ion.
This fragment corresponds to the first ion in an a+ series.
A protein modification that effectively converts an N-terminal L-phenylalanine residue to phenylalanine immonium ion.
A protein modification that effectively converts an an N-terminal L-tyrosine residue to tyrosine immonium ion.
A protein modification that effectively converts an N-terminal phosphohistidine residue to phosphohistidine immonium ion.
A protein modification that effectively converts an N-terminal O4'-phospho-L-tyrosine residue to tyrosine immonium ion.
A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine sulfoxide.
S-carboxamidomethyl-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.
1x(13)C,3x(2)H labeled monomethylated residue
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.
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 sulfoxide.
1x(13)C,3x(2)H C(6)-labeled L-methionine sulfoxide
A protein modification that effectively converts an N-terminal 1'-phosphohistidine residue to 1'-phosphohistidine immonium ion.
A protein modification that effectively converts an N-terminal 3'-phosphohistidine residue to 3'-phosphohistidine immonium ion.
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.
A protein modification that effectively replaces an L-serine alpha amino hydrogen with a methyl group.
A protein modification that effectively converts an L-serine residue to an L-serinium (protonated L-serine).
protonated L-serine (L-serinium) residue
A protein modification that effectively converts an L-serinium (protonated L-serine) residue to an N,N,N-trimethyl-L-serine.
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-threonine residue to a methylated threonine, such as O-methyl-L-threonine or L-threonine methyl ester.
A protein modification that effectively results from forming an adduct with a glycosylphosphate through a phosphodiester bond.
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.
CROSSLNK Isoaspartyl glycine isopeptide (Asp-Gly)
CROSSLNK Isoaspartyl glycine isopeptide (Gly-Asp)
A protein modification that effectively converts an L-leucine residue to N,N-dimethyl-L-leucine.
(2S)-2-(dimethylamino)-4-methylpentanoic acid
2-(dimethylazanyl)-4-methylpentanoic acid
A protein modification that effectively converts an L-glutamic acid residue to N-formyl-L-glutamic acid.
A protein modification that effectively replaces an L-leucine alpha amino hydrogen with a methyl group.
A protein modification that effectively converts a residue containing common isotopes to a 5x(13)C,1x(15)N labeled residue.
A protein modification that effectively converts an L-proline residue to 5x(13)C,1x(15)N labeled L-proline.
A protein modification that effectively converts an L-methionine residue to 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 sulfoxide.
5x(13)C,1x(15)N labeled L-methionine sulfoxide
A protein modification that effectively substitutes a morpholine-2-acetyl group for a hydrogen atom.
N-succinimidylmorpholine-2-acetate derivative
A protein modification that effectively cross-links a cysteine and two serine residues to form L-cysteine 3-hydroxy-2,5-pyridinedicarboxylic acid.
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.
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)
A protein modification that effectively converts an L-tryptophan residue to a 2'-hydroxy-L-tryptophan.
(2S)-2-amino-3-(2-hydroxy-1H-indol-3-yl)propanoic acid
2-azanyl-3-(2-hydroxy-1H-indol-3-yl)propanoic acid
A protein modification that effectively converts an L-tryptophan residue to a 2'-oxo-L-tryptophan.
(2S)-2-amino-3-[(3S)-2-oxo-2,3-dihydro-1H-indol-3-yl]propanoic acid
2-azanyl-3-[(3S)-2-oxo-2,3-dihydro-1H-indol-3-yl]propanoic acid
A protein modification that effectively cross-links two tryptophan residues to form 1'-(L-tryptophan-3'-yl)-L-tryptophan.
(2S,2'S)-3,3'-(3'H-1,3'-biindole-3,3'-diyl)bis(2-aminopropanoic acid)
2-amino-3-[2-[2-amino-3-(2-carboxyethyl)-1H-indol-4-yl]-1H-indol-3-yl]propanoic acid
A protein modification that effectively converts an L-lysine residue to N6-succinyl-L-lysine.
