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DESCRIBE <http://purl.uniprot.org/SHA-384/69EBCB13F16853BAE4DEBAD15214B384C41718E41A6E2315D418EB2B4EDFA3F45909F7AB7E46DC17E5EE53584A6D4E26>
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http://purl.uniprot.org/SHA-384/69EBCB13F16853BAE4DEBAD15214B384C41718E41A6E2315D418EB2B4EDFA3F45909F7AB7E46DC17E5EE53584A6D4E26
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/69EBCB13F16853BAE4DEBAD15214B384C41718E41A6E2315D418EB2B4EDFA3F45909F7AB7E46DC17E5EE53584A6D4E26
http://www.w3.org/2000/01/rdf-schema#comment
"Data indicate that the effects of irisin were abolished by the inhibition of phosphoinositide 3-kinase (PI3K) p110alpha subunit and the phosphorylation of Akt/protein kinase B."
xsd:string
http://purl.uniprot.org/uniprot/#_6626315227D9022DDFB3769AF4A975487064A56292B9B78FA45D5349F1A844F5AC30E910C860E7B0F96F478E8379F49E
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/69EBCB13F16853BAE4DEBAD15214B384C41718E41A6E2315D418EB2B4EDFA3F45909F7AB7E46DC17E5EE53584A6D4E26
http://purl.uniprot.org/uniprot/Q8BS26
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/69EBCB13F16853BAE4DEBAD15214B384C41718E41A6E2315D418EB2B4EDFA3F45909F7AB7E46DC17E5EE53584A6D4E26
http://purl.uniprot.org/uniprot/#_Q8BS26-mappedCitation-26201094
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/69EBCB13F16853BAE4DEBAD15214B384C41718E41A6E2315D418EB2B4EDFA3F45909F7AB7E46DC17E5EE53584A6D4E26