Alternative titles; symbols
HGNC Approved Gene Symbol: UBE2E2
Cytogenetic location: 3p24.3 Genomic coordinates (GRCh38): 3:23,203,098-23,591,925 (from NCBI)
The ubiquitin/proteasome system mediates a major pathway involved in selective protein degradation. In this pathway, the substrate proteins are first required to form a covalent bond with ubiquitin (191339), a highly conserved 76-amino acid protein, before being targeted by a proteasome. Protein ubiquitination involves 3 classes of enzymes. At first, ubiquitin-activating enzyme (UBE1; 314370), encoded by a gene on the X chromosome, forms a thioester bond between the C-terminal glycine of ubiquitin and a cysteine residue of E1 in an ATP-dependent manner. The activated ubiquitin is transferred to a ubiquitin-conjugating enzyme (e.g., UBE2H; 601082) that catalyzes the attachment of ubiquitin to a substrate protein, often in concert with ubiquitin ligases (E3s; e.g., 601623). E3s have been proposed to function in specific binding to targeted substrate proteins that are not recognized by E2 enzymes. The ubiquitin-protein conjugates are then recognized and degraded by the 26S proteasome.
From a human B-cell library, Kimura et al. (1997) isolated a novel human E2 enzyme, UBE2E2, with a unique N-terminal extension. The bacterially expressed UBE2E2 protein formed an E1-dependent ubiquitin thioester.
By fluorescence in situ hybridization, Kimura et al. (1997) mapped the UBE2E2 gene to chromosome 3p24.2. The gene is homologous to yeast Ubc4/5.
Kimura, M., Hattori, T., Matsuda, Y., Yoshioka, T., Sumi, N., Umeda, Y., Nakashima, S., Okano, Y. cDNA cloning, characterization, and chromosome mapping of UBE2E2 encoding a human ubiquitin-conjugating E2 enzyme. Cytogenet. Cell Genet. 78: 107-111, 1997. [PubMed: 9371400] [Full Text: https://doi.org/10.1159/000134639]