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DESCRIBE <http://purl.uniprot.org/SHA-384/881A3FEBD0A89484E92A2CCE7FE371D2F5C389AE653B72D5296634C5E87D535819F2C5C66E5AAC22894ABDD948363C46>
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http://purl.uniprot.org/SHA-384/881A3FEBD0A89484E92A2CCE7FE371D2F5C389AE653B72D5296634C5E87D535819F2C5C66E5AAC22894ABDD948363C46
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/881A3FEBD0A89484E92A2CCE7FE371D2F5C389AE653B72D5296634C5E87D535819F2C5C66E5AAC22894ABDD948363C46
http://www.w3.org/2000/01/rdf-schema#comment
"Authors show that phosphorylation at Thr378 and Ser379 sites is dependent on the ataxia-telangiectasia mutated (ATM) and Rad3-related (ATR) a kinase activated during infectious bronchitis virus replication."
xsd:string
http://purl.uniprot.org/uniprot/#_036E7A488CD35FE385FA9B2B7CBC00C9F6B503D7543F8C2201F3883542D129ACB6DDED3E60536F2CFF3883EE1BDAF851
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/881A3FEBD0A89484E92A2CCE7FE371D2F5C389AE653B72D5296634C5E87D535819F2C5C66E5AAC22894ABDD948363C46
http://purl.uniprot.org/uniprot/P69596
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/881A3FEBD0A89484E92A2CCE7FE371D2F5C389AE653B72D5296634C5E87D535819F2C5C66E5AAC22894ABDD948363C46
http://purl.uniprot.org/uniprot/#_P69596-mappedCitation-23849791
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/881A3FEBD0A89484E92A2CCE7FE371D2F5C389AE653B72D5296634C5E87D535819F2C5C66E5AAC22894ABDD948363C46