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Addition of multiple ubiquitin moieties to a protein, forming a ubiquitin chain. A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 29 of the ubiquitin monomers, is added to a protein. K29-linked ubiquitination targets the substrate protein for degradation. The process by which one or more ubiquitin moieties are added to a protein. Addition of a single ubiquitin moiety to a protein. The modification of histones by addition of ubiquitin groups. 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 ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink. A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 63 of the ubiquitin monomers, is added to a protein. K63-linked ubiquitination does not target the substrate protein for degradation, but is involved in several pathways, notably as a signal to promote error-free DNA postreplication repair. A protein ubiquitination process in which ubiquitin monomers are attached to a protein, and then ubiquitin polymers are formed by linkages between lysine residues at position 11 of the ubiquitin monomers. K11-linked polyubiquitination targets the substrate protein for degradation. The anaphase-promoting complex promotes the degradation of mitotic regulators by assembling K11-linked polyubiquitin chains. The process by which a ubiquitin moiety, or multiple moieties, are covalently attached to the target protein, thereby initiating the degradation of that protein. Any process that activates or increases the frequency, rate or extent of the addition of ubiquitin moieties to a protein. 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 or removed from a target protein. Any process that modulates the frequency, rate or extent of the addition of ubiquitin moieties to a protein. Any process that stops, prevents or reduces the frequency, rate or extent of the addition of ubiquitin moieties to a protein. null 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. A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 48 of the ubiquitin monomers, is added to a protein. K48-linked ubiquitination targets the substrate protein for degradation. 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 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: protein ubiquitination
Acc: GO:0016567
Aspect: Biological Process
Desc: The process by which one or more ubiquitin moieties are added to a protein.
Synonyms:
  • protein ubiquitinylation
  • protein ubiquitylation
Proteins in PDR annotated with:
   This term: 436 [Search]
   Term or descendants: 741 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0016567 - protein ubiquitination (interactive image map)

YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle