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The removal of one or more ubiquitin moieties from a protein. Any process that modulates the frequency, rate or extent of protein deubiquitination. Protein deubiquitination is the removal of one or more ubiquitin moieties from a protein. Any process that decreases the frequency, rate or extent of protein deubiquitination. Protein deubiquitination is the removal of one or more ubiquitin moieties from a protein. Any process that modulates the frequency, rate or extent of the covalent alteration of one or more amino acid residues within a protein. A protein modification process by which one or more covalently attached moieties of a small protein, such as ubiquitin or a ubiquitin-like protein, are removed from a target protein. Any process that stops, prevents or reduces the frequency, rate or extent of the chemical reactions and pathways involving a protein, occurring at the level of an individual cell. 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). Any process that stops, prevents or reduces the frequency, rate or extent of the covalent alteration of one or more amino acid residues within a protein. 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: negative regulation of protein deubiquitination
Acc: GO:0090086
Aspect: Biological Process
Desc: Any process that decreases the frequency, rate or extent of protein deubiquitination. Protein deubiquitination is the removal of one or more ubiquitin moieties from a protein.
Proteins in PDR annotated with:
   This term: 1 [Search]
   Term or descendants: 1 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0090086 - negative regulation of protein deubiquitination (interactive image map)

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Created and Maintained by: Michael Riffle