USP13 Antibody – Rabbit Polyclonal

USP13: Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum- associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34- containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data. Belongs to the peptidase C19 family. 2 isoforms of the human protein are produced by alternative splicing.

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

Chromosomal Location of Human Ortholog: 3q26.2-q26.3

Cellular Component: lysosome

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

Biological Process: cell proliferation; proteasomal ubiquitin-dependent protein catabolic process; regulation of transcription, DNA-dependent; protein stabilization; melanocyte differentiation; autophagy; regulation of autophagy