PubMed:1498423 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":698,"end":709},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T2","span":{"begin":1474,"end":1485},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":698,"end":709},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":1474,"end":1485},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":98},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":99,"end":230},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":231,"end":348},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":349,"end":471},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":472,"end":648},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":649,"end":761},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":762,"end":896},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":897,"end":1056},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1057,"end":1247},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1248,"end":1410},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1411,"end":1527},"obj":"Sentence"},{"id":"TextSentencer_T12","span":{"begin":1528,"end":1794},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":98},"obj":"Sentence"},{"id":"T2","span":{"begin":99,"end":230},"obj":"Sentence"},{"id":"T3","span":{"begin":231,"end":348},"obj":"Sentence"},{"id":"T4","span":{"begin":349,"end":471},"obj":"Sentence"},{"id":"T5","span":{"begin":472,"end":648},"obj":"Sentence"},{"id":"T6","span":{"begin":649,"end":761},"obj":"Sentence"},{"id":"T7","span":{"begin":762,"end":896},"obj":"Sentence"},{"id":"T8","span":{"begin":897,"end":1056},"obj":"Sentence"},{"id":"T9","span":{"begin":1057,"end":1247},"obj":"Sentence"},{"id":"T10","span":{"begin":1248,"end":1410},"obj":"Sentence"},{"id":"T11","span":{"begin":1411,"end":1527},"obj":"Sentence"},{"id":"T12","span":{"begin":1528,"end":1794},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":98},"obj":"Sentence"},{"id":"T2","span":{"begin":99,"end":230},"obj":"Sentence"},{"id":"T3","span":{"begin":231,"end":348},"obj":"Sentence"},{"id":"T4","span":{"begin":349,"end":471},"obj":"Sentence"},{"id":"T5","span":{"begin":472,"end":648},"obj":"Sentence"},{"id":"T6","span":{"begin":649,"end":761},"obj":"Sentence"},{"id":"T7","span":{"begin":762,"end":896},"obj":"Sentence"},{"id":"T8","span":{"begin":897,"end":1056},"obj":"Sentence"},{"id":"T9","span":{"begin":1057,"end":1247},"obj":"Sentence"},{"id":"T10","span":{"begin":1248,"end":1410},"obj":"Sentence"},{"id":"T11","span":{"begin":1411,"end":1527},"obj":"Sentence"},{"id":"T12","span":{"begin":1528,"end":1794},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":698,"end":709},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T2","span":{"begin":1474,"end":1485},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":12,"end":18},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T2","span":{"begin":290,"end":296},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T3","span":{"begin":889,"end":895},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T4","span":{"begin":1592,"end":1598},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T5","span":{"begin":1738,"end":1744},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":12,"end":18},"obj":"FMAID:7203"},{"id":"_T2","span":{"begin":12,"end":18},"obj":"FMAID:93681"},{"id":"_T3","span":{"begin":19,"end":24},"obj":"FMAID:199098"},{"id":"_T4","span":{"begin":93,"end":97},"obj":"FMAID:198663"},{"id":"_T5","span":{"begin":222,"end":229},"obj":"FMAID:256050"},{"id":"_T6","span":{"begin":267,"end":272},"obj":"FMAID:199098"},{"id":"_T7","span":{"begin":290,"end":296},"obj":"FMAID:93681"},{"id":"_T8","span":{"begin":290,"end":296},"obj":"FMAID:7203"},{"id":"_T9","span":{"begin":503,"end":508},"obj":"FMAID:7209"},{"id":"_T10","span":{"begin":503,"end":508},"obj":"FMAID:93687"},{"id":"_T11","span":{"begin":515,"end":520},"obj":"FMAID:169002"},{"id":"_T12","span":{"begin":515,"end":520},"obj":"FMAID:68646"},{"id":"_T13","span":{"begin":587,"end":595},"obj":"FMAID:167180"},{"id":"_T14","span":{"begin":675,"end":687},"obj":"FMAID:200942"},{"id":"_T15","span":{"begin":675,"end":687},"obj":"FMAID:212684"},{"id":"_T16","span":{"begin":680,"end":687},"obj":"FMAID:50594"},{"id":"_T17","span":{"begin":680,"end":687},"obj":"FMAID:146300"},{"id":"_T18","span":{"begin":772,"end":777},"obj":"FMAID:199098"},{"id":"_T19","span":{"begin":889,"end":895},"obj":"FMAID:93681"},{"id":"_T20","span":{"begin":889,"end":895},"obj":"FMAID:7203"},{"id":"_T21","span":{"begin":999,"end":1010},"obj":"FMAID:82739"},{"id":"_T22","span":{"begin":999,"end":1010},"obj":"FMAID:196728"},{"id":"_T23","span":{"begin":1066,"end":1073},"obj":"FMAID:82757"},{"id":"_T24","span":{"begin":1066,"end":1073},"obj":"FMAID:196746"},{"id":"_T25","span":{"begin":1225,"end":1237},"obj":"FMAID:200942"},{"id":"_T26","span":{"begin":1225,"end":1237},"obj":"FMAID:212684"},{"id":"_T27","span":{"begin":1230,"end":1237},"obj":"FMAID:146300"},{"id":"_T28","span":{"begin":1230,"end":1237},"obj":"FMAID:50594"},{"id":"_T29","span":{"begin":1238,"end":1246},"obj":"FMAID:165447"},{"id":"_T30","span":{"begin":1238,"end":1246},"obj":"FMAID:67257"},{"id":"_T31","span":{"begin":1267,"end":1272},"obj":"FMAID:68646"},{"id":"_T32","span":{"begin":1267,"end":1272},"obj":"FMAID:169002"},{"id":"_T33","span":{"begin":1396,"end":1403},"obj":"FMAID:165447"},{"id":"_T34","span":{"begin":1396,"end":1403},"obj":"FMAID:67257"},{"id":"_T35","span":{"begin":1498,"end":1510},"obj":"FMAID:212684"},{"id":"_T36","span":{"begin":1498,"end":1510},"obj":"FMAID:200942"},{"id":"_T37","span":{"begin":1503,"end":1510},"obj":"FMAID:146300"},{"id":"_T38","span":{"begin":1503,"end":1510},"obj":"FMAID:50594"},{"id":"_T39","span":{"begin":1511,"end":1526},"obj":"FMAID:82782"},{"id":"_T40","span":{"begin":1511,"end":1526},"obj":"FMAID:196776"},{"id":"_T41","span":{"begin":1579,"end":1584},"obj":"FMAID:199098"},{"id":"_T42","span":{"begin":1592,"end":1598},"obj":"FMAID:93681"},{"id":"_T43","span":{"begin":1592,"end":1598},"obj":"FMAID:7203"},{"id":"_T44","span":{"begin":1600,"end":1607},"obj":"FMAID:67257"},{"id":"_T45","span":{"begin":1600,"end":1607},"obj":"FMAID:165447"},{"id":"_T46","span":{"begin":1629,"end":1635},"obj":"FMAID:256050"},{"id":"_T47","span":{"begin":1688,"end":1695},"obj":"FMAID:165447"},{"id":"_T48","span":{"begin":1688,"end":1695},"obj":"FMAID:67257"},{"id":"_T49","span":{"begin":1738,"end":1744},"obj":"FMAID:93681"},{"id":"_T50","span":{"begin":1738,"end":1744},"obj":"FMAID:7203"},{"id":"_T51","span":{"begin":1785,"end":1793},"obj":"FMAID:165447"},{"id":"_T52","span":{"begin":1785,"end":1793},"obj":"FMAID:67257"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":48,"end":52},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T2","span":{"begin":48,"end":52},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T3","span":{"begin":99,"end":103},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T4","span":{"begin":99,"end":103},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T5","span":{"begin":222,"end":229},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T6","span":{"begin":515,"end":520},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T7","span":{"begin":1200,"end":1210},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/2759"},{"id":"T8","span":{"begin":1267,"end":1272},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T9","span":{"begin":1629,"end":1635},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T10","span":{"begin":1701,"end":1703},