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http://purl.uniprot.org/citations/10779557http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10779557http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10779557http://www.w3.org/2000/01/rdf-schema#comment"hDlg, the human homologue of the Drosophila Discs-large (Dlg) tumor suppressor protein, is known to interact with the tumor suppressor protein APC and the human papillomavirus E6 transforming protein. In a two-hybrid screen, we identified a 322-aa serine/threonine kinase that binds to the PDZ2 domain of hDlg. The mRNA for this PDZ-binding kinase, or PBK, is most abundant in placenta and absent from adult brain tissue. The protein sequence of PBK has all the characteristic protein kinase subdomains and a C-terminal PDZ-binding T/SXV motif. In vitro, PBK binds specifically to PDZ2 of hDlg through its C-terminal T/SXV motif. PBK and hDlg are phosphorylated at mitosis in HeLa cells, and the mitotic phosphorylation of PBK is required for its kinase activity. In vitro, cdc2/cyclin B phosphorylates PBK. This evidence shows how PBK could link hDlg or other PDZ-containing proteins to signal transduction pathways regulating the cell cycle or cellular proliferation."xsd:string
http://purl.uniprot.org/citations/10779557http://purl.org/dc/terms/identifier"doi:10.1073/pnas.090102397"xsd:string
http://purl.uniprot.org/citations/10779557http://purl.org/dc/terms/identifier"doi:10.1073/pnas.090102397"xsd:string
http://purl.uniprot.org/citations/10779557http://purl.uniprot.org/core/author"Branton D."xsd:string
http://purl.uniprot.org/citations/10779557http://purl.uniprot.org/core/author"Branton D."xsd:string
http://purl.uniprot.org/citations/10779557http://purl.uniprot.org/core/author"Gaudet S."xsd:string
http://purl.uniprot.org/citations/10779557http://purl.uniprot.org/core/author"Gaudet S."xsd:string
http://purl.uniprot.org/citations/10779557http://purl.uniprot.org/core/author"Lue R.A."xsd:string
http://purl.uniprot.org/citations/10779557http://purl.uniprot.org/core/author"Lue R.A."xsd:string
http://purl.uniprot.org/citations/10779557http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10779557http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10779557http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/10779557http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/10779557http://purl.uniprot.org/core/pages"5167-5172"xsd:string
http://purl.uniprot.org/citations/10779557http://purl.uniprot.org/core/pages"5167-5172"xsd:string
http://purl.uniprot.org/citations/10779557http://purl.uniprot.org/core/title"Characterization of PDZ-binding kinase, a mitotic kinase."xsd:string
http://purl.uniprot.org/citations/10779557http://purl.uniprot.org/core/title"Characterization of PDZ-binding kinase, a mitotic kinase."xsd:string
http://purl.uniprot.org/citations/10779557http://purl.uniprot.org/core/volume"97"xsd:string
http://purl.uniprot.org/citations/10779557http://purl.uniprot.org/core/volume"97"xsd:string
http://purl.uniprot.org/citations/10779557http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10779557
http://purl.uniprot.org/citations/10779557http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10779557
http://purl.uniprot.org/citations/10779557http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10779557
http://purl.uniprot.org/citations/10779557http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10779557