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DESCRIBE <http://purl.uniprot.org/SHA-384/A026D38037EC2021F30E82C9A91567BDC7DB2AAE1A97CE4F3961048F2B84B5A637E737E1B1DE1C2AE2BD80708CD583FF>
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http://purl.uniprot.org/SHA-384/A026D38037EC2021F30E82C9A91567BDC7DB2AAE1A97CE4F3961048F2B84B5A637E737E1B1DE1C2AE2BD80708CD583FF
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/A026D38037EC2021F30E82C9A91567BDC7DB2AAE1A97CE4F3961048F2B84B5A637E737E1B1DE1C2AE2BD80708CD583FF
http://www.w3.org/2000/01/rdf-schema#comment
"Studies sugget the effect of CaMKII autophosphorylation at Thr286 on calmodulin trapping that it stabilises the active state and therefore makes the high-affinity binding site accessible."
xsd:string
http://purl.uniprot.org/uniprot/#_910855D2210FFFAAA5CB09B0F8052644F14064301A121A61DBB6053E989B62869054FFED7F4353D079A48AC98F9BDA7D
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/A026D38037EC2021F30E82C9A91567BDC7DB2AAE1A97CE4F3961048F2B84B5A637E737E1B1DE1C2AE2BD80708CD583FF
http://purl.uniprot.org/uniprot/G5EDZ5
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/A026D38037EC2021F30E82C9A91567BDC7DB2AAE1A97CE4F3961048F2B84B5A637E737E1B1DE1C2AE2BD80708CD583FF
http://purl.uniprot.org/uniprot/#_G5EDZ5-mappedCitation-22279535
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/A026D38037EC2021F30E82C9A91567BDC7DB2AAE1A97CE4F3961048F2B84B5A637E737E1B1DE1C2AE2BD80708CD583FF