Ubiquitin carboxyl-terminal hydrolase 17-like protein 13 (USP17L13)

Ubiquitin carboxyl-terminal hydrolase 17-like protein 13 (USP17L13) is a cysteine-type deubiquitinating enzyme that is predicted to remove conjugated ubiquitin from specific protein substrates, thereby regulating processes such as protein stability and apoptosis. While it shares functional features with other USPs, its biological activities and disease associations have not been thoroughly characterized. Available bioinformatics data indicate a likely role in protein regulatory networks typical of the USP family, with potential involvement in cell cycle control and cell signaling. No definitive drug interactions, validated disease roles, or established biomarkers are currently reported for USP17L13 specifically[4][3].

Other names

USP17L13Ubiquitin specific peptidase 17-like family member 13Ubiquitin carboxyl-terminal hydrolase 17-like protein 13U17LD proteinGeneCards identifiers: GC04P009216, GC04P009230, GC04P009238, GC04P010112

For any future targeted drugs: inhibition of enzymatic deubiquitinating activity would increase ubiquitinated protein turnover. For USP inhibitors in general: promote degradation of USP substrates by blocking deubiquitination.