Alternative titles; symbols
HGNC Approved Gene Symbol: UBE2E3
Cytogenetic location: 2q31.3 Genomic coordinates (GRCh38) : 2:180,980,360-181,063,425 (from NCBI)
Ubiquitination of a protein substrate requires sequential reactions by 3 types of enzymes: E1 ubiquitin-activating enzymes, E2 ubiquitin-conjugating enzymes, and E3 ubiquitin protein ligases. See 600012. Class I E2 enzymes contain a conserved core UBC domain, while class II and class III E2 proteins have C- and N-terminal extensions, respectively, in addition to the UBC domain. Matuschewski et al. (1996) identified the related class III E2 genes UbcD2 (ubiquitin-conjugating enzyme-2 from Drosophila), UbcM2 (Ubc-2 from mice), and UbcM3. Although the UBC domains of the 3 enzymes are 94% identical, the N-terminal extensions show little sequence similarity. The UBC domains of UbcD2, UbcM2, and UbcM3 are homologous to those of S. cerevisiae UBC4 and UBC5 proteins and share 64% identity with the UBC domains of UBC4-related enzymes from higher eukaryotes. Matuschewski et al. (1996) demonstrated that the UbcD2, UbcM2, and UbcM3 genes partially complemented double mutant ubc4/ubc5 yeast. By searching sequence databases, the authors identified a partial cDNA encoding UbcH9, a human UbcM2 homolog. Ito et al. (1999) isolated additional cDNAs corresponding to the complete coding region of UbcH9 (UBE2E3). The predicted 207-amino acid human protein is identical to UbcM2. Northern blot hybridization revealed that UBE2E3 is expressed as a 1.9-kb mRNA primarily in skeletal muscle. Recombinant enzyme formed a thioester bond with ubiquitin in an E1-dependent manner, indicating that UBE2E3 is a functional E2.
By fluorescence in situ hybridization, and by analysis of somatic cell and radiation hybrids, Ito et al. (1999) mapped the UBE2E3 gene to 2q32.1.
Ito, K., Kato, S., Matsuda, Y., Kimura, M., Okano, Y. cDNA cloning, characterization, and chromosome mapping of UBE2E3 (alias UbcH9), encoding an N-terminally extended human ubiquitin-conjugating enzyme. Cytogenet. Cell Genet. 84: 99-104, 1999. [PubMed: 10343118] [Full Text: https://doi.org/10.1159/000015229]
Matuschewski, K., Hauser, H.-P., Treier, M., Jentsch, S. Identification of a novel family of ubiquitin-conjugating enzymes with distinct amino-terminal extensions. J. Biol. Chem. 271: 2789-2794, 1996. [PubMed: 8576256] [Full Text: https://doi.org/10.1074/jbc.271.5.2789]