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http://purl.uniprot.org/citations/1647215http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1647215http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1647215http://www.w3.org/2000/01/rdf-schema#comment"cDNAs encoding three protein phosphatases, termed PP2Bw (Da Cruz e Silva, E.F. and Cohen, P.T.W. (1989) Biochim. Biophys. Acta 1009, 293-296), PPZ1 and PPZ2 that have been isolated from a Clontech 'rabbit brain' library are shown to be Saccharomyces cerevisiae clones. PPZ1 and PPZ2 are two novel yeast phosphatases showing 93% amino acid sequence identity to one another. PPZ1 shows approx. 60% sequence identity to S. cerevisiae or mammalian PP1 and approx. 40% identity to S. cerevisiae or mammalian PP2A. These and other observations suggest that the two isoforms of PPZ have functions distinct from those of PP1."xsd:string
http://purl.uniprot.org/citations/1647215http://purl.org/dc/terms/identifier"doi:10.1016/0167-4781(91)90023-f"xsd:string
http://purl.uniprot.org/citations/1647215http://purl.org/dc/terms/identifier"doi:10.1016/0167-4781(91)90023-f"xsd:string
http://purl.uniprot.org/citations/1647215http://purl.org/dc/terms/identifier"doi:10.1016/0167-4781(91)90023-F"xsd:string
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/author"Stark M.J.R."xsd:string
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/author"Stark M.J.R."xsd:string
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/author"Cohen P.T.W."xsd:string
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/author"Cohen P.T.W."xsd:string
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/author"Hughes V."xsd:string
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/author"Hughes V."xsd:string
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/author"McDonald P."xsd:string
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/author"McDonald P."xsd:string
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/author"Da Cruz e Silva E.F."xsd:string
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/author"Da Cruz e Silva E.F."xsd:string
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/pages"269-272"xsd:string
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/pages"269-272"xsd:string
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/title"Protein phosphatase 2Bw and protein phosphatase Z are Saccharomyces cerevisiae enzymes."xsd:string
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/title"Protein phosphatase 2Bw and protein phosphatase Z are Saccharomyces cerevisiae enzymes."xsd:string
http://purl.uniprot.org/citations/1647215http://purl.uniprot.org/core/volume"1089"xsd:string