Ubiquitin-conjugating enzyme E2 G2 is a protein that in humans is encoded by the UBE2G2gene.[1][2][3]
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, ubiquin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. The encoded protein shares 100% sequence identity with the mouse counterpart. This gene is ubiquitously expressed, with high expression seen in adult muscle. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.[3] Ube2g2 is known to interact with a variety of other proteins, including ubiquitin, the E3 gp78, and the Hrd1 RING.
References
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↑Rose SA, Leek JP, Moynihan TP, Ardley HC, Markham AF, Robinson PA (Mar 1999). "Assignment1 of the ubiquitin conjugating enzyme gene, UBE2G2, to human chromosome band 21q22.3 by in situ hybridization". Cytogenet Cell Genet. 83 (1–2): 98–9. doi:10.1159/000015141. PMID9925943.
Chen P, Johnson P, Sommer T, et al. (1993). "Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor". Cell. 74 (2): 357–69. doi:10.1016/0092-8674(93)90426-Q. PMID8393731.
Moynihan TP, Ardley HC, Nuber U, et al. (1999). "The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1". J. Biol. Chem. 274 (43): 30963–8. doi:10.1074/jbc.274.43.30963. PMID10521492.
Huang L, Kinnucan E, Wang G, et al. (1999). "Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade". Science. 286 (5443): 1321–6. doi:10.1126/science.286.5443.1321. PMID10558980.
Hattori M, Fujiyama A, Taylor TD, et al. (2000). "The DNA sequence of human chromosome 21". Nature. 405 (6784): 311–9. doi:10.1038/35012518. PMID10830953.
Lenk U, Sommer T (2001). "Ubiquitin-mediated proteolysis of a short-lived regulatory protein depends on its cellular localization". J. Biol. Chem. 275 (50): 39403–10. doi:10.1074/jbc.M006949200. PMID10991948.
Webster JM, Tiwari S, Weissman AM, Wojcikiewicz RJ (2003). "Inositol 1,4,5-trisphosphate receptor ubiquitination is mediated by mammalian Ubc7, a component of the endoplasmic reticulum-associated degradation pathway, and is inhibited by chelation of intracellular Zn2+". J. Biol. Chem. 278 (40): 38238–46. doi:10.1074/jbc.M305600200. PMID12869571.
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Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID16189514.