The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s.
This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is located in the membrane of the endoplasmic reticulum (ER) and may contribute to quality control ER-associated degradation by the ubiquitin-proteasome system.[6]
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Lenk U, Yu H, Walter J, et al. (2002). "A role for mammalian Ubc6 homologues in ER-associated protein degradation". J. Cell Sci. 115 (Pt 14): 3007–14. doi:10.1242/jcs.115.14.3007. PMID12082160.