Peptide Sequence: MAAATLTSKL YSLLFRRTST FALTIIVGVM FFERAFDQGA DAIYDHINEG KLWKHIKHKY ENK
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.
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Protein Aliases: Complex III subunit 9; Complex III subunit X; Cytochrome b-c1 complex subunit 9; Cytochrome c1 non-heme 7 kDa protein; cytochrome C1, nonheme 7kDa protein; HSPC051; HSPC119; HSPC151; QCR9; Ubiquinol-cytoChrome c reductase; ubiquinol-cytochrome c reductase complex (7.2 kD); Ubiquinol-cytochrome c reductase complex 7.2 kDa protein; ubiquinol-cytochrome c reductase, complex III subunit X, 7.2kDa; UCCR7.2; UCRC
Gene Aliases: HSPC051; HSPC119; HSPC151; QCR9; UCCR7.2; UCRC; UQCR10
UniProt ID: (Human) Q9UDW1
Entrez Gene ID: (Human) 29796