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/13893"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":145,"end":149},"obj":"http://purl.obolibrary.org/obo/GO_0008118"},{"id":"T2","span":{"begin":260,"end":264},"obj":"http://purl.obolibrary.org/obo/GO_0008118"},{"id":"T3","span":{"begin":329,"end":333},"obj":"http://purl.obolibrary.org/obo/GO_0008118"},{"id":"T4","span":{"begin":464,"end":468},"obj":"http://purl.obolibrary.org/obo/GO_0008118"},{"id":"T5","span":{"begin":580,"end":584},"obj":"http://purl.obolibrary.org/obo/GO_0008118"},{"id":"T6","span":{"begin":863,"end":867},"obj":"http://purl.obolibrary.org/obo/GO_0008118"},{"id":"T7","span":{"begin":1389,"end":1393},"obj":"http://purl.obolibrary.org/obo/GO_0008118"},{"id":"T8","span":{"begin":1572,"end":1576},"obj":"http://purl.obolibrary.org/obo/GO_0008118"},{"id":"T9","span":{"begin":1726,"end":1730},"obj":"http://purl.obolibrary.org/obo/GO_0008118"},{"id":"T10","span":{"begin":1778,"end":1782},"obj":"http://purl.obolibrary.org/obo/GO_0008118"},{"id":"T11","span":{"begin":336,"end":347},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T12","span":{"begin":386,"end":396},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T13","span":{"begin":510,"end":513},"obj":"http://purl.obolibrary.org/obo/GO_0043848"},{"id":"T14","span":{"begin":1263,"end":1266},"obj":"http://purl.obolibrary.org/obo/GO_0043848"},{"id":"T15","span":{"begin":629,"end":647},"obj":"http://purl.obolibrary.org/obo/GO_0051645"},{"id":"T16","span":{"begin":635,"end":647},"obj":"http://purl.obolibrary.org/obo/GO_0051179"},{"id":"T17","span":{"begin":1175,"end":1181},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T18","span":{"begin":1225,"end":1246},"obj":"http://purl.obolibrary.org/obo/GO_0034394"},{"id":"T19","span":{"begin":1225,"end":1246},"obj":"http://purl.obolibrary.org/obo/GO_0033575"},{"id":"T20","span":{"begin":1225,"end":1246},"obj":"http://purl.obolibrary.org/obo/GO_0033580"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":587,"end":595},"obj":"http://purl.obolibrary.org/obo/GO_0003823"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":515,"end":520},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":675,"end":679},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":1225,"end":1229},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":1498,"end":1502},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":629,"end":634},"obj":"http://purl.obolibrary.org/obo/GO_0005794"},{"id":"T6","span":{"begin":1372,"end":1377},"obj":"http://purl.obolibrary.org/obo/GO_0005794"},{"id":"T7","span":{"begin":675,"end":687},"obj":"http://purl.obolibrary.org/obo/GO_0009986"},{"id":"T8","span":{"begin":1225,"end":1237},"obj":"http://purl.obolibrary.org/obo/GO_0009986"},{"id":"T9","span":{"begin":1498,"end":1510},"obj":"http://purl.obolibrary.org/obo/GO_0009986"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":12,"end":18},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"T2","span":{"begin":290,"end":296},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"T3","span":{"begin":889,"end":895},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"T4","span":{"begin":1592,"end":1598},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"T5","span":{"begin":1738,"end":1744},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"T6","span":{"begin":222,"end":229},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"T7","span":{"begin":1629,"end":1635},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":19,"end":24},"obj":"http://edamontology.org/topic_3512"},{"id":"T2","span":{"begin":267,"end":272},"obj":"http://edamontology.org/topic_3512"},{"id":"T3","span":{"begin":336,"end":347},"obj":"http://edamontology.org/topic_0110"},{"id":"T4","span":{"begin":336,"end":347},