RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/20041275http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20041275http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20041275http://www.w3.org/2000/01/rdf-schema#comment"The ability of three isoforms of protein kinase CK1 (alpha, gamma(1), and delta) to phosphorylate the N-terminal region of p53 has been assessed using either recombinant p53 or a synthetic peptide reproducing its 1-28 sequence. Both substrates are readily phosphoylated by CK1delta and CK1alpha, but not by the gamma isoform. Affinity of full size p53 for CK1 is 3 orders of magnitude higher than that of its N-terminal peptide (K (m) 0.82 muM vs 1.51 mM). The preferred target is S20, whose phosphorylation critically relies on E17, while S6 is unaffected despite displaying the same consensus (E-x-x-S). Our data support the concept that non-primed phosphorylation of p53 by CK1 is an isoform-specific reaction preferentially affecting S20 by a mechanism which is grounded both on a local consensus and on a remote docking site mapped to the K(221)RQK(224) loop according to modeling and mutational analysis."xsd:string
http://purl.uniprot.org/citations/20041275http://purl.org/dc/terms/identifier"doi:10.1007/s00018-009-0236-7"xsd:string
http://purl.uniprot.org/citations/20041275http://purl.org/dc/terms/identifier"doi:10.1007/s00018-009-0236-7"xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/author"Pinna L.A."xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/author"Pinna L.A."xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/author"Marin O."xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/author"Marin O."xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/author"Sarno S."xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/author"Sarno S."xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/author"Cozza G."xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/author"Cozza G."xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/author"Bustos V.H."xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/author"Bustos V.H."xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/author"Venerando A."xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/author"Venerando A."xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/name"Cell. Mol. Life Sci."xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/name"Cell. Mol. Life Sci."xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/pages"1105-1118"xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/pages"1105-1118"xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/title"Isoform specific phosphorylation of p53 by protein kinase CK1."xsd:string
http://purl.uniprot.org/citations/20041275http://purl.uniprot.org/core/title"Isoform specific phosphorylation of p53 by protein kinase CK1."xsd:string