(2S)-2-amino-6-[(3-carboxypropanoyl)amino]hexanoic acid
2-azanyl-6-[(3-carboxypropanoyl)azanyl]hexanoic acid
A protein modification that effectively replaces a cysteine sulhydryl hydrogen with an isotope tagged sulfhydryl reagent group.
isotope tagged sufhydryl reagent modified cysteine
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex reporter+balance group.
cysteine-reactive Sixplex Tandem Mass Tag(TM)
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-zero reporter+balance group.
Native cysteine-reactive Tandem Mass Tag(TM)
cysTMT6plex-zero reporter+balance reagent cysteine disulfide
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-126 reporter+balance group.
cysTMT6plex-126 reporter+balance reagent cysteine disulfide
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-127 reporter+balance group.
cysTMT6plex-127 reporter+balance reagent cysteine disulfide
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-128 reporter+balance group.
cysTMT6plex-128 reporter+balance reagent cysteine disulfide
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-129 reporter+balance group.
cysTMT6plex-129 reporter+balance reagent cysteine disulfide
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-130 reporter+balance group.
cysTMT6plex-130 reporter+balance reagent cysteine disulfide
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-131 reporter+balance group.
cysTMT6plex-131 reporter+balance reagent cysteine disulfide
A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine sulfoxide.
A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine sulfone.
A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine sulfone.
A protein modification that effectively converts a residue containing common isotopes to a 5x(13)C-labeled residue.
A protein modification that effectively converts an L-methionine residue containing common isotopes to 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 sulfoxide.
A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine sulfone.
A protein modification that effectively converts an L-lysine residue to N6-[([1-(6-nitro-2H-1,3-benzodioxol-5-yl)ethoxy]carbonyl]lysine.
(2S)-2-amino-6-[([1-(6-nitro-1,3-benzodioxol-5-yl)ethoxy]carbonyl)amino]hexanoic acid
A protein modification that effectively cross-links two L-cysteine residues with a thioether bond to form L-lanthionine.
A protein modification that effectively converts an L-lysine residue to L-lysinoalanine.
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.
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.
Cross-link 2. For the natural form of the lanthionine cross-link see MOD:00120 meso-lanthionine [JSG].
A protein modification that effectively converts an L-isoleucine residue to L-allo-isoleucine.
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.
A protein modification that effectively converts two L-cysteine residues to S-(2-aminovinyl)-L-cysteine.
(2R)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid
A protein modification that effectively converts an L-tryptophan residue to 5'-chloro-L-tryptophan.
(2S)-2-amino-3-(5-chloro-1H-indol-3-yl)propanoic 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.
(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.
(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
L-proline 5-hydroxyoxazole-4-carbothionic acid
A protein modification that effectively converts two L-cysteine residues, and a copper atom to the methanobactin OB3b copper complex.
METAL copper [Cu-methanobactin OB3b complex]
A protein modification that effectively converts an L-cysteine residue to L-cysteine sulfinyl phosphate.
(2R)-2-amino-3-[(phosphonooxy)sulfinyl]propanoic acid
A protein modification that effectively converts an L-cysteine residue to S-(spermidinoglutathion-S-yl)-L-cysteine.
(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
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.
CROSSLNK S-(2-aminovinyl)-D-cysteine (Cys-Cys)
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.
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.
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.
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]
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.
A protein modification that effectively adds one oxygen atom to a sulfur atom of a residue without removing hydrogen atoms.
A protein modification that effectively adds two oxygen atoms to a sulfur atom of a residue without removing hydrogen atoms.
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.
oxazole/oxazoline ring crosslinked residues (Cys)
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.
(2R)-2-amino-2-([2-amino-2-carboxyethyl]sulfanyl)-4-(methylsulfanyl)butanoic acid
CROSSLNK 2-(S-cysteinyl)-methionine (Cys-Met)
Cross-link 2. The chirality around the methionine alpha-carbon has not been determined.
A protein modification that effectively converts an L-cysteine residue to S-(N-acetylamino)glucosyl-L-cysteine.
(2R)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosylsulfanyl)propanoic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form 4-amino-3-isothiazolidinone-L-phenylalanine.
(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
CROSSLNK N,N-(cysteine-1,S-diyl)phenylalanine (Cys-Phe)
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.
