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http://purl.uniprot.org/citations/9647734http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9647734http://www.w3.org/2000/01/rdf-schema#comment"Kell and Kx are two quantitatively minor proteins from the human erythrocyte membrane which carry blood groups antigens and are thought to be a metalloprotease and a membrane transporter, respectively. In the red cell membrane, these proteins form a complex stabilized by disulfide bond(s). Phosphorylation status of these proteins was studied, in the presence or absence of effectors of several kinases, either on intact cells incubated with [32P]-orthophosphate or on ghosts incubated with [gamma-32P]ATP. Purification of Kell-Kx complex, by immunochromatography on an immobilized human monoclonal antibody of Kell blood group specificity allowed to establish that (i) neither protein is phosphorylated on tyrosine; (ii) the Kell protein is a putative substrate for Casein Kinase II (CKII) and Casein Kinase I (CKI) but not for protein kinase C (PKC), whereas Kx protein is phosphorylated by CKII and PKC but not by CKI; (iii) Protein Kinase A neither phosphorylates the Kell nor the Kx proteins."xsd:string
http://purl.uniprot.org/citations/9647734http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.1998.8743"xsd:string
http://purl.uniprot.org/citations/9647734http://purl.uniprot.org/core/author"Cartron J.P."xsd:string
http://purl.uniprot.org/citations/9647734http://purl.uniprot.org/core/author"Hattab C."xsd:string
http://purl.uniprot.org/citations/9647734http://purl.uniprot.org/core/author"Bertrand O."xsd:string
http://purl.uniprot.org/citations/9647734http://purl.uniprot.org/core/author"Carbonnet F."xsd:string
http://purl.uniprot.org/citations/9647734http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9647734http://purl.uniprot.org/core/name"Biochem Biophys Res Commun"xsd:string
http://purl.uniprot.org/citations/9647734http://purl.uniprot.org/core/pages"569-575"xsd:string
http://purl.uniprot.org/citations/9647734http://purl.uniprot.org/core/title"Kell and Kx, two disulfide-linked proteins of the human erythrocyte membrane are phosphorylated in vivo."xsd:string
http://purl.uniprot.org/citations/9647734http://purl.uniprot.org/core/volume"247"xsd:string
http://purl.uniprot.org/citations/9647734http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9647734
http://purl.uniprot.org/citations/9647734http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9647734
http://purl.uniprot.org/uniprot/P23276#attribution-8F3C0FEE09360BF3C73EACABBD97B592http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9647734
http://purl.uniprot.org/uniprot/P51811#attribution-8F3C0FEE09360BF3C73EACABBD97B592http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9647734