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DESCRIBE <http://purl.uniprot.org/SHA-384/B0979C9E7A0E36FE13CEB9B7E565BF7F997E95F53F28E3F79EDB7C19D798B16E8E93D2DCCA590DE4A47347E55AFB992A>
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http://purl.uniprot.org/SHA-384/B0979C9E7A0E36FE13CEB9B7E565BF7F997E95F53F28E3F79EDB7C19D798B16E8E93D2DCCA590DE4A47347E55AFB992A
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/B0979C9E7A0E36FE13CEB9B7E565BF7F997E95F53F28E3F79EDB7C19D798B16E8E93D2DCCA590DE4A47347E55AFB992A
http://www.w3.org/2000/01/rdf-schema#comment
"Results suggest that Gly594 and Glu595 in transmembrane domain 10 of hPEPT1 have key roles in substrate transport and that Tyr588 may have an important secondary mechanistic role."
xsd:string
http://purl.uniprot.org/uniprot/#_D447C38AFE2B1B50D1BDBF5E9B9D28B0A6F818537FAD65350B4F6E5619BDE10464214A03660F3943A34C347B287983F0
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/B0979C9E7A0E36FE13CEB9B7E565BF7F997E95F53F28E3F79EDB7C19D798B16E8E93D2DCCA590DE4A47347E55AFB992A
http://purl.uniprot.org/uniprot/Q6GV26
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/B0979C9E7A0E36FE13CEB9B7E565BF7F997E95F53F28E3F79EDB7C19D798B16E8E93D2DCCA590DE4A47347E55AFB992A
http://purl.uniprot.org/uniprot/#_Q6GV26-mappedCitation-19685173
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/B0979C9E7A0E36FE13CEB9B7E565BF7F997E95F53F28E3F79EDB7C19D798B16E8E93D2DCCA590DE4A47347E55AFB992A