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http://purl.uniprot.org/citations/15465032http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15465032http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15465032http://www.w3.org/2000/01/rdf-schema#comment"HIF-1 is closely involved in various biological processes, including angiogenesis, energy metabolism, and cell survival. HIF-1 consists of an oxygen-sensitive HIF-1alpha and oxygen-insensitive HIF-1beta. Oxygen-sensitive HIF-1alpha is subjected to post-translational modifications such as hydroxylation, ubiquitination, and acetylation, which are related to the regulation of its stability. In this present study, we found that the ectopic expression of SUMO-1 increased HIF-1alpha stability by the co-transfection study with HIF-1alpha and SUMO-1. Furthermore, the ectopic expression of SUMO-1 enhanced the transcriptional activity of HIF-1alpha. In the subsequent immunoprecipitation assay, SUMO-1 was co-immunoprecipitated with HIF-1alpha, implying that HIF-1alpha is covalently modified by SUMO-1. Thereafter, using a series of lysine mutants in the ODD domain, we found that HIF-1alpha was sumoylated at Lys(391) and Lys(477), suggesting that sumoylation at these two lysine residues enhances HIF-1alpha stability by possibly modulating other post-translational modifications. Altogether, we demonstrate that HIF-1alpha is upregulated through SUMO-1 modification at Lys(391)/Lys(477) residues, which may stabilize HIF-1alpha and enhance its transcriptional activity."xsd:string
http://purl.uniprot.org/citations/15465032http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2004.09.068"xsd:string
http://purl.uniprot.org/citations/15465032http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2004.09.068"xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/author"Kim S.-H."xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/author"Kim S.-H."xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/author"Kim K.-W."xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/author"Kim K.-W."xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/author"Bae S.-H."xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/author"Bae S.-H."xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/author"Park J.A."xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/author"Park J.A."xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/author"Choi S.-J."xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/author"Choi S.-J."xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/author"Bae M.-K."xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/author"Bae M.-K."xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/author"Jeong J.-W."xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/author"Jeong J.-W."xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/pages"394-400"xsd:string
http://purl.uniprot.org/citations/15465032http://purl.uniprot.org/core/pages"394-400"xsd:string