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http://purl.uniprot.org/citations/10557092http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10557092http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10557092http://www.w3.org/2000/01/rdf-schema#comment"prk encodes a protein serine/threonine kinase involved in regulating M phase functions during the cell cycle. We have expressed His6-Prk and His6-Cdc25C proteins using the baculoviral vector expression system. Purified recombinant His6-Prk, but not a kinase-defective mutant His6-PrkK52R, is capable of strongly phosphorylating His6-Cdc25C in vitro. Co-immunoprecipitation and affinity column chromatography experiments demonstrate that GST-Prk and native Cdc25C interact. When co-infected with His6-Prk and His6-Cdc25C recombinant baculoviruses, sf-9 cells produce His6-Cdc25C antigen with an additional slower mobility band on denaturing polyacrylamide gels compared with cells infected with His6-Cdc25C baculovirus alone. In addition, His6-Cdc25C immunoprecipitated from sf-9 cells co-infected with His6-Prk and His6-Cdc25C baculoviruses, but not with His6-PrkK52R and His6-Cdc25C baculoviruses, contains a greatly enhanced kinase activity that phosphorylates His6-Cdc25C in vitro. Moreover, phosphopeptide mapping shows that His6-Prk phosphorylates His6-Cdc25C at two sites in vitro and that the major phosphorylation site co-migrates with the one that is phosphorylated in vivo in asynchonized cells. Further studies reveal that His6-Prk phosphorylates Cdc25C on serine216, a residue also phosphorylated by Chk1 and Chk2. Together, these observations strongly suggest that Prk's role in mitosis is at least partly mediated through direct regulation of Cdc25C."xsd:string
http://purl.uniprot.org/citations/10557092http://purl.org/dc/terms/identifier"doi:10.1038/sj.onc.1202983"xsd:string
http://purl.uniprot.org/citations/10557092http://purl.org/dc/terms/identifier"doi:10.1038/sj.onc.1202983"xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/author"Li W."xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/author"Li W."xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/author"Pan H."xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/author"Pan H."xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/author"Dai W."xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/author"Dai W."xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/author"Hoffmann I."xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/author"Hoffmann I."xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/author"Ouyang B."xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/author"Ouyang B."xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/author"Meadows J."xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/author"Meadows J."xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/name"Oncogene"xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/name"Oncogene"xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/pages"6029-6036"xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/pages"6029-6036"xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/title"The physical association and phosphorylation of Cdc25C protein phosphatase by Prk."xsd:string
http://purl.uniprot.org/citations/10557092http://purl.uniprot.org/core/title"The physical association and phosphorylation of Cdc25C protein phosphatase by Prk."xsd:string