PubMed:12407114 JSONTXT

{"project":"GGDB-2020","denotations":[{"id":"T1","span":{"begin":140,"end":150},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T2","span":{"begin":532,"end":542},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T3","span":{"begin":572,"end":582},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T4","span":{"begin":636,"end":645},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T5","span":{"begin":682,"end":692},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T6","span":{"begin":859,"end":868},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T7","span":{"begin":873,"end":883},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T8","span":{"begin":1040,"end":1050},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T9","span":{"begin":1159,"end":1168},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T10","span":{"begin":1186,"end":1196},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T11","span":{"begin":1237,"end":1246},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T12","span":{"begin":1251,"end":1261},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T13","span":{"begin":1421,"end":1431},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T14","span":{"begin":1597,"end":1607},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T15","span":{"begin":1627,"end":1637},"obj":"https://acgg.asia/db/ggdb/info/gg099"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"ggdb-test","denotations":[{"id":"T1","span":{"begin":140,"end":150},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T2","span":{"begin":532,"end":542},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T3","span":{"begin":572,"end":582},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T4","span":{"begin":636,"end":645},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T5","span":{"begin":682,"end":692},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T6","span":{"begin":859,"end":868},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T7","span":{"begin":873,"end":883},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T8","span":{"begin":1040,"end":1050},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T9","span":{"begin":1159,"end":1168},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T10","span":{"begin":1186,"end":1196},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T11","span":{"begin":1237,"end":1246},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T12","span":{"begin":1251,"end":1261},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T13","span":{"begin":1421,"end":1431},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T14","span":{"begin":1597,"end":1607},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"T15","span":{"begin":1627,"end":1637},"obj":"https://acgg.asia/db/ggdb/info/gg099"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":1547,"end":1557},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":1725,"end":1735},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G57321FI"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G57321FI"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":248},"obj":"Sentence"},{"id":"T2","span":{"begin":249,"end":417},"obj":"Sentence"},{"id":"T3","span":{"begin":418,"end":543},"obj":"Sentence"},{"id":"T4","span":{"begin":544,"end":646},"obj":"Sentence"},{"id":"T5","span":{"begin":647,"end":1169},"obj":"Sentence"},{"id":"T6","span":{"begin":1170,"end":1488},"obj":"Sentence"},{"id":"T7","span":{"begin":1489,"end":1755},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":1547,"end":1557},"obj":"https://glytoucan.org/Structures/Glycans/G57321FI"},{"id":"T2","span":{"begin":1725,"end":1735},"obj":"https://glytoucan.org/Structures/Glycans/G57321FI"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":1547,"end":1557},"obj":"http://www.glycoepitope.jp/epitopes/EP0021"},{"id":"T2","span":{"begin":1725,"end":1735},"obj":"http://www.glycoepitope.jp/epitopes/EP0021"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":741,"end":746},"obj":"http://purl.obolibrary.org/obo/MAT_0000098"},{"id":"T2","span":{"begin":1576,"end":1586},"obj":"http://purl.obolibrary.org/obo/MAT_0000110"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"glycogenes","denotations":[{"id":"PD-GlycoGenes20190927-B_T1","span":{"begin":126,"end":136},"obj":"url"},{"id":"PD-GlycoGenes20190927-B_T2","span":{"begin":140,"end":150},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"PD-GlycoGenes20190927-B_T3","span":{"begin":361,"end":369},"obj":"https://acgg.asia/db/ggdb/info/gg104"},{"id":"PD-GlycoGenes20190927-B_T4","span":{"begin":473,"end":481},"obj":"https://acgg.asia/db/ggdb/info/gg104"},{"id":"PD-GlycoGenes20190927-B_T5","span":{"begin":532,"end":542},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"PD-GlycoGenes20190927-B_T6","span":{"begin":572,"end":582},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"PD-GlycoGenes20190927-B_T7","span":{"begin":636,"end":645},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"PD-GlycoGenes20190927-B_T8","span":{"begin":682,"end":692},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"PD-GlycoGenes20190927-B_T9","span":{"begin":859,"end":868},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"PD-GlycoGenes20190927-B_T10","span":{"begin":873,"end":883},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"PD-GlycoGenes20190927-B_T11","span":{"begin":1040,"end":1050},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"PD-GlycoGenes20190927-B_T12","span":{"begin":1159,"end":1168},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"PD-GlycoGenes20190927-B_T13","span":{"begin":1186,"end":1196},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"PD-GlycoGenes20190927-B_T14","span":{"begin":1237,"end":1246},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"PD-GlycoGenes20190927-B_T15","span":{"begin":1251,"end":1261},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"PD-GlycoGenes20190927-B_T16","span":{"begin":1421,"end":1431},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"PD-GlycoGenes20190927-B_T17","span":{"begin":1597,"end":1607},"obj":"https://acgg.asia/db/ggdb/info/gg099"},{"id":"PD-GlycoGenes20190927-B_T18","span":{"begin":1627,"end":1637},"obj":"https://acgg.asia/db/ggdb/info/gg099"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":916,"end":929},"obj":"Disease"},{"id":"T2","span":{"begin":985,"end":997},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005072"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0018177"},{"id":"A3","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0020690"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":741,"end":746},"obj":"Body_part"},{"id":"T2","span":{"begin":1576,"end":1586},"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_0000110"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":916,"end":929},"obj":"Phenotype"},{"id":"T2","span":{"begin":985,"end":997},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0003006"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0012174"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":140,"end":146},"obj":"Glycan"},{"id":"T2","span":{"begin":210,"end":216},"obj":"Glycan"},{"id":"T3","span":{"begin":361,"end":367},"obj":"Glycan"},{"id":"T4","span":{"begin":473,"end":479},"obj":"Glycan"},{"id":"T5","span":{"begin":532,"end":538},"obj":"Glycan"},{"id":"T6","span":{"begin":572,"end":578},"obj":"Glycan"},{"id":"T7","span":{"begin":636,"end":642},"obj":"Glycan"},{"id":"T8","span":{"begin":682,"end":688},"obj":"Glycan"},{"id":"T9","span":{"begin":859,"end":865},"obj":"Glycan"},{"id":"T10","span":{"begin":873,"end":879},"obj":"Glycan"},{"id":"T11","span":{"begin":1040,"end":1046},"obj":"Glycan"},{"id":"T12","span":{"begin":1096,"end":1102},"obj":"Glycan"},{"id":"T13","span":{"begin":1159,"end":1165},"obj":"Glycan"},{"id":"T14","span":{"begin":1186,"end":1192},"obj":"Glycan"},{"id":"T15","span":{"begin":1237,"end":1243},"obj":"Glycan"},{"id":"T16","span":{"begin":1251,"end":1257},"obj":"Glycan"},{"id":"T17","span":{"begin":1319,"end":1325},"obj":"Glycan"},{"id":"T18","span":{"begin":1421,"end":1427},"obj":"Glycan"},{"id":"T19","span":{"begin":1547,"end":1557},"obj":"Glycan"},{"id":"T20","span":{"begin":1597,"end":1603},"obj":"Glycan"},{"id":"T21","span":{"begin":1627,"end":1633},"obj":"Glycan"},{"id":"T22","span":{"begin":1725,"end":1735},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A23","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A24","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A25","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A26","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A27","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A28","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A29","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A30","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A31","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A10","pred":"glycosmos_id","subj":"T10","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A32","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A11","pred":"glycosmos_id","subj":"T11","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A33","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A12","pred":"glycosmos_id","subj":"T12","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A34","pred":"image","subj":"T12","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A13","pred":"glycosmos_id","subj":"T13","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A35","pred":"image","subj":"T13","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A14","pred":"glycosmos_id","subj":"T14","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A36","pred":"image","subj":"T14","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A15","pred":"glycosmos_id","subj":"T15","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A37","pred":"image","subj":"T15","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A16","pred":"glycosmos_id","subj":"T16","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A38","pred":"image","subj":"T16","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A17","pred":"glycosmos_id","subj":"T17","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A39","pred":"image","subj":"T17","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A18","pred":"glycosmos_id","subj":"T18","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A40","pred":"image","subj":"T18","