Ubiquitin Specific Peptidase 5 (USP5) Antibody – Rabbit Polyclonal

Ubiquitin (see MIM 191339)-dependent proteolysis is a complex pathway of protein metabolism implicated in such diverse cellular functions as maintenance of chromatin structure, receptor function, and degradation of abnormal proteins. A late step of the process involves disassembly of the polyubiquitin chains on degraded proteins into ubiquitin monomers. USP5 disassembles branched polyubiquitin chains by a sequential exo mechanism, starting at the proximal end of the chain (Wilkinson et al., 1995 [PubMed 7578059]).[supplied by OMIM, Mar 2010]

USP5: Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys- 63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition. Belongs to the peptidase C19 family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 3.4.19.12; Ubiquitin-specific protease; Protease

Chromosomal Location of Human Ortholog: 12p13

Cellular Component: lysosome

Molecular Function: protein binding; omega peptidase activity; zinc ion binding; cysteine-type endopeptidase activity; ubiquitin-specific protease activity

Biological Process: ubiquitin-dependent protein catabolic process; positive regulation of proteasomal ubiquitin-dependent protein catabolic process