USP7
USP7, also known as HAUSP or ubiquitin C-terminal hydrolase 7, is a ubiquitin specific peptidase of the peptidase C19 family. It removes ubiquitin from target proteins, including p53 and WASH, and so regulates their activity. Browse Assay Genie's current range of USP7 research reagents below, or read on for the biology behind the target.
USP7 is a deubiquitinating enzyme that belongs to the peptidase C19 family, which includes the ubiquitinyl hydrolases. It deubiquitinates target proteins such as the tumour suppressor p53 and WASH, which is essential for endosomal protein recycling. In doing so it regulates their activities by counteracting the opposing ubiquitin ligase activity of other proteins, namely HDM2 for p53 and TRIM27 for WASH. This balance between ubiquitin ligases and deubiquitinases makes USP7 a useful node for studying how protein stability is controlled.
The USP7 gene encodes a protein that UniProt records in the nucleus, the cytoplasm, PML bodies and on chromosomes. This spread of locations is consistent with a role in several cellular processes. HGNC places the gene in the ubiquitin specific peptidases group, and orthologues are annotated in both mouse and rat as Usp7. Researchers who work with the USP7 protein often study it alongside other members of the USP family.
The symbol HAUSP comes from the previous HGNC name, ubiquitin specific peptidase 7 (herpes virus-associated). That name reflects a link to viral infection. Upon Epstein-Barr virus infection, the viral EBNA1 protein interacts with USP7 and increases its association with PML proteins. This is required for the polyubiquitylation and degradation of PML. On the disease side, mutations in the USP7 gene have been implicated in a neurodevelopmental disorder.
USP7 deubiquitinates p53 and opposes the ubiquitin ligase activity of HDM2, making it central to studies of tumour suppressor regulation.
USP7 deubiquitinates WASH, which is essential for endosomal protein recycling, and counteracts TRIM27 ligase activity in this process.
In Epstein-Barr virus infection, EBNA1 raises USP7 association with PML proteins, driving PML polyubiquitylation and degradation.
Mutations in the USP7 gene have been implicated in a neurodevelopmental disorder, so the protein is relevant to disease genetics studies.
USP7 is a ubiquitinyl hydrolase that removes ubiquitin from substrate proteins such as p53 and WASH. It regulates their activities by counteracting ubiquitin ligases, including HDM2 and TRIM27, which act in the respective pathways.
USP7 is also known as HAUSP. UniProt names the protein ubiquitin C-terminal hydrolase 7, and its previous HGNC name was ubiquitin specific peptidase 7 (herpes virus-associated). The enzyme carries the EC number 3.4.19.12.
Mouse and rat both have a Usp7 orthologue. In humans, mutations in the gene have been implicated in a neurodevelopmental disorder. Check the datasheet of any product for its validated reactivity.
Other ubiquitin specific peptidases and deubiquitinating enzymes with research reagents at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q93009; product specifications from Assay Genie datasheets.