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http://purl.uniprot.org/citations/30100186http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30100186http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30100186http://www.w3.org/2000/01/rdf-schema#comment"The methylation of histone 3 lysine 4 (H3K4) is carried out by an evolutionarily conserved family of methyltransferases referred to as complex of proteins associated with Set1 (COMPASS). The activity of the catalytic SET domain (su(var)3-9, enhancer-of-zeste, and trithorax) is endowed through forming a complex with a set of core proteins that are widely shared from yeast to humans. We obtained cryo-electron microscopy (cryo-EM) maps of the yeast Set1/COMPASS core complex at overall 4.0-to 4.4-Å resolution, providing insights into its structural organization and conformational dynamics. The Cps50 C-terminal tail weaves within the complex to provide a central scaffold for assembly. The SET domain, snugly positioned at the junction of the Y-shaped complex, is extensively contacted by Cps60 (Bre2), Cps50 (Swd1), and Cps30 (Swd3). The mobile SET-I motif of the SET domain is engaged by Cps30, explaining its key role in COMPASS catalytic activity toward higher H3K4 methylation states."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2018.07.020"xsd:string
http://purl.uniprot.org/citations/30100186http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2018.07.020"xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Hu H."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Hu H."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Qu Q."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Qu Q."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Skiniotis G."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Skiniotis G."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Yang Y."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Yang Y."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Brunzelle J.S."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Brunzelle J.S."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Couture J.F."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Couture J.F."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Shilatifard A."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Shilatifard A."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Takahashi Y.H."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/author"Takahashi Y.H."xsd:string
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/30100186http://purl.uniprot.org/core/date"2018"xsd:gYear