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A19","pred":"glycosmos_id","subj":"T19","obj":"https://glycosmos.org/glycans/show/G57321FI"},{"id":"A41","pred":"image","subj":"T19","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G57321FI"},{"id":"A20","pred":"glycosmos_id","subj":"T20","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A42","pred":"image","subj":"T20","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A21","pred":"glycosmos_id","subj":"T21","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A43","pred":"image","subj":"T21","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A22","pred":"glycosmos_id","subj":"T22","obj":"https://glycosmos.org/glycans/show/G57321FI"},{"id":"A44","pred":"image","subj":"T22","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G57321FI"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":1547,"end":1557},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":1725,"end":1735},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0021"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0021"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"GlyCosmos15-HP","denotations":[{"id":"T1","span":{"begin":916,"end":929},"obj":"Phenotype"},{"id":"T2","span":{"begin":985,"end":997},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0003006"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0012174"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":916,"end":929},"obj":"Disease"},{"id":"T2","span":{"begin":985,"end":997},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005072"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0018177"},{"id":"A3","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0020690"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":38,"end":43},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":411,"end":416},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":464,"end":469},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":1442,"end":1446},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":1617,"end":1622},"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":"10088"},{"id":"A5","pred":"db_id","subj":"T5","obj":"10088"},{"id":"A6","pred":"db_id","subj":"T5","obj":"10090"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":186,"end":193},"obj":"Cell"},{"id":"T2","span":{"begin":966,"end":973},"obj":"Cell"},{"id":"T3","span":{"begin":1025,"end":1035},"obj":"Cell"},{"id":"T4","span":{"begin":1409,"end":1416},"obj":"Cell"},{"id":"T5","span":{"begin":1747,"end":1754},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000540"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000540"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000127"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000540"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000540"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":741,"end":746},"obj":"Body_part"},{"id":"T3","span":{"begin":1025,"end":1035},"obj":"Body_part"},{"id":"T4","span":{"begin":1576,"end":1586},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000955"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_6110636"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL_0000127"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0002037"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":741,"end":746},"obj":"Body_part"},{"id":"T2","span":{"begin":1576,"end":1586},"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_0000110"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":248},"obj":"Sentence"},{"id":"T2","span":{"begin":249,"end":417},"obj":"Sentence"},{"id":"T3","span":{"begin":418,"end":543},"obj":"Sentence"},{"id":"T4","span":{"begin":544,"end":646},"obj":"Sentence"},{"id":"T5","span":{"begin":647,"end":1169},"obj":"Sentence"},{"id":"T6","span":{"begin":1170,"end":1488},"obj":"Sentence"},{"id":"T7","span":{"begin":1489,"end":1755},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":248},"obj":"Sentence"},{"id":"T2","span":{"begin":249,"end":417},"obj":"Sentence"},{"id":"T3","span":{"begin":418,"end":543},"obj":"Sentence"},{"id":"T4","span":{"begin":544,"end":646},"obj":"Sentence"},{"id":"T5","span":{"begin":647,"end":1169},"obj":"Sentence"},{"id":"T6","span":{"begin":1170,"end":1488},"obj":"Sentence"},{"id":"T7","span":{"begin":1489,"end":1755},"obj":"Sentence"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":140,"end":146},"obj":"Glycan"},{"id":"T2","span":{"begin":210,"end":216},"obj":"Glycan"},{"id":"T3","span":{"begin":361,"end":367},"obj":"Glycan"},{"id":"T4","span":{"begin":473,"end":479},"obj":"Glycan"},{"id":"T5","span":{"begin":532,"end":538},"obj":"Glycan"},{"id":"T6","span":{"begin":572,"end":578},"obj":"Glycan"},{"id":"T7","span":{"begin":636,"end":642},"obj":"Glycan"},{"id":"T8","span":{"begin":682,"end":688},"obj":"Glycan"},{"id":"T9","span":{"begin":859,"end":865},"obj":"Glycan"},{"id":"T10","span":{"begin":873,"end":879},"obj":"Glycan"},{"id":"T11","span":{"begin":1040,"end":1046},"obj":"Glycan"},{"id":"T12","span":{"begin":1096,"end":1102},"obj":"Glycan"},{"id":"T13","span":{"begin":1159,"end":1165},"obj":"Glycan"},{"id":"T14","span":{"begin":1186,"end":1192},"obj":"Glycan"},{"id":"T15","span":{"begin":1237,"end":1243},"obj":"Glycan"},{"id":"T16","span":{"begin":1251