ubiquitin carboxyl-terminal hydrolase 47; deubiquitinating enzyme 47; ubiquitin thiolesterase 47; ubiquitin-specific-processing protease 47 (USP47)
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Function
- ubiquitin-specific protease that specifically deubiquitinates monoubiquitinated DNA polymerase beta (POLB), stabilizing POLB thereby playing a role in base-excision repair[3]
- acts as a regulator of cell growth & genome integrity
- may also indirectly regulates CDC25A expression at a transcriptional level
- thiol-dependent hydrolysis of ester, thioester, amide, peptide & isopeptide bonds formed by the C-terminal Gly of ubiquitin
- interacts with BTRC & FBXW11
- interacts with POLB
Structure
belongs to the peptidase C19 family
Compartment
Alternative splicing
named isoforms=3
Expression
- expressed in skeletal muscle, heart & testis
Notes
- initially thought to catalytically inactive[2]
More general terms
Additional terms
References
- ↑ UniProt http://www.uniprot.org/uniprot/Q96K76.html
- ↑ 2.0 2.1 Quesada V et al Cloning and enzymatic analysis of 22 novel human ubiquitin- specific proteases. Biochem Biophys Res Commun. 2004 Jan 30;314(1):54-62. PMID: https://www.ncbi.nlm.nih.gov/pubmed/14715245
- ↑ 3.0 3.1 Parsons JL et al USP47 is a deubiquitylating enzyme that regulates base excision repair by controlling steady-state levels of DNA polymerase beta. Mol Cell. 2011 Mar 4;41(5):609-15. PMID: https://www.ncbi.nlm.nih.gov/pubmed/21362556