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DESCRIBE <http://purl.uniprot.org/SHA-384/4AD43DFBA21B9760EEC5163535A3F364B08AFF058A92EF02B620C6347E2AA7B8A7C0F38D537A1A0300DBD1E06DA4B550>
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http://purl.uniprot.org/SHA-384/4AD43DFBA21B9760EEC5163535A3F364B08AFF058A92EF02B620C6347E2AA7B8A7C0F38D537A1A0300DBD1E06DA4B550
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/4AD43DFBA21B9760EEC5163535A3F364B08AFF058A92EF02B620C6347E2AA7B8A7C0F38D537A1A0300DBD1E06DA4B550
http://www.w3.org/2000/01/rdf-schema#comment
"Furthermore mammalian target of rapamycin was implicated in ORP9L phosphorylation in HEK293 cells. These studies identify ORP9 as a PDK-2 substrate and negative regulator of Akt phosphorylation at the PDK-2 site."
xsd:string
http://purl.uniprot.org/uniprot/#_77CA10D46517B4D4B1AE65546FCBF5EC3C0C6A56CC4FC26312BF3F9C7156D9D99E69AE3A7A367174A4DBA1D26565976F
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/4AD43DFBA21B9760EEC5163535A3F364B08AFF058A92EF02B620C6347E2AA7B8A7C0F38D537A1A0300DBD1E06DA4B550
http://purl.uniprot.org/uniprot/Q96SU4
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/4AD43DFBA21B9760EEC5163535A3F364B08AFF058A92EF02B620C6347E2AA7B8A7C0F38D537A1A0300DBD1E06DA4B550
http://purl.uniprot.org/uniprot/#_Q96SU4-mappedCitation-16962287
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/4AD43DFBA21B9760EEC5163535A3F364B08AFF058A92EF02B620C6347E2AA7B8A7C0F38D537A1A0300DBD1E06DA4B550