Ubiquitin-conjugating enzyme E2 E3 (UBE2E3)

Ubiquitin-conjugating enzyme E2 E3 (UBE2E3) is a highly conserved enzyme in the E2 family of ubiquitin-conjugating enzymes, responsible for accepting activated ubiquitin from the E1 enzyme and collaborating with E3 ubiquitin-protein ligases to transfer ubiquitin to specific substrate proteins. This posttranslational modification typically signals proteins for degradation via the proteasome or alters their cellular location and function. UBE2E3 is involved in forming various ubiquitin linkages, including Lys-11, Lys-48, and Lys-63, implicating it in multiple cellular processes. It participates in modulation of transepithelial sodium transport, particularly in renal cells, by regulating the activity and cell-surface expression of the epithelial sodium channel (ENaC), often in concert with E3 ligase Nedd4-2. Mutations or alterations in these pathways may contribute to or be associated with disorders such as hypertension (via ENaC regulation) and neurodegenerative diseases such as Parkinson's disease[2][3][4][5][6]. There are currently no direct clinical drugs or well-established biomarkers associated specifically with UBE2E3, but its centrality in ubiquitin-proteasome mediated protein homeostasis marks it as a potential therapeutic target in relevant diseases[3][4].

Other names

UbcH9UBCH9UbcM2Ubiquitin carrier protein E3Ubiquitin-conjugating enzyme E2E 3 (homologous to yeast UBC4/5)Ubiquitin-conjugating enzyme E2-23 kDaE2 ubiquitin-conjugating enzyme E3Ubiquitin-protein ligase E3

Enzyme accepts ubiquitin from the E1 enzyme and catalyzes the transfer (conjugation) of ubiquitin to target proteins, facilitating polyubiquitination (notably Lys-11, Lys-48, Lys-63 linkages)