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DESCRIBE <http://purl.uniprot.org/SHA-384/A153A08F5D34F2F49524CDE273C7042710145A1F20DF6FB77F134752E4041A7B2CA41D5B1B8BF3CFC1CC00E793F19A1C>
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http://purl.uniprot.org/SHA-384/A153A08F5D34F2F49524CDE273C7042710145A1F20DF6FB77F134752E4041A7B2CA41D5B1B8BF3CFC1CC00E793F19A1C
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/A153A08F5D34F2F49524CDE273C7042710145A1F20DF6FB77F134752E4041A7B2CA41D5B1B8BF3CFC1CC00E793F19A1C
http://www.w3.org/2000/01/rdf-schema#comment
"This study reports how phosphorylation of a regulatory site (Ser-500) integrates with Ca(2+) and CaM to influence eEF-2K activity."
xsd:string
http://purl.uniprot.org/uniprot/#_A1257446391262EC408F4C86D3BE6366BFFEC40AF22E55ABD1AD82D898075E8A27304B759EBB38DB77D2F0D6276DEE0E
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/A153A08F5D34F2F49524CDE273C7042710145A1F20DF6FB77F134752E4041A7B2CA41D5B1B8BF3CFC1CC00E793F19A1C
http://purl.uniprot.org/uniprot/B4DJ51
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/A153A08F5D34F2F49524CDE273C7042710145A1F20DF6FB77F134752E4041A7B2CA41D5B1B8BF3CFC1CC00E793F19A1C
http://purl.uniprot.org/uniprot/#_B4DJ51-mappedCitation-27956550
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/A153A08F5D34F2F49524CDE273C7042710145A1F20DF6FB77F134752E4041A7B2CA41D5B1B8BF3CFC1CC00E793F19A1C