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http://purl.uniprot.org/citations/17643117http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17643117http://www.w3.org/2000/01/rdf-schema#comment"The serine/threonine kinase human Pim1 (hereafter PIM1) cooperates with human c-Myc (hereafter MYC) in cell cycle progression and tumorigenesis. However, the nature of this cooperation is still unknown. Here we show that, after stimulation with growth factor, PIM1 forms a complex with the dimer of MYC with MAX (Myc-associated factor X) via the MYC BoxII (MBII) domain. MYC recruits PIM1 to the E boxes of the MYC-target genes FOSL1 (FRA-1) and ID2, and PIM1 phosphorylates serine 10 of histone H3 (H3S10) on the nucleosome at the MYC-binding sites, contributing to their transcriptional activation. MYC and PIM1 colocalize at sites of active transcription, and expression profile analysis revealed that PIM1 contributes to the regulation of 20% of the MYC-regulated genes. Moreover, PIM1-dependent H3S10 phosphorylation contributes to MYC transforming capacity. These results establish a new function for PIM1 as a MYC cofactor that phosphorylates the chromatin at MYC-target loci and suggest that nucleosome phosphorylation, at E boxes, contributes to MYC-dependent transcriptional activation and cellular transformation."xsd:string
http://purl.uniprot.org/citations/17643117http://purl.org/dc/terms/identifier"doi:10.1038/ncb1618"xsd:string
http://purl.uniprot.org/citations/17643117http://purl.uniprot.org/core/author"Oliviero S."xsd:string
http://purl.uniprot.org/citations/17643117http://purl.uniprot.org/core/author"Zippo A."xsd:string
http://purl.uniprot.org/citations/17643117http://purl.uniprot.org/core/author"Serafini R."xsd:string
http://purl.uniprot.org/citations/17643117http://purl.uniprot.org/core/author"De Robertis A."xsd:string
http://purl.uniprot.org/citations/17643117http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17643117http://purl.uniprot.org/core/name"Nat Cell Biol"xsd:string
http://purl.uniprot.org/citations/17643117http://purl.uniprot.org/core/pages"932-944"xsd:string
http://purl.uniprot.org/citations/17643117http://purl.uniprot.org/core/title"PIM1-dependent phosphorylation of histone H3 at serine 10 is required for MYC-dependent transcriptional activation and oncogenic transformation."xsd:string
http://purl.uniprot.org/citations/17643117http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/17643117http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17643117
http://purl.uniprot.org/citations/17643117http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17643117
http://purl.uniprot.org/uniprot/#_A0A0B4J1R1-mappedCitation-17643117http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17643117
http://purl.uniprot.org/uniprot/#_A0N2G3-mappedCitation-17643117http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17643117
http://purl.uniprot.org/uniprot/#_A0A224B085-mappedCitation-17643117http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17643117
http://purl.uniprot.org/uniprot/#_B3CJ86-mappedCitation-17643117http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17643117
http://purl.uniprot.org/uniprot/#_B3CJ87-mappedCitation-17643117http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17643117
http://purl.uniprot.org/uniprot/#_B3CJ88-mappedCitation-17643117http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17643117
http://purl.uniprot.org/uniprot/#_B3CJB3-mappedCitation-17643117http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17643117
http://purl.uniprot.org/uniprot/#_B3CJB8-mappedCitation-17643117http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17643117
http://purl.uniprot.org/uniprot/#_B3CJ63-mappedCitation-17643117http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17643117
http://purl.uniprot.org/uniprot/#_B3CJ64-mappedCitation-17643117http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17643117
http://purl.uniprot.org/uniprot/#_B3CJ76-mappedCitation-17643117http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17643117