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DESCRIBE <http://purl.uniprot.org/SHA-384/5B5D42D73709261004F67B4CEC8D158AA404D1E69106DA092686C067B344534556E54CFD26DDF6646C860B7A585FAC95>
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http://purl.uniprot.org/SHA-384/5B5D42D73709261004F67B4CEC8D158AA404D1E69106DA092686C067B344534556E54CFD26DDF6646C860B7A585FAC95
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/5B5D42D73709261004F67B4CEC8D158AA404D1E69106DA092686C067B344534556E54CFD26DDF6646C860B7A585FAC95
http://www.w3.org/2000/01/rdf-schema#comment
"nonmyristoylated CaBP1 and VILIP-2 bind to CaV2.1 channels and regulate them like CaM whereas myristoylation allows differential Ca2+-independent regulation by the inactive EF-hands of CaBP1 and VILIP-2"
xsd:string
http://purl.uniprot.org/uniprot/#_E9B438459B1A779CCC0F2479536C76E0DE0EFBEBC78AB29473870E310BBD9B14C6F9A592B13C2B21D12ECE880A12CDFC
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/5B5D42D73709261004F67B4CEC8D158AA404D1E69106DA092686C067B344534556E54CFD26DDF6646C860B7A585FAC95
http://purl.uniprot.org/uniprot/P54282
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/5B5D42D73709261004F67B4CEC8D158AA404D1E69106DA092686C067B344534556E54CFD26DDF6646C860B7A585FAC95
http://purl.uniprot.org/uniprot/#_P54282-mappedCitation-16049184
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/5B5D42D73709261004F67B4CEC8D158AA404D1E69106DA092686C067B344534556E54CFD26DDF6646C860B7A585FAC95