Ubiquitin-activating enzyme-like
IPR035985
Definition
This entry describes the ubiquitin-activating enzymes E1, ubiquitin-like modifier-activating enzymes, and related enzymes. It also includes adenylyltransferase and sulfurtransferase from the MOCS3 (humans) and UBA4 (yeast) complexes, which are enzymes involved in ubiquitin-like pathways. These enzymes play critical roles in activating ubiquitin-like proteins (UBLs) such as Urm1 [[cite:PMID:32901956], [cite:PMID:21245332]]. The post-translational attachment of ubiquitin ([interpro:IPR000626]) to proteins (ubiquitinylation) alters the function, location or trafficking of a protein, or targets it to the 26S proteasome for degradation [[cite:PMID:15556404], [cite:PMID:15454246], [cite:PMID:15196553]]. Ubiquitinylation is an ATP-dependent process that involves the action of at least three enzymes: a ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (E2, [interpro:IPR000608]), and a ubiquitin ligase (E3, [interpro:IPR000569], [interpro:IPR003613]), which work sequentially in a cascade PMID:14998368. The E1 enzyme is responsible for activating ubiquitin, the first step in ubiquitinylation. The E1 enzyme hydrolyses ATP and adenylates the C-terminal glycine residue of ubiquitin, and then links this residue to the active site cysteine of E1, yielding a ubiquitin-thioester and free AMP. To be fully active, E1 must non-covalently bind to and adenylate a second ubiquitin molecule. The E1 enzyme can then transfer the thioester-linked ubiquitin molecule to a cysteine residue on the ubiquitin-conjugating enzyme, E2, in an ATP-dependent reaction.
10 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.
Loading the interactive Seroatlas explorer...