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DESCRIBE <http://purl.uniprot.org/SHA-384/0CC037FB4A77F9FAFE01D9BFC6FEE9820A797B2CE5DBAD0FABA99BA447DABF8B5ADD335F8C4F75C4846830746CCF36CC>
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http://purl.uniprot.org/SHA-384/0CC037FB4A77F9FAFE01D9BFC6FEE9820A797B2CE5DBAD0FABA99BA447DABF8B5ADD335F8C4F75C4846830746CCF36CC
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/0CC037FB4A77F9FAFE01D9BFC6FEE9820A797B2CE5DBAD0FABA99BA447DABF8B5ADD335F8C4F75C4846830746CCF36CC
http://www.w3.org/2000/01/rdf-schema#comment
"IP7 formed by IP6K2 binds CK2 to enhance its phosphorylation of the Tti1/Tel2 complex thereby stabilizing DNA-PKcs and ATM. This process stimulates p53 phosphorylation at serine 15 to activate the cell death program."
xsd:string
http://purl.uniprot.org/uniprot/#_F8E5D2B92C95344F60D186BC605CFE32DE6A193348811C8253257866E20493EC5CEA1AC6B3B91DA76D52B4B6F929D20A
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/0CC037FB4A77F9FAFE01D9BFC6FEE9820A797B2CE5DBAD0FABA99BA447DABF8B5ADD335F8C4F75C4846830746CCF36CC
http://purl.uniprot.org/uniprot/Q91V83
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/0CC037FB4A77F9FAFE01D9BFC6FEE9820A797B2CE5DBAD0FABA99BA447DABF8B5ADD335F8C4F75C4846830746CCF36CC
http://purl.uniprot.org/uniprot/#_Q91V83-mappedCitation-24657168
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/0CC037FB4A77F9FAFE01D9BFC6FEE9820A797B2CE5DBAD0FABA99BA447DABF8B5ADD335F8C4F75C4846830746CCF36CC