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http://purl.uniprot.org/citations/12080076http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12080076http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12080076http://www.w3.org/2000/01/rdf-schema#comment"We have identified and characterized an N-acetylgalactosamine-4-O-sulfotransferase designated chondroitin-4-sulfotransferase-3 (C4ST-3) (GenBank accession number AY120869) based on its homology to HNK-1 sulfotransferase (HNK-1 ST). The cDNA predicts an open reading frame encoding a type II membrane protein of 341 amino acids with a 12-amino acid cytoplasmic domain and a 311-amino acid luminal domain containing a single potential N-linked glycosylation site. C4ST-3 has the greatest amino acid sequence identity when aligned with chondroitin-4-O-sulfotransferase 1 (C4ST-1) (45%) but also shows significant amino acid identity with chondroitin-4-O-sulfotransferase 2 (C4ST-2) (27%), dermatan-4-O-sulfotransferase 1 (29%), HNK-1 ST (26%), N-acetylgalactosamine-4-O-sulfotransferase 1 (26%), and N-acetylgalactosamine-4-O-sulfotransferase 2 (23%). C4ST-3 transfers sulfate to the C-4 hydroxyl of beta1,4-linked GalNAc that is substituted with a beta-linked glucuronic acid at the C-3 hydroxyl. The open reading frame of C4ST-3 is encoded by three exons located on human chromosome 3q21.3. Northern blot analysis reveals a single 2.1-kilobase transcript. C4ST-3 message is expressed in adult liver and at lower levels in adult kidney, lymph nodes, and fetal liver. Although C4ST-3 and C4ST-1 have similar specificities, the highly restricted pattern of expression seen for C4ST-3 suggests that it has a different role than C4ST-1."xsd:string
http://purl.uniprot.org/citations/12080076http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m204907200"xsd:string
http://purl.uniprot.org/citations/12080076http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m204907200"xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/author"Baenziger J.U."xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/author"Baenziger J.U."xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/author"Schachner M."xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/author"Schachner M."xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/author"Xia G."xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/author"Xia G."xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/author"Kang H.-G."xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/author"Kang H.-G."xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/author"Evers M.R."xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/author"Evers M.R."xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/pages"34766-34772"xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/pages"34766-34772"xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/title"Molecular cloning and characterization of chondroitin-4-O-sulfotransferase-3. A novel member of the HNK-1 family of sulfotransferases."xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/title"Molecular cloning and characterization of chondroitin-4-O-sulfotransferase-3. A novel member of the HNK-1 family of sulfotransferases."xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/12080076http://purl.uniprot.org/core/volume"277"xsd:string