PubMed:11333265 JSONTXT

{"project":"ggdb-test","denotations":[{"id":"T1","span":{"begin":222,"end":230},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"T2","span":{"begin":346,"end":354},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"T3","span":{"begin":518,"end":526},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"T4","span":{"begin":572,"end":580},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"T5","span":{"begin":629,"end":637},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"T6","span":{"begin":688,"end":696},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T7","span":{"begin":717,"end":725},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"T8","span":{"begin":817,"end":825},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"T9","span":{"begin":983,"end":991},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"T10","span":{"begin":1499,"end":1507},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"T11","span":{"begin":1594,"end":1602},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"T12","span":{"begin":1604,"end":1612},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"T13","span":{"begin":1614,"end":1622},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T14","span":{"begin":1628,"end":1636},"obj":"https://acgg.asia/db/ggdb/info/gg044"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":56,"end":65},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":183,"end":192},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A4","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}

{"project":"GGDB-2020","denotations":[{"id":"T1","span":{"begin":222,"end":230},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"T2","span":{"begin":346,"end":354},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"T3","span":{"begin":518,"end":526},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"T4","span":{"begin":572,"end":580},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"T5","span":{"begin":629,"end":637},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"T6","span":{"begin":688,"end":696},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T7","span":{"begin":717,"end":725},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"T8","span":{"begin":817,"end":825},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"T9","span":{"begin":983,"end":991},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"T10","span":{"begin":1499,"end":1507},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"T11","span":{"begin":1594,"end":1602},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"T12","span":{"begin":1604,"end":1612},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"T13","span":{"begin":1614,"end":1622},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T14","span":{"begin":1628,"end":1636},"obj":"https://acgg.asia/db/ggdb/info/gg044"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":155},"obj":"Sentence"},{"id":"T2","span":{"begin":156,"end":356},"obj":"Sentence"},{"id":"T3","span":{"begin":357,"end":490},"obj":"Sentence"},{"id":"T4","span":{"begin":491,"end":712},"obj":"Sentence"},{"id":"T5","span":{"begin":713,"end":802},"obj":"Sentence"},{"id":"T6","span":{"begin":803,"end":982},"obj":"Sentence"},{"id":"T7","span":{"begin":983,"end":1147},"obj":"Sentence"},{"id":"T8","span":{"begin":1148,"end":1356},"obj":"Sentence"},{"id":"T9","span":{"begin":1357,"end":1471},"obj":"Sentence"},{"id":"T10","span":{"begin":1472,"end":1701},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":56,"end":65},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T2","span":{"begin":56,"end":65},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T3","span":{"begin":183,"end":192},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T4","span":{"begin":183,"end":192},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}

{"project":"FSU-PRGE","denotations":[{"id":"T1","span":{"begin":56,"end":86},"obj":"protein"},{"id":"T2","span":{"begin":183,"end":213},"obj":"protein"},{"id":"T3","span":{"begin":222,"end":230},"obj":"protein"},{"id":"T4","span":{"begin":313,"end":344},"obj":"protein"},{"id":"T5","span":{"begin":346,"end":354},"obj":"protein"},{"id":"T6","span":{"begin":518,"end":526},"obj":"protein"},{"id":"T7","span":{"begin":572,"end":580},"obj":"protein"},{"id":"T8","span":{"begin":582,"end":594},"obj":"protein"},{"id":"T9","span":{"begin":594,"end":595},"obj":"protein"},{"id":"T10","span":{"begin":595,"end":607},"obj":"protein"},{"id":"T11","span":{"begin":607,"end":608},"obj":"protein"},{"id":"T12","span":{"begin":608,"end":627},"obj":"protein"},{"id":"T13","span":{"begin":629,"end":637},"obj":"protein"},{"id":"T14","span":{"begin":643,"end":655},"obj":"protein"},{"id":"T15","span":{"begin":655,"end":656},"obj":"protein"},{"id":"T16","span":{"begin":656,"end":666},"obj":"protein"},{"id":"T17","span":{"begin":666,"end":667},"obj":"protein"},{"id":"T18","span":{"begin":667,"end":686},"obj":"protein"},{"id":"T19","span":{"begin":688,"end":696},"obj":"protein"},{"id":"T20","span":{"begin":717,"end":725},"obj":"protein"},{"id":"T21","span":{"begin":817,"end":825},"obj":"protein"},{"id":"T22","span":{"begin":852,"end":868},"obj":"protein"},{"id":"T23","span":{"begin":983,"end":991},"obj":"protein"},{"id":"T24","span":{"begin":1499,"end":1507},"obj":"protein"},{"id":"T25","span":{"begin":1534,"end":1540},"obj":"protein"},{"id":"T26","span":{"begin":1540,"end":1541},"obj":"protein"},{"id":"T27","span":{"begin":1541,"end":1566},"obj":"protein"},{"id":"T28","span":{"begin":1594,"end":1602},"obj":"protein"},{"id":"T29","span":{"begin":1604,"end":1612},"obj":"protein"},{"id":"T30","span":{"begin":1614,"end":1622},"obj":"protein"},{"id":"T31","span":{"begin":1628,"end":1636},"obj":"protein"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}

