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DESCRIBE <http://purl.uniprot.org/SHA-384/F9272680954152D0254E2106775D074583539B6C209E48D242989EB3484FC9A522053FFECEACF49075CB643433F2E85B>
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http://purl.uniprot.org/SHA-384/F9272680954152D0254E2106775D074583539B6C209E48D242989EB3484FC9A522053FFECEACF49075CB643433F2E85B
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/F9272680954152D0254E2106775D074583539B6C209E48D242989EB3484FC9A522053FFECEACF49075CB643433F2E85B
http://www.w3.org/2000/01/rdf-schema#comment
"phosphorylation and K201 acted similarly to change the conformation of RyR1/2 and regulate FKBP12/12.6 binding."
xsd:string
http://purl.uniprot.org/uniprot/#_33BDB37BCF44252F45A81188FD91E0846CE9F51EDAFFCD8BC226CA1A861F1D4A70A414A7680E2C7058DC405C69F3F269
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/F9272680954152D0254E2106775D074583539B6C209E48D242989EB3484FC9A522053FFECEACF49075CB643433F2E85B
http://purl.uniprot.org/uniprot/P62943
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/F9272680954152D0254E2106775D074583539B6C209E48D242989EB3484FC9A522053FFECEACF49075CB643433F2E85B
http://purl.uniprot.org/uniprot/#_P62943-mappedCitation-19661110
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/F9272680954152D0254E2106775D074583539B6C209E48D242989EB3484FC9A522053FFECEACF49075CB643433F2E85B