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DESCRIBE <http://purl.uniprot.org/SHA-384/DDB1F3A80B521A358F569B89D20F3DCF2B6772D864E71E9DB1D3503E3F30EDCFF72FA3371FB75EAE77B50D8468849EAF>
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http://purl.uniprot.org/SHA-384/DDB1F3A80B521A358F569B89D20F3DCF2B6772D864E71E9DB1D3503E3F30EDCFF72FA3371FB75EAE77B50D8468849EAF
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/DDB1F3A80B521A358F569B89D20F3DCF2B6772D864E71E9DB1D3503E3F30EDCFF72FA3371FB75EAE77B50D8468849EAF
http://www.w3.org/2000/01/rdf-schema#comment
"results provide evidence that PDK1 and ASK1 directly interact and phosphorylate each other and act as negative regulators of their respective kinases in resting cells"
xsd:string
http://purl.uniprot.org/uniprot/#_2F831D335A2A86E22C07EA2A321B5A4910882CE3D3E72481A206753533DD79D718DA6172DF4DFE6E7088282115D83E6A
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/DDB1F3A80B521A358F569B89D20F3DCF2B6772D864E71E9DB1D3503E3F30EDCFF72FA3371FB75EAE77B50D8468849EAF
http://purl.uniprot.org/uniprot/Q9UI25
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/DDB1F3A80B521A358F569B89D20F3DCF2B6772D864E71E9DB1D3503E3F30EDCFF72FA3371FB75EAE77B50D8468849EAF
http://purl.uniprot.org/uniprot/#_Q9UI25-mappedCitation-19920149
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/DDB1F3A80B521A358F569B89D20F3DCF2B6772D864E71E9DB1D3503E3F30EDCFF72FA3371FB75EAE77B50D8468849EAF