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http://purl.uniprot.org/citations/7958845http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7958845http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7958845http://www.w3.org/2000/01/rdf-schema#comment"The Saccharomyces cerevisiae protein kinase Dbf2 carries out an essential function in late mitosis, and its kinase activity is cell-cycle regulated around anaphase/telophase. We have isolated SDB25, a high copy suppressor of temperature-sensitive dbf2 mutants, and genetic analysis suggests that the two proteins may function in parallel pathways in late mitosis. SDB25 encodes p40, a previously characterized substrate and potent inhibitor of Cdc28 kinase activity. Sdb25 is a phosphoprotein, and Sdb25 immunoprecipitates have a histone H1 kinase activity that is CDC28-dependent. Remarkably, Sdb25 transcript levels, protein levels, and associated kinase activity are precisely cell-cycle regulated, sharing a common peak in late mitosis. Moreover, Sdb25 protein levels and associated kinase activity are sharply up-regulated at the peak of Dbf2 kinase activity in cells released from a dbf2 ts block. The Sdb25 protein then disappears around Start in the next cell cycle. This indicates that SDB25 function is confined to M/G1, and morphological analysis of sdb25 delta cells supports this conclusion. Our data suggest that Sdb25 functions in a pathway in late mitosis leading to the down-regulation of Cdc28 kinase activity as cells traverse the M/G1 boundary."xsd:string
http://purl.uniprot.org/citations/7958845http://purl.org/dc/terms/identifier"doi:10.1101/gad.8.14.1640"xsd:string
http://purl.uniprot.org/citations/7958845http://purl.org/dc/terms/identifier"doi:10.1101/gad.8.14.1640"xsd:string
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/author"Toyn J.H."xsd:string
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/author"Toyn J.H."xsd:string
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/author"Johnson A.L."xsd:string
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/author"Johnson A.L."xsd:string
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/author"Johnston L.H."xsd:string
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/author"Johnston L.H."xsd:string
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/author"Donovan J.D."xsd:string
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/author"Donovan J.D."xsd:string
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/pages"1640-1653"xsd:string
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/pages"1640-1653"xsd:string
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/title"P40SDB25, a putative CDK inhibitor, has a role in the M/G1 transition in Saccharomyces cerevisiae."xsd:string
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/title"P40SDB25, a putative CDK inhibitor, has a role in the M/G1 transition in Saccharomyces cerevisiae."xsd:string
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/7958845http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/7958845http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7958845
http://purl.uniprot.org/citations/7958845http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7958845