USP15 Proteins

Protein Information

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.

Synonyms

4921514G19Rik; AI327321; deubiquitinating enzyme 15; deubiquitinating enzyme Ubp109; E430033I05Rik; Gcap18; granule cell antiserum positive 18; Kiaa0529; MGC131982; MGC149838; MGC74854; Ubiquitin carboxyl-terminal hydrolase 15; ubiquitin carboxyl-terminal hydrolase of 109 kDa; ubiquitin specific peptidase 15; ubiquitin specific protease 15; ubiquitin thioesterase 15; ubiquitin thiolesterase 15; ubiquitin-specific-processing protease 15; ubp109; UNPH-2; Unph4; Usp15