(2S)-(2-[S-(L-cystein-S-yl)-L-cysteinyl]amino-2-deoxy-alpha-D-glucopyranosyloxy)-butanedioic acid
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.
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 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.
A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems mTRAQ reagent reporter+balance groups.
mTRAQ 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.
mTRAQ light reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems mTRAQ light reporter+balance group.
mTRAQ light reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces the N6-amino hydrogen atom of a lysine residue with the Applied Biosystems mTRAQ light reporter+balance group.
mTRAQ light reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems mTRAQ light reporter+balance group.
mTRAQ light reporter+balance reagent O4'-acylated tyrosine
Modifications that have monoisotopic mass differences from their respective origins of 140.094963 Da.
modifications with monoisotopic mass differences that are nominally equal at 140.094963 Da
The protein modification reporter fragment produced by an Applied Biosystems mTRAQ light reagent derivatized residue.
A protein modification reporter fragment produced by an Applied Biosystems mTRAQ reagent derivatized residue.
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.
cyclized N-terminal S-carboxamidomethyl-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.
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 converts an L-alanine residue to N-carboxy-L-alanine.
This metastable modification can be formed by a protein N-terminal in solutions with a high concentration of dissolved carbon dioxide [JSG].
A protein modification that effectively converts an L-alanine residue to N-carboxy-L-valine.
A protein modification that effectively replaces an N6-amino hydrogen atom of L-lysine with an acyl group.
4x(1)H,4x(12)C-labeled alpha-amino succinylated residue
A protein modification that effectively converts an L-cysteine residue and an L-arginine residue to 2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid.
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.
(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
L-threonine 5-hydroxyoxazole-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.
METAL copper [Cu-methanobactin SB2 complex]
(2S)-2-amino-6-[(4-aminobutyl)amino]hexanoic acid
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.
(2S)-2-amino-4-(2-[(2S)-2-amino-2-carboxyethyl]phenyl)-3-methylbutanoic acid
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.
5-imidazolinone ring crosslinked residues (Gly)
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.
5-imidazolinone ring crosslinked residues (Cys)
A protein modification that effectively replaces a hydrogen atom with a 4-aminobutyl group, usually derived from spermidine.
A protein modification that effectively replaces a hydrogen atom with a biotinyl group.
A protein modification that effectively replaces a hydrogen atom with an sulfanyl or substituted sulfanyl group.
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.
A protein modification that effectively removes two neutral hydrogen atoms (proton and electron) from a residue.
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.
(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
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.
(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 (fMet)
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.
N-[(L-histidin-1'-yl)methyl]-L-methionine (Met)
A protein modification that effectively converts an L-lysine residue to N6-crotonyl-L-lysine.
(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
A protein modification that effectively converts an L-lysine residue to N6-malonyl-L-lysine.
(2S)-2-amino-6-[(carboxyacetyl)amino]hexanoic acid
2-azanyl-6-[(carboxyacetyl)azanyl]hexanoic acid
A protein modification that effectively replaces a hydrogen atom with an propanoyl group.
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 3x(12)C-labeled propanoyl group.
alpha-amino 3x(12)C-labeled propanoylated residue
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.
Trifluoroacetic acid has been observed to form adducts in both negative and positive mode analysis (Mark Collins, private communication) [JSG].
A protein modification that effectively converts an L-isoleucine residue to 5-hydroxy-3-methyl-L-proline.
(2S)-5-[(diaminomethylidene)amino]-2-(dimethylamino)pentanoic acid
(2S)-5-carbamimidamido-2-(dimethylamino)pentanoic acid [tautomer]
A protein modification that effectively crosslinks an L-arginine residue and an L-cysteine residue to form arginine thiazole-4-carboxylic acid.
2-[(1S)-1-amino-4-([diaminomethylidene]amino)butyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Arg-Cys)
A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-cysteine 5-methyloxazole-4-carboxylic acid.
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.
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.
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)
A protein modification that effectively crosslinks two L-serine residues to form serine oxazole-4-carboxylic acid.
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)
A protein modification that effectively crosslinks an L-serine residue and an L-threonine residue to form L-serine 5-methyloxazoline-4-carboxylic acid.
