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DESCRIBE <http://purl.uniprot.org/SHA-384/63E049C333172C04D71A0E8A9218E339331C3EB473430A79955C96B7E60BA673C668C1E6F034F20026D649B7014930E3>
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http://purl.uniprot.org/SHA-384/63E049C333172C04D71A0E8A9218E339331C3EB473430A79955C96B7E60BA673C668C1E6F034F20026D649B7014930E3
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/63E049C333172C04D71A0E8A9218E339331C3EB473430A79955C96B7E60BA673C668C1E6F034F20026D649B7014930E3
http://www.w3.org/2000/01/rdf-schema#comment
"Substitution of the autophosphorylation site Thr516 with a negatively charged residue confers constitutive activity to mouse 3-phosphoinositide-dependent protein kinase-1 in cells"
xsd:string
http://purl.uniprot.org/uniprot/#_4657A0EE3E9C99319275AA855F8F8008284249A72D2A746A7E11DD942B133809E01C25B1FE2E63EBECF0CD7C52E83037
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/63E049C333172C04D71A0E8A9218E339331C3EB473430A79955C96B7E60BA673C668C1E6F034F20026D649B7014930E3
http://purl.uniprot.org/uniprot/F2Z3X6
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/63E049C333172C04D71A0E8A9218E339331C3EB473430A79955C96B7E60BA673C668C1E6F034F20026D649B7014930E3
http://purl.uniprot.org/uniprot/#_F2Z3X6-mappedCitation-11877406
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/63E049C333172C04D71A0E8A9218E339331C3EB473430A79955C96B7E60BA673C668C1E6F034F20026D649B7014930E3