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From Proteopedia
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</table> | </table> | ||
== Function == | == Function == | ||
- | [https://www.uniprot.org/uniprot/ | + | [https://www.uniprot.org/uniprot/H3_DROME H3_DROME] |
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Histone H2A monoubiquitination (H2Aub1) by the PRC1 subunit RING1B entails a positive feedback loop, mediated by the RING1B-interacting protein RYBP. We uncover that human RYBP-PRC1 binds unmodified nucleosomes via RING1B but H2Aub1-modified nucleosomes via RYBP. RYBP interactions with both ubiquitin and the nucleosome acidic patch create the high binding affinity that favors RYBP- over RING1B-directed PRC1 binding to H2Aub1-modified nucleosomes; this enables RING1B to monoubiquitinate H2A in neighboring unmodified nucleosomes. | ||
+ | |||
+ | Structural basis of the histone ubiquitination read-write mechanism of RYBP-PRC1.,Ciapponi M, Karlukova E, Schkolziger S, Benda C, Muller J Nat Struct Mol Biol. 2024 Jul;31(7):1023-1027. doi: 10.1038/s41594-024-01258-x. , Epub 2024 Mar 25. PMID:38528151<ref>PMID:38528151</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 8pp6" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Current revision
human RYBP-PRC1 bound to H2AK118ub1 nucleosome
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