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DESCRIBE <http://purl.uniprot.org/SHA-384/3BD75A5DFEBBFE8704295932037AD4952E9EF3C862F3AAA71BE9FB32D75B42C987DC432F49B37837889D7BEEBCD7F15F>
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http://purl.uniprot.org/SHA-384/3BD75A5DFEBBFE8704295932037AD4952E9EF3C862F3AAA71BE9FB32D75B42C987DC432F49B37837889D7BEEBCD7F15F
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/3BD75A5DFEBBFE8704295932037AD4952E9EF3C862F3AAA71BE9FB32D75B42C987DC432F49B37837889D7BEEBCD7F15F
http://www.w3.org/2000/01/rdf-schema#comment
"Glutamic acid-153 substitution inhibits multisite tyrosine hydroxylase dephosphorylation without compromising PP2A/B'beta holoenzyme assembly or in vitro dephosphorylation of model substrates."
xsd:string
http://purl.uniprot.org/uniprot/#_8857088C61500D7122083D3B2E40D23C711A4E790E40DDE8A3531CC5448EC3D615D4B8331894BC6BB470DC03D4ED6CE4
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/3BD75A5DFEBBFE8704295932037AD4952E9EF3C862F3AAA71BE9FB32D75B42C987DC432F49B37837889D7BEEBCD7F15F
http://purl.uniprot.org/uniprot/P62716
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/3BD75A5DFEBBFE8704295932037AD4952E9EF3C862F3AAA71BE9FB32D75B42C987DC432F49B37837889D7BEEBCD7F15F
http://purl.uniprot.org/uniprot/#_P62716-mappedCitation-20017541
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/3BD75A5DFEBBFE8704295932037AD4952E9EF3C862F3AAA71BE9FB32D75B42C987DC432F49B37837889D7BEEBCD7F15F