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http://purl.uniprot.org/citations/10644717http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10644717http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10644717http://www.w3.org/2000/01/rdf-schema#comment"We report the isolation and characterization of a cDNA encoding the novel mammalian serine protease Omi. Omi protein consists of 458 amino acids and has homology to bacterial HtrA endoprotease, which acts as a chaperone at low temperatures and as a proteolytic enzyme that removes denatured or damaged substrates at elevated temperatures. The carboxyl terminus of Omi has extensive homology to a mammalian protein called L56 (human HtrA), but unlike L56, which is secreted, Omi is localized in the endoplasmic reticulum. Omi has several novel putative protein-protein interaction motifs, as well as a PDZ domain and a Src homology 3-binding domain. Omi mRNA is expressed ubiquitously, and the gene is localized on human chromosome 2p12. Omi interacts with Mxi2, an alternatively spliced form of the p38 stress-activated kinase. Omi protein, when made in a heterologous system, shows proteolytic activity against a nonspecific substrate beta-casein. The proteolytic activity of Omi is markedly up-regulated in the mouse kidney following ischemia/reperfusion."xsd:string
http://purl.uniprot.org/citations/10644717http://purl.org/dc/terms/identifier"doi:10.1074/jbc.275.4.2581"xsd:string
http://purl.uniprot.org/citations/10644717http://purl.org/dc/terms/identifier"doi:10.1074/jbc.275.4.2581"xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/author"Chen A."xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/author"Chen A."xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/author"Zervos A.S."xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/author"Zervos A.S."xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/author"Fusco C."xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/author"Fusco C."xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/author"Bonventre J.V."xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/author"Bonventre J.V."xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/author"Faccio L."xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/author"Faccio L."xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/author"Martinotti S."xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/author"Martinotti S."xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/pages"2581-2588"xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/pages"2581-2588"xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/title"Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia."xsd:string
http://purl.uniprot.org/citations/10644717http://purl.uniprot.org/core/title"Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia."xsd:string