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.
A protein modification that effectively converts an L-methionine residue to dehydromethionine.
A protein modification that effectively converts an L-methioninium (protonated L-methionine) residue to dehydromethionine.
This process accounts only for cyclizaation and not protonation. The alternative process (MOD:01906) accounts for both protonation and cyclization.
A protein modification that effectively converts a residue to the 4-sulfophenyl isothiocyanate adduct, alpha-amino-[(4-sulfophenyl)carbamothioyl] residue.
alpha-amino-[(4-sulfophenyl)carbamothioyl] residue
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.
6x(13)C labeled 4-sulfophenyl isothiocyanate alpha-amino derivatized residue
A protein modification that effectively substitutes one hydrogen atom of a residue with one fluorine atom.
A protein modification that effectively substitutes one hydrogen atom of a residue with one chlorine atom.
A protein modification that effectively substitutes one hydrogen atom of a residue with one bromine atom.
A protein modification that effectively substitutes one hydrogen atom of an L-tryptophan residue with one chlorine atom.
A protein modification that effectively converts a 5-hydroxy-L-lysine residue to O5-galactosyl-L-hydroxylysine.
Secondary to RESID:AA0028. This intermediate is rarely observed [JSG].
A protein modification that effectively converts an L-alanine residue to N-formyl-L-alanine.
A protein modification that effectively converts an L-tyrosine residue to O4'-(N-acetylamino)galactosyl-L-tyrosine.
(2S)-2-amino-3-(D-2-acetamido-2-deoxygalactopyranosyloxy)phenylpropanoic acid
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.
A protein modification that effectively converts an L-lysine residue to (2S,5S)-5-hydroxylysine.
(2S,5S)-2,6-diamino-5-hydroxyhexanoic acid
2,6-diamino-2,3,4,6-tetradeoxyhexonic acid
alpha,epsilon-diamino-delta-hydroxycaproic acid
A protein modification that effectively converts an L-aspartic acid residue to (2S,3S)-3-hydroxyaspartic acid.
(2S,3S)-2-amino-3-hydroxybutanedioic acid
A protein modification that effectively converts an L-histidine residue to 3-hydroxy-L-histidine.
(2S)-2-amino-3-hydroxy-3-(1H-imidazol-4-yl)propanoic acid
A protein modification that effectively converts an L-aspartic acid residue to D-aspartic acid.
A protein modification that effectively converts an L-serine residue to 3-methoxydehydroalanine.
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.
(2S)-2-amino-6-([(2S)-2-amino-3-carboxypropanoyl]amino)hexanoic acid
A protein modification that effectively converts an L-cysteine residue to S-octanoyl-L-cysteine.
(2S)-2-amino-3-(octanoylsulfanyl)propanoic acid
A protein modification that effectively converts an L-lysine residue to (2S,5R)-5-hydroxylysine.
(2S,5R)-2,6-diamino-5-hydroxyhexanoic acid
A protein modification that effectively converts an L-aspartic acid residue to one of the diastereomeric 3-hydroxy-L-aspartic acid residues.
A protein modification that effectively converts an L-tyrosine residue to O4'-glycosyltyrosine.
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.
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.
A protein modification that effectively converts an L-asparagine residue to D-aspartic acid.
A protein modification that effectively converts an L-lysine residue to N6-phospho-L-lysine.
(2S)-2-amino-6-(phosphonoamino)hexanoic acid
(2S)-2-azanyl-6-(phosphonoamino)hexanoic acid
A protein modification that effectively cross-links two lysine residues with a carbon-nitrogen bond to form L-lysinonorleucine..
(2S)-2-amino-6-([(5S)-5-amino-5-carboxypentyl]amino)hexanoic acid
(2S,2'S)-6,6'-iminobis(2-aminohexanoic acid)
A protein modification that effectively cross-links four L-lysine residues to form desmosine.
A protein modification that effectively cross-links four L-lysine residues to form isodesmosine.
A protein modification that effectively converts an L-lysine residue to N6-oleoyl-L-lysine.
