EC Number   |
Substrates |
Organism |
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 |
Homo sapiens |
? |
- |
? |
| 6.2.1.45 | ATP + ubiquitin + ubiquitin-fold modifier 1 |
- |
Homo sapiens |
? |
- |
? |
| 6.2.1.45 | ATP + ubiquitin + Ufm1 |
- |
Homo sapiens |
? |
- |
? |
| 6.2.1.45 | more |
impaired nucleotide excision repair upon macrophage differentiation is corrected by E1 ubiquitin-activating enzyme |
Homo sapiens |
? |
- |
? |
| 6.2.1.45 | more |
UBE1L2 transfers activated ubiquitin onto UbcH5b and supports E3-mediated polyubiquitylation |
Homo sapiens |
? |
- |
? |
| 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 |
Escherichia coli |
? |
- |
? |
| 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 |
Mus musculus |
? |
- |
? |
| 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 |
Mus musculus |
? |
- |
? |
| 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 |
Homo sapiens |
? |
- |
? |
| 6.2.1.45 | more |
kinetics for Uba1a-catalyzed transthiolation of Ubc2b are used as a reporter assay for determining the Km and kcat values for the three cosubstrates of the ubiquitin-activating enzyme. The E2 transthiolation assays are more sensitive to the potential presence of trace catalytically active fragments than the single turnover end point assays used for quantitating ternary complex stoichiometry |
Homo sapiens |
? |
- |
? |
