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USP7

Official Full Name
ubiquitin specific peptidase 7 (herpes virus-associated)
Background
Ubiquitin carboxyl-terminal hydrolase 7 (USP7) is a ubiquitin specific protease or a deubiquitylating enzyme that cleaves ubiquitin from its substrates.[Saridakis, 2005] Since ubiquitylation (polyubiquitination) is most commonly associated with the stability and degradation of cellular proteins, Ubiquitin carboxyl-terminal hydrolase 7 activity generally stabilizes its substrate proteins. Ubiquitin carboxyl-terminal hydrolase 7 is most popularly known as a direct antagonist of Mdm2, the E3 ubiquitin ligase for the tumor suppressor protein, p53.[Canning, 2004]
Synonyms
USP7; ubiquitin specific peptidase 7 (herpes virus-associated); HAUSP, ubiquitin specific protease 7 (herpes virus associated); ubiquitin carboxyl-terminal hydrolase 7; ubiquitin thioesterase 7; deubiquitinating enzyme 7; ubiquitin-specific-processing protease 7; herpesvirus-associated ubiquitin-specific protease; Herpes virus-associated ubiquitin-specific protease; ubiquitin specific protease 7 (herpes virus-associated); TEF1; HAUSP; UBP; ubiquitin specific protease 7

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