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DESCRIBE <http://purl.uniprot.org/SHA-384/D19019A09C77E80CEB7E2012981089EDFA4400FD6762D91D6B83E3D05EA9F654A2312DBEC1D252DDC67C485D526FD1F9>
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http://purl.uniprot.org/SHA-384/D19019A09C77E80CEB7E2012981089EDFA4400FD6762D91D6B83E3D05EA9F654A2312DBEC1D252DDC67C485D526FD1F9
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/D19019A09C77E80CEB7E2012981089EDFA4400FD6762D91D6B83E3D05EA9F654A2312DBEC1D252DDC67C485D526FD1F9
http://www.w3.org/2000/01/rdf-schema#comment
"These findings indicate that most if not all human adenovirus E4-ORF1 proteins share a conserved molecular mechanism of PI3K activation via Dlg1 binding and confer a common capacity to promote oncogenic transformation."
xsd:string
http://purl.uniprot.org/uniprot/#_2755D09D071A860170353B71BDE821F51A8DA4D30C0E28FBE974CAE33A9E925F0FE171B3A693B215A0D5F03E4792E77E
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/D19019A09C77E80CEB7E2012981089EDFA4400FD6762D91D6B83E3D05EA9F654A2312DBEC1D252DDC67C485D526FD1F9
http://purl.uniprot.org/uniprot/B4E2H8
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/D19019A09C77E80CEB7E2012981089EDFA4400FD6762D91D6B83E3D05EA9F654A2312DBEC1D252DDC67C485D526FD1F9
http://purl.uniprot.org/uniprot/#_B4E2H8-mappedCitation-25253337
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/D19019A09C77E80CEB7E2012981089EDFA4400FD6762D91D6B83E3D05EA9F654A2312DBEC1D252DDC67C485D526FD1F9