USP24 Products

Description

Modification of target proteins by ubiquitin participates in a wide array of biological functions. Proteins destined for degradation or processing via the 26 S proteasome are coupled to multiple copies of ubiquitin. However, attachment of ubiquitin or ubiquitin-related molecules may also result in changes in subcellular distribution or modification of protein activity. An additional level of ubiquitin regulation, deubiquitination, is catalyzed by proteases called deubiquitinating enzymes, which fall into four distinct families. Ubiquitin C-terminal hydrolases, ubiquitin-specific processing proteases (USPs),1 OTU-domain ubiquitin-aldehyde-binding proteins, and Jab1/Pad1/MPN-domain-containing metallo-enzymes. Among these four families, USPs represent the most widespread and represented deubiquitinating enzymes across evolution. USPs tend to release ubiquitin from a conjugated protein. They display similar catalytic domains containing conserved Cys and His boxes but divergent N-terminal and occasionally C-terminal extensions, which are thought to function in substrate recognition, subcellular localization, and protein-protein interactions.

Bioinformatics

Entrez	23358 Human
Uniprot	AAH29660 Human AAH29660.1 Human Q9UPU5 Human
Product By Gene ID	23358
Alternate Names	Deubiquitinating enzyme 24 EC 3.4.19.12 FLJ31309 KIAA1057ubiquitin carboxyl-terminal hydrolase 24 ubiquitin specific peptidase 24 ubiquitin specific protease 24 ubiquitin thioesterase 24 Ubiquitin thiolesterase 24 ubiquitin-specific processing protease 24 Ubiquitin-specific-processing protease 24