RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/11733001http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11733001http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11733001http://www.w3.org/2000/01/rdf-schema#comment"p70ik3-1 (a 70-kDa protein) contains a cyclin box, and binds to p35cdk3 in vivo and in vitro [Matsuoka, M., Matsuura, Y., Semba, K. & Nishimoto, I. (2000) Biochem. Biophys. Res. Commun. 273, 442-447]. In spite of its structural similarity to cyclins, p70ik3-1 does not activate cyclin-dependent kinase 3 (cdk3)-mediated phosphorylation of pRb, histone H1, or the C-terminal domain of RNA polymerase II. Here, we report that Ser274 of p70ik3-1 is phosphorylated by cdk2 or cdk3 bound to cyclin A and to cyclin E in vitro. We also found that in COS7 cells in which cyclin E and cdk3 were ectopically overexpressed, the phosphorylation level of Ser274 in coexpressed p70ik3-1 is upregulated. We therefore conclude that p70ik3-1 is a substrate for cdk3-mediated phosphorylation."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.org/dc/terms/identifier"doi:10.1046/j.0014-2956.2001.02555.x"xsd:string
http://purl.uniprot.org/citations/11733001http://purl.org/dc/terms/identifier"doi:10.1046/j.0014-2956.2001.02555.x"xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/author"Matsuura Y."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/author"Matsuura Y."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/author"Tsuji K."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/author"Tsuji K."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/author"Sato H."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/author"Sato H."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/author"Matsuoka M."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/author"Matsuoka M."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/author"Mizumoto K."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/author"Mizumoto K."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/author"Nishimoto I."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/author"Nishimoto I."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/author"Semba K."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/author"Semba K."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/author"Yamochi T."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/author"Yamochi T."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/11733001http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string