"obj":"http://edamontology.org/topic_0203"},{"id":"T5","span":{"begin":336,"end":347},"obj":"http://edamontology.org/topic_3308"},{"id":"T6","span":{"begin":336,"end":347},"obj":"http://edamontology.org/topic_3512"},{"id":"T7","span":{"begin":386,"end":396},"obj":"http://edamontology.org/topic_3512"},{"id":"T8","span":{"begin":386,"end":396},"obj":"http://edamontology.org/topic_3308"},{"id":"T9","span":{"begin":386,"end":396},"obj":"http://edamontology.org/topic_0203"},{"id":"T10","span":{"begin":386,"end":396},"obj":"http://edamontology.org/topic_0110"},{"id":"T11","span":{"begin":710,"end":718},"obj":"http://edamontology.org/topic_0102"},{"id":"T12","span":{"begin":772,"end":777},"obj":"http://edamontology.org/topic_3512"},{"id":"T13","span":{"begin":870,"end":881},"obj":"http://edamontology.org/topic_0110"},{"id":"T14","span":{"begin":870,"end":881},"obj":"http://edamontology.org/topic_0203"},{"id":"T15","span":{"begin":870,"end":881},"obj":"http://edamontology.org/topic_3308"},{"id":"T16","span":{"begin":870,"end":881},"obj":"http://edamontology.org/topic_3512"},{"id":"T17","span":{"begin":961,"end":969},"obj":"http://edamontology.org/topic_0749"},{"id":"T18","span":{"begin":999,"end":1010},"obj":"http://edamontology.org/topic_0154"},{"id":"T19","span":{"begin":1026,"end":1034},"obj":"http://edamontology.org/topic_0749"},{"id":"T20","span":{"begin":1035,"end":1043},"obj":"http://edamontology.org/topic_3168"},{"id":"T21","span":{"begin":1035,"end":1043},"obj":"http://edamontology.org/topic_0080"},{"id":"T22","span":{"begin":1079,"end":1086},"obj":"http://edamontology.org/topic_0154"},{"id":"T23","span":{"begin":1138,"end":1146},"obj":"http://edamontology.org/topic_0080"},{"id":"T24","span":{"begin":1138,"end":1146},"obj":"http://edamontology.org/topic_3168"},{"id":"T25","span":{"begin":1200,"end":1210},"obj":"http://edamontology.org/topic_2818"},{"id":"T26","span":{"begin":1238,"end":1246},"obj":"http://edamontology.org/topic_0078"},{"id":"T27","span":{"begin":1396,"end":1403},"obj":"http://edamontology.org/topic_0078"},{"id":"T28","span":{"begin":1486,"end":1494},"obj":"http://edamontology.org/topic_0102"},{"id":"T29","span":{"begin":1579,"end":1584},"obj":"http://edamontology.org/topic_3512"},{"id":"T30","span":{"begin":1600,"end":1607},"obj":"http://edamontology.org/topic_0078"},{"id":"T31","span":{"begin":1688,"end":1695},"obj":"http://edamontology.org/topic_0078"},{"id":"T32","span":{"begin":1785,"end":1793},"obj":"http://edamontology.org/topic_0078"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":0,"end":8},"obj":"http://edamontology.org/operation_2945"},{"id":"T2","span":{"begin":190,"end":214},"obj":"http://edamontology.org/operation_3742"},{"id":"T3","span":{"begin":416,"end":424},"obj":"http://edamontology.org/operation_2423"},{"id":"T4","span":{"begin":870,"end":884},"obj":"http://edamontology.org/data_2769"},{"id":"T5","span":{"begin":974,"end":982},"obj":"http://edamontology.org/data_1756"},{"id":"T6","span":{"begin":1035,"end":1043},"obj":"http://edamontology.org/operation_3218"},{"id":"T7","span":{"begin":1035,"end":1043},"obj":"http://edamontology.org/data_2044"},{"id":"T8","span":{"begin":1035,"end":1055},"obj":"http://edamontology.org/data_1771"},{"id":"T9","span":{"begin":1079,"end":1086},"obj":"http://edamontology.org/data_2906"},{"id":"T10","span":{"begin":1138,"end":1146},"obj":"http://edamontology.org/data_2044"},{"id":"T11","span":{"begin":1138,"end":1146},"obj":"http://edamontology.org/operation_3218"},{"id":"T12","span":{"begin":1138,"end":1157},"obj":"http://edamontology.org/data_1413"},{"id":"T13","span":{"begin":1138,"end":1157},"obj":"http://edamontology.org/data_0865"},{"id":"T14","span":{"begin":1138,"end":1157},"obj":"http://edamontology.org/data_2161"},{"id":"T15","span