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http://purl.uniprot.org/citations/11331269http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11331269http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11331269http://www.w3.org/2000/01/rdf-schema#comment"We have cloned and characterized a new member of the phosphatidylinositol kinase (PIK)-related kinase family. This gene, which we term human SMG-1 (hSMG-1), is orthologous to Caenorhabditis elegans SMG-1, a protein that functions in nonsense-mediated mRNA decay (NMD). cDNA sequencing revealed that hSMG-1 encodes a protein of 3031 amino acids containing a conserved kinase domain, a C-terminal domain unique to the PIK-related kinases and an FKBP12-rapamycin binding-like domain similar to that found in the PIK-related kinase mTOR. Immunopurified FLAG-tagged hSMG-1 exhibits protein kinase activity as measured by autophosphorylation and phosphorylation of the generic PIK-related kinase substrate PHAS-1. hSMG-1 kinase activity is inhibited by high nanomolar concentrations of wortmannin (IC(50) = 105 nm) but is not inhibited by a FKBP12-rapamycin complex. Mutation of conserved residues within the kinase domain of hSMG-1 abolishes both autophosphorylation and substrate phosphorylation, demonstrating that hSMG-1 exhibits intrinsic protein kinase activity. hSMG-1 phosphorylates purified hUpf1 protein, a phosphoprotein that plays a critical role in NMD, at sites that are also phosphorylated in whole cells. Based on these data, we conclude that hSMG-1 is the human orthologue to C. elegans SMG-1. Our data indicate that hSMG-1 may function in NMD by directly phosphorylating hUpf1 protein at physiologically relevant sites."xsd:string
http://purl.uniprot.org/citations/11331269http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c100144200"xsd:string
http://purl.uniprot.org/citations/11331269http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c100144200"xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/author"Maquat L.E."xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/author"Maquat L.E."xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/author"Jamieson L."xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/author"Jamieson L."xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/author"Thompson E.A."xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/author"Thompson E.A."xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/author"Fields A.P."xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/author"Fields A.P."xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/author"Denning G."xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/author"Denning G."xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/pages"22709-22714"xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/pages"22709-22714"xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/title"Cloning of a novel phosphatidylinositol kinase-related kinase: characterization of the human SMG-1 RNA surveillance protein."xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/title"Cloning of a novel phosphatidylinositol kinase-related kinase: characterization of the human SMG-1 RNA surveillance protein."xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/volume"276"xsd:string
http://purl.uniprot.org/citations/11331269http://purl.uniprot.org/core/volume"276"xsd:string