Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P61086 | - |
- |
Saccharomyces cerevisiae | P21734 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 N6-monoubiquitinyl-[Ubc1]-L-lysine | - |
Saccharomyces cerevisiae | N6-diubiquitinyl-[Ubc1]-L-lysine + [Ube2K]-L-lysine | - |
? | |
2 N6-monoubiquitinyl-[Ube2K]-L-lysine | - |
Homo sapiens | N6-diubiquitinyl-[Ube2K]-L-lysine + [Ube2K]-L-lysine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
HIP2 | - |
Homo sapiens |
Ubc1 | - |
Saccharomyces cerevisiae |
UBE2K | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | E2 enzyme HIP2-ubiquitin thioester complexes remain predominantly monomeric in solution | Saccharomyces cerevisiae |
physiological function | E2 enzyme HIP2-ubiquitin thioester complexes remain predominantly monomeric in solution. Models of the HIP2-ubiquitin complex show an open or backbent conformation similar to UbcH5b-ubiquitin where the ubiquitin-associated UBA domain and covalently attached ubiquitin reside on opposite ends of the catalytic domain. Full length HIP2 exhibits a fivefold increase in the formation rate of diubiquitin compared to a HIP2 lacking the UBA domain | Homo sapiens |