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The posttranslational cross-linking of a tyrosine residue to a tryptophan residue and a methionine residue to form S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium. The posttranslational hydroxylation of peptidyl-tryptophan, to form peptidyl-L-3-hydroxytryptophan. The posttranslational cross-linking of a tryptophan residue to tryptophyl quinone to form 4'-(L-tryptophan)-L-tryptophyl quinone, a cofactor found at the active site of methylamine dehydrogenase. The alteration of an amino acid residue in a peptide. The posttranslational oxidation of peptidyl-tryptophan to form tryptophan-6,7-dione, otherwise known as tryptophyl quinone, which is further modified by cross-linking to either tryptophan or cysteine. The formation of a C-terminal peptidyl-tryptophan amide by hydrolysis and oxidation of an interior Trp-Gly peptide in a secreted protein. The posttranslational glycosylation of protein via peptidyl-tryptophan, 1'-glycosyl-L-tryptophan; it is uncertain whether this is an N-glycoside linkage (as indicated), and which particular hexose is involved. The glycosylation of a carbon atom of a peptidyl-tryptophan residue. The posttranslational modification of an N-terminal peptidyl-tryptophan residue to form peptidyl-N2-succinyl-L-tryptophan. The posttranslational bromination of peptidyl-tryptophan, to form peptidyl-L-6'-bromotryptophan. The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification). The chemical alteration of a tryptophan residue in a peptide.

View Gene Ontology (GO) Term


Name: peptidyl-tryptophan modification
Acc: GO:0018211
Aspect: Biological Process
Desc: The chemical alteration of a tryptophan residue in a peptide.
Proteins in PDR annotated with:
   This term: 0
   Term or descendants: 0


GO:0018211 - peptidyl-tryptophan modification (interactive image map)

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