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DESCRIBE <http://purl.uniprot.org/SHA-384/1F08F85FBAF1920089C3C0296A295FBED5F5EC5FE00ED7E04B5850EC7E269D979610D653AAEE11DFB7BC6BD2A824D44F>
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http://purl.uniprot.org/SHA-384/1F08F85FBAF1920089C3C0296A295FBED5F5EC5FE00ED7E04B5850EC7E269D979610D653AAEE11DFB7BC6BD2A824D44F
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/1F08F85FBAF1920089C3C0296A295FBED5F5EC5FE00ED7E04B5850EC7E269D979610D653AAEE11DFB7BC6BD2A824D44F
http://www.w3.org/2000/01/rdf-schema#comment
"Study identifies the residues on EZH2 that are critical for its interaction with VAV and demonstrate that EZH2 interactions with VAV proteins are crucial for the regulation of adhesion dynamics and cellular transformation."
xsd:string
http://purl.uniprot.org/uniprot/#_E39C8EDD25E3EAF134D4E5DB94E6590764E8465FD8C7961D4B198A868480016C884968A938CC724154A0BECAF127936B
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/1F08F85FBAF1920089C3C0296A295FBED5F5EC5FE00ED7E04B5850EC7E269D979610D653AAEE11DFB7BC6BD2A824D44F
http://purl.uniprot.org/uniprot/P15498
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/1F08F85FBAF1920089C3C0296A295FBED5F5EC5FE00ED7E04B5850EC7E269D979610D653AAEE11DFB7BC6BD2A824D44F
http://purl.uniprot.org/uniprot/#_P15498-mappedCitation-28967906
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/1F08F85FBAF1920089C3C0296A295FBED5F5EC5FE00ED7E04B5850EC7E269D979610D653AAEE11DFB7BC6BD2A824D44F