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The process by which one or more ubiquitin moieties are added to a protein. The formation of a covalent cross-link between or within protein chains. The formation of a covalent cross-link between or within peptide chains, where either the amino group or the carboxyl group, or both, are not attached to the alpha carbon. The alteration of an amino acid residue in a peptide. A protein modification process by which one or more moieties of a small protein, such as ubiquitin or a ubiquitin-like protein, are covalently attached to a target protein. The modification of peptidyl-lysine. The formation of an isopeptide cross-link between peptidyl-lysine and peptidyl-glycine to produce N6-glycyl-L-lysine. This is distinct from the formation of the thiolester intermediate, which occurs during ubiquitination. The modification of peptidyl-glycine. The covalent alteration of one or more amino acids occurring in a protein after the protein has been completely translated and released from the ribosome.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: isopeptide cross-linking via N6-glycyl-L-lysine
Acc: GO:0018276
Aspect: Biological Process
Desc: The formation of an isopeptide cross-link between peptidyl-lysine and peptidyl-glycine to produce N6-glycyl-L-lysine. This is distinct from the formation of the thiolester intermediate, which occurs during ubiquitination.
Proteins in PDR annotated with:
   This term: 0
   Term or descendants: 0


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0018276 - isopeptide cross-linking via N6-glycyl-L-lysine (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle