PubMed:9592121 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":78,"end":99},"obj":"https://glytoucan.org/Structures/Glycans/G27025MB"},{"id":"T2","span":{"begin":183,"end":205},"obj":"https://glytoucan.org/Structures/Glycans/G27025MB"}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":78,"end":99},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":183,"end":205},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G27025MB"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G27025MB"}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":78,"end":99},"obj":"https://glytoucan.org/Structures/Glycans/G27025MB"},{"id":"T2","span":{"begin":183,"end":205},"obj":"https://glytoucan.org/Structures/Glycans/G27025MB"}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":0,"end":7},"obj":"FMAID:198062"},{"id":"_T2","span":{"begin":0,"end":7},"obj":"FMAID:84116"},{"id":"_T3","span":{"begin":8,"end":20},"obj":"FMAID:166081"},{"id":"_T4","span":{"begin":8,"end":20},"obj":"FMAID:67498"},{"id":"_T5","span":{"begin":25,"end":36},"obj":"FMAID:67093"},{"id":"_T6","span":{"begin":25,"end":36},"obj":"FMAID:165175"},{"id":"_T7","span":{"begin":25,"end":36},"obj":"FMAID:226764"},{"id":"_T8","span":{"begin":25,"end":36},"obj":"FMAID:197979"},{"id":"_T9","span":{"begin":25,"end":36},"obj":"FMAID:84056"},{"id":"_T10","span":{"begin":25,"end":36},"obj":"FMAID:84055"},{"id":"_T11","span":{"begin":25,"end":36},"obj":"FMAID:197978"},{"id":"_T12","span":{"begin":78,"end":99},"obj":"FMAID:82786"},{"id":"_T13","span":{"begin":78,"end":99},"obj":"FMAID:196780"},{"id":"_T14","span":{"begin":183,"end":205},"obj":"FMAID:196780"},{"id":"_T15","span":{"begin":183,"end":205},"obj":"FMAID:82786"},{"id":"_T16","span":{"begin":336,"end":346},"obj":"FMAID:196728"},{"id":"_T17","span":{"begin":336,"end":346},"obj":"FMAID:82739"},{"id":"_T18","span":{"begin":394,"end":406},"obj":"FMAID:108656"},{"id":"_T19","span":{"begin":394,"end":406},"obj":"FMAID:17537"},{"id":"_T20","span":{"begin":398,"end":406},"obj":"FMAID:256633"},{"id":"_T21","span":{"begin":398,"end":406},"obj":"FMAID:256627"},{"id":"_T22","span":{"begin":398,"end":406},"obj":"FMAID:256626"},{"id":"_T23","span":{"begin":398,"end":406},"obj":"FMAID:256632"},{"id":"_T24","span":{"begin":398,"end":406},"obj":"FMAID:256628"},{"id":"_T25","span":{"begin":398,"end":406},"obj":"FMAID:256630"},{"id":"_T26","span":{"begin":398,"end":406},"obj":"FMAID:256629"},{"id":"_T27","span":{"begin":398,"end":406},"obj":"FMAID:256625"},{"id":"_T28","span":{"begin":398,"end":406},"obj":"FMAID:256624"},{"id":"_T29","span":{"begin":398,"end":406},"obj":"FMAID:99729"},{"id":"_T30","span":{"begin":398,"end":406},"obj":"FMAID:11367"},{"id":"_T31","span":{"begin":398,"end":406},"obj":"FMAID:256631"},{"id":"_T32","span":{"begin":528,"end":535},"obj":"FMAID:198062"},{"id":"_T33","span":{"begin":528,"end":535},"obj":"FMAID:84116"},{"id":"_T34","span":{"begin":536,"end":548},"obj":"FMAID:67498"},{"id":"_T35","span":{"begin":536,"end":548},"obj":"FMAID:166081"},{"id":"_T36","span":{"begin":599,"end":604},"obj":"FMAID:198663"},{"id":"_T37","span":{"begin":626,"end":637},"obj":"FMAID:84055"},{"id":"_T38","span":{"begin":626,"end":637},"obj":"FMAID:84056"},{"id":"_T39","span":{"begin":626,"end":637},"obj":"FMAID:197979"},{"id":"_T40","span":{"begin":626,"end":637},"obj":"FMAID:226764"},{"id":"_T41","span":{"begin":626,"end":637},"obj":"FMAID:165175"},{"id":"_T42","span":{"begin":626,"end":637},"obj":"FMAID:197978"},{"id":"_T43","span":{"begin":626,"end":637},"obj":"FMAID:67093"},{"id":"_T44","span":{"begin":684,"end":686},"obj":"FMAID:63504"},{"id":"_T45","span":{"begin":684,"end":686},"obj":"FMAID:167732"},{"id":"_T46","span":{"begin":694,"end":696},"obj":"FMAID:167733"},{"id":"_T47","span":{"begin":694,"end":696},"obj":"FMAID:63505"},{"id":"_T48","span":{"begin":731,"end":736},"obj":"FMAID:84120"},{"id":"_T49","span":{"begin":731,"end":736},"obj":"FMAID:198073"},{"id":"_T50","span":{"begin":760,"end":766},"obj":"FMAID:84121"},{"id":"_T51","span":{"begin":760,"end":766},"obj":"FMAID:198075"},{"id":"_T52","span":{"begin":767,"end":771},"obj":"FMAID:198073"},{"id":"_T53","span":{"begin":767,"end":771},"obj":"FMAID:84120"},{"id":"_T54","span":{"begin":815,"end":820},"obj":"FMAID:198663"},{"id":"_T55","span":{"begin":902,"end":906},"obj":"FMAID:198663"},{"id":"_T56","span":{"begin":965,"end":967},"obj":"FMAID:167732"},{"id":"_T57","span":{"begin":965,"end":967},"obj":"FMAID:63504"},{"id":"_T58","span":{"begin":975,"end":977},"obj":"FMAID:63505"},{"id":"_T59","span":{"begin":975,"end":977},"obj":"FMAID:167733"},{"id":"_T60","span":{"begin":995,"end":1006},"obj":"FMAID:226764"},{"id":"_T61","span":{"begin":995,"end":1006},"obj":"FMAID:197978"},{"id":"_T62","span":{"begin":995,"end":1006},"obj":"FMAID:84055"},{"id":"_T63","span":{"begin":995,"end":1006},"obj":"FMAID:165175"},{"id":"_T64","span":{"begin":995,"end":1006},"obj":"FMAID:197979"},{"id":"_T65","span":{"begin":995,"end":1006},"obj":"FMAID:67093"},{"id":"_T66","span":{"begin":995,"end":1006},"obj":"FMAID:84056"},{"id":"_T67","span":{"begin":1192,"end":1196},"obj":"FMAID:198663"},{"id":"_T68","span":{"begin":1205,"end":1209},"obj":"FMAID:198663"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":263,"end":275},"obj":"http://www.uniprot.org/uniprot/Q99484"},{"id":"T2","span":{"begin":309,"end":321},"obj":"http://www.uniprot.org/uniprot/Q99484"},{"id":"T3","span":{"begin":587,"end":598},"obj":"http://www.uniprot.org/uniprot/Q99484"},{"id":"T4","span":{"begin":890,"end":901},"obj":"http://www.uniprot.org/uniprot/Q99484"},{"id":"T5","span":{"begin":1121,"end":1132},"obj":"http://www.uniprot.org/uniprot/Q99484"},{"id":"T6","span":{"begin":674,"end":680},"obj":"http://www.uniprot.org/uniprot/Q10472"},{"id":"T7","span":{"begin":955,"end":961},"obj":"http://www.uniprot.org/uniprot/Q10472"},{"id":"T8","span":{"begin":684,"end":686},"obj":"http://www.uniprot.org/uniprot/P24752"},{"id":"T9","span":{"begin":965,"end":967},"obj":"http://www.uniprot.org/uniprot/P24752"}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":263,"end":275},"obj":"http://www.uniprot.org/uniprot/P38649"},{"id":"T2","span":{"begin":309,"end":321},"obj":"http://www.uniprot.org/uniprot/P38649"},{"id":"T3","span":{"begin":587,"end":598},"obj":"http://www.uniprot.org/uniprot/P38649"},{"id":"T4","span":{"begin":890,"end":901},"obj":"http://www.uniprot.org/uniprot/P38649"},{"id":"T5","span":{"begin":1121,"end":1132},"obj":"http://www.uniprot.org/uniprot/P38649"},{"id":"T6","span":{"begin":684,"end":686},"obj":"http://www.uniprot.org/uniprot/Q06666"},{"id":"T7","span":{"begin":965,"end":967},"obj":"http://www.uniprot.org/uniprot/Q06666"}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":336,"end":355},"obj":"http://purl.bioontology.org/ontology/STY/T087"}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":154},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":155,"end":302},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":303,"end":496},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":497,"end":651},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":652,"end":751},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":752,"end":821},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":822,"end":907},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":908,"end":1055},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1056,"end":1222},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":154},"obj":"Sentence"},{"id":"T2","span":{"begin":155,"end":302},"obj":"Sentence"},{"id":"T3","span":{"begin":303,"end":496},"obj":"Sentence"},{"id":"T4","span":{"begin":497,"end":651},"obj":"Sentence"},{"id":"T5","span":{"begin":652,"end":751},"obj":"Sentence"},{"id":"T6","span":{"begin":752,"end":821},"obj":"Sentence"},{"id":"T7","span":{"begin":822,"end":907},"obj":"Sentence"},{"id":"T8","span":{"begin":908,"end":1055},"obj":"Sentence"},{"id":"T9","span":{"begin":1056,"end":1222},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":154},"obj":"Sentence"},{"id":"T2","span":{"begin":155,"end":302},"obj":"Sentence"},{"id":"T3","span":{"begin":303,"end":496},"obj":"Sentence"},{"id":"T4","span":{"begin":497,"end":651},"obj":"Sentence"},{"id":"T5","span":{"begin":652,"end":751},"obj":"Sentence"},{"id":"T6","span":{"begin":752,"end":821},"obj":"Sentence"},{"id":"T7","span":{"begin":822,"end":907},"obj":"Sentence"},{"id":"T8","span":{"begin":908,"end":1055},"obj":"Sentence"},{"id":"T9","span":{"begin":1056,"end":1222},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":8,"end":36},"obj":"http://purl.obolibrary.org/obo/GO_0051276"},{"id":"T2","span":{"begin":25,"end":49},"obj":"http://