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DESCRIBE <http://purl.uniprot.org/SHA-384/A1E9976D5CCE472FC9D34924E96547C9447D0C104C97CD6C7EEC48352DD0FBA6F7AD95775E6F418A423AC8772872E5FC>
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http://purl.uniprot.org/SHA-384/A1E9976D5CCE472FC9D34924E96547C9447D0C104C97CD6C7EEC48352DD0FBA6F7AD95775E6F418A423AC8772872E5FC
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/A1E9976D5CCE472FC9D34924E96547C9447D0C104C97CD6C7EEC48352DD0FBA6F7AD95775E6F418A423AC8772872E5FC
http://www.w3.org/2000/01/rdf-schema#comment
"A yeast mutagenesis system successfully identified three completely different amino acid substitutions that are each able to suppress the constitutive activity of the disease-associated R201H mutation in Gs."
xsd:string
http://purl.uniprot.org/uniprot/#_9E1B0A8F5012EC7A668482C65235C9A4C397B451CCFFEFD5DE314A3D386606780A40AAA9082D9E2B0873C9D0F7328BAC
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/A1E9976D5CCE472FC9D34924E96547C9447D0C104C97CD6C7EEC48352DD0FBA6F7AD95775E6F418A423AC8772872E5FC
http://purl.uniprot.org/uniprot/P63092
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/A1E9976D5CCE472FC9D34924E96547C9447D0C104C97CD6C7EEC48352DD0FBA6F7AD95775E6F418A423AC8772872E5FC
http://purl.uniprot.org/uniprot/#_P63092-mappedCitation-24850831
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/A1E9976D5CCE472FC9D34924E96547C9447D0C104C97CD6C7EEC48352DD0FBA6F7AD95775E6F418A423AC8772872E5FC