(2S)-2-amino-6-([(9Z)-octadec-9-enoyl]amino)hexanoic acid
A protein modification that effectively converts an L-methionine residue to N-palmitoyl-L-methionine.
(2S)-2-(hexadecanoylamino)-4-(methylsulfanyl)butanoic acid
2-(hexadecanamido)-4-(methylsulfanyl)butanoic acid
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.
(2R)-2-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-3-sulfanylpropanoic acid
2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid
2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid (Asn)
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.
2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid (Asp)
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.
(4S)-4-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-5-oxopentanoic acid
2-(2-aminosuccinimidyl)pentanedioic acid
2-(2-aminosuccinimidyl)pentanedioic acid (Asn)
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.
2-(2-aminosuccinimidyl)pentanedioic acid (Asp)
A protein modification that effectively converts a source amino acid residue to D-aspartic acid.
A protein modification that crosslinks two adjacent residues by formation of a pyrrolidione ring.
A protein modification that forms (2-aminosuccinimidyl)acetic acid by crosslinking either an aspartic acid residue or an asparagine residue with the following residue.
2-aminosuccinimide ring crosslinked residues
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.
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.
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.
CROSSLNK isoaspartyl threonine ester (Thr-Asp)
O-(L-isoaspartyl)-L-threonine (cross-link)
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.
(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
A protein modification that effectively cross-links a phenylalanine and two tyrosine residues to form coelenterazine.
A protein modification that effectively converts an L-glutamine residue to L-isoglutamyl histamine.
(2S)-2-amino-5-([2-(1H-imidazol-5-yl)ethyl]amino)-5-oxopentanoic acid
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.
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.
A protein modification that effectively converts four L-cysteine residues and a four-iron cluster to tetrakis-L-cysteinyl tetrairon octanitrosyl.
tetrakis-L-cysteinyl tetrairon octanitrosyl
A protein modification that effectively converts an L-selenocysteine residue to dehydroalanine.
L-alaninato bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese pentoxide
A protein modification that effectively converts an L-arginine residue to (3R)-3-hydroxy-L-arginine.
(2S,3R)-2-amino-5-[(diaminomethylidene)amino]-3-hydroxypentanoic acid
2-amino-5-(carbamimidamido)-3-hydroxypentanoic acid [tautomer]
2-amino-5-[(aminoiminomethyl)amino]-3-hydroxypentanoic acid [tautomer]
2-amino-5-guanidino-3-hydroxypentanoic acid
A protein modification that effectively converts an L-proline residue to 2-hydroxyproline.
(2R)-2-hydroxypyrrolidine-2-carboxylic acid
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.
bis-L-cysteinyl bisglutathion-S-yl diiron disulfide
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.
tris-L-cysteinyl L-glutamato 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.
tris-L-cysteinyl L-glutamin-O6-yl tetrairon tetrasulfide
OBSOLETE because redundant and identical to MOD:01785. Remap to MOD:01785.
A protein modification that effectively converts an L-asparagine residue to N4-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-asparagine.
(2S)-2-amino-4-[(2,4-diacetylamino-2,4,6-trideoxy-beta-D-glucopyranosyl)amino]-4-oxobutanoic acid
A protein modification that effectively converts an L-serine residue to O-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-serine.
(2S)-2-amino-4-[(2,4-diacetamido-2,4,6-trideoxy-beta-D-glucopyranosyl)oxy]propanoic acid
A protein modification that effectively converts an L-serine residue to O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucosyl)-L-serine.
(2S)-2-amino-3-[(2-acetamido-4-glycerylamino-2,4,6-trideoxy-D-glucopyranosyl)oxy]propanoic acid
A protein modification that effectively converts an L-lysine residue to 2xC(13),3x(2)H labeled N6-acetyl-L-lysine.
Acetate labeling reagent (K) (heavy form, +5amu)
2xC(13),3x(2)H labeled N6-acetyl-L-lysine
OBSOLETE because redundant and identical to MOD:00720. Remap to MOD:00720.
A protein modification that effectively converts an L-arginine residue to omega-N-(N-acetylamino)glucosyl-L-arginine.
(2S)-2-amino-5-[(amino[(2-N-acetylamino-2-deoxy-D-glucopyranosyl)amino]methylidene)amino]pentanoic acid
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.
