EC Number   |
Protein Variants |
Reference |
|---|
   6.2.1.45 | more |
a mutational reduction in Uba1 function (Uba1B2 mutation) reduces the efficacy of cell death, a complete loss of Uba1 function (Uba1A1 mutation) results in poor survival of mutant tissue and overgrowth of adjacent wild type tissue |
692413 |
| 6.2.1.45 | more |
construction of a mouse Aos1-Uba2 chimeric SUMO(small ubiquitin-related modifier)-E1 enzyme, mAU. The SUMO-E1 enzyme consists of two subunits, a heterodimer of activation of Smt3p 1 (Aos1) and ubiquitin activating enzyme 2 (Uba2), which resembles the N- and C-terminal halves of ubiquitin E1 (Uba1), the functional domains appear to be arranged in a fashion similar to Uba1. mAU has SUMO-E1 activity, indicating that mAU can be expressed in baculovirus-insect cells and represents a suitable source of SUMO-E1, enzymatic mechanism and structure of SUMO-E1, overview |
733442 |
| 6.2.1.45 | more |
enzyme silencing in HEK293 cells by lentiviral expression of shRNA. Generation of orthogonal pairs of xUB-xUBA6 and xUB-xUBA1, analysis of orthogonal interaction of xUB-xE1 in mammalian cells and identification of xUB-conjugated proteins. 697 potential Uba6 targets and 527 potential Uba1 targets with 258 overlaps are identified |
745863 |
| 6.2.1.45 | C632A |
generation of an active site cysteine mutant of HA-UBE1 |
735013 |
| 6.2.1.45 | more |
genotyping-phenotyping |
735079 |
| 6.2.1.45 | A189T |
improved stability and activity compared to mutant A189T/W714C, but when incubated at 39°C, cells expressing the mutant show increased apoptotic rate ompared to wild-type. Mutant is able to monoubiquitinate histone H2A and to support growth of TS20 cells at 39°C. Compared to mutant A189T/W714C, mutation A189T significantly improves the ubiquitination-dependent disposal of HIF-1alpha |
728028 |
| 6.2.1.45 | D290K/C250A |
in this heterodimer, the UBA5 subunit that can form the thioester bond with UFM1 is missing the UFC1 binding site. In the UBA5 (D290K)-UBA5 (K271D/C250A DELTADUIS) heterodimer, binding to the UIS and charging can only take place on the same monomer, thereby supporting a cis-binding mechanism |
744655 |
| 6.2.1.45 | more |
isolation of a mutant in ubiquitin-activiting enzyme Uba1. The mutation alters sensitivity to various environmental stresses and reduces wild-type Uba1 protein function. Protein modification by ubiquitin is strongly impaired in the mutant, inhibiting degradation of ubiquitin-proteasome pathway substrates as well as ubiquitin-dependent but proteasome-independent degradation of membrane receptors |
727501 |
| 6.2.1.45 | K528A |
Km-value for ATP is 1.6fold higher than wild-type value, KM-value for ubiquitin is 2.9fold higher than wild-type value. kcat for ubiquitin adenylate formation is 400fold lower than wild-type value. kcat for ubiquitin carrier protein E2 transthiolation is 309fold lower than wild-type value |
674561 |
| 6.2.1.45 | D576A |
Km-value for ATP is 37.8fold higher than wild-type value, KM-value for ubiquitin is 36fold higher than wild-type value. kcat for ubiquitin adenylate formation is 250fold lower than wild-type value. kcat for ubiquitin carrier protein E2 transthiolation is 28.3fold lower than wild-type value |
674561 |
