Crystallization (Comment) | Organism |
---|---|
heterodimeric structure of the complex of Ring1b and Bmi1. Complex formation depends on an N-terminal arm of Ring1b that embraces the Bmi1 Ring-domain. Catalytic activity resides in Ring1b and not in Bmi1 | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
I53A | the Ring1b/Bmi1 complex with an I53A mutation in Ring1b has almost no catalytic activity | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q99496 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [histone H2A]-L-lysine | - |
Homo sapiens | [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[histone H2A]-L-lysine | E3-ligase activity of isoform Ring1b on histone H2A is enhanced by polycomb group protein Bmi1 in vitro. The N-terminal Ring-domains are sufficient for this activity and Ring1a can replace Ring1b. E2 enzymes UbcH5a, b, c or UbcH6 support this activity with varying processivity and selectivity | ? | |
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [Ring1b]-L-lysine | - |
Homo sapiens | [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[Ring1b]-L-lysine | autoubiquitination reaction, E2 enzymes UbcH5a, b, c or UbcH6 support autoubiquitination | ? |
Synonyms | Comment | Organism |
---|---|---|
Ring1B | - |
Homo sapiens |
RNF2 | - |
Homo sapiens |