(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,6R)-2,6-diamino-3-methyl-4-thiaheptanedioic acid
2-azanyl-3-[(2-azanyl-2-carboxyethyl)sulfanyl]butanoic acid
A protein modification that effectively converts an L-cysteine residue to S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine.
(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
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.
(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
A protein modification that effectively converts an L-glutamic acid residue to N2-ornithine.
(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
A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl coenzyme A thioester.
(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 intermediate
A protein modification that effectively converts an L-lysine residue to N6-(3-phosphoglyceryl)-L-lysine.
(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
A protein modification that effectively converts an L-methionine residue to S-methyl-L-methionine.
A protein modification that effectively converts an L-cysteine residue to S-(poly-3-hydroxybutyrate)-L-cysteine.
MOD_RES S-poly(beta-hydroxybutyryl)lysine
A protein modification that effectively converts an L-serine residue to O3-(poly-3-hydroxybutyrate)-L-serine.
(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
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.
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.
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.
A protein modification that effectively converts an L-arginine residue to N4-glycosyl-arginine.
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.
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
A protein modification that effectively converts a glycine residue to N,N-dimethyllglycine.
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.
(2R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid
(2R,5R)-2,5-diamino-5-methyl-4-thiahexanedioic acid
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.
(2S)-2,4-diamino-2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-4-oxobutanoic 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)-L-serine.
(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.
(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.
(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
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.
(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
A protein modification that effectively converts a glycine residue to a glycinium (protonated glycine).
A protein modification that effectively converts a glycinium (protonated glycine) residue to an N,N,N-trimethylglycine.
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.
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.
alpha-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.
These are typical lanthionine-like crosslinks.
beta-carbon thioether crosslinked residues
A protein modification that effectively converts an L-tryptophan residue to N1'-formyl-L-tryptophan.
This modifications has not been reported as commonly encountered [JSG].
A protein modification that effectively converts an L-tryptophan residue to N2-formyl-L-tryptophan.
A protein modification that effectively replaces a hydrogen atom with an butanoyl group.
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).
A protein modification that effectively replaces a residue amino or imino hydrogen with a butanoyl group.
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a butanoyl group.
A protein modification that effectively converts an L-lysine residue to N6-retinylidene-(11-cis)-L-lysine.
(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).
(2S)-2-amino-6-[3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid
N6-retinylidene-L-lysine (unspecified geometric isomer)
A protein modification that effectively replaces a hydrogen atom with a stearoyl group.
A protein modification that effectively replaces a residue sulfanyl group with a palmitoleylsulfanyl group.
A protein modification that effectively replaces an O3-hydroxy hydrogen atom of L-serine with an acyl group.
A protein modification that effectively replaces an O3-hydroxy hydrogen atom of L-threonine with an acyl group.
A protein modification that effectively replaces an sulfanyl hydrogen atom of L-cysteine with an acyl group.
A protein modification that effectively replaces a residue sulfanyl group with a stearoylsulfanyl group.
A protein modification that effectively converts an L-lysine residue to N6-palmitoleyl-L-lysine.
A protein modification that effectively replaces a residue amino group with a palmitoleylamino group.
A protein modification that effectively converts an L-lysine residue to N6-stearoyl-L-lysine.
A protein modification that effectively replaces a residue amino group with a stearoylamino group.
A protein modification that effectively replaces a residue amino group with a oleoylamino group.
A protein modification that effectively replaces a hydrogen atom with a oleoyl group.
A protein modification that effectively converts an L-lysine residue to N6-linoloyl-L-lysine.
A protein modification that effectively replaces a residue amino group with a linoloylamino group.
A protein modification that effectively replaces a hydrogen atom with a linoloyl group.
A protein modification that effectively converts an L-lysine residue to N6-arachidonoyl-L-lysine.
A protein modification that effectively replaces a residue amino group with an arachidonoylamino group.
A protein modification that effectively replaces a hydrogen atom with an arachidonoyl group.
A protein modification that effectively converts an L-lysine residue to N6-timnodonoyl-L-lysine.
