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DESCRIBE <http://purl.uniprot.org/SHA-384/63000CD6358BD6306EA3F55B3197F58127C0F4D8D3CDB21EE39CE3BB21CE1A97F25D51A7C92B5578FEDD99223BAB2B26>
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http://purl.uniprot.org/SHA-384/63000CD6358BD6306EA3F55B3197F58127C0F4D8D3CDB21EE39CE3BB21CE1A97F25D51A7C92B5578FEDD99223BAB2B26
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/63000CD6358BD6306EA3F55B3197F58127C0F4D8D3CDB21EE39CE3BB21CE1A97F25D51A7C92B5578FEDD99223BAB2B26
http://www.w3.org/2000/01/rdf-schema#comment
"Mutation of a key residue (K273A) within the canonical phosphatidylinositol phosphate - binding site of Grp1 significantly reduced the free energy of phosphatidylinositol phosphate binding."
xsd:string
http://purl.uniprot.org/uniprot/#_085EBB947725D86D60CA7D0486FC252AEF9D21B722821786AAC901C7F0DE4E71C207873879555F482E708C4617062606
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/63000CD6358BD6306EA3F55B3197F58127C0F4D8D3CDB21EE39CE3BB21CE1A97F25D51A7C92B5578FEDD99223BAB2B26
http://purl.uniprot.org/uniprot/Q5DTF5
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/63000CD6358BD6306EA3F55B3197F58127C0F4D8D3CDB21EE39CE3BB21CE1A97F25D51A7C92B5578FEDD99223BAB2B26
http://purl.uniprot.org/uniprot/#_Q5DTF5-mappedCitation-26977543
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/63000CD6358BD6306EA3F55B3197F58127C0F4D8D3CDB21EE39CE3BB21CE1A97F25D51A7C92B5578FEDD99223BAB2B26