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http://purl.uniprot.org/SHA-384/17FB4CF514EDA6F87B42D2FCFA80073C0EEB05369EF8F4ACD0D28B3803001BE1B4FC08BF6711D5692D490705156F03ABhttp://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/17FB4CF514EDA6F87B42D2FCFA80073C0EEB05369EF8F4ACD0D28B3803001BE1B4FC08BF6711D5692D490705156F03ABhttp://www.w3.org/2000/01/rdf-schema#comment"Binding of phosphatidylinositol 4 5-biphosphate to ezrin induces a conformational change permitting the insertion of the LOK C-terminal domain to wedge apart the membrane and F-actin-binding domains of ezrin. The N-terminal LOK kinase domain can then access a site 40 residues distal from the consensus sequence that collectively direct phosphorylation of the appropriate threonine residue."xsd:string
http://purl.uniprot.org/uniprot/#_B440E33F600EB52D61EF7FC22C8EE863661093D28A160825CA00947B108720B7111FE9A97FEE6C8420E7865B14AEAF5Ahttp://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/17FB4CF514EDA6F87B42D2FCFA80073C0EEB05369EF8F4ACD0D28B3803001BE1B4FC08BF6711D5692D490705156F03AB
http://purl.uniprot.org/uniprot/Q9UJZ2http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/17FB4CF514EDA6F87B42D2FCFA80073C0EEB05369EF8F4ACD0D28B3803001BE1B4FC08BF6711D5692D490705156F03AB
http://purl.uniprot.org/uniprot/#_Q9UJZ2-mappedCitation-28430576http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/17FB4CF514EDA6F87B42D2FCFA80073C0EEB05369EF8F4ACD0D28B3803001BE1B4FC08BF6711D5692D490705156F03AB