Ube2G2 is a Class I E2 enzyme and shares 60% and 100% sequence identity with S.cerevisiae Ubc7 and mouse respectively. In yeast, Ubc7 is a endoplasmic reticulum (ER)-bound molecule and the active site faces the cystosol. The Ube2G2 E2 enzyme and the GP78 E3 ligase are active components of ERAD (endoplasmic reticulum-associated degradation) pathway which is essential for the degradation of misfolded ER proteins. The mechanism of K48-linked poly-ubiquitination by Ube2G2/GP78 appears to involve the transfer of preassembled Ub chains from Ube2G2 to lysine residues in a substrate. The E2 and E3 enzymes form a large hetero-oligomer which brings multiple Ube2G2 molecules into close proximity which allows for Ub transfer between neighboring E2s. This Ube2G2 contains an N-terminal His₆ tag. Accession # NP_003334.