purl.obolibrary.org/obo/GO_0050000"},{"id":"T3","span":{"begin":626,"end":650},"obj":"http://purl.obolibrary.org/obo/GO_0050000"},{"id":"T4","span":{"begin":982,"end":1006},"obj":"http://purl.obolibrary.org/obo/GO_0050000"},{"id":"T5","span":{"begin":37,"end":49},"obj":"http://purl.obolibrary.org/obo/GO_0051179"},{"id":"T6","span":{"begin":638,"end":650},"obj":"http://purl.obolibrary.org/obo/GO_0051179"},{"id":"T7","span":{"begin":982,"end":991},"obj":"http://purl.obolibrary.org/obo/GO_0051179"},{"id":"T8","span":{"begin":207,"end":254},"obj":"http://purl.obolibrary.org/obo/GO_0004653"},{"id":"T9","span":{"begin":288,"end":301},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T10","span":{"begin":398,"end":406},"obj":"http://purl.obolibrary.org/obo/GO_0035282"}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":25,"end":36},"obj":"http://purl.obolibrary.org/obo/GO_0005694"},{"id":"T2","span":{"begin":626,"end":637},"obj":"http://purl.obolibrary.org/obo/GO_0005694"},{"id":"T3","span":{"begin":995,"end":1006},"obj":"http://purl.obolibrary.org/obo/GO_0005694"}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G23425WZ\""},{"id":"GlycanIUPAC_T2","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G23425WZ\""},{"id":"GlycanIUPAC_T3","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G23425WZ\""},{"id":"GlycanIUPAC_T4","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G23425WZ\""},{"id":"GlycanIUPAC_T5","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G02874VH\""},{"id":"GlycanIUPAC_T6","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G02874VH\""},{"id":"GlycanIUPAC_T7","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G02874VH\""},{"id":"GlycanIUPAC_T8","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G02874VH\""},{"id":"GlycanIUPAC_T9","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G99699DW\""},{"id":"GlycanIUPAC_T10","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G99699DW\""},{"id":"GlycanIUPAC_T11","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G99699DW\""},{"id":"GlycanIUPAC_T12","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G99699DW\""},{"id":"GlycanIUPAC_T13","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G22074RM\""},{"id":"GlycanIUPAC_T14","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G22074RM\""},{"id":"GlycanIUPAC_T15","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G22074RM\""},{"id":"GlycanIUPAC_T16","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G22074RM\""},{"id":"GlycanIUPAC_T17","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G48535VZ\""},{"id":"GlycanIUPAC_T18","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G48535VZ\""},{"id":"GlycanIUPAC_T19","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G48535VZ\""},{"id":"GlycanIUPAC_T20","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G48535VZ\""},{"id":"GlycanIUPAC_T21","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G39738WL\""},{"id":"GlycanIUPAC_T22","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G39738WL\""},{"id":"GlycanIUPAC_T23","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G39738WL\""},{"id":"GlycanIUPAC_T24","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G39738WL\""},{"id":"GlycanIUPAC_T25","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G42313WU\""},{"id":"GlycanIUPAC_T26","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G42313WU\""},{"id":"GlycanIUPAC_T27","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G42313WU\""},{"id":"GlycanIUPAC_T28","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G42313WU\""},{"id":"GlycanIUPAC_T29","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G00393CK\""},{"id":"GlycanIUPAC_T30","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G00393CK\""},{"id":"GlycanIUPAC_T31","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G00393CK\""},{"id":"GlycanIUPAC_T32","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G00393CK\""},{"id":"GlycanIUPAC_T33","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G42649EX\""},{"id":"GlycanIUPAC_T34","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G42649EX\""},{"id":"GlycanIUPAC_T35","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G42649EX\""},{"id":"GlycanIUPAC_T36","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G42649EX\""},{"id":"GlycanIUPAC_T37","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G46880SB\""},{"id":"GlycanIUPAC_T38","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G46880SB\""},{"id":"GlycanIUPAC_T39","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G46880SB\""},{"id":"GlycanIUPAC_T40","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G46880SB\""},{"id":"GlycanIUPAC_T41","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G75599IR\""},{"id":"GlycanIUPAC_T42","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G75599IR\""},{"id":"GlycanIUPAC_T43","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G75599IR\""},{"id":"GlycanIUPAC_T44","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G75599IR\""},{"id":"GlycanIUPAC_T45","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G58985MU\""},{"id":"GlycanIUPAC_T46","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G58985MU\""},{"id":"GlycanIUPAC_T47","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G58985MU\""},{"id":"GlycanIUPAC_T48","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G58985MU\""},{"id":"GlycanIUPAC_T49","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G92517PO\""},{"id":"GlycanIUPAC_T50","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G92517PO\""},{"id":"GlycanIUPAC_T51","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G92517PO\""},{"id":"GlycanIUPAC_T52","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G92517PO\""},{"id":"GlycanIUPAC_T53","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G88512YL\""},{"id":"GlycanIUPAC_T54","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G88512YL\""},{"id":"GlycanIUPAC_T55","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G88512YL\""},{"id":"GlycanIUPAC_T56","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G88512YL\""},{"id":"GlycanIUPAC_T57","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G41473NX\""},{"id":"GlycanIUPAC_T58","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G41473NX\""},{"id":"GlycanIUPAC_T59","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G41473NX\""},{"id":"GlycanIUPAC_T60","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G41473NX\""},{"id":"GlycanIUPAC_T61","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G71089RB\""},{"id":"GlycanIUPAC_T62","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G71089RB\""},{"id":"GlycanIUPAC_T63","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G71089RB\""},{"id":"GlycanIUPAC_T64","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G71089RB\""},{"id":"GlycanIUPAC_T65","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G73485GZ\""},{"id":"GlycanIUPAC_T66","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G73485GZ\""},{"id":"GlycanIUPAC_T67","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G73485GZ\""},{"id":"GlycanIUPAC_T68","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G73485GZ\""},{"id":"GlycanIUPAC_T69","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G61406KC\""},{"id":"GlycanIUPAC_T70","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G61406KC\""},{"id":"GlycanIUPAC_T71","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G61406KC\""},{"id":"GlycanIUPAC_T72","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G61406KC\""},{"id":"GlycanIUPAC_T73","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G34412GZ\""},{"id":"GlycanIUPAC_T74","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G34412GZ\""},{"id":"GlycanIUPAC_T75","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G34412GZ\""},{"id":"GlycanIUPAC_T76","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G34412GZ\""},{"id":"GlycanIUPAC_T77","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G67209FP\""},{"id":"GlycanIUPAC_T78","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G67209FP\""},{"id":"GlycanIUPAC_T79","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G67209FP\""},{"id":"GlycanIUPAC_T80","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G67209FP\""},{"id":"GlycanIUPAC_T81","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G61442IL\""},{"id":"GlycanIUPAC_T82","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G61442IL\""},{"id":"GlycanIUPAC_T83","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G61442IL\""},{"id":"GlycanIUPAC_T84","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