PubMed:8663203 JSONTXT

{"project":"GGDB-2020","denotations":[{"id":"T1","span":{"begin":128,"end":137},"obj":"https://acgg.asia/db/ggdb/info/gg089"},{"id":"T2","span":{"begin":373,"end":382},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T3","span":{"begin":535,"end":544},"obj":"https://acgg.asia/db/ggdb/info/gg089"},{"id":"T4","span":{"begin":677,"end":686},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T5","span":{"begin":915,"end":924},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T6","span":{"begin":1000,"end":1009},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T7","span":{"begin":1036,"end":1045},"obj":"https://acgg.asia/db/ggdb/info/gg089"},{"id":"T8","span":{"begin":1047,"end":1056},"obj":"https://acgg.asia/db/ggdb/info/gg089"},{"id":"T9","span":{"begin":1301,"end":1310},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T10","span":{"begin":1403,"end":1412},"obj":"https://acgg.asia/db/ggdb/info/gg089"}],"text":"cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3.\nThe glycosylation of serine and threonine residues during mucin-type O-linked protein glycosylation is carried out by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferase). Previously two members, GalNAc-T1 and -T2, have been isolated and the genes cloned and characterized. Here we report the cDNA cloning and expression of a novel GalNAc-transferase termed GalNAc-T3. The gene was isolated and cloned based on the identification of a GalNAc-transferase motif (61 amino acids) that is shared between GalNAc-T1 and -T2 as well as a homologous Caenorhabditis elegans gene. The cDNA sequence has a 633-amino acid coding region indicating a protein of 72.5 kDa with a type II domain structure. The overall amino acid sequence similarity with GalNAc-T1 and -T2 is approximately 45%; 12 cysteine residues that are shared between GalNAc-T1 and -T2 are also found in GalNAc-T3. GalNAc-T3 was expressed as a soluble protein without the hydrophobic transmembrane domain in insect cells using a Baculo-virus vector, and the expressed GalNAc-transferase activity showed substrate specificity different from that previously reported for GalNAc-T1 and -T2. Northern analysis of human organs revealed a very restricted expression pattern of GalNAc-T3."}

{"project":"ggdb-test","denotations":[{"id":"T1","span":{"begin":128,"end":137},"obj":"https://acgg.asia/db/ggdb/info/gg089"},{"id":"T2","span":{"begin":373,"end":382},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T3","span":{"begin":535,"end":544},"obj":"https://acgg.asia/db/ggdb/info/gg089"},{"id":"T4","span":{"begin":677,"end":686},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T5","span":{"begin":915,"end":924},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T6","span":{"begin":1000,"end":1009},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T7","span":{"begin":1036,"end":1045},"obj":"https://acgg.asia/db/ggdb/info/gg089"},{"id":"T8","span":{"begin":1047,"end":1056},"obj":"https://acgg.asia/db/ggdb/info/gg089"},{"id":"T9","span":{"begin":1301,"end":1310},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"T10","span":{"begin":1403,"end":1412},"obj":"https://acgg.asia/db/ggdb/info/gg089"}],"text":"cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3.\nThe glycosylation of serine and threonine residues during mucin-type O-linked protein glycosylation is carried out by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferase). Previously two members, GalNAc-T1 and -T2, have been isolated and the genes cloned and characterized. Here we report the cDNA cloning and expression of a novel GalNAc-transferase termed GalNAc-T3. The gene was isolated and cloned based on the identification of a GalNAc-transferase motif (61 amino acids) that is shared between GalNAc-T1 and -T2 as well as a homologous Caenorhabditis elegans gene. The cDNA sequence has a 633-amino acid coding region indicating a protein of 72.5 kDa with a type II domain structure. The overall amino acid sequence similarity with GalNAc-T1 and -T2 is approximately 45%; 12 cysteine residues that are shared between GalNAc-T1 and -T2 are also found in GalNAc-T3. GalNAc-T3 was expressed as a soluble protein without the hydrophobic transmembrane domain in insect cells using a Baculo-virus vector, and the expressed GalNAc-transferase activity showed substrate specificity different from that previously reported for GalNAc-T1 and -T2. Northern analysis of human organs revealed a very restricted expression pattern of GalNAc-T3."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":80},"obj":"Sentence"},{"id":"T2","span":{"begin":81,"end":138},"obj":"Sentence"},{"id":"T3","span":{"begin":139,"end":348},"obj":"Sentence"},{"id":"T4","span":{"begin":349,"end":450},"obj":"Sentence"},{"id":"T5","span":{"begin":451,"end":545},"obj":"Sentence"},{"id":"T6","span":{"begin":546,"end":747},"obj":"Sentence"},{"id":"T7","span":{"begin":748,"end":866},"obj":"Sentence"},{"id":"T8","span":{"begin":867,"end":1046},"obj":"Sentence"},{"id":"T9","span":{"begin":1047,"end":1319},"obj":"Sentence"},{"id":"T10","span":{"begin":1320,"end":1413},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":80},"obj":"Sentence"},{"id":"T2","span":{"begin":81,"end":138},"obj":"Sentence"},{"id":"T3","span":{"begin":139,"end":348},"obj":"Sentence"},{"id":"T4","span":{"begin":349,"end":450},"obj":"Sentence"},{"id":"T5","span":{"begin":451,"end":545},"obj":"Sentence"},{"id":"T6","span":{"begin":546,"end":747},"obj":"Sentence"},{"id":"T7","span":{"begin":748,"end":866},"obj":"Sentence"},{"id":"T8","span":{"begin":867,"end":1046},"obj":"Sentence"},{"id":"T9","span":{"begin":1047,"end":1319},"obj":"Sentence"},{"id":"T10","span":{"begin":1320,"end":1413},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3.\nThe glycosylation of serine and threonine residues during mucin-type O-linked protein glycosylation is carried out by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferase). Previously two members, GalNAc-T1 and -T2, have been isolated and the genes cloned and characterized. Here we report the cDNA cloning and expression of a novel GalNAc-transferase termed GalNAc-T3. The gene was isolated and cloned based on the identification of a GalNAc-transferase motif (61 amino acids) that is shared between GalNAc-T1 and -T2 as well as a homologous Caenorhabditis elegans gene. The cDNA sequence has a 633-amino acid coding region indicating a protein of 72.5 kDa with a type II domain structure. The overall amino acid sequence similarity with GalNAc-T1 and -T2 is approximately 45%; 12 cysteine residues that are shared between GalNAc-T1 and -T2 are also found in GalNAc-T3. GalNAc-T3 was expressed as a soluble protein without the hydrophobic transmembrane domain in insect cells using a Baculo-virus vector, and the expressed GalNAc-transferase activity showed substrate specificity different from that previously reported for GalNAc-T1 and -T2. Northern analysis of human organs revealed a very restricted expression pattern of GalNAc-T3."}

