http://purl.uniprot.org/citations/15502158 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15502158 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15502158 | http://www.w3.org/2000/01/rdf-schema#comment | "Jade-1 was identified as a protein partner of the von Hippel-Lindau tumor suppressor pVHL. The interaction of Jade-1 and pVHL correlates with renal cancer risk. We have investigated the molecular function of Jade-1. Jade-1 has two zinc finger motifs called plant homeodomains (PHD). A line of evidence suggests that the PHD finger functions in chromatin remodeling and protein-protein interactions. We determined the cellular localization of Jade-1 and examined whether Jade-1 might have transcriptional and histone acetyltransferase (HAT) functions. Biochemical cell fractionation studies as well as confocal images of cells immunostained with a specific Jade-1 antibody revealed that endogenous Jade-1 is localized predominantly in the cell nucleus. Tethering of Gal4-Jade-1 fusion protein to Gal4-responsive promoters in co-transfection experiments activated transcription 5-6-fold, indicating that Jade-1 is a possible transcriptional activator. It was remarkable that overexpression of Jade-1 in cultured cells specifically increased levels of endogenous acetylated histone H4, but not histone H3, strongly suggesting that Jade-1 associates with HAT activity specific for histone H4. Deletion of the two PHD fingers completely abolished Jade-1 transcriptional and HAT activities, indicating that these domains are indispensable for Jade-1 nuclear functions. In addition, we demonstrated that TIP60, a known HAT with histone H4/H2A specificity, physically associates with Jade-1 and is able to augment Jade-1 HAT function in live cells, strongly suggesting that TIP60 might mediate Jade-1 HAT activity. Thus, Jade-1 is a novel candidate transcriptional co-activator associated with HAT activity and may play a key role in the pathogenesis of renal cancer and von Hippel-Lindau disease."xsd:string |
http://purl.uniprot.org/citations/15502158 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m410487200"xsd:string |
http://purl.uniprot.org/citations/15502158 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m410487200"xsd:string |
http://purl.uniprot.org/citations/15502158 | http://purl.uniprot.org/core/author | "Cohen H.T."xsd:string |
http://purl.uniprot.org/citations/15502158 | http://purl.uniprot.org/core/author | "Cohen H.T."xsd:string |
http://purl.uniprot.org/citations/15502158 | http://purl.uniprot.org/core/author | "Panchenko M.V."xsd:string |
http://purl.uniprot.org/citations/15502158 | http://purl.uniprot.org/core/author | "Panchenko M.V."xsd:string |
http://purl.uniprot.org/citations/15502158 | http://purl.uniprot.org/core/author | "Zhou M.I."xsd:string |
http://purl.uniprot.org/citations/15502158 | http://purl.uniprot.org/core/author | "Zhou M.I."xsd:string |
http://purl.uniprot.org/citations/15502158 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
http://purl.uniprot.org/citations/15502158 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
http://purl.uniprot.org/citations/15502158 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/15502158 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/15502158 | http://purl.uniprot.org/core/pages | "56032-56041"xsd:string |
http://purl.uniprot.org/citations/15502158 | http://purl.uniprot.org/core/pages | "56032-56041"xsd:string |
http://purl.uniprot.org/citations/15502158 | http://purl.uniprot.org/core/title | "von Hippel-Lindau partner Jade-1 is a transcriptional co-activator associated with histone acetyltransferase activity."xsd:string |
http://purl.uniprot.org/citations/15502158 | http://purl.uniprot.org/core/title | "von Hippel-Lindau partner Jade-1 is a transcriptional co-activator associated with histone acetyltransferase activity."xsd:string |
http://purl.uniprot.org/citations/15502158 | http://purl.uniprot.org/core/volume | "279"xsd:string |
http://purl.uniprot.org/citations/15502158 | http://purl.uniprot.org/core/volume | "279"xsd:string |
http://purl.uniprot.org/citations/15502158 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15502158 |
http://purl.uniprot.org/citations/15502158 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15502158 |
http://purl.uniprot.org/citations/15502158 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15502158 |
http://purl.uniprot.org/citations/15502158 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15502158 |