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Literature summary for 2.3.2.27 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 PubMed
Search for more literature for 2.3.2.27

Crystallization (Commentary)

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

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

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Homo sapiens Q99496
-
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
Ring1B
-
 Homo sapiens
RNF2
-
 Homo sapiens