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DESCRIBE <http://purl.uniprot.org/SHA-384/8760F7C1D9C91E4FC130DB9027A8FC59CF2494DB0FDFBBB0F89F15D54B65923DC2E2DC8B51023EA875B16E4D6AB86236>
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http://purl.uniprot.org/SHA-384/8760F7C1D9C91E4FC130DB9027A8FC59CF2494DB0FDFBBB0F89F15D54B65923DC2E2DC8B51023EA875B16E4D6AB86236
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/8760F7C1D9C91E4FC130DB9027A8FC59CF2494DB0FDFBBB0F89F15D54B65923DC2E2DC8B51023EA875B16E4D6AB86236
http://www.w3.org/2000/01/rdf-schema#comment
"These results suggest a conserved lipid binding mechanism in which Ca(2+)-independent interactions are mediated via a lysine rich region of the C2B domain while Ca(2+)-dependent interactions are mediated via the Ca(2+)-binding loops."
xsd:string
http://purl.uniprot.org/uniprot/#_5D9BB1DE399344867C96238625F0DB8B3FF0F8C02EEE2DB2A77E64F933AF429669F857448BD248A9F73FF0DF5327B7E6
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/8760F7C1D9C91E4FC130DB9027A8FC59CF2494DB0FDFBBB0F89F15D54B65923DC2E2DC8B51023EA875B16E4D6AB86236
http://purl.uniprot.org/uniprot/P21707
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/8760F7C1D9C91E4FC130DB9027A8FC59CF2494DB0FDFBBB0F89F15D54B65923DC2E2DC8B51023EA875B16E4D6AB86236
http://purl.uniprot.org/uniprot/#_P21707-mappedCitation-21928778
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/8760F7C1D9C91E4FC130DB9027A8FC59CF2494DB0FDFBBB0F89F15D54B65923DC2E2DC8B51023EA875B16E4D6AB86236