EC Number   |
Substrates |
Products  |
Reversibility |
|---|
   6.2.1.45 | ATP + ubiquitin + SUMO2 |
UBE1DC1 greatly activates SUMO2 in the nucleus or transfers activated-SUMO2 to nucleus after conjugation of SUMO2 in the cytoplasm |
? |
- |
? |
| 6.2.1.45 | ATP + ubiquitin + ubiquitin-fold modifier 1 |
- |
? |
- |
? |
| 6.2.1.45 | ATP + ubiquitin + Ufm1 |
- |
? |
- |
? |
| 6.2.1.45 | more |
UBE1L2 transfers activated ubiquitin onto UbcH5b and supports E3-mediated polyubiquitylation |
? |
- |
? |
| 6.2.1.45 | more |
impaired nucleotide excision repair upon macrophage differentiation is corrected by E1 ubiquitin-activating enzyme |
? |
- |
? |
| 6.2.1.45 | more |
a lysine 48-linked polyubiquitin chain, assembled upon an internal lysine residue of a substrate protein, becomes the principle signal for recognition and target degradation by the 26S proteasome. E1 is not only essential for the initial ATP-dependent activation of ubiquitin in the ubiquitin degradtion pathway, but also capable of the catalytic extension of the polyubiquitin chain on a mono-ubiquitinated substrate |
? |
- |
? |
| 6.2.1.45 | more |
E1 consumes ATP and converts ubiquitin to a transfer-competent, enzyme-bound thioester. The reaction begins with ubiquitin-adenylate formation and the release of diphosohate. The active site cysteine of the E1 then displaces the AMP leading to a ubiquitin-E1 thioester complex |
? |
- |
? |
| 6.2.1.45 | more |
the thioester formation assay is performed using recombinant proteins expressed in Escherichia coli. The activation of ubiquitin by purified UBE1 is identified in vitro by SDS-PAGE |
? |
- |
? |
| 6.2.1.45 | more |
E1 activity is assesssed by the capacity of the enzyme to form a thiol ester conjugate with ubiquitin in an ATP-dependent process and to transfer this activated ubiquitin molecule to an conjugating enzyme |
? |
- |
? |
| 6.2.1.45 | more |
residue Cys194 lies within a region of identity to active-site Cys88 of the ubiquitin carrier protein E2, suggesting a potential role for this region in enzymatic function. Residue Cys454 lies within a region of identity to the thiol ester consensus sequence of several proteins involved in thioester formation |
? |
- |
? |
