Ubiquitin carboxyl-terminal hydrolases
IPR050164
Definition
The peptidase C19 family, also known as ubiquitin carboxyl-terminal hydrolases, encompasses deubiquitinating enzymes that play crucial roles in various cellular processes by removing ubiquitin from specific proteins and polyubiquitin chains. These enzymes are involved in the regulation of protein turnover, DNA damage repair, cell cycle progression, apoptosis, immune response, and signal transduction pathways such as Wnt and TGF-beta/BMP. They function by processing ubiquitin precursors, recycling ubiquitin molecules, editing polyubiquitin chains, and preventing proteasomal degradation of substrates. Some family members are also implicated in the regulation of mitophagy, endosomal protein recycling, and maintenance of circadian rhythm. The family includes enzymes that act as tumor suppressors, regulators of cell growth and differentiation, and modulators of inflammatory and antiviral responses.
45 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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