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http://purl.uniprot.org/citations/9480836http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9480836http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9480836http://www.w3.org/2000/01/rdf-schema#comment"A novel protein kinase that has significant sequence homology to mitogen-activated protein kinase (MAPK)-activated protein kinase (MAPKAPK) was identified. This novel protein kinase has a nucleotide sequence that encodes a protein of 473 amino acids and shares 45%, 46%, and 44% amino acid sequence identities to MAPKAPK2, 3 and 4 respectively. Northern blot analysis revealed that it has a wide tissue distribution. This novel protein kinase designated MAPKAPK5 can be phosphorylated by extracellular-regulated kinase (ERK), and p38 kinase but not by c-jun N-terminal kinase (JNK) in vitro. Recombinant GST-MAPKAPK5 protein can phosphorylate a peptide derived from the regulatory light chain of myosin II. Phosphorylation of MAPKAPK5 by ERK and p38 kinase increased its activity by 9 and 15 fold respectively. Taken together, these data suggest that MAPKAPK5 is a novel in vitro substrate for ERK and p38 kinase."xsd:string
http://purl.uniprot.org/citations/9480836http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.1998.8135"xsd:string
http://purl.uniprot.org/citations/9480836http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.1998.8135"xsd:string
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/author"Yao Z."xsd:string
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/author"Yao Z."xsd:string
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/author"Ni H."xsd:string
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/author"Ni H."xsd:string
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/author"Wang X.S."xsd:string
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/author"Wang X.S."xsd:string
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/author"Diener K."xsd:string
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/author"Diener K."xsd:string
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/pages"492-496"xsd:string
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/pages"492-496"xsd:string
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/title"MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase."xsd:string
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/title"MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase."xsd:string
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/volume"243"xsd:string
http://purl.uniprot.org/citations/9480836http://purl.uniprot.org/core/volume"243"xsd:string
http://purl.uniprot.org/citations/9480836http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9480836
http://purl.uniprot.org/citations/9480836http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9480836