EC Number |
Natural Substrates |
---|
6.2.1.45 | ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine |
- |
6.2.1.45 | ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine |
E1-activating enzyme activates ubiquitin via an adenylated intermediate and catalyzes its transfer to an E2 enzyme |
6.2.1.45 | more |
impaired nucleotide excision repair upon macrophage differentiation is corrected by E1 ubiquitin-activating enzyme |
6.2.1.45 | more |
UBE1L2 transfers activated ubiquitin onto UbcH5b and supports E3-mediated polyubiquitylation |
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 |
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 |