Ubiquitin carboxyl-terminal hydrolase 17-like protein 1 (USP17L1)

Ubiquitin carboxyl-terminal hydrolase 17-like protein 1 (USP17L1) is a cysteine-type deubiquitinating enzyme that removes ubiquitin from conjugated proteins to regulate cellular functions such as protein stability, cell proliferation, the cell cycle, apoptosis, cell migration, and response to viral infection[2][3]. It belongs to the ubiquitin-specific protease family, whose members influence cellular homeostasis by recycling ubiquitin and modulating the degradation and function of numerous protein substrates. Evidence for direct disease association, biomarkers, or drug interactions specific to USP17L1 is currently lacking, but the family is broadly studied in cancer biology and infection. USP17L1 is predicted to localize to the cytosol, nucleus, and endoplasmic reticulum, reflecting roles in diverse intracellular processes[2].

Other names

USP17L1Ubiquitin specific peptidase 17 like family member 1Deubiquitinating enzyme 17-like protein 1Ubiquitin thioesterase 17-like protein 1Ubiquitin-specific-processing protease 17-like protein 1USP17LUSP17L1Pputative ubiquitin carboxyl-terminal hydrolase 17-like protein 1

Inhibition of deubiquitinating activity (theoretical; no known drugs) Modulation of cell cycle regulation, apoptosis, and protein stability via effects on ubiquitin removal