A protein modification that effectively replaces a residue amino group with a timnodonoylamino group.
A protein modification that effectively replaces a hydrogen atom with a timnodonoyl group.
A protein modification that effectively converts an L-lysine residue to N6-cervonoyl-L-lysine.
A protein modification that effectively replaces a residue amino group with a cervonoylamino group.
A protein modification that effectively replaces a hydrogen atom with a cervonoyl group.
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.
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.
Glutamyl-transpeptidase cleaves glutathione into cysteinylglycine (Cys-Gly) and a Glu residue. [PubMed:28537416]
A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a URM1 protein.
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 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)
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)
modification from Unimod N-linked glycosylation, dHex Hex(4) HexNAc(5)
dHex1Hex4HexNAc5 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, dHex(2) Hex(4) HexNAc(5)
dHex2Hex4HexNAc5 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, dHex Hex(5) HexNAc(3)
dHex1Hex5HexNAc3 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, dHex Hex(3) HexNAc(6)
dHex1Hex3HexNAc6 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, dHex Hex(6) HexNAc(3)
dHex1Hex6HexNAc3 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, Hex(9)HexNAc(2)
modification from Unimod N-linked glycosylation, Hex(7) HexNAc(2)
A protein modification that effectively replaces one hydrogen atom of an L-histidine residue with one methyl group.
A protein modification that effectively replaces a hydrogen group with a amino group
A protein modification that contains an L-alanine residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-arginine residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-asparagine residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-aspartic acid residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-cysteine residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-glutamic acid residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-glutamine residue crosslinked to one or more amino acid residues.
A protein modification that contains a glycine residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-histidine residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-isoleucine residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-leucine residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-lysine residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-methionine residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-phenylalanine residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-proline residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-serine residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-threonine residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-tryptophan residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-tyrosine residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-valine residue crosslinked to one or more amino acid residues.
A protein modification that contains an D-asparagine residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-selenocysteine residue crosslinked to one or more amino acid residues.
A protein modification that contains an N-formyl-L-methionine residue crosslinked to one or more amino acid residues.
crosslinked N-formyl-L-methionine residue
A protein modification that contains an D-phenylalanine residue crosslinked to one or more amino acid residues.
A protein modification that contains an D-serine residue crosslinked to one or more amino acid residues.
A protein modification that contains an L-alanine residue coordinated to one or more metal atoms or metal clusters.
metal or metal cluster coordinated L-alanine residue
A protein modification that contains an L-aspartic acid residue coordinated to one or more metal atoms or metal clusters.
metal or metal cluster coordinated L-aspartic acid residue
A protein modification that contains an L-cysteine residue coordinated to one or more metal atoms or metal clusters.
metal or metal cluster coordinated L-cysteine residue
A protein modification that contains an L-glutamic acid residue coordinated to one or more metal atoms or metal clusters.
metal or metal cluster coordinated L-glutamic acid residue
A protein modification that contains an L-glutamine residue coordinated to one or more metal atoms or metal clusters.
metal or metal cluster coordinated L-glutamine residue
A protein modification that contains an L-histidine residue coordinated to one or more metal atoms or metal clusters.
metal or metal cluster coordinated L-histidine residue
A protein modification that contains an L-methionine residue coordinated to one or more metal atoms or metal clusters.
metal or metal cluster coordinated L-methionine residue
A protein modification that contains an L-serine residue coordinated to one or more metal atoms or metal clusters.
metal or metal cluster coordinated L-serine residue
A protein modification that contains an L-selenocysteine residue coordinated to one or more metal atoms or metal clusters.
metal or metal cluster coordinated L-selenocysteine residue
A protein modification that contains an L-lysine residue coordinated to one or more metal atoms or metal clusters.
metal or metal cluster coordinated L-lysine residue
A protein modification that contains an L-tyrosine residue coordinated to one or more metal atoms or metal clusters.
metal or metal cluster coordinated L-tyrosine residue
A protein modification that contains an L-arginine residue coordinated to one or more metal atoms or metal clusters.
metal or metal cluster coordinated L-arginine residue
A protein modification that effectively replaces a hydrogen atom with an nitrosyl (NO) group.
