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http://purl.uniprot.org/citations/8810321http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8810321http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8810321http://www.w3.org/2000/01/rdf-schema#comment"We report here the characterization of the human tissue inhibitor of metalloproteinases-2 (TIMP-2) gene. The gene is 83 kilobase pairs (kb) long with exon-intron splicing sites located in preserved positions among the three members of the TIMP family. A 2.6-kb genomic DNA fragment flanking the 5'-end of the gene contains several regulatory elements including five Sp1, two AP-2, one AP-1, and three PEA-3 binding sites. Despite the presence of a complete AP-1 consensus at position -281, the promoter did not respond to 12-O-tetradecanoylphorbol-13-acetate treatment. However, 12-O-tetradecanoylphorbol-13-acetate response was generated by insertion of a similar AP-1 consensus at position -71, indicating the importance of the positioning of this motif. The promoter contains a typical CpG island; however, methylation of this island did not seem to influence gene expression. Analysis of the 3'-end of the gene revealed that the two mRNAs for TIMP-2 (1.2 and 3.8 kb) differ by the selection of their polyadenylation signal sites, but selection of these sites does not affect RNA stability. In summary, the TIMP-2 gene has several features observed in housekeeping genes, and differs significantly from TIMP-1 and TIMP-3 genes. These differences are likely to explain the specific roles that these inhibitors play in the regulation of matrix metalloproteinases."xsd:string
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8810321http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.41.25498"xsd:string
http://purl.uniprot.org/citations/8810321http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.41.25498"xsd:string
http://purl.uniprot.org/citations/8810321http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8810321
http://purl.uniprot.org/citations/8810321http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8810321
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/author"Schmutte C."xsd:string
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/author"Schmutte C."xsd:string
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/author"Hammani K."xsd:string
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/author"Hammani K."xsd:string
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/author"Bowcock A."xsd:string
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/author"Bowcock A."xsd:string
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/author"Henriet P."xsd:string
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/author"Henriet P."xsd:string
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/author"Blakis A."xsd:string
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/author"Blakis A."xsd:string
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/author"Declerck Y.A."xsd:string
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/author"Declerck Y.A."xsd:string
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/author"Morsette D."xsd:string
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/author"Morsette D."xsd:string
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8810321http://purl.uniprot.org/core/date"1996"xsd:gYear