EC Number   |
Substrates |
Products |
Reversibility |
|---|
   6.2.1.45 | ATP + Ufm1 + [ubiquitin-activating protein UBA5]-L-cysteine |
Ufm1, ubiquitin-fold modifier 1, an ubiquitin-like protein |
AMP + diphosphate + [ubiquitin-activating protein UBA5]-S-Ufm1-L-cysteine |
- |
? |
| 6.2.1.45 | more |
UBE1L2 transfers activated ubiquitin onto UbcH5b and supports E3-mediated polyubiquitylation |
? |
- |
? |
| 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 | 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 |
the non-canonical E1, UBA5, binds to the ubiquitin-like protein UFM1 using a trans-binding mechanism in which UFM1 interacts with distinct sites in both subunits of the UBA5 dimer. Mechanism of UFM1 activation by UBA5 and trans-binding mechanism of UFM1 transfer to the E2, UFC1. UFM1 contains a C-terminal Val-Gly dipeptide instead of the canonical Gly-Gly dipeptide present in ubiquitin and other ubiquitin-like proteins |
? |
- |
? |
| 6.2.1.45 | ATP + ubiquitin + [ubiquitin-activating enzyme Uba5]-L-cysteine |
the catalytic cysteine residue of isoform Uba5 is part of the adenylation domain in a alpha-helical motif |
AMP + diphosphate + [ubiquitin-activating enzyme Uba5]-S-ubiquitinyl-L-cysteine |
- |
? |
| 6.2.1.45 | ATP + ubiquitin fold modifier1 + [ubiquitin-activating enzyme Uba5]-L-cysteine |
the catalytic cysteine residue of isoform Uba5 is part of the adenylation domain in a alpha-helical motif |
AMP + diphosphate + [ubiquitin-activating enzyme Uba5]-S-(ubiquitin fold modifier1)-L-cysteine |
- |
? |
| 6.2.1.45 | ATP + SUMO2 + [ubiquitin-activating protein UBA5]-L-cysteine |
SUMO2, small ubiquitin-like modifier2, an ubiquitin-like protein |
AMP + diphosphate + [ubiquitin-activating protein UBA5]-S-SUMO2-L-cysteine |
enzyme greatly activates SUMO2 in the nucleus or transfers activated SUMO2 to the nucleus after it conjugated SUMO2 in the cytoplasm |
? |
| 6.2.1.45 | ATP + ubiquitin + [6His-ubiquitin-activating enzyme E1]W-8His-Strep-HA |
Strep, i.e.WSHPQFEK, HA, i.e. YPYDVPDYAS, under non-reducing conditions, the intermediate complex of the thioester formation is not observed without ATP |
AMP + diphosphate + [6His-ubiquitin-activating enzyme E1]W-8His-Strep-HA-ubiquitinyl-L-cysteine |
- |
? |
| 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 |
? |
- |
? |
