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Ubiquitin specific peptidase 17 like family member 25 (USP17L25)
- Target
- USP17L25
- Molecular classification
- Enzyme, Deubiquitinating enzyme, Cysteine-type peptidase, Ubiquitin-specific protease
01
Overview
Ubiquitin specific peptidase 17 like family member 25 (USP17L25) is a member of the ubiquitin-specific protease (USP) family of cysteine proteases that specifically removes ubiquitin from conjugated proteins. This enzyme plays a critical role in regulating the stability, localization, and activity of numerous proteins involved in cell proliferation, apoptosis, and cell migration. It has RNA binding and hyaluronic acid binding activity, localizes mainly to the nucleolus, and influences epithelial cell apoptosis and other ubiquitin-dependent proteolytic processes. USP17L25 and its broader gene family have been implicated as potential targets in cancer biology, especially in the regulation of epithelial-mesenchymal transition and in neurodegenerative conditions such as Machado-Joseph disease.
- Other names
- Ubiquitin carboxyl-terminal hydrolase 17-like protein 24USP17L24USP17USP17HUSP17IUSP17JUSP17KUSP17LUSP17MDeubiquitinating enzyme 17Ubiquitin thioesterase 17Ubiquitin-specific-processing protease 17
02
Mechanism of action
Removal of conjugated ubiquitin from substrate proteins, thereby regulating protein degradation, signaling, and function
03
Biological functions
Protein deubiquitinationRegulation of ubiquitin-dependent protein catabolic processPositive regulation of epithelial cell apoptotic processCell proliferationCell cycle progressionApoptosisCell migrationCellular response to viral infection
04
Disease associations
Cancer (implicated via epithelial-mesenchymal transition, oncogenesis)Neurodegenerative disease (association with Machado-Joseph disease)
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