Title : BAHCC1 binds H3K27me3 via a conserved BAH module to mediate gene silencing and oncogenesis.

Pub. Date : 2020 Dec

PMID : 33139953






3 Functional Relationships(s)
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1 Biochemical, structural and integrated chromatin immunoprecipitation-sequencing-based analyses demonstrate that direct readout of H3K27me3 by BAHCC1 is achieved through a hydrophobic trimethyl-L-lysine-binding "cage" formed by BAHCC1BAH, mediating colocalization of BAHCC1 and H3K27me3-marked genes. trimethyllysine BAH domain and coiled-coil containing 1 Homo sapiens
2 Biochemical, structural and integrated chromatin immunoprecipitation-sequencing-based analyses demonstrate that direct readout of H3K27me3 by BAHCC1 is achieved through a hydrophobic trimethyl-L-lysine-binding "cage" formed by BAHCC1BAH, mediating colocalization of BAHCC1 and H3K27me3-marked genes. trimethyllysine BAH domain and coiled-coil containing 1 Homo sapiens
3 Biochemical, structural and integrated chromatin immunoprecipitation-sequencing-based analyses demonstrate that direct readout of H3K27me3 by BAHCC1 is achieved through a hydrophobic trimethyl-L-lysine-binding "cage" formed by BAHCC1BAH, mediating colocalization of BAHCC1 and H3K27me3-marked genes. trimethyllysine BAH domain and coiled-coil containing 1 Homo sapiens