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http://purl.uniprot.org/SHA-384/AA3499C046B72D4D87B4972B7B7A4B160A1FB3075CBC6D65FCBF08116E611112E186B315065256B08B482513E680F00Ehttp://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/AA3499C046B72D4D87B4972B7B7A4B160A1FB3075CBC6D65FCBF08116E611112E186B315065256B08B482513E680F00Ehttp://www.w3.org/2000/01/rdf-schema#comment"HSF1 phosphorylation at both Ser303 (S303) and Ser307 (S307) has been shown to repress HSF1 transcriptional activity under normal physiological growth conditions. Our results confirmed that loss of phosphorylation in HSF1(303A/307A) cells and tissues increases protein stability but also markedly sensitizes HSF1 activation under normal and heat- or nutrient-induced stress conditions."xsd:string
http://purl.uniprot.org/uniprot/#_13CDF42DA10203A43F8DB4BC4F4FD99B678791CFADB82A560812A42A59ACB779035781B8D1377184D20EDEF47FEC2075http://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/AA3499C046B72D4D87B4972B7B7A4B160A1FB3075CBC6D65FCBF08116E611112E186B315065256B08B482513E680F00E
http://purl.uniprot.org/uniprot/P38532http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/AA3499C046B72D4D87B4972B7B7A4B160A1FB3075CBC6D65FCBF08116E611112E186B315065256B08B482513E680F00E
http://purl.uniprot.org/uniprot/#_P38532-mappedCitation-29941492http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/AA3499C046B72D4D87B4972B7B7A4B160A1FB3075CBC6D65FCBF08116E611112E186B315065256B08B482513E680F00E