Target intelligence / Profile preview

Ubiquitin carboxyl-terminal hydrolase 5 (USP5)

Target
USP5
Molecular classification
Enzyme, Deubiquitinase, Endopeptidase
01

Overview

Ubiquitin carboxyl-terminal hydrolase 5 (USP5), also known as isopeptidase T, is an enzyme in the ubiquitin-specific peptidase (USP) family that disassembles unanchored (not protein-conjugated) polyubiquitin chains and is critical for maintaining the free monoubiquitin pool in cells[1][2][3]. USP5 cleaves isopeptide bonds at the proximal end of polyubiquitin chains through a sequential exo mechanism, regulating protein turnover, DNA repair, localization, and cellular homeostasis[1][2][3]. Dysregulation of USP5 is implicated in cancer, neurological disease, and inflammatory processes, and USP5 is being explored as a therapeutic target with several small molecule inhibitors identified[1].

Other names
Ubiquitin specific peptidase 5Isopeptidase TISOTUbiquitin isopeptidase
02

Mechanism of action

Inhibition of deubiquitinating activity Disruption of polyubiquitin chain cleavage

03

Biological functions

Protein degradationUbiquitination and deubiquitinationProtein stabilizationProtein localizationDNA repairSignal transduction
04

Disease associations

CancerNeurological diseaseInflammation
05

Safety considerations

Potential for off-target effects due to broad cellular roleImpact on protein homeostasisUnknown long-term consequences of chronic inhibition
06

Interacting drugs

WP1130

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