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http://purl.uniprot.org/citations/15796912http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15796912http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15796912http://www.w3.org/2000/01/rdf-schema#comment"Intracellular signaling pathways and their relationship to malignant progression have become a major focus of cancer biology. The dual-specificity phosphatase (DSP) family is a more recently identified family of intracellular signaling modulators. We have identified a novel protein phosphatase with a well-conserved DSP catalytic domain containing the DSP catalytic motif, xHCxxGxSRS, and mitogen-activated protein kinase phosphatase (MKP) motif, AYLM. Because of these unique characteristics, the protein was named mitogen-activated protein kinase phosphatase-8 (MKP-8). This protein is approximately 20kDa in size and mainly localizes to the nuclear compartment of the cell. MKP-8 is expressed in embryonal cancers (retinoblastoma, neuroepithelioma, and neuroblastoma) and has limited expression in normal tissues. MKP-8 displays significant phosphatase activity that is inhibited by a cysteine to serine substitution in the catalytic domain. When co-expressed with activated MAPKs, MKP-8 is able to inhibit p38 kinase phosphorylation and downstream activity."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2005.03.028"xsd:string
http://purl.uniprot.org/citations/15796912http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2005.03.028"xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/author"Yang J."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/author"Yang J."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/author"Wang K."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/author"Wang K."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/author"Patel P.N."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/author"Patel P.N."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/author"Lazo J.S."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/author"Lazo J.S."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/author"Burlingame S.M."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/author"Burlingame S.M."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/author"Nuchtern J.G."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/author"Nuchtern J.G."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/author"Skoko J."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/author"Skoko J."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/author"Vasudevan S.A."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/author"Vasudevan S.A."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/15796912http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string