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http://purl.uniprot.org/citations/10036776http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10036776http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10036776http://www.w3.org/2000/01/rdf-schema#comment"Mitogen-activated protein kinases (MAPKs) play a key role in plant responses to stress and pathogens. Activation and inactivation of MAPKs involve phosphorylation and dephosphorylation on both threonine and tyrosine residues in the kinase domain. Here we report the identification of an Arabidopsis gene encoding a dual-specificity protein phosphatase capable of hydrolysing both phosphoserine/threonine and phosphotyrosine in protein substrates. This enzyme, designated AtDsPTP1 (Arabidopsis thaliana dual-specificity protein tyrosine phosphatase), dephosphorylated and inactivated AtMPK4, a MAPK member from the same plant. Replacement of a highly conserved cysteine by serine abolished phosphatase activity of AtDsPTP1, indicating a conserved catalytic mechanism of dual-specificity protein phosphatases from all eukaryotes."xsd:string
http://purl.uniprot.org/citations/10036776http://purl.org/dc/terms/identifier"doi:10.1046/j.1365-313x.1998.00327.x"xsd:string
http://purl.uniprot.org/citations/10036776http://purl.org/dc/terms/identifier"doi:10.1046/j.1365-313x.1998.00327.x"xsd:string
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/author"Gupta R."xsd:string
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/author"Gupta R."xsd:string
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/author"Huang Y."xsd:string
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/author"Huang Y."xsd:string
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/author"Luan S."xsd:string
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/author"Luan S."xsd:string
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/author"Kieber J."xsd:string
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/author"Kieber J."xsd:string
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/name"Plant J."xsd:string
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/name"Plant J."xsd:string
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/pages"581-589"xsd:string
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/pages"581-589"xsd:string
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/title"Identification of a dual-specificity protein phosphatase that inactivates a MAP kinase from Arabidopsis."xsd:string
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/title"Identification of a dual-specificity protein phosphatase that inactivates a MAP kinase from Arabidopsis."xsd:string
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/volume"16"xsd:string
http://purl.uniprot.org/citations/10036776http://purl.uniprot.org/core/volume"16"xsd:string
http://purl.uniprot.org/citations/10036776http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10036776
http://purl.uniprot.org/citations/10036776http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10036776