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SubjectPredicateObject
http://purl.uniprot.org/SHA-384/E5F3CF66094E932C54C2BE8E295830B5E9175E4D2468A5772C79C09B9E6D2263D40E219BC7C8C1833D915A15EAE2FBD6http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/E5F3CF66094E932C54C2BE8E295830B5E9175E4D2468A5772C79C09B9E6D2263D40E219BC7C8C1833D915A15EAE2FBD6http://www.w3.org/2000/01/rdf-schema#comment"Chromatin immunoprecipitation kinetics revealed that HDAC2 accumulates at the RNASE1 promoter upon TNF-alpha stimulation indicating an essential role for HDAC2 in regulating RNase1 expression. Thus proinflammatory stimulation induced recruitment of HDAC2 to attenuate histone acetylation at the RNASE1 promoter site."xsd:string
http://purl.uniprot.org/uniprot/#_288785C5D3552B32D320D7F27AE47366AAAA74075D9AF02E10F5E325EAF3F73CCDB8289463BC7701CEC244E81A06ECABhttp://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/E5F3CF66094E932C54C2BE8E295830B5E9175E4D2468A5772C79C09B9E6D2263D40E219BC7C8C1833D915A15EAE2FBD6
http://purl.uniprot.org/uniprot/P07998http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/E5F3CF66094E932C54C2BE8E295830B5E9175E4D2468A5772C79C09B9E6D2263D40E219BC7C8C1833D915A15EAE2FBD6
http://purl.uniprot.org/uniprot/#_P07998-mappedCitation-31039328http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/E5F3CF66094E932C54C2BE8E295830B5E9175E4D2468A5772C79C09B9E6D2263D40E219BC7C8C1833D915A15EAE2FBD6