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The formation of the non-fluorescent protein chromophore cross-link from the alpha-carboxyl carbon of residue n, a glutamic acid, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. This modification is found in the GFP-like non-fluorescent red chromoprotein from the sea anemone Radianthus macrodactylus. null The covalent linkage of heme to peroxidase via dihydroxyheme-L-aspartyl ester-L-glutamyl ester-L-methionine sulfonium. The acetylation of the N-terminal glutamic acid of proteins; catalyzed by peptide alpha-N-acetyltransferase. The incorporation of iron into an iron-sulfur cluster by tris-L-cysteinyl-L-cysteine persulfido-bis-L-glutamato-L-histidino tetrairon. The covalent linkage of heme to peroxidase via dihydroxyheme-L-aspartyl ester-L-glutamyl ester. The modification of peptidyl-glutamic acid. The incorporation of nickel into a 3Fe-2S complex by tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide. The incorporation of nickel into a 3Fe-2S complex by tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide. The incorporation of iron into a 3Fe-2S cluster by tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide. The posttranslational cross-linking of a cysteine residue to a glutamic acid residue to form 4-(S-L-cysteinyl)-L-glutamic acid. The posttranslational modification of peptidyl-glutamic acid residues by the covalent attachment of ethanolamine, itself further modified by the addition of a phosphoglycerol unit. The formation of a C-terminal peptidyl-polyglutamic acid to form a peptidyl-N-L-glutamyl-poly-L-glutamic acid C-terminus. The posttranslational addition of one or more alpha-linked glutamyl units to the gamma carboxyl group of peptidyl-glutamic acid. This modification produces peptidyl-glutamic acid poly-ADP-ribose found in a number of nuclear proteins under certain conditions including the repair of single strand DNA breaks. The activated form of the generating enzyme poly(ADP-ribose) polymerase is itself modified in this way. The gamma-carboxylation of peptidyl-glutamic acid; catalyzed by the vitamin K dependent gamma-glutamyl carboxylase. The incorporation of iron into a 3Fe-2S cluster via tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide. The alteration of an amino acid residue in a peptide. The formation of an isopeptide cross-link between peptidyl-glutamate and peptidyl-glycine to produce N-(L-isoglutamyl)-glycine, as found in the antibiotic microcin J25. The addition of an ester group to a glutamic acid residue in a protein. 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).

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: peptidyl-glutamic acid modification
Acc: GO:0018200
Aspect: Biological Process
Desc: The modification of peptidyl-glutamic acid.
Proteins in PDR annotated with:
   This term: 0
   Term or descendants: 8 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0018200 - peptidyl-glutamic acid modification (interactive image map)
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