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DESCRIBE <http://purl.uniprot.org/SHA-384/E73C6C5340CC6AC5D757C69C386C7DB6BEBA35B24BA0F67E774BC1E008C586ABAA52B5F7DB2A2DE402E6E6CB2AF1476F>
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http://purl.uniprot.org/SHA-384/E73C6C5340CC6AC5D757C69C386C7DB6BEBA35B24BA0F67E774BC1E008C586ABAA52B5F7DB2A2DE402E6E6CB2AF1476F
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/E73C6C5340CC6AC5D757C69C386C7DB6BEBA35B24BA0F67E774BC1E008C586ABAA52B5F7DB2A2DE402E6E6CB2AF1476F
http://www.w3.org/2000/01/rdf-schema#comment
"These studies establish that the binding of HEG1 to Rasip1 mediates Rap1-dependent recruitment of Rasip1 to and stabilization of endothelial cell cell-cell junctions."
xsd:string
http://purl.uniprot.org/uniprot/#_8130FEB95A6E6E738D8C88214938F54B23B329FB9A16DCA407BD48A9234ED3EF8F2CA945EAD09FC6E1D7DDF64BCA9182
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/E73C6C5340CC6AC5D757C69C386C7DB6BEBA35B24BA0F67E774BC1E008C586ABAA52B5F7DB2A2DE402E6E6CB2AF1476F
http://purl.uniprot.org/uniprot/Q9NX72
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/E73C6C5340CC6AC5D757C69C386C7DB6BEBA35B24BA0F67E774BC1E008C586ABAA52B5F7DB2A2DE402E6E6CB2AF1476F
http://purl.uniprot.org/uniprot/#_Q9NX72-mappedCitation-26780829
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/E73C6C5340CC6AC5D757C69C386C7DB6BEBA35B24BA0F67E774BC1E008C586ABAA52B5F7DB2A2DE402E6E6CB2AF1476F