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http://purl.uniprot.org/citations/15671017http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15671017http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15671017http://www.w3.org/2000/01/rdf-schema#comment"Cyclin-dependent kinase 2 (cdk2) activation requires phosphorylation of Thr160 and dissociation from cyclin A. The T-loop of cdk2 contains a regulatory phosphorylation site at Thr160. An interaction between cdc-associated phosphatase (KAP) and cdk2 compromises the interaction between cdk2 and cyclin A, which permits access of KAP, a Thr160-directed phosphatase, to its substrate, cdk2. We have reported that KAP is bound and activated by a nuclear membrane protein, HTm4. Here, we present in vitro data showing the direct interaction between the HTm4 C terminus and KAP Tyr141. We show that this interaction not only facilitates access of KAP to Thr160 and accelerates KAP kinetics, but also forces exclusion of cyclin A from the KAP.cdk2 complex."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m413437200"xsd:string
http://purl.uniprot.org/citations/15671017http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m413437200"xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Yang X."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Yang X."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Shirakawa T."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Shirakawa T."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Yano Y."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Yano Y."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Moriyama K."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Moriyama K."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Shiroishi M."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Shiroishi M."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Chinami M."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Chinami M."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Salahuddin S."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Salahuddin S."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Adra C.N."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Adra C.N."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Turner H."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/author"Turner H."xsd:string
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15671017http://purl.uniprot.org/core/date"2005"xsd:gYear