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http://purl.uniprot.org/SHA-384/78A2183CA74E709CFA8BBEF9953CAC46028691F892B28C0F1867AB438F6FEF31D3BAC4ACB0F6865209F38533F20EAD96http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/78A2183CA74E709CFA8BBEF9953CAC46028691F892B28C0F1867AB438F6FEF31D3BAC4ACB0F6865209F38533F20EAD96http://www.w3.org/2000/01/rdf-schema#comment"Findings reveal a RACK7/KDM5C-regulated dynamic interchange between histone H3K4me1 and H3K4me3 at active enhancers representing an additional layer of regulation of enhancer activity. Authors propose that RACK7/KDM5C functions as an enhancer "brake" to ensure appropriate enhancer activity which when compromised could contribute to tumorigenesis."xsd:string
http://purl.uniprot.org/uniprot/#_A681508BA81183FCF3DF3D5FD9A974F55F7B5826C9ED8FAE5A95BE9EB5C636A1FA683584833F9A70AD43B2101A34779Chttp://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/78A2183CA74E709CFA8BBEF9953CAC46028691F892B28C0F1867AB438F6FEF31D3BAC4ACB0F6865209F38533F20EAD96
http://purl.uniprot.org/uniprot/P41229http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/78A2183CA74E709CFA8BBEF9953CAC46028691F892B28C0F1867AB438F6FEF31D3BAC4ACB0F6865209F38533F20EAD96
http://purl.uniprot.org/uniprot/#_P41229-mappedCitation-27058665http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/78A2183CA74E709CFA8BBEF9953CAC46028691F892B28C0F1867AB438F6FEF31D3BAC4ACB0F6865209F38533F20EAD96