PubMed:11323440 JSON TXT

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ggdb-test

{"project":"ggdb-test","denotations":[{"id":"T1","span":{"begin":307,"end":347},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"T2","span":{"begin":363,"end":371},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"T3","span":{"begin":442,"end":450},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T4","span":{"begin":734,"end":742},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T5","span":{"begin":976,"end":984},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"T6","span":{"begin":1122,"end":1130},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T7","span":{"begin":1139,"end":1147},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"T8","span":{"begin":1278,"end":1286},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T9","span":{"begin":1350,"end":1358},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"T10","span":{"begin":1363,"end":1371},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T11","span":{"begin":1407,"end":1415},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T12","span":{"begin":1454,"end":1462},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"T13","span":{"begin":1479,"end":1487},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"T14","span":{"begin":1578,"end":1586},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T15","span":{"begin":1771,"end":1779},"obj":"https://acgg.asia/db/ggdb/info/gg043"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

GlyCosmos6-Glycan-Motif-Image

GGDB-2020

{"project":"GGDB-2020","denotations":[{"id":"T1","span":{"begin":307,"end":347},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"T2","span":{"begin":363,"end":371},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"T3","span":{"begin":442,"end":450},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T4","span":{"begin":734,"end":742},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T5","span":{"begin":976,"end":984},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"T6","span":{"begin":1122,"end":1130},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T7","span":{"begin":1139,"end":1147},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"T8","span":{"begin":1278,"end":1286},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T9","span":{"begin":1350,"end":1358},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"T10","span":{"begin":1363,"end":1371},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T11","span":{"begin":1407,"end":1415},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T12","span":{"begin":1454,"end":1462},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"T13","span":{"begin":1479,"end":1487},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"T14","span":{"begin":1578,"end":1586},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"T15","span":{"begin":1771,"end":1779},"obj":"https://acgg.asia/db/ggdb/info/gg043"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

sentences

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":148},"obj":"Sentence"},{"id":"T2","span":{"begin":149,"end":372},"obj":"Sentence"},{"id":"T3","span":{"begin":373,"end":547},"obj":"Sentence"},{"id":"T4","span":{"begin":548,"end":705},"obj":"Sentence"},{"id":"T5","span":{"begin":706,"end":934},"obj":"Sentence"},{"id":"T6","span":{"begin":935,"end":940},"obj":"Sentence"},{"id":"T7","span":{"begin":941,"end":946},"obj":"Sentence"},{"id":"T8","span":{"begin":947,"end":1111},"obj":"Sentence"},{"id":"T9","span":{"begin":1112,"end":1335},"obj":"Sentence"},{"id":"T10","span":{"begin":1336,"end":1520},"obj":"Sentence"},{"id":"T11","span":{"begin":1521,"end":1725},"obj":"Sentence"},{"id":"T12","span":{"begin":1726,"end":1866},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

GlyCosmos6-Glycan-Motif-Structure

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":108,"end":127},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T2","span":{"begin":171,"end":180},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T3","span":{"begin":171,"end":180},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T4","span":{"begin":307,"end":326},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T5","span":{"begin":477,"end":496},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T6","span":{"begin":786,"end":795},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T7","span":{"begin":786,"end":795},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T8","span":{"begin":1048,"end":1053},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T9","span":{"begin":1386,"end":1405},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T10","span":{"begin":1687,"end":1706},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T11","span":{"begin":1821,"end":1840},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

Glycosmos6-GlycoEpitope

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":307,"end":326},"obj":"http://www.glycoepitope.jp/epitopes/EP0074"},{"id":"T2","span":{"begin":1386,"end":1405},"obj":"http://www.glycoepitope.jp/epitopes/EP0074"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

Glycosmos6-MAT

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":1622,"end":1627},"obj":"http://purl.obolibrary.org/obo/MAT_0000098"},{"id":"T2","span":{"begin":1629,"end":1635},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T3","span":{"begin":1641,"end":1648},"obj":"http://purl.obolibrary.org/obo/MAT_0000081"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

glycogenes

{"project":"glycogenes","denotations":[{"id":"PD-GlycoGenes20190927-B_T1","span":{"begin":307,"end":347},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"PD-GlycoGenes20190927-B_T2","span":{"begin":363,"end":371},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"PD-GlycoGenes20190927-B_T3","span":{"begin":442,"end":450},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"PD-GlycoGenes20190927-B_T4","span":{"begin":734,"end":742},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"PD-GlycoGenes20190927-B_T5","span":{"begin":976,"end":984},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"PD-GlycoGenes20190927-B_T6","span":{"begin":1122,"end":1130},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"PD-GlycoGenes20190927-B_T7","span":{"begin":1139,"end":1147},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"PD-GlycoGenes20190927-B_T8","span":{"begin":1278,"end":1286},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"PD-GlycoGenes20190927-B_T9","span":{"begin":1350,"end":1358},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"PD-GlycoGenes20190927-B_T10","span":{"begin":1363,"end":1371},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"PD-GlycoGenes20190927-B_T11","span":{"begin":1407,"end":1415},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"PD-GlycoGenes20190927-B_T12","span":{"begin":1454,"end":1462},"obj":"https://acgg.asia/db/ggdb/info/gg042"},{"id":"PD-GlycoGenes20190927-B_T13","span":{"begin":1479,"end":1487},"obj":"https://acgg.asia/db/ggdb/info/gg041"},{"id":"PD-GlycoGenes20190927-B_T14","span":{"begin":1578,"end":1586},"obj":"https://acgg.asia/db/ggdb/info/gg043"},{"id":"PD-GlycoGenes20190927-B_T15","span":{"begin":1707,"end":1710},"obj":"https://acgg.asia/db/ggdb/info/gg135"},{"id":"PD-GlycoGenes20190927-B_T16","span":{"begin":1771,"end":1779},"obj":"https://acgg.asia/db/ggdb/info/gg043"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

