YOD1 Human Recombinant Protein

Protein ubiquitination controls many intracellular processes, including cell cycle progression, transcriptional activation, and signal transduction. This dynamic process, involving ubiquitin conjugating enzymes and deubiquitinating enzymes, adds and removes ubiquitin. Deubiquitinating enzymes are cysteine proteases that specifically cleave ubiquitin from ubiquitin-conjugated protein substrates. The protein encoded by this gene belongs to a DUB subfamily characterized by an ovarian tumor (OTU) domain. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2013]

YOD1: Hydrolase that can remove conjugated ubiquitin from proteins and participates in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by triming the ubiquitin chain on the associated substrate to facilitate their threading through the VCP/p97 pore. Ubiquitin moieties on substrates may present a steric impediment to the threading process when the substrate is transferred to the VCP pore and threaded through VCP's axial channel. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Able to cleave both polyubiquitin and di- ubiquitin. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Lipid Metabolism - unsaturated fatty acid biosynthesis; Secondary Metabolites Metabolism - limonene and pinene degradation; Protease; C2H2-type zinc finger protein; Ubiquitin-specific protease; EC 3.4.19.12

Chromosomal Location of Human Ortholog: 1q32.2

Molecular Function: protein binding; metal ion binding; ubiquitin-specific protease activity

Biological Process: ER-associated protein catabolic process; unfolded protein response