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Literature summary extracted from

  • Buchwald, G.; van der Stoop, P.; Weichenrieder, O.; Perrakis, A.; van Lohuizen, M.; Sixma, T.K.
    Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b (2006), EMBO J., 25, 2465-2474.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.2.27 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

EC Number Protein Variants Comment Organism
2.3.2.27 I53A the Ring1b/Bmi1 complex with an I53A mutation in Ring1b has almost no catalytic activity Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.27 Homo sapiens Q99496
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.27 S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [histone H2A]-L-lysine
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 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 ?
2.3.2.27 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

EC Number Synonyms Comment Organism
2.3.2.27 Ring1B
-
 Homo sapiens
2.3.2.27 RNF2
-
 Homo sapiens