Description

IPR000608 is a Ubiquitin-conjugating enzyme E2.

<p>Ubiquitin-conjugating enzymes (UBC or E2 enzymes) ([ec:2.3.2.23]) [[cite:PUB00005354], [cite:PUB00000623], [cite:PUB00005373]] catalyse the covalent attachment of ubiquitin to target proteins. Ubiquitinylation is an ATP-dependent process that involves the action of at least three enzymes: a ubiquitin-activating enzyme (E1, [interpro:IPR000011]), a ubiquitin-conjugating enzyme (E2), and a ubiquitin ligase (E3, [interpro:IPR000569], [interpro:IPR003613]), which work sequentially in a cascade [[cite:PUB00015620]]. The E1 enzyme mediates an ATP-dependent transfer of a thioester-linked ubiquitin molecule to a cysteine residue on the E2 enzyme. The E2 enzyme then either transfers the ubiquitin moiety directly to a substrate, or to an E3 ligase, which can also ubiquitinylate a substrate.</p> <p>There are several different E2 enzymes (over 30 in humans), which are broadly grouped into four classes, all of which have a core catalytic domain (containing the active site cysteine), and some of which have short N- and C-terminal amino acid extensions: class I enzymes consist of just the catalytic core domain (UBC), class II possess a UBC and a C-terminal extension, class III possess a UBC and an N-terminal extension, and class IV possess a UBC and both N- and C-terminal extensions. These extensions appear to be important for some subfamily function, including E2 localisation and protein-protein interactions [[cite:PUB00015626]]. In addition, there are proteins with an E2-like fold that are devoid of catalytic activity (such as protein crossbronx from flies), but which appear to assist in poly-ubiquitin chain formation.</p>

This description is obtained from EB-eye REST.

Associated GO terms

Unable to find any GO terms for the transcript with the identifier.

Associated Lotus transcripts 163