,"end":1257},"obj":"Glycan"},{"id":"T17","span":{"begin":1319,"end":1325},"obj":"Glycan"},{"id":"T18","span":{"begin":1421,"end":1427},"obj":"Glycan"},{"id":"T19","span":{"begin":1547,"end":1557},"obj":"Glycan"},{"id":"T20","span":{"begin":1597,"end":1603},"obj":"Glycan"},{"id":"T21","span":{"begin":1627,"end":1633},"obj":"Glycan"},{"id":"T22","span":{"begin":1725,"end":1735},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A10","pred":"glycosmos_id","subj":"T10","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A11","pred":"glycosmos_id","subj":"T11","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A12","pred":"glycosmos_id","subj":"T12","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A13","pred":"glycosmos_id","subj":"T13","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A14","pred":"glycosmos_id","subj":"T14","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A15","pred":"glycosmos_id","subj":"T15","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A16","pred":"glycosmos_id","subj":"T16","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A17","pred":"glycosmos_id","subj":"T17","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A18","pred":"glycosmos_id","subj":"T18","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A19","pred":"glycosmos_id","subj":"T19","obj":"https://glycosmos.org/glycans/show/G57321FI"},{"id":"A20","pred":"glycosmos_id","subj":"T20","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A21","pred":"glycosmos_id","subj":"T21","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A22","pred":"glycosmos_id","subj":"T22","obj":"https://glycosmos.org/glycans/show/G57321FI"},{"id":"A23","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A24","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A25","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A26","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A27","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A28","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A29","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A30","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A31","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A32","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A33","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A34","pred":"image","subj":"T12","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A35","pred":"image","subj":"T13","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A36","pred":"image","subj":"T14","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A37","pred":"image","subj":"T15","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A38","pred":"image","subj":"T16","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A39","pred":"image","subj":"T17","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A40","pred":"image","subj":"T18","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A41","pred":"image","subj":"T19","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G57321FI"},{"id":"A42","pred":"image","subj":"T20","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A43","pred":"image","subj":"T21","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A44","pred":"image","subj":"T22","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G57321FI"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":1547,"end":1557},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":1725,"end":1735},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0021"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0021"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":38,"end":43},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":411,"end":416},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":464,"end":469},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":1442,"end":1446},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":1617,"end":1622},"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":"10088"},{"id":"A5","pred":"db_id","subj":"T5","obj":"10088"},{"id":"A6","pred":"db_id","subj":"T5","obj":"10090"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":741,"end":746},"obj":"Body_part"},{"id":"T3","span":{"begin":1025,"end":1035},"obj":"Body_part"},{"id":"T4","span":{"begin":1576,"end":1586},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000955"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_6110636"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL_0000127"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0002037"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":186,"end":193},"obj":"Cell"},{"id":"T2","span":{"begin":966,"end":973},"obj":"Cell"},{"id":"T3","span":{"begin":1025,"end":1035},"obj":"Cell"},{"id":"T4","span":{"begin":1409,"end":1416},"obj":"Cell"},{"id":"T5","span":{"begin":1747,"end":1754},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000540"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000540"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000127"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000540"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000540"}],"text":"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.\nTo date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons."}