The SUMO activating enzyme E1 enzyme facilitates conjugation of ubiquitin and ubiquitin-like proteins through adenylation, thioester transfer within E1, and thioester transfer from E1 to E2 conjugating proteins []. This entry represents a subunit of the E1 enzyme, including Uba2 from yeasts []and its homologue, SAE2 from animals []. E1 enzymes mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2 [, ].
This is the C-terminal domain found in SUMO-activating enzyme subunit 2 (Uba2) []. Uba2 forms a heterodimer with Aos1 which acts as a E1 ligase for SUMO (small ubiquitin-like modifier) proteins [].
scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14 (MEROPS identifier C19.083), is the Saccharomyces cerevisiae orthologue of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast [, ]. Members in this family contain two tandem ubiquitin-association (UBA) domains.This entry corresponds to the UBA2 domain in Saccharomyces cerevisiae UBP14 and related proteins [].
