Alternative titles; symbols
HGNC Approved Gene Symbol: UBE2E1
Cytogenetic location: 3p24.2 Genomic coordinates (GRCh38) : 3:23,805,955-23,891,640 (from NCBI)
The ubiquitin system plays a major role in selective protein degradation. This pathway first requires the covalent attachment of ubiquitin, a highly conserved 76-amino acid protein, to defined lysine residues of substrate proteins. Ubiquitin-protein conjugates are then recognized and degraded by a specific protease complex, the 26 S proteasome. Protein ubiquitination involves 3 classes of enzymes: the ubiquitin-activating enzymes E1 (e.g., UBE1; 314370), the ubiquitin-conjugating enzymes E2, and the ubiquitin-protein ligases E3 (e.g., UBE3A; 601623). One evolutionarily conserved subfamily of E2s includes human UBCH5A (UBE2D1; 602961), S. cerevisiae UBC4 and UBC5, and Arabidopsis thaliana UBC8.
By RT-PCR using degenerate oligonucleotides corresponding to highly conserved regions of S. cerevisiae UBC4 and A. thaliana UBC8, Nuber et al. (1996) cloned human cDNAs encoding UBE2E1, which they called UBCH6. They noted that the isolated cDNAs may not contain the complete UBCH6 coding sequence since an in-frame stop codon was not found upstream of the first methionine codon. The deduced 193-amino acid UBCH6 protein shows the highest sequence similarity to members of the UBCH5 E2 subfamily, with 74% similarity to UBCH5. UBCH6 appears unique among these E2s in containing an N-terminal extension of approximately 40 amino acids.
Nuber et al. (1996) found that UBCH6 did not efficiently mediate UBE3A (E6AP)-dependent ubiquitination in an in vitro assay.
Nuber, U., Schwarz, S., Kaiser, P., Schneider, R., Scheffner, M. Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5. J. Biol. Chem. 271: 2795-2800, 1996. [PubMed: 8576257] [Full Text: https://doi.org/10.1074/jbc.271.5.2795]