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Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3.\nThe glycosylation of serine and threonine residues during mucin-type O-linked protein glycosylation is carried out by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferase). Previously two members, GalNAc-T1 and -T2, have been isolated and the genes cloned and characterized. Here we report the cDNA cloning and expression of a novel GalNAc-transferase termed GalNAc-T3. The gene was isolated and cloned based on the identification of a GalNAc-transferase motif (61 amino acids) that is shared between GalNAc-T1 and -T2 as well as a homologous Caenorhabditis elegans gene. The cDNA sequence has a 633-amino acid coding region indicating a protein of 72.5 kDa with a type II domain structure. The overall amino acid sequence similarity with GalNAc-T1 and -T2 is approximately 45%; 12 cysteine residues that are shared between GalNAc-T1 and -T2 are also found in GalNAc-T3. GalNAc-T3 was expressed as a soluble protein without the hydrophobic transmembrane domain in insect cells using a Baculo-virus vector, and the expressed GalNAc-transferase activity showed substrate specificity different from that previously reported for GalNAc-T1 and -T2. Northern analysis of human organs revealed a very restricted expression pattern of GalNAc-T3."}

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Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3.\nThe glycosylation of serine and threonine residues during mucin-type O-linked protein glycosylation is carried out by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferase). Previously two members, GalNAc-T1 and -T2, have been isolated and the genes cloned and characterized. Here we report the cDNA cloning and expression of a novel GalNAc-transferase termed GalNAc-T3. The gene was isolated and cloned based on the identification of a GalNAc-transferase motif (61 amino acids) that is shared between GalNAc-T1 and -T2 as well as a homologous Caenorhabditis elegans gene. The cDNA sequence has a 633-amino acid coding region indicating a protein of 72.5 kDa with a type II domain structure. The overall amino acid sequence similarity with GalNAc-T1 and -T2 is approximately 45%; 12 cysteine residues that are shared between GalNAc-T1 and -T2 are also found in GalNAc-T3. GalNAc-T3 was expressed as a soluble protein without the hydrophobic transmembrane domain in insect cells using a Baculo-virus vector, and the expressed GalNAc-transferase activity showed substrate specificity different from that previously reported for GalNAc-T1 and -T2. Northern analysis of human organs revealed a very restricted expression pattern of GalNAc-T3."}

