Ubiquitin-conjugating enzyme, active site
IPR023313
Definition
Ubiquitin-conjugating enzymes ([ec:2.3.2.23], UBC or E2 enzymes) catalyse the covalent attachment of ubiquitin to target proteins. Ubiquitin is conjugated to the target protein through the coordinated action of three enzyme activities designated E1, E2, and E3. The E1 or ubiquitin-activating enzyme forms, in an ATP-dependent manner, a thioester linkage between its active site cysteine and the carboxy terminus of ubiquitin. The activated ubiquitin moiety is then transferred from E1 to the active site cysteine in E2 through a trans-thiol esterification reaction. The UBC enzyme later ligates ubiquitin directly to substrate proteins with or without the assistance of 'N-end' recognizing proteins (E3) [[cite:PMID:2193438], [cite:PMID:1647207], [cite:PMID:1656558]]. In most species there are many forms of UBC (at least 9 in yeast) which are implicated in diverse cellular functions.
26 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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