Ubiquitin specific peptidase 17 like family member 15 (USP17L15)

Ubiquitin specific peptidase 17 like family member 15 (USP17L15) is a cysteine-type deubiquitinase enzyme that removes conjugated ubiquitin from substrate proteins, thereby regulating protein stability and participating in cellular pathways such as apoptosis, cell cycle progression, protein deubiquitination, and cellular stress responses[1][3][5][6][7][11]. USP17L15 is predicted to localize to the cytosol, nucleus, and endoplasmic reticulum, and is part of a gene family with related deubiquitinase paralogs[1][10][12]. Although its detailed tissue distribution and disease associations are not well characterized, its involvement in protein and cell cycle regulation suggests it may have broader relevance for diseases characterized by apoptosis and abnormal cell proliferation[3][7]. No specific drugs, mechanisms of action, or established biomarkers are currently documented for this target.

Other names

Ubiquitin carboxyl-terminal hydrolase 17-like protein 15USP17L15USP17-like family member 15

Enzyme inhibition (for any potential drugs, general to deubiquitinases; no specific known drugs or MOA documented)