NGLY1-deficiency

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":1182,"end":1188},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":1250,"end":1256},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T3","span":{"begin":1307,"end":1313},"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 expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

GlyCosmos15-Glycan

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":307,"end":326},"obj":"Glycan"},{"id":"T2","span":{"begin":522,"end":527},"obj":"Glycan"},{"id":"T3","span":{"begin":659,"end":664},"obj":"Glycan"},{"id":"T4","span":{"begin":1048,"end":1053},"obj":"Glycan"},{"id":"T5","span":{"begin":1386,"end":1405},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G65889KE"},{"id":"A6","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G65889KE"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G00033MO"},{"id":"A7","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00033MO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G00033MO"},{"id":"A8","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00033MO"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A9","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G65889KE"},{"id":"A10","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G65889KE"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

Anatomy-MAT

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":1622,"end":1627},"obj":"Body_part"},{"id":"T2","span":{"begin":1629,"end":1635},"obj":"Body_part"},{"id":"T3","span":{"begin":1641,"end":1648},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000098"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000081"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

Glycan-GlyCosmos

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":307,"end":326},"obj":"Glycan"},{"id":"T2","span":{"begin":1386,"end":1405},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G65889KE"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G65889KE"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G65889KE"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G65889KE"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

GlyCosmos-GlycoEpitope

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":307,"end":326},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":1386,"end":1405},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0074"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0074"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

GlyCosmos15-UBERON

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":636,"end":641},"obj":"Body_part"},{"id":"T2","span":{"begin":1622,"end":1627},"obj":"Body_part"},{"id":"T3","span":{"begin":1629,"end":1635},"obj":"Body_part"},{"id":"T4","span":{"begin":1641,"end":1648},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000992"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000955"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0002046"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

GlyCosmos15-Taxon

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":44,"end":49},"obj":"Organism"},{"id":"T2","span":{"begin":620,"end":635},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"10029"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

GlyCosmos15-Sentences

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":148},"obj":"Sentence"},{"id":"T2","span":{"begin":149,"end":372},"obj":"Sentence"},{"id":"T3","span":{"begin":373,"end":547},"obj":"Sentence"},{"id":"T4","span":{"begin":548,"end":705},"obj":"Sentence"},{"id":"T5","span":{"begin":706,"end":1111},"obj":"Sentence"},{"id":"T6","span":{"begin":1112,"end":1335},"obj":"Sentence"},{"id":"T7","span":{"begin":1336,"end":1520},"obj":"Sentence"},{"id":"T8","span":{"begin":1521,"end":1725},"obj":"Sentence"},{"id":"T9","span":{"begin":1726,"end":1866},"obj":"Sentence"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

GlyCosmos15-GlycoEpitope

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":307,"end":326},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":1386,"end":1405},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0074"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0074"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

GlyCosmos15-FMA

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":636,"end":641},"obj":"Body_part"},{"id":"T2","span":{"begin":1622,"end":1627},"obj":"Body_part"},{"id":"T3","span":{"begin":1629,"end":1635},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:7209"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:50801"},{"id":"A3","pred":"db_id","subj":"T3","obj":"FMA:7203"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

GlyCosmos15-MAT

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":1622,"end":1627},"obj":"Body_part"},{"id":"T2","span":{"begin":1629,"end":1635},"obj":"Body_part"},{"id":"T3","span":{"begin":1641,"end":1648},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000098"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000081"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":44,"end":49},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":620,"end":635},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"10029"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":636,"end":641},"obj":"Body_part"},{"id":"T2","span":{"begin":1622,"end":1627},"obj":"Body_part"},{"id":"T4","span":{"begin":1629,"end":1635},"obj":"Body_part"},{"id":"T5","span":{"begin":1641,"end":1648},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000992"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000955"},{"id":"A3","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_6110636"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0002046"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

GlyCosmos15-Lectin

{"project":"GlyCosmos15-Lectin","denotations":[{"id":"T1","span":{"begin":55,"end":60},"obj":"GL_000491"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}

Lectin_test

{"project":"Lectin_test","denotations":[{"id":"T1","span":{"begin":55,"end":60},"obj":"GL_000491"}],"text":"Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.\nA novel cDNA-encoding galactose 3-O-sulfotransferase was cloned by screening the expressed sequence tag data base using the previously cloned cDNA encoding a galactosyl ceramide 3-O-sulfotransferase, which we term Gal3ST-1. The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. These conclusions were confirmed by analyzing CD43 chimeric proteins in Chinese hamster ovary cells expressing core2 beta1,6-N-acetylglucosaminyltransferase. The acceptor specificity of Gal3ST-3 contrasts with that of the recently cloned galactose 3-O-sulfotransferase (Honke, K., Tsuda, M., Koyota, S., Wada, Y., Iida-Tanaka, N., Ishizuka, I., Nakayama, J., and Taniguchi, N. (2001) J. Biol. Chem. 276, 267-274), which we term Gal3ST-2 in the present study because the latter enzyme can also act on core1 O-glycan and type 1 oligosaccharides, Galbeta1--\u003e3GlcNAc. Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1--\u003e4(sulfo--\u003e6)GlcNAc, indicating that disulfated sulfo--\u003e3Galbeta1--\u003e4(sulfo--\u003e6) GlcNAc--\u003eR may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase. Although both Gal3ST-2 and Gal3ST-3 do not act on galactosyl ceramide, Gal3ST-3 is only moderately more homologous to Gal3ST-2 (40.1%) than to Gal3ST-1 (38.0%) at the amino acid level. Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported. These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans."}