EC Number   |
Substrates |
Products |
Reversibility |
|---|
   6.2.1.45 | more |
chimeric mutant Aos1-Uba2 SUMO-E1 enzyme shows SUMO-E1 activity. The E1 enzyme catalyzes the formation of a thioester-linked complex between SUMO and the E2 enzyme. This process is initiated by activation of the carboxyl terminus of SUMO by adenylation, followed by a thioesterification reaction in which SUMO is conjugated to a cysteine residue at the active site of Uba2 in the E1 enzyme. SUMO is then transferred to the active site cysteine of the E2 enzyme, Ubc9, via a trans-thioesterification reaction. A SUMO-charged E2 enzyme and substrate are finally bound with or without the assistance of a distinct class of SUMO E3-ligases, resulting in the activated SUMO bound to the substrate through an isopeptide linkage |
? |
- |
? |
| 6.2.1.45 | more |
E1 ubiquitin-activating enzyme UBA6 is the only E1 enzyme that can activate both ubiquitin and ubiquitin-like protein HLA-F adjacent transcript 10 (FAT10). FAT10 consists of two ubiquitin-like domains with 29% and 36% identity to ubiquitin, respectively, that are separated by a short linker region |
? |
- |
? |
| 6.2.1.45 | more |
orthogonal ubiquitin transfer (OUT) technology to profile their ubiquitination targets in mammalian cells of isozymes Uba1 and Uba6 |
? |
- |
? |
| 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 | more |
CDC42 is a substrate of UBA6-initiated ubiquitination |
? |
- |
? |
