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UBC6 Ubc6p

UBC6, Ubc6p
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. [provided by RefSeq, Jul 2008] (from NCBI)
Papers on UBC6
HRD1 and UBE2J1 target misfolded MHC class I heavy chains for endoplasmic reticulum-associated degradation.
Lehner et al., Cambridge, United Kingdom. In Proc Natl Acad Sci U S A, 2011
data support a physiological role for HRD1 and UBE2J1 in the homeostatic regulation of MHC class I assembly and expression
Ube2j2 ubiquitinates hydroxylated amino acids on ER-associated degradation substrates.
Hansen et al., Saint Louis, United States. In J Cell Biol, 2009
Ube2j2 is the primary cellular E2 recruited by the mK3 ligase, and this E2-E3 pair is capable of conjugating Ub on lysine or serine residues of substrates.
Human homologs of Ubc6p ubiquitin-conjugating enzyme and phosphorylation of HsUbc6e in response to endoplasmic reticulum stress.
Rommens et al., Toronto, Canada. In J Biol Chem, 2006
Ubc6e is phosphorylated in response to endoplasmic reticulum stress
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