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http://purl.uniprot.org/citations/12383260http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12383260http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12383260http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/12383260http://www.w3.org/2000/01/rdf-schema#comment"Protein histidine phosphorylation in eukaryotes has been sparsely studied compared to protein serine/threonine and tyrosine phosphorylation. In an attempt to rectify this by probing porcine liver cytosol with the phosphohistidine-containing peptide succinyl-Ala-His(P)-Pro-Phe-p-nitroanilide (phosphopeptide I), we observed a phosphatase activity that was insensitive towards okadaic acid and EDTA. This suggested the existence of a phosphohistidine phosphatase different from protein phosphatase 1, 2A and 2C. A 1000-fold purification to apparent homogeneity gave a 14-kDa phosphatase with a specific activity of 3 micro mol.min-1.mg-1 at pH 7.5 with 7 micro m phosphopeptide I as substrate. Partial amino-acid sequence determination of the purified porcine enzyme by MS revealed similarity with a human sequence representing a human chromosome 9 gene of hitherto unknown function. Molecular cloning from a human embryonic kidney cell cDNA-library followed by expression and purification, yielded a protein with a molecular mass of 13 700 Da, and an EDTA-insensitive phosphohistidine phosphatase activity of 9 micro mol.min-1.mg-1 towards phosphopeptide I. No detectable activity was obtained towards a set of phosphoserine-, phosphothreonine-, and phosphotyrosine peptides. Northern blot analysis indicated that the human phosphohistidine phosphatase mRNA was present preferentially in heart and skeletal muscle. These results provide a new tool for studying eukaryotic histidine phosphorylation/dephosphorylation."xsd:string
http://purl.uniprot.org/citations/12383260http://purl.org/dc/terms/identifier"doi:10.1046/j.1432-1033.2002.03206.x"xsd:string
http://purl.uniprot.org/citations/12383260http://purl.org/dc/terms/identifier"doi:10.1046/j.1432-1033.2002.03206.x"xsd:string
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/author"Gong F."xsd:string
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/author"Gong F."xsd:string
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/author"Pettersson G."xsd:string
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/author"Pettersson G."xsd:string
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/author"Li J.-P."xsd:string
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/author"Li J.-P."xsd:string
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/author"Ek B."xsd:string
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/author"Ek B."xsd:string
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/author"Ek P."xsd:string
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/author"Ek P."xsd:string
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/author"Zetterqvist O."xsd:string
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/author"Zetterqvist O."xsd:string
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/pages"5016-5023"xsd:string
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/pages"5016-5023"xsd:string
http://purl.uniprot.org/citations/12383260http://purl.uniprot.org/core/title"Identification and characterization of a mammalian 14-kDa phosphohistidine phosphatase."xsd:string