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Ubiquitin-conjugating enzyme E2 J1 is a protein that in humans is encoded by the UBE2J1gene.[5][6]
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]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Lester D, Farquharson C, Russell G, Houston B (Apr 2000). "Identification of a family of noncanonical ubiquitin-conjugating enzymes structurally related to yeast UBC6". Biochem Biophys Res Commun. 269 (2): 474–80. doi:10.1006/bbrc.2000.2302. PMID10708578.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
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.
This page was last edited on 3 March 2023, at 23:37