deubiquitinase activity

Definition

Target type: molecularfunction

An isopeptidase activity that cleaves ubiquitin from a target protein to which it is conjugated. [GOC:mec, PMID:30783221]

Deubiquitinases (DUBs) are a diverse family of enzymes that catalyze the removal of ubiquitin (Ub) moieties from target proteins. Ubiquitination is a reversible post-translational modification that involves the attachment of Ub to a substrate protein, and it plays a critical role in regulating a wide range of cellular processes, including protein degradation, signal transduction, DNA repair, and immune responses. DUBs counterbalance the action of ubiquitin ligases (E3s), which attach Ub to substrates. They do this by hydrolyzing the isopeptide bond that links Ub to the target protein, releasing free Ub and the deubiquitinated substrate. DUBs possess a highly conserved catalytic cysteine residue within their active site that is essential for the hydrolysis reaction.
DUBs are classified into six major families based on their structural and functional characteristics: Ubiquitin-specific proteases (USPs), Ubiquitin C-terminal hydrolases (UCHs), Ovarian tumor domain (OTU) proteases, Josephin domain proteases, Machado-Joseph disease protein domain (MJD) proteases, and Deubiquitinase with a Zinc finger domain (Znf-DUB).
DUBs are essential for maintaining cellular homeostasis and are implicated in a variety of human diseases. Dysregulation of DUB activity can lead to aberrant protein degradation, impaired signal transduction, and developmental defects. For example, mutations in DUB genes have been linked to cancer, neurodegenerative disorders, and immune system dysfunction.'
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Proteins (5)

Compounds (11)