":{"begin":1238,"end":1246},"obj":"http://edamontology.org/format_1208"},{"id":"T16","span":{"begin":1238,"end":1246},"obj":"http://edamontology.org/data_1467"},{"id":"T17","span":{"begin":1396,"end":1403},"obj":"http://edamontology.org/data_1467"},{"id":"T18","span":{"begin":1396,"end":1403},"obj":"http://edamontology.org/format_1208"},{"id":"T19","span":{"begin":1600,"end":1607},"obj":"http://edamontology.org/data_1467"},{"id":"T20","span":{"begin":1600,"end":1607},"obj":"http://edamontology.org/format_1208"},{"id":"T21","span":{"begin":1600,"end":1621},"obj":"http://edamontology.org/operation_2502"},{"id":"T22","span":{"begin":1613,"end":1621},"obj":"http://edamontology.org/operation_2945"},{"id":"T23","span":{"begin":1688,"end":1695},"obj":"http://edamontology.org/format_1208"},{"id":"T24","span":{"begin":1688,"end":1695},"obj":"http://edamontology.org/data_1467"},{"id":"T25","span":{"begin":1785,"end":1793},"obj":"http://edamontology.org/format_1208"},{"id":"T26","span":{"begin":1785,"end":1793},"obj":"http://edamontology.org/data_1467"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":12,"end":18},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T2","span":{"begin":290,"end":296},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T3","span":{"begin":889,"end":895},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T4","span":{"begin":1592,"end":1598},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T5","span":{"begin":1738,"end":1744},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":222,"end":229},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":1629,"end":1635},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":12,"end":18},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":290,"end":296},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"PD-UBERON-AE-B_T5","span":{"begin":889,"end":895},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"PD-UBERON-AE-B_T6","span":{"begin":1592,"end":1598},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"PD-UBERON-AE-B_T7","span":{"begin":1738,"end":1744},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":12,"end":18},"obj":"Body_part"},{"id":"T2","span":{"begin":290,"end":296},"obj":"Body_part"},{"id":"T3","span":{"begin":889,"end":895},"obj":"Body_part"},{"id":"T4","span":{"begin":1592,"end":1598},"obj":"Body_part"},{"id":"T5","span":{"begin":1738,"end":1744},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000119"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"Lectin-Jamboree","denotations":[{"id":"T1","span":{"begin":736,"end":742},"obj":"lectin"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T1","span":{"begin":0,"end":98},"obj":"Sentence"},{"id":"T2","span":{"begin":99,"end":230},"obj":"Sentence"},{"id":"T3","span":{"begin":231,"end":348},"obj":"Sentence"},{"id":"T4","span":{"begin":349,"end":471},"obj":"Sentence"},{"id":"T5","span":{"begin":472,"end":648},"obj":"Sentence"},{"id":"T6","span":{"begin":649,"end":761},"obj":"Sentence"},{"id":"T7","span":{"begin":762,"end":896},"obj":"Sentence"},{"id":"T8","span":{"begin":897,"end":1056},"obj":"Sentence"},{"id":"T9","span":{"begin":1057,"end":1247},"obj":"Sentence"},{"id":"T10","span":{"begin":1248,"end":1410},"obj":"Sentence"},{"id":"T11","span":{"begin":1411,"end":1527},"obj":"Sentence"},{"id":"T12","span":{"begin":1528,"end":1794},"obj":"Sentence"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":44,"end":47},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":218,"end":221},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":286,"end":289},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":487,"end":502},"obj":"OrganismTaxon"},{"id":"T8","span":{"begin":885,"end":888},"obj":"OrganismTaxon"},{"id":"T10","span":{"begin":1588,"end":1591},"obj":"OrganismTaxon"},{"id":"T12","span":{"begin":1625,"end":1628},"obj":"OrganismTaxon"},{"id":"T14","span":{"begin":1734,"end":1737},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10114"},{"id":"A2","pred":"db_id","subj":"T1","obj":"10116"},{"id":"A3","pred":"db_id","subj":"T3","obj":"10114"},{"id":"A4","pred":"db_id","subj":"T3","obj":"10116"},{"id":"A5","pred":"db_id","subj":"T5","obj":"10114"},{"id":"A6","pred":"db_id","subj":"T5","obj":"10116"},{"id":"A7","pred":"db_id","subj":"T7","obj":"10029"},{"id":"A8","pred":"db_id","subj":"T8","obj":"10114"},{"id":"A9","pred":"db_id","subj":"T8","obj":"10116"},{"id":"A10","pred":"db_id","subj":"T10","obj":"10114"},{"id":"A11","pred":"db_id","subj":"T10","obj":"10116"},{"id":"A12","pred":"db_id","subj":"T12","obj":"10114"},{"id":"A13","pred":"db_id","subj":"T12","obj":"10116"},{"id":"A14","pred":"db_id","subj":"T14","obj":"10114"},{"id":"A15","pred":"db_id","subj":"T14","obj":"10116"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":12,"end":18},"obj":"Body_part"},{"id":"T2","span":{"begin":290,"end":296},"obj":"Body_part"},{"id":"T3","span":{"begin":503,"end":508},"obj":"Body_part"},{"id":"T4","span":{"begin":629,"end":634},"obj":"Body_part"},{"id":"T5","span":{"begin":889,"end":895},"obj":"Body_part"},{"id":"T6","span":{"begin":1211,"end":1229},"obj":"Body_part"},{"id":"T7","span":{"begin":1372,"end":1377},"obj":"Body_part"},{"id":"T8","span":{"begin":1592,"end":1598},"obj":"Body_part"},{"id":"T9","span":{"begin":1629,"end":1635},"obj":"Body_part"},{"id":"T10","span":{"begin":1738,"end":1744},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0000992"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0005794"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL_0000151"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/GO_0005794"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"A10","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":1211,"end":1229},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000151"}],"text":"Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.\nbeta-Galactoside alpha 2,6-sialyltransferase (SiaT-1), like other glycosyltransferases, is differentially expressed in rat tissues. Two distinct size classes of SiaT-1 mRNAs expressed in rat kidney are comprised of at least three SiaT-1 transcripts. One mRNA, RKE, represents the larger transcript class (4.7 kb) and predicts a polypeptide identical to the hepatic SiaT-1. In transfected Chinese hamster ovary (CHO) cells, RKE polypeptides exhibit hemi-perinuclear staining with a SiaT-1 antibody (Ab-267) that is consistent with Golgi localization. RKE transfectants display cell-surface alpha 2,6-sialic acid linkages as determined by lectin affinity staining. Two other mRNAs, RKA and RKB, are members of a smaller size class (3.6 kb) that comprise predominant SiaT-1 transcripts in rat kidney. Both RKA and RKB encode polypeptides that are missing the amino-terminal 232 residues, but retain 171 amino acids of RKE carboxy-terminal sequence information. A short, leucine-rich peptide present in the divergent amino-terminus of RKA has sequence similarity to the secretory signal domain of several eukaryotic secretory and cell-surface proteins. In transfected CHO cells, both RKA and RKB polypeptides display an immunostaining pattern that is distinct from that of the Golgi-associated SiaT-1 protein (RKE). Furthermore, RKA or RKB transfectants do not display alpha 2,6-sialic acid linkages on cell-surface glycoconjugates. Consistent with the expression of divergent SiaT-1 mRNAs in rat kidney, protein blot analysis of rat tissue homogenates with Ab-267 reveals that in addition to protein that co-migrates with hepatic SiaT-1, rat kidney expresses a unique size class of SiaT-1 proteins."}