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http://purl.uniprot.org/citations/24130829http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24130829http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24130829http://www.w3.org/2000/01/rdf-schema#comment"Mixed Lineage Leukemia 5 (MLL5) is a histone methyltransferase that plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. In addition to its catalytic domain, MLL5 contains a PHD finger domain, a protein module that is often involved in binding to the N-terminus of histone H3. Here we report the NMR solution structure of the MLL5 PHD domain showing a variant of the canonical PHD fold that combines conserved H3 binding features from several classes of other PHD domains (including an aromatic cage) along with a novel C-terminal α-helix, not previously seen. We further demonstrate that the PHD domain binds with similar affinity to histone H3 tail peptides di- and tri-methylated at lysine 4 (H3K4me2 and H3K4me3), the former being the putative product of the MLL5 catalytic reaction. This work establishes the PHD domain of MLL5 as a bone fide 'reader' domain of H3K4 methyl marks suggesting that it may guide the spreading or further methylation of this site on chromatin."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0077020"xsd:string
http://purl.uniprot.org/citations/24130829http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0077020"xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Arrowsmith C.H."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Arrowsmith C.H."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Wu H."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Wu H."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Zeng H."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Zeng H."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Yee A."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Yee A."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Aparicio S."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Aparicio S."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Houliston S."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Houliston S."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Dombrovski L."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Dombrovski L."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Lemak A."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Lemak A."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Yap D."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/author"Yap D."xsd:string
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24130829http://purl.uniprot.org/core/date"2013"xsd:gYear