Ubiquitin specific peptidase 17-like family member 2 (USP17L2)

Ubiquitin specific peptidase 17-like family member 2 (USP17L2, commonly called DUB3) is a cysteine-type deubiquitinating enzyme in the peptidase C19 family. It removes ubiquitin from specific protein substrates, thereby regulating multiple cellular processes. Key functions include controlling cell proliferation by stabilizing critical cell cycle proteins (such as CDC25A) and modulating localization and activation of small GTPases (such as NRAS and HRAS) via the deubiquitination of RCE1. USP17L2 also regulates cell migration, apoptosis, and the innate immune response by acting on proteins such as SUDS3, and cytoplasmic immune receptors like RIG-I and IFIH1. Dysregulation of USP17L2 has been linked to cancer and other proliferative diseases. The enzyme is not currently directly targeted by approved drugs, but its biological roles make it an area of active research as a potential therapeutic target, especially in oncology.

Other names

DUB3USP17USP17HUSP17IUSP17JUSP17KUSP17LUSP17MDeubiquitinating enzyme 3Deubiquitinating protein 3Ubiquitin carboxyl-terminal hydrolase 17Ubiquitin carboxyl-terminal hydrolase 17-like protein 2Ubiquitin thioesterase 17-like protein 2Ubiquitin-specific-processing protease 17-like protein 2Deubiquitinating enzyme 17-like protein 2Ubiquitin specific peptidase 17-like 2

Inhibition of deubiquitinase activity (theoretically, for any substances or tool compounds developed in research may act by inhibiting USP17L2’s cysteine-type deubiquitinase activity, leading to increased ubiquitination and degradation of its substrates)