Ubiquitin specific peptidase 17 like family member 30 (USP17L30)

Ubiquitin specific peptidase 17 like family member 30 (USP17L30) is an enzyme part of the deubiquitinase (DUB) family, specifically characterized as a cysteine-type peptidase with deubiquitinase activity. It is responsible for removing ubiquitin moieties from target proteins, thereby regulating their stability, cellular location, or activity. USP17L30 is implicated in multiple cellular processes, including the positive regulation of epithelial cell apoptosis, cell cycle progression, cell proliferation, migration, and response to viral infection. It exerts its function primarily within the nucleolus and acts via protein deubiquitination as part of ubiquitin-dependent protein catabolic pathways. While its paralogs and other DUB family members are more frequently studied in the context of cancer and neurodegeneration, USP17L30’s specific involvement in disease is being explored due to its fundamental roles in cell death and proliferation control.

Other names

USP17L30Ubiquitin carboxyl-terminal hydrolase 17-like protein 24USP17L24USP17USP17HUSP17IUSP17JUSP17KUSP17LUSP17MDeubiquitinating enzyme 17Ubiquitin thioesterase 17Ubiquitin-specific-processing protease 17

Drugs targeting deubiquitinases (DUBs) generally act as inhibitors, blocking the enzyme's catalytic activity to modulate ubiquitination of substrates and downstream pathways. For USP17L30, theoretical mechanisms would involve inhibiting its ability to remove ubiquitin from target proteins, affecting cell cycle, proliferation, or apoptosis pathways. No drug-specific mechanism is recorded for USP17L30.