Ubiquitin specific peptidase 17 like family member 24 (USP17L24)

Ubiquitin specific peptidase 17 like family member 24 (USP17L24) is a cysteine-type deubiquitinating enzyme that removes conjugated ubiquitin from specific substrate proteins, thereby regulating cellular processes such as protein degradation, cell proliferation, cell cycle progression, apoptosis, migration, and responses to viral infection. It is primarily localized in the nucleolus and contributes to the positive regulation of epithelial cell apoptosis and protein catabolism via the ubiquitin-proteasome system. Disease associations include acute intermittent porphyria and processes linked to cancer biology due to its fundamental role in controlling protein turnover and signaling pathways.

Other names

Ubiquitin carboxyl-terminal hydrolase 17-like protein 24Ubiquitin-specific-processing protease 17Deubiquitinating enzyme 17Ubiquitin thioesterase 17USP17USP17HUSP17IUSP17JUSP17KUSP17LUSP17MUSP17L25USP17L26USP17L27EC 3.4.19.12

Inhibition of deubiquitinase activity could reduce protein stabilization, influence apoptosis, and modulate cellular signaling.