Biology:UBE2G2
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Ubiquitin-conjugating enzyme E2 G2 is a protein that in humans is encoded by the UBE2G2 gene.[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
- ↑ "Identification, expression, and chromosomal localization of ubiquitin conjugating enzyme 7 (UBE2G2), a human homologue of the Saccharomyces cerevisiae ubc7 gene". Genomics 51 (1): 128–31. Sep 1998. doi:10.1006/geno.1998.5263. PMID 9693041.
- ↑ "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. Mar 1999. doi:10.1159/000015141. PMID 9925943.
- ↑ 3.0 3.1 "Entrez Gene: UBE2G2 ubiquitin-conjugating enzyme E2G 2 (UBC7 homolog, yeast)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7327.
Further reading
- 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. PMID 8393731.
- 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. PMID 10521492.
- 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. PMID 10558980.
- 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. PMID 10830953. Bibcode: 2000Natur.405..311H.
- "Ubiquitin-mediated proteolysis of a short-lived regulatory protein depends on its cellular localization". J. Biol. Chem. 275 (50): 39403–10. 2001. doi:10.1074/jbc.M006949200. PMID 10991948.
- "Biochemistry. Ubiquitination--more than two to tango". Science 289 (5487): 2061–2. 2000. doi:10.1126/science.289.5487.2061. PMID 11032556.
- "Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s)". J. Biol. Chem. 276 (19): 16193–200. 2001. doi:10.1074/jbc.M007640200. PMID 11278356.
- Fang S; Ferrone M; Yang C et al. (2002). "The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum". Proc. Natl. Acad. Sci. U.S.A. 98 (25): 14422–7. doi:10.1073/pnas.251401598. PMID 11724934.
- Strausberg RL; Feingold EA; Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "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. 2003. doi:10.1074/jbc.M305600200. PMID 12869571.
- Ota T; Suzuki Y; Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Gerhard DS; Wagner L; Feingold EA et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
- 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. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- Chen B; Mariano J; Tsai YC et al. (2006). "The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site". Proc. Natl. Acad. Sci. U.S.A. 103 (2): 341–6. doi:10.1073/pnas.0506618103. PMID 16407162. Bibcode: 2006PNAS..103..341C.
- Arai R; Yoshikawa S; Murayama K et al. (2006). "Structure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7)". Acta Crystallographica Section F 62 (Pt 4): 330–4. doi:10.1107/S1744309106009006. PMID 16582478.
- Hu YH; Warnatz HJ; Vanhecke D et al. (2006). "Cell array-based intracellular localization screening reveals novel functional features of human chromosome 21 proteins". BMC Genomics 7: 155. doi:10.1186/1471-2164-7-155. PMID 16780588.
- Ewing RM; Chu P; Elisma F et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMID 17353931.
External links
- Overview of all the structural information available in the PDB for UniProt: P60604 (Ubiquitin-conjugating enzyme E2 G2) at the PDBe-KB.
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