EC Number   |
General Information |
Reference  |
|---|
   6.2.1.45 | metabolism |
ubiquitin-activating enzyme E1 catalyzes the first step in the ubiquitination reaction, which targets a protein for degradation via a proteasome pathway. The enzyme plays an important role in metabolic processes |
733931 |
| 6.2.1.45 | more |
the enzyme has six ATP binding sites, one catalytic residue, and one E2 binding domain |
733931 |
| 6.2.1.45 | physiological function |
UBE1s catalyze the first steps in the ubiquitin conjugation cascade and are potentially involved in compatible pollination and ubiquitinmediated S-RNase degradation |
733931 |
| 6.2.1.45 | physiological function |
comparative proteomic analysis of wild-type and SAP domain-mutant Foot-and-mouth disease virus-infected porcine cells identifies the ubiquitin-activating enzyme UBE1 required for virus replication. Overexpression of the enzyme UBE1 enhances the replication of the virus, and knockdown of UBE1 decreases virus replication. te virus manipulates UBE1 for increased viral replication, and the SAP domain is involved in this process, overview |
734563 |
| 6.2.1.45 | metabolism |
the ubiquitin E1 activating enzyme ubiquitin-activating enzyme 1 (UBE1) is a putative substrate of FAT10. The ubiquitin-like modifier HLA-F adjacent transcript 10 (FAT10) directly targets its substrates for proteasomal degradation by becoming covalently attached via its C-terminal diglycine motif to internal lysine residues of its substrate proteins. UBE1 and FAT10 formed a stable isopeptide linkage. The conjugation machinery consists of the bispecific E1 activating enzyme ubiquitin-like modifier activating enzyme 6 (UBA6), the likewise bispecific E2 conjugating enzyme UBA6-specific E2 enzyme 1 (USE1), and possibly E3 ligases, overview. UBE1 and FAT10 form a stable non-reducible conjugate, FAT10ylation of UBE1 depends on the diglycine motif of FAT10 |
735013 |
| 6.2.1.45 | more |
conjugation of the ubiquitin activating enzyme UBE1 with the ubiquitin-like modifier FAT10 targets it for proteasomal degradation. UBE1 uses Cys632 in the active site |
735013 |
| 6.2.1.45 | physiological function |
ubiquitin-activating enzyme 1 does not act as a second E1 activating enzyme for ubiquitin-like modifier HLA-F adjacent transcript but FAT10ylation of UBE1 leads to its proteasomal degradation |
735013 |
| 6.2.1.45 | malfunction |
identification of loss-of-function mutations in the Drosophila ubiquitin activating enzyme, the most upstream enzyme in the ubiquitin pathway. Loss of only one functional copy of E1 caused a significant reduction in adult lifespan. Rare homozygous hypomorphic E1 mutants reach adulthood, but mutants exhibit further reduced lifespan and show inappropriate Ras activation in the brain. Removing just one functional copy of Ras restores the lifespan of heterozygous E1 mutants to that of wild-type flies and increase the survival of homozygous E1 mutants. E1 homozygous mutants also show severe motor impairment involved in early mortality. Phenotypes, detailed overview |
735079 |
| 6.2.1.45 | malfunction |
local delivery of potent chemical UBA1 inhibitor PYR-41 and UBA1 shRNA lentivirus both result in a substantial decrease in intimal hyperplasia at 2 weeks and 4 weeks after balloon injury. UBA1 inhibition also reduces Ki-67 positive cell percentage and inflammatory response in the carotid artery wall. In vitro UBA1 inhibition is able to ameliorate TNF-alpha-induced nuclear factor-kappa B (NF-kappaB) activation by reducing IkappaB degradation in vascular smooth muscle cells (VSMCs). UBA1 inhibition also leads to the accumulation of short-lived proteins such as p53, p21 and c-jun, which may account for the UBA1 inhibition-induced cell cycle delay. Thus, VSMCs proliferation is blocked. UBA1 inhibition effectively suppresses neointimal thickening through its anti-proliferative and anti-inflammatory effects |
744190 |
| 6.2.1.45 | metabolism |
the ubiquitin-activating enzyme E1 (UBA1, E1) is the apex of the ubiquitin proteasome pathway |
744190 |
