Ubiquitin specific peptidase 17 like family member 27 (USP17L27)

Ubiquitin specific peptidase 17 like family member 27 (USP17L27) is an enzyme that removes conjugated ubiquitin from specific proteins, regulating cellular processes including protein turnover via the ubiquitin-proteasome system. USP17L27 is implicated in controlling cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. It is part of the cysteine-type deubiquitinase family and is mainly localized in the nucleolus, acting as a regulatory protein in the deubiquitination pathway. Paralogs of USP17L27 share similar functions and clinical associations. Defects or dysregulation of related deubiquitinating enzymes have been linked to cancer and neurodegenerative diseases, but direct disease association for USP17L27 remains to be clarified.

Other names

Ubiquitin carboxyl-terminal hydrolase 17-like protein 24USP17L24USP17USP17HUSP17IUSP17JUSP17KUSP17LUSP17MDeubiquitinating enzyme 17Ubiquitin thioesterase 17Ubiquitin-specific-processing protease 17

Not defined for drugs targeting this molecule; deubiquitinating enzyme inhibitors are a class of candidate molecules in general, but none specific to USP17L27 reported