DESCRIBE <http://purl.uniprot.org/SHA-384/7DCA4ABD7F483616A049C27BD1B3870EA9E9BD0D89506ADA90C9327812AA6AA1AA89BCB84D2FD7A528FF865E57F372B4>

Subject	Predicate	Object
http://purl.uniprot.org/SHA-384/7DCA4ABD7F483616A049C27BD1B3870EA9E9BD0D89506ADA90C9327812AA6AA1AA89BCB84D2FD7A528FF865E57F372B4	http://www.w3.org/1999/02/22-rdf-syntax-ns#type	http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/7DCA4ABD7F483616A049C27BD1B3870EA9E9BD0D89506ADA90C9327812AA6AA1AA89BCB84D2FD7A528FF865E57F372B4	http://www.w3.org/2000/01/rdf-schema#comment	"Using molecular modeling and molecular dynamics simulations we show that Asp344 Asp352 and Thr356 in kindlin-2 and Arg243 and Arg334 in ILK kinase domain (KD) are important in kindlin-2/ILK complex formation. Mutations that disrupt these interactions abrogate kindlin-2 and ILK colocalization in HeLa cells."xsd:string
http://purl.uniprot.org/uniprot/#_5BDD1F490DAE976EBF189A68E551FE01B4964D36BD2C1C4FC900A0E5EFC0D7BAF004FD6D3E794353B7788966B4840628	http://www.w3.org/1999/02/22-rdf-syntax-ns#subject	http://purl.uniprot.org/SHA-384/7DCA4ABD7F483616A049C27BD1B3870EA9E9BD0D89506ADA90C9327812AA6AA1AA89BCB84D2FD7A528FF865E57F372B4
http://purl.uniprot.org/uniprot/V9HWF0	http://purl.uniprot.org/core/mappedAnnotation	http://purl.uniprot.org/SHA-384/7DCA4ABD7F483616A049C27BD1B3870EA9E9BD0D89506ADA90C9327812AA6AA1AA89BCB84D2FD7A528FF865E57F372B4
http://purl.uniprot.org/uniprot/#_V9HWF0-mappedCitation-29237230	http://purl.uniprot.org/core/mappedAnnotation	http://purl.uniprot.org/SHA-384/7DCA4ABD7F483616A049C27BD1B3870EA9E9BD0D89506ADA90C9327812AA6AA1AA89BCB84D2FD7A528FF865E57F372B4