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http://purl.uniprot.org/citations/8999954http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8999954http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8999954http://www.w3.org/2000/01/rdf-schema#comment"Estrogen receptors (ER) are ligand-inducible transcription factors regulated by Ser(Thr)-O-phosphorylation. Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc). Here we report that subpopulations of murine, bovine, and human estrogen receptors are modified by O-GlcNAc. O-GlcNAc moieties were detected on insect cell-expressed, mouse ER (mER) by probing with bovine milk galactosyltransferase, followed by structural analysis. Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation. These data suggest that greater than 10% of these populations of estrogen receptors bear O-GlcNAc. Site mapping of insect cell expressed mER localized one major site of O-GlcNAc addition to Thr-575, within a PEST region of the carboxyl-terminal F domain. Based upon their relative resistance to both hexosaminidase and to in vitro galactosylation, O-GlcNAc moieties appear to be largely buried on native mER. This dynamic saccharide modification, like phosphorylation, may play a role in modulating the dimerization, stability, or transactivation functions of estrogen receptors."xsd:string
http://purl.uniprot.org/citations/8999954http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.4.2421"xsd:string
http://purl.uniprot.org/citations/8999954http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.4.2421"xsd:string
http://purl.uniprot.org/citations/8999954http://purl.uniprot.org/core/author"Hart G.W."xsd:string
http://purl.uniprot.org/citations/8999954http://purl.uniprot.org/core/author"Hart G.W."xsd:string
http://purl.uniprot.org/citations/8999954http://purl.uniprot.org/core/author"Jiang M.S."xsd:string
http://purl.uniprot.org/citations/8999954http://purl.uniprot.org/core/author"Jiang M.S."xsd:string
http://purl.uniprot.org/citations/8999954http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/8999954http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/8999954http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8999954http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8999954http://purl.uniprot.org/core/pages"2421-2428"xsd:string
http://purl.uniprot.org/citations/8999954http://purl.uniprot.org/core/pages"2421-2428"xsd:string
http://purl.uniprot.org/citations/8999954http://purl.uniprot.org/core/title"A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine."xsd:string
http://purl.uniprot.org/citations/8999954http://purl.uniprot.org/core/title"A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine."xsd:string
http://purl.uniprot.org/citations/8999954http://purl.uniprot.org/core/volume"272"xsd:string
http://purl.uniprot.org/citations/8999954http://purl.uniprot.org/core/volume"272"xsd:string
http://purl.uniprot.org/citations/8999954http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8999954
http://purl.uniprot.org/citations/8999954http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8999954
http://purl.uniprot.org/citations/8999954http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8999954
http://purl.uniprot.org/citations/8999954http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8999954
http://purl.uniprot.org/uniprot/P49884http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8999954
http://purl.uniprot.org/uniprot/P19785http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8999954