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":39,"end":44},"obj":"Organism"},{"id":"T2","span":{"begin":719,"end":741},"obj":"Organism"},{"id":"T3","span":{"begin":1341,"end":1346},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"6239"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"}],"text":"cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3.\nThe glycosylation of serine and threonine residues during mucin-type O-linked protein glycosylation is carried out by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferase). Previously two members, GalNAc-T1 and -T2, have been isolated and the genes cloned and characterized. Here we report the cDNA cloning and expression of a novel GalNAc-transferase termed GalNAc-T3. The gene was isolated and cloned based on the identification of a GalNAc-transferase motif (61 amino acids) that is shared between GalNAc-T1 and -T2 as well as a homologous Caenorhabditis elegans gene. The cDNA sequence has a 633-amino acid coding region indicating a protein of 72.5 kDa with a type II domain structure. The overall amino acid sequence similarity with GalNAc-T1 and -T2 is approximately 45%; 12 cysteine residues that are shared between GalNAc-T1 and -T2 are also found in GalNAc-T3. GalNAc-T3 was expressed as a soluble protein without the hydrophobic transmembrane domain in insect cells using a Baculo-virus vector, and the expressed GalNAc-transferase activity showed substrate specificity different from that previously reported for GalNAc-T1 and -T2. Northern analysis of human organs revealed a very restricted expression pattern of GalNAc-T3."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":80},"obj":"Sentence"},{"id":"T2","span":{"begin":81,"end":138},"obj":"Sentence"},{"id":"T3","span":{"begin":139,"end":348},"obj":"Sentence"},{"id":"T4","span":{"begin":349,"end":450},"obj":"Sentence"},{"id":"T5","span":{"begin":451,"end":545},"obj":"Sentence"},{"id":"T6","span":{"begin":546,"end":747},"obj":"Sentence"},{"id":"T7","span":{"begin":748,"end":866},"obj":"Sentence"},{"id":"T8","span":{"begin":867,"end":1046},"obj":"Sentence"},{"id":"T9","span":{"begin":1047,"end":1319},"obj":"Sentence"},{"id":"T10","span":{"begin":1320,"end":1413},"obj":"Sentence"}],"text":"cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3.\nThe glycosylation of serine and threonine residues during mucin-type O-linked protein glycosylation is carried out by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferase). Previously two members, GalNAc-T1 and -T2, have been isolated and the genes cloned and characterized. Here we report the cDNA cloning and expression of a novel GalNAc-transferase termed GalNAc-T3. The gene was isolated and cloned based on the identification of a GalNAc-transferase motif (61 amino acids) that is shared between GalNAc-T1 and -T2 as well as a homologous Caenorhabditis elegans gene. The cDNA sequence has a 633-amino acid coding region indicating a protein of 72.5 kDa with a type II domain structure. The overall amino acid sequence similarity with GalNAc-T1 and -T2 is approximately 45%; 12 cysteine residues that are shared between GalNAc-T1 and -T2 are also found in GalNAc-T3. GalNAc-T3 was expressed as a soluble protein without the hydrophobic transmembrane domain in insect cells using a Baculo-virus vector, and the expressed GalNAc-transferase activity showed substrate specificity different from that previously reported for GalNAc-T1 and -T2. Northern analysis of human organs revealed a very restricted expression pattern of GalNAc-T3."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":39,"end":44},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":719,"end":741},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1341,"end":1346},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"6239"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"}],"text":"cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3.\nThe glycosylation of serine and threonine residues during mucin-type O-linked protein glycosylation is carried out by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferase). Previously two members, GalNAc-T1 and -T2, have been isolated and the genes cloned and characterized. Here we report the cDNA cloning and expression of a novel GalNAc-transferase termed GalNAc-T3. The gene was isolated and cloned based on the identification of a GalNAc-transferase motif (61 amino acids) that is shared between GalNAc-T1 and -T2 as well as a homologous Caenorhabditis elegans gene. The cDNA sequence has a 633-amino acid coding region indicating a protein of 72.5 kDa with a type II domain structure. The overall amino acid sequence similarity with GalNAc-T1 and -T2 is approximately 45%; 12 cysteine residues that are shared between GalNAc-T1 and -T2 are also found in GalNAc-T3. GalNAc-T3 was expressed as a soluble protein without the hydrophobic transmembrane domain in insect cells using a Baculo-virus vector, and the expressed GalNAc-transferase activity showed substrate specificity different from that previously reported for GalNAc-T1 and -T2. Northern analysis of human organs revealed a very restricted expression pattern of GalNAc-T3."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":1116,"end":1129},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0016020"}],"text":"cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3.\nThe glycosylation of serine and threonine residues during mucin-type O-linked protein glycosylation is carried out by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferase). Previously two members, GalNAc-T1 and -T2, have been isolated and the genes cloned and characterized. Here we report the cDNA cloning and expression of a novel GalNAc-transferase termed GalNAc-T3. The gene was isolated and cloned based on the identification of a GalNAc-transferase motif (61 amino acids) that is shared between GalNAc-T1 and -T2 as well as a homologous Caenorhabditis elegans gene. The cDNA sequence has a 633-amino acid coding region indicating a protein of 72.5 kDa with a type II domain structure. The overall amino acid sequence similarity with GalNAc-T1 and -T2 is approximately 45%; 12 cysteine residues that are shared between GalNAc-T1 and -T2 are also found in GalNAc-T3. GalNAc-T3 was expressed as a soluble protein without the hydrophobic transmembrane domain in insect cells using a Baculo-virus vector, and the expressed GalNAc-transferase activity showed substrate specificity different from that previously reported for GalNAc-T1 and -T2. Northern analysis of human organs revealed a very restricted expression pattern of GalNAc-T3."}