RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/11042394http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11042394http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11042394http://www.w3.org/2000/01/rdf-schema#comment"The cDNA and gene encoding human N-acetylglucosamine-6-O-sulfotransferase (Gn6ST) have been cloned. Comparative analysis of this cDNA with the mouse Gn6ST sequence indicates 96% amino acid identity between the two sequences. The expression of a soluble recombinant form of the protein in COS-1 cells produced an active sulfotransferase, which transferred sulfate to the terminal GlcNAc in GlcNAcbeta1-O-CH(3), GlcNAcbeta1-3Galbeta1-O-CH(3) and GlcNAcbeta1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Gl cNAc but not in GlcNAcalpha1-4GlcAbeta1-3Galbeta1-3Galbeta1-4 Xylbeta1-O-Ser. In addition, neither Galbeta1-4GlcNAcbeta1-O-naphthalenemethanol nor GalNAcbeta1-4GlcAbeta1-3Galbeta1-3Galbeta1-4X ylbeta1-O-Ser were utilized as acceptors. These findings indicate that a terminal beta-linked GlcNAc residue is necessary for acceptor substrates of Gn6ST. The human Gn6ST gene spans about 7 kb, consists of two exons and exhibits an intron-less coding region."xsd:string
http://purl.uniprot.org/citations/11042394http://purl.org/dc/terms/identifier"doi:10.1016/s0304-4165(00)00136-7"xsd:string
http://purl.uniprot.org/citations/11042394http://purl.org/dc/terms/identifier"doi:10.1016/s0304-4165(00)00136-7"xsd:string
http://purl.uniprot.org/citations/11042394http://purl.uniprot.org/core/author"Kitagawa H."xsd:string
http://purl.uniprot.org/citations/11042394http://purl.uniprot.org/core/author"Kitagawa H."xsd:string
http://purl.uniprot.org/citations/11042394http://purl.uniprot.org/core/author"Sugahara K."xsd:string
http://purl.uniprot.org/citations/11042394http://purl.uniprot.org/core/author"Sugahara K."xsd:string
http://purl.uniprot.org/citations/11042394http://purl.uniprot.org/core/author"Sakaguchi H."xsd:string
http://purl.uniprot.org/citations/11042394http://purl.uniprot.org/core/author"Sakaguchi H."xsd:string
http://purl.uniprot.org/citations/11042394http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11042394http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11042394http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/11042394http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/11042394http://purl.uniprot.org/core/pages"269-276"xsd:string
http://purl.uniprot.org/citations/11042394http://purl.uniprot.org/core/pages"269-276"xsd:string
http://purl.uniprot.org/citations/11042394http://purl.uniprot.org/core/title"Functional expression and genomic structure of human N-acetylglucosamine-6-O-sulfotransferase that transfers sulfate to b-N-acetylglucosamine at the nonreducing end of an N-acetyllactosamine sequence."xsd:string
http://purl.uniprot.org/citations/11042394http://purl.uniprot.org/core/title"Functional expression and genomic structure of human N-acetylglucosamine-6-O-sulfotransferase that transfers sulfate to b-N-acetylglucosamine at the nonreducing end of an N-acetyllactosamine sequence."xsd:string
http://purl.uniprot.org/citations/11042394http://purl.uniprot.org/core/volume"1523"xsd:string
http://purl.uniprot.org/citations/11042394http://purl.uniprot.org/core/volume"1523"xsd:string
http://purl.uniprot.org/citations/11042394http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11042394
http://purl.uniprot.org/citations/11042394http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11042394
http://purl.uniprot.org/citations/11042394http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11042394
http://purl.uniprot.org/citations/11042394http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11042394