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http://purl.uniprot.org/citations/30604749http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30604749http://www.w3.org/2000/01/rdf-schema#comment"MLL3 and MLL4 are two closely related members of the SET1/MLL family of histone H3K4 methyltransferases and are responsible for monomethylating histone H3K4 on enhancers, which are essential in regulating cell-type-specific gene expression. Mutations of MLL3 or MLL4 have been reported in different types of cancer. Recently, the PHD domains of MLL3/4 have been reported to recruit the MLL3/4 complexes to their target genes by binding to histone H4 during the NT2/D1 stem cell differentiation. Here we show that an extended PHD domain (ePHD6) involving the sixth PHD domain and its preceding zinc finger in MLL3 and MLL4 specifically recognizes an H4H18-containing histone H4 fragment and that modifications of residues surrounding H4H18 modulate H4 binding to MLL3/4. Our in vitro methyltransferase assays and cellular experiments further reveal that the interaction between ePHD6 of MLL3/4 and histone H4 is required for their nucleosomal methylation activity and MLL4-mediated neuronal differentiation of NT2/D1 cells."xsd:string
http://purl.uniprot.org/citations/30604749http://purl.org/dc/terms/identifier"doi:10.1038/s41467-018-07906-3"xsd:string
http://purl.uniprot.org/citations/30604749http://purl.uniprot.org/core/author"Liu Y."xsd:string
http://purl.uniprot.org/citations/30604749http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/30604749http://purl.uniprot.org/core/author"Lei M."xsd:string
http://purl.uniprot.org/citations/30604749http://purl.uniprot.org/core/author"Qin S."xsd:string
http://purl.uniprot.org/citations/30604749http://purl.uniprot.org/core/author"Min J."xsd:string
http://purl.uniprot.org/citations/30604749http://purl.uniprot.org/core/author"Dong A."xsd:string
http://purl.uniprot.org/citations/30604749http://purl.uniprot.org/core/author"Loppnau P."xsd:string
http://purl.uniprot.org/citations/30604749http://purl.uniprot.org/core/author"Lee M.G."xsd:string
http://purl.uniprot.org/citations/30604749http://purl.uniprot.org/core/author"Chen T.Y."xsd:string
http://purl.uniprot.org/citations/30604749http://purl.uniprot.org/core/author"Ho J.C."xsd:string
http://purl.uniprot.org/citations/30604749http://purl.uniprot.org/core/author"Dhar S.S."xsd:string
http://purl.uniprot.org/citations/30604749http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/30604749http://purl.uniprot.org/core/name"Nat Commun"xsd:string
http://purl.uniprot.org/citations/30604749http://purl.uniprot.org/core/pages"36"xsd:string
http://purl.uniprot.org/citations/30604749http://purl.uniprot.org/core/title"Structural insights into trans-histone regulation of H3K4 methylation by unique histone H4 binding of MLL3/4."xsd:string
http://purl.uniprot.org/citations/30604749http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/30604749http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/30604749
http://purl.uniprot.org/citations/30604749http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/30604749
http://purl.uniprot.org/uniprot/#_P62805-mappedCitation-30604749http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30604749
http://purl.uniprot.org/uniprot/#_Q9UMN6-mappedCitation-30604749http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30604749
http://purl.uniprot.org/uniprot/#_Q8NEZ4-mappedCitation-30604749http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30604749
http://purl.uniprot.org/uniprot/Q8NEZ4http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/30604749