{"project":"glycogenes","denotations":[{"id":"PD-GlycoGenes20190927-B_T1","span":{"begin":222,"end":230},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"PD-GlycoGenes20190927-B_T2","span":{"begin":346,"end":354},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"PD-GlycoGenes20190927-B_T3","span":{"begin":464,"end":466},"obj":"https://acgg.asia/db/ggdb/info/gg111"},{"id":"PD-GlycoGenes20190927-B_T4","span":{"begin":518,"end":526},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"PD-GlycoGenes20190927-B_T5","span":{"begin":572,"end":580},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"PD-GlycoGenes20190927-B_T6","span":{"begin":629,"end":637},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"PD-GlycoGenes20190927-B_T7","span":{"begin":688,"end":696},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"PD-GlycoGenes20190927-B_T8","span":{"begin":717,"end":725},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"PD-GlycoGenes20190927-B_T9","span":{"begin":817,"end":825},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"PD-GlycoGenes20190927-B_T10","span":{"begin":983,"end":991},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"PD-GlycoGenes20190927-B_T11","span":{"begin":1499,"end":1507},"obj":"https://acgg.asia/db/ggdb/info/gg044"},{"id":"PD-GlycoGenes20190927-B_T12","span":{"begin":1604,"end":1612},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"PD-GlycoGenes20190927-B_T13","span":{"begin":1614,"end":1622},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"PD-GlycoGenes20190927-B_T14","span":{"begin":1628,"end":1636},"obj":"https://acgg.asia/db/ggdb/info/gg044"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":1043,"end":1049},"obj":"chem:24139"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":1061,"end":1067},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":786,"end":796},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0005694"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":50,"end":55},"obj":"Organism"},{"id":"T2","span":{"begin":307,"end":312},"obj":"Organism"},{"id":"T3","span":{"begin":566,"end":571},"obj":"Organism"},{"id":"T4","span":{"begin":780,"end":785},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9606"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":1061,"end":1067},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":155},"obj":"Sentence"},{"id":"T2","span":{"begin":156,"end":356},"obj":"Sentence"},{"id":"T3","span":{"begin":357,"end":490},"obj":"Sentence"},{"id":"T4","span":{"begin":491,"end":712},"obj":"Sentence"},{"id":"T5","span":{"begin":713,"end":802},"obj":"Sentence"},{"id":"T6","span":{"begin":803,"end":1147},"obj":"Sentence"},{"id":"T7","span":{"begin":1148,"end":1356},"obj":"Sentence"},{"id":"T8","span":{"begin":1357,"end":1471},"obj":"Sentence"},{"id":"T9","span":{"begin":1472,"end":1701},"obj":"Sentence"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":786,"end":796},"obj":"Body_part"},{"id":"T2","span":{"begin":1463,"end":1470},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:67093"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:9637"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":50,"end":55},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":307,"end":312},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":566,"end":571},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":780,"end":785},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9606"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":467,"end":480},"obj":"Body_part"},{"id":"T2","span":{"begin":786,"end":796},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/GO_0005694"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}

{"project":"GlyCosmos15-Lectin","denotations":[{"id":"T1","span":{"begin":1534,"end":1542},"obj":"GL_000491"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}

{"project":"Lectin_test","denotations":[{"id":"T1","span":{"begin":1534,"end":1542},"obj":"GL_000491"}],"text":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1--\u003e3galNAc residue in O-glycans.\nWe have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by analysis of an expression sequence tag using the amino acid sequence of human cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single open reading frame coding for a protein of 486 amino acids with a type II transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1--\u003e3/4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-2) and Gal beta 1--\u003e4GlcNAc:--\u003e3'-sulfotransferase (Gal3ST-3), respectively. The Gal3ST-4 gene comprised at least four exons and was located on human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the C-3' position of Gal beta 1--\u003e3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 1--\u003e3GalNAc and Gal beta 1--\u003e3(GlcNAc beta 1--\u003e6)GalNAc as good substrates, but not Gal beta 1--\u003e3GalNAc(OH) or Gal beta 1--\u003e3/4GlcNAc. Asialofetuin is also a good substrate, and the sulfation was found exclusively in O-linked glycans that consist of the Gal beta 1--\u003e3GalNAc moiety, suggesting that the enzyme is specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase mRNA for the enzyme is expressed extensively in various tissues. These results suggest that Gal3ST-4 is the fourth member of a Gal:--\u003e3-sulfotransferase family and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are responsible for sulfation of different acceptor substrates."}