G61442IL\""},{"id":"GlycanIUPAC_T85","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G93729MV\""},{"id":"GlycanIUPAC_T86","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G93729MV\""},{"id":"GlycanIUPAC_T87","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G93729MV\""},{"id":"GlycanIUPAC_T88","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G93729MV\""},{"id":"GlycanIUPAC_T89","span":{"begin":256,"end":262},"obj":"\"http://rdf.glycoinfo.org/glycan/G92144AE\""},{"id":"GlycanIUPAC_T90","span":{"begin":580,"end":586},"obj":"\"http://rdf.glycoinfo.org/glycan/G92144AE\""},{"id":"GlycanIUPAC_T91","span":{"begin":883,"end":889},"obj":"\"http://rdf.glycoinfo.org/glycan/G92144AE\""},{"id":"GlycanIUPAC_T92","span":{"begin":1114,"end":1120},"obj":"\"http://rdf.glycoinfo.org/glycan/G92144AE\""}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":8,"end":20},"obj":"http://purl.obolibrary.org/obo/UBERON_0000062"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":536,"end":548},"obj":"http://purl.obolibrary.org/obo/UBERON_0000062"}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":256,"end":262},"obj":"Glycan"},{"id":"T2","span":{"begin":580,"end":586},"obj":"Glycan"},{"id":"T3","span":{"begin":883,"end":889},"obj":"Glycan"},{"id":"T4","span":{"begin":1114,"end":1120},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A5","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":"A6","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":"A7","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":"A8","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":256,"end":262},"obj":"Glycan"},{"id":"T2","span":{"begin":580,"end":586},"obj":"Glycan"},{"id":"T3","span":{"begin":883,"end":889},"obj":"Glycan"},{"id":"T4","span":{"begin":1114,"end":1120},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A5","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":"A6","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":"A7","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":"A8","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":398,"end":406},"obj":"Body_part"},{"id":"T2","span":{"begin":995,"end":1006},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000914"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/GO_0005694"}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":154},"obj":"Sentence"},{"id":"T2","span":{"begin":155,"end":302},"obj":"Sentence"},{"id":"T3","span":{"begin":303,"end":496},"obj":"Sentence"},{"id":"T4","span":{"begin":497,"end":651},"obj":"Sentence"},{"id":"T5","span":{"begin":652,"end":751},"obj":"Sentence"},{"id":"T6","span":{"begin":752,"end":821},"obj":"Sentence"},{"id":"T7","span":{"begin":822,"end":907},"obj":"Sentence"},{"id":"T8","span":{"begin":908,"end":1055},"obj":"Sentence"},{"id":"T9","span":{"begin":1056,"end":1222},"obj":"Sentence"}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":25,"end":36},"obj":"Body_part"},{"id":"T2","span":{"begin":626,"end":637},"obj":"Body_part"},{"id":"T3","span":{"begin":995,"end":1006},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:67093"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:67093"},{"id":"A3","pred":"db_id","subj":"T3","obj":"FMA:67093"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":398,"end":406},"obj":"Body_part"},{"id":"T2","span":{"begin":995,"end":1006},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000914"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/GO_0005694"}],"text":"Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.\nA homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here we have characterized the genomic organization of the coding regions of three GalNAc-transferase genes and determined their chromosomal localization. The coding regions of GALNT1 , -T2 , and -T3 were found to span 11, 16, and 10 exons, respectively. Several intron/exon boundaries were conserved within the three genes. One conserved boundary was shared in a homologous C. elegans GalNAc-transferase gene. Fluorescence in situ hybridization showed that GALNT1 , -T2 , and -T3 are localized at chromosomes 18q12-q21, 1q41-q42, and 2q24-q31, respectively. These results suggest that the members of the polypeptide GalNAc-transferase family diverged early in evolution from a common ancestral gene through gene duplication."}