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Ubiquitin specific peptidase 17 like family member 28 (USP17L28)
- Target
- USP17L28
- Molecular classification
- Enzyme, Deubiquitinase, Cysteine-type peptidase
01
Overview
Ubiquitin specific peptidase 17 like family member 28 (USP17L28) encodes a deubiquitinating enzyme that removes conjugated ubiquitin from substrate proteins, regulating their stability and turnover. It is a protein-coding gene belonging to the USP17 family and contributes to important cellular mechanisms, including cell cycle progression, apoptosis, cell migration, and response to viral infection. USP17L28 is localized in the nucleolus and exhibits cysteine-type deubiquitinase activity along with RNA and hyaluronic acid binding[1][8][9]. Its functional paralog, USP17L27, shares related activities. While USP17L28 has not yet been directly linked to specific drug interactions or validated as a clinical biomarker or therapeutic target, its family members have associations with cancer and cell death regulation.
- Other names
- Ubiquitin carboxyl-terminal hydrolase 17-like protein 24USP17L24USP17USP17HUSP17IUSP17JUSP17KUSP17LUSP17MDeubiquitinating enzyme 17Ubiquitin thioesterase 17Ubiquitin-specific-processing protease 17
02
Biological functions
Protein deubiquitinationRegulation of epithelial cell apoptosisPositive regulation of cell cycleCell proliferationCell migrationCellular response to viral infectionRNA bindingHyaluronic acid binding
03
Disease associations
Cancer (role inferred by paralogs and family, direct associations unreported for USP17L28)Other (potential roles in apoptosis and cell cycle regulation suggest possible relevance to other proliferative or apoptotic disorders)
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