| http://purl.uniprot.org/citations/19716809 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19716809 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19716809 | http://www.w3.org/2000/01/rdf-schema#comment | "IkappaB kinase beta (IKKbeta), a major kinase downstream of various proinflammatory signals, mediates multiple cellular functions through phosphorylation and regulation of its substrates. On the basis of protein sequence analysis, we identified arrest-defective protein 1 (ARD1), a protein involved in apoptosis and cell proliferation processes in many human cancer cells, as a new IKKbeta substrate. We provided evidence showing that ARD1 is indeed a bona fide substrate of IKKbeta. IKKbeta physically associated with ARD1 and phosphorylated it at Ser209. Phosphorylation by IKKbeta destabilized ARD1 and induced its proteasome-mediated degradation. Impaired growth suppression was observed in ARD1 phosphorylation-mimic mutant (S209E)-transfected cells as compared with ARD1 non-phosphorylatable mutant (S209A)-transfected cells. Our findings of molecular interactions between ARD1 and IKKbeta may enable further understanding of the upstream regulation mechanisms of ARD1 and of the diverse functions of IKKbeta."xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2009.08.127"xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2009.08.127"xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/author | "Xia W."xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/author | "Xia W."xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/author | "Lai C.C."xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/author | "Lai C.C."xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/author | "Li L.Y."xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/author | "Li L.Y."xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/author | "Hung M.C."xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/author | "Hung M.C."xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/author | "Kuo H.P."xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/author | "Kuo H.P."xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/author | "Lee D.F."xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/author | "Lee D.F."xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/pages | "156-161"xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/pages | "156-161"xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/title | "Phosphorylation of ARD1 by IKKbeta contributes to its destabilization and degradation."xsd:string |
| http://purl.uniprot.org/citations/19716809 | http://purl.uniprot.org/core/title | "Phosphorylation of ARD1 by IKKbeta contributes to its destabilization and degradation."xsd:string |