| UniProt functional annotation for O94609 | |||
| UniProt code: O94609. |
| Organism: | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). | |
| Taxonomy: | Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces. | |
| Function: | Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system. Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. {ECO:0000269|PubMed:23416107}. | |
| Catalytic activity: | Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]- L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000269|PubMed:23416107}; | |
| Pathway: | Protein modification; protein ubiquitination. {ECO:0000269|PubMed:23416107}. | |
| Subunit: | Monomer. Interacts with the E2 ubiquitin-conjugating enzyme ubc4. {ECO:0000269|PubMed:23416107}. | |
| Subcellular location: | Cytoplasm. Nucleus. | |
| Miscellaneous: | There are two active sites within the E1 molecule, allowing it to accommodate two ubiquitin moieties at a time, with a new ubiquitin forming an adenylate intermediate as the previous one is transferred to the thiol site. {ECO:0000250|UniProtKB:P22515}. | |
| Similarity: | Belongs to the ubiquitin-activating E1 family. {ECO:0000305}. | |
Annotations taken from UniProtKB at the EBI.