A protein modification that effectively replaces one or more hydrogen atoms with one or more acetyl groups.
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a succinyl group.
A protein modification that effectively removes two neutral hydrogen atoms (proton and electron) and a water moiety from a 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.
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.
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.
A protein modification that effectively substitutes a hydrogen atom of an L-phenylalanine residue with a bromine atom.
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.
adenosine diphosphoribosyl (ADP-ribosyl) modified residue
A protein modification that effectively replaces a natural, standard, encoded residue.
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 crosslinks an L-serine residue and 5'-phosphouridine through a phosphodiester bond to form O-(phospho-5'-uridine)-L-serine.
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.
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.
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.
A protein modification that effectively converts an L-lysine residue to N6-(2-hydroxyisobutanoyl)-L-lysine.
A protein modification that effectively converts an L-lysine residue to N6-((3R)-3-hydroxybutanoyl)-L-lysine.
A protein modification that effectively converts an L-lysine residue to N6-glutaryl-L-lysine.
A protein modification that effectively converts a D-asparagine residue to N4-methyl-D-asparagine.
A protein modification that modifies a D-asparagine residue.
A chemical transformation driven by a radical reaction.
A hydroxyl substition induced by a radical reaction.
residue modified by radical hydroxylation
A protein modification that effectively transforms an L-histidine residue to N2-formyl asparagine
(2S)-4-amino-2-formamido-4-oxobutanoic acid
A protein modification that effectively transforms a histidine side chain to that of 2-Amino-4,5-dioxopentanoic acid
A protein modification that effectively converts a L-Phenylalanine residue to 2-hydroxy-L-phenylalanine.
2-amino-3-(2-hydroxyphenyl)propanoic acid
A protein modification that effectively substitutes a hydroxy group at position 4 of L-phenylalanine
(2S)-2-amino-3-(4-hydroxyphenyl)propanoic acid
A protein modification that effectively converts an L-tyrosine residue to L-2',5'-dihydroxyphenylalanine.
2-amino-3-(2,5-dihydroxyphenyl)propanoic acid
A protein modification that effectively converts an L-tryptophan residue to a 4-hydroxy-L-tryptophan.
(S)-2-Amino-3-(4-hydroxy-1H-indol-3-yl)propanoic acid
A protein modification that effectively converts an L-tryptophan residue to a 5-hydroxy-L-tryptophan.
(S)-2-Amino-3-(5-hydroxy-1H-indol-3-yl)propanoic acid
A protein modification that effectively converts an L-tryptophan residue to a 6-hydroxy-L-tryptophan.
A protein modification that effectively converts an L-tryptophan residue to a oxindolylalanine.
2-amino-3-(2-oxoindolin-3-yl)propanoic acid
A protein modification that effectively converts an L-proline residue to 5-hydroxy-L-proline
(2S,5S)-5-hydroxypyrrolidine-2-carboxylic acid
A protein modification that effectively converts an L-leucine residue to a (2S,4S)-5-hydroxyleucine.
(2S,4S)-2-amino-5-hydroxy-4-methylpentanoic acid
A protein modification that converts an L-tryptophan residue to 4,5-Dihydroxytryptophan.
(2S)-2-amino-3-(4,5-dihydroxy-1H-indol-3-yl)propanoic acid
A protein modification that converts an L-tryptophan residue to 5,6-Dihydroxytryptophan.
(2S)-2-amino-3-(5,6-dihydroxy-1H-indol-3-yl)propanoic acid
A protein modification that converts an L-tryptophan residue to 5,7-Dihydroxytryptophan.
(2S)-2-amino-3-(5,7-dihydroxy-1H-indol-3-yl)propanoic acid
A protein modification that converts an L-tryptophan residue to dioxindolylalanine.
(2S)-2-amino-3-(3-hydroxy-2-oxo-1H-indol-3-yl)propanoic acid
(alphaS)-alpha-Amino-2,3-dihydro-3-hydroxy-2-oxo-1H-indole-3-propanoic acid
A protein modification that effectively converts an L-phenylalanine residue to a monohydroxylated phenylalanine.