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http://purl.uniprot.org/SHA-384/4C97E4DCA11E43420CED83A0B66F9124E5B904FB9DA22F29891076D4341516B023F39AF776E81BD392976B9CFF68320Ahttp://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/4C97E4DCA11E43420CED83A0B66F9124E5B904FB9DA22F29891076D4341516B023F39AF776E81BD392976B9CFF68320Ahttp://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/#_1B31D33034019E655711315D82F52917A45A488EBC2D61BA4ADB67CC82923CAFE7E899B5F7629656B82B0CAD188393EBhttp://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/4C97E4DCA11E43420CED83A0B66F9124E5B904FB9DA22F29891076D4341516B023F39AF776E81BD392976B9CFF68320A
http://purl.uniprot.org/uniprot/Q9UJZ8http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/4C97E4DCA11E43420CED83A0B66F9124E5B904FB9DA22F29891076D4341516B023F39AF776E81BD392976B9CFF68320A
http://purl.uniprot.org/uniprot/#_Q9UJZ8-mappedCitation-28430576http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/4C97E4DCA11E43420CED83A0B66F9124E5B904FB9DA22F29891076D4341516B023F39AF776E81BD392976B9CFF68320A