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Protein Page:
USP7 (human)

Overview
USP7 an enzyme that removes ubiquitin from its protein substrates. Binds to the herpes virus protein VMW110 that may therefore modulate its substrate specificity or activity to stabilize viral proteins. Regulates MDM2 and has a dynamic role in the p53-MDM2 pathway. Is reported to deubiquitinate and stabilize p53. Note: This description may include information from UniProtKB.
Protein type: EC 3.4.19.12; Protease; Ubiquitin conjugating system; Ubiquitin-specific protease
Chromosomal Location of Human Ortholog: 16p13.3
Cellular Component: cytosol; nuclear body; nucleoplasm; nucleus
Molecular Function: cysteine-type endopeptidase activity; p53 binding; protein binding; protein C-terminus binding; transcription factor binding; ubiquitin protein ligase binding; ubiquitin-specific protease activity
Biological Process: inhibition of NF-kappaB transcription factor; maintenance of DNA methylation; protein deubiquitination; protein stabilization; regulation of transcription factor activity; transcription-coupled nucleotide-excision repair
Reference #:  Q93009 (UniProtKB)
Alt. Names/Synonyms: Deubiquitinating enzyme 7; HAUSP; Herpes virus-associated ubiquitin-specific protease; Herpesvirus-associated ubiquitin-specific protease; TEF1; Ubiquitin carboxyl-terminal hydrolase 7; ubiquitin specific peptidase 7 (herpes virus-associated); ubiquitin specific protease 7 (herpes virus-associated); Ubiquitin thioesterase 7; Ubiquitin-specific-processing protease 7; UBP7; USP7
Gene Symbols: USP7
Molecular weight: 128,302 Da
Basal Isoelectric point: 5.33  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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USP7

Protein Structure Not Found.
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