PubMed:12773476 JSONTXT

{"project":"GlyCosmos600-CLO","denotations":[{"id":"T1","span":{"begin":359,"end":364},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":692,"end":697},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":933,"end":940},"obj":"http://purl.obolibrary.org/obo/CLO_0052141"},{"id":"T4","span":{"begin":933,"end":940},"obj":"http://purl.obolibrary.org/obo/CLO_0052139"},{"id":"T5","span":{"begin":933,"end":940},"obj":"http://purl.obolibrary.org/obo/CLO_0052135"},{"id":"T6","span":{"begin":933,"end":940},"obj":"http://purl.obolibrary.org/obo/CLO_0051795"},{"id":"T7","span":{"begin":933,"end":940},"obj":"http://purl.obolibrary.org/obo/CLO_0009015"},{"id":"T8","span":{"begin":941,"end":945},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":174,"end":182},"obj":"FMAID:67257"},{"id":"_T2","span":{"begin":174,"end":182},"obj":"FMAID:165447"},{"id":"_T3","span":{"begin":310,"end":317},"obj":"FMAID:67257"},{"id":"_T4","span":{"begin":310,"end":317},"obj":"FMAID:165447"},{"id":"_T5","span":{"begin":352,"end":364},"obj":"FMAID:167570"},{"id":"_T6","span":{"begin":352,"end":364},"obj":"FMAID:63179"},{"id":"_T7","span":{"begin":359,"end":364},"obj":"FMAID:169002"},{"id":"_T8","span":{"begin":359,"end":364},"obj":"FMAID:68646"},{"id":"_T9","span":{"begin":394,"end":401},"obj":"FMAID:165447"},{"id":"_T10","span":{"begin":394,"end":401},"obj":"FMAID:67257"},{"id":"_T11","span":{"begin":685,"end":697},"obj":"FMAID:63179"},{"id":"_T12","span":{"begin":685,"end":697},"obj":"FMAID:167570"},{"id":"_T13","span":{"begin":692,"end":697},"obj":"FMAID:169002"},{"id":"_T14","span":{"begin":692,"end":697},"obj":"FMAID:68646"},{"id":"_T15","span":{"begin":752,"end":780},"obj":"FMAID:196801"},{"id":"_T16","span":{"begin":752,"end":780},"obj":"FMAID:82806"},{"id":"_T17","span":{"begin":752,"end":780},"obj":"FMAID:199790"},{"id":"_T18","span":{"begin":752,"end":780},"obj":"FMAID:85436"},{"id":"_T19","span":{"begin":796,"end":803},"obj":"FMAID:67257"},{"id":"_T20","span":{"begin":796,"end":803},"obj":"FMAID:165447"},{"id":"_T21","span":{"begin":1174,"end":1182},"obj":"FMAID:67257"},{"id":"_T22","span":{"begin":1174,"end":1182},"obj":"FMAID:165447"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":782,"end":785},"obj":"http://www.uniprot.org/uniprot/P06744"},{"id":"T2","span":{"begin":1071,"end":1074},"obj":"http://www.uniprot.org/uniprot/P06744"},{"id":"T3","span":{"begin":787,"end":813},"obj":"http://www.uniprot.org/uniprot/Q3KP22"},{"id":"T4","span":{"begin":827,"end":830},"obj":"http://www.uniprot.org/uniprot/P16444"},{"id":"T5","span":{"begin":1106,"end":1109},"obj":"http://www.uniprot.org/uniprot/P16444"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":28,"end":31},"obj":"http://www.uniprot.org/uniprot/Q61024"},{"id":"T2","span":{"begin":216,"end":219},"obj":"http://www.uniprot.org/uniprot/Q61024"},{"id":"T3","span":{"begin":435,"end":438},"obj":"http://www.uniprot.org/uniprot/Q61024"},{"id":"T4","span":{"begin":451,"end":454},"obj":"http://www.uniprot.org/uniprot/Q61024"},{"id":"T5","span":{"begin":699,"end":702},"obj":"http://www.uniprot.org/uniprot/Q61024"},{"id":"T6","span":{"begin":782,"end":785},"obj":"http://www.uniprot.org/uniprot/Q8C675"},{"id":"T7","span":{"begin":1071,"end":1074},"obj":"http://www.uniprot.org/uniprot/Q8C675"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":359,"end":364},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T2","span":{"begin":388,"end":393},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/94193"},{"id":"T3","span":{"begin":388,"end":393},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/94464"},{"id":"T4","span":{"begin":692,"end":697},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":0,"end":13},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T2","span":{"begin":199,"end":212},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T3","span":{"begin":367,"end":380},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T4","span":{"begin":668,"end":681},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T5","span":{"begin":988,"end":1000},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T6","span":{"begin":129,"end":142},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T7","span":{"begin":143,"end":154},"obj":"http://purl.obolibrary.org/obo/GO_0006412"},{"id":"T8","span":{"begin":782,"end":803},"obj":"http://purl.obolibrary.org/obo/GO_0016255"},{"id":"T9","span":{"begin":1088,"end":1096},"obj":"http://purl.obolibrary.org/obo/GO_0046903"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":292,"end":317},"obj":"http://purl.obolibrary.org/obo/GO_0008022"},{"id":"T2","span":{"begin":787,"end":795},"obj":"http://purl.obolibrary.org/obo/GO_0043495"},{"id":"T3","span":{"begin":1075,"end":1083},"obj":"http://purl.obolibrary.org/obo/GO_0043495"},{"id":"T4","span":{"begin":787,"end":803},"obj":"http://purl.obolibrary.org/obo/GO_0043495"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":98,"end":106},"obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"T2","span":{"begin":805,"end":813},"obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"T3","span":{"begin":359,"end":364},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":692,"end":697},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":941,"end":945},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":86,"end":97},"obj":"http://edamontology.org/topic_0749"},{"id":"T2","span":{"begin":129,"end":142},"obj":"http://edamontology.org/topic_0203"},{"id":"T3","span":{"begin":129,"end":142},"obj":"http://edamontology.org/topic_3308"},{"id":"T4","span":{"begin":129,"end":142},"obj":"http://edamontology.org/topic_3512"},{"id":"T5","span":{"begin":129,"end":142},"obj":"http://edamontology.org/topic_0110"},{"id":"T6","span":{"begin":143,"end":154},"obj":"http://edamontology.org/topic_0108"},{"id":"T7","span":{"begin":155,"end":162},"obj":"http://edamontology.org/topic_3678"},{"id":"T8","span":{"begin":174,"end":182},"obj":"http://edamontology.org/topic_0078"},{"id":"T9","span":{"begin":310,"end":317},"obj":"http://edamontology.org/topic_0078"},{"id":"T10","span":{"begin":394,"end":401},"obj":"http://edamontology.org/topic_0078"},{"id":"T11","span":{"begin":796,"end":803},"obj":"http://edamontology.org/topic_0078"},{"id":"T12","span":{"begin":913,"end":918},"obj":"http://edamontology.org/topic_2815"},{"id":"T13","span":{"begin":1054,"end":1065},"obj":"http://edamontology.org/topic_0749"},{"id":"T14","span":{"begin":1174,"end":1182},"obj":"http://edamontology.org/topic_0078"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":174,"end":182},"obj":"http://edamontology.org/data_1467"},{"id":"T2","span":{"begin":174,"end":182},"obj":"http://edamontology.org/format_1208"},{"id":"T3","span":{"begin":276,"end":284},"obj":"http://edamontology.org/data_1756"},{"id":"T4","span":{"begin":310,"end":317},"obj":"http://edamontology.org/data_1467"},{"id":"T5","span":{"begin":310,"end":317},"obj":"http://edamontology.org/format_1208"},{"id":"T6","span":{"begin":394,"end":401},"obj":"http://edamontology.org/format_1208"},{"id":"T7","span":{"begin":394,"end":401},"obj":"http://edamontology.org/data_1467"},{"id":"T8","span":{"begin":488,"end":496},"obj":"http://edamontology.org/data_1756"},{"id":"T9","span":{"begin":643,"end":650},"obj":"http://edamontology.org/operation_3429"},{"id":"T10","span":{"begin":796,"end":803},"obj":"http://edamontology.org/data_1467"},{"id":"T11","span":{"begin":796,"end":803},"obj":"http://edamontology.org/format_1208"},{"id":"T12","span":{"begin":1034,"end":1042},"obj":"http://edamontology.org/data_1756"},{"id":"T13","span":{"begin":1117,"end":1121},"obj":"http://edamontology.org/data_0006"},{"id":"T14","span":{"begin":1122,"end":1133},"obj":"http://edamontology.org/operation_2246"},{"id":"T15","span":{"begin":1174,"end":1182},"obj":"http://edamontology.org/format_1208"},{"id":"T16","span":{"begin":1174,"end":1182},"obj":"http://edamontology.org/data_1467"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"GlyCosmos600-GlycoEpitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":566,"end":569},"obj":"http://www.glycoepitope.jp/epitopes/AN0622"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"GlyCosmos600-FMA","denotations":[{"id":"T1","span":{"begin":174,"end":182},"obj":"Body_part"},{"id":"T2","span":{"begin":310,"end":317},"obj":"Body_part"},{"id":"T3","span":{"begin":359,"end":364},"obj":"Body_part"},{"id":"T4","span":{"begin":394,"end":401},"obj":"Body_part"},{"id":"T5","span":{"begin":403,"end":406},"obj":"Body_part"},{"id":"T6","span":{"begin":692,"end":697},"obj":"Body_part"},{"id":"T7","span":{"begin":796,"end":803},"obj":"Body_part"},{"id":"T8","span":{"begin":886,"end":889},"obj":"Body_part"},{"id":"T9","span":{"begin":941,"end":945},"obj":"Body_part"},{"id":"T10","span":{"begin":1174,"end":1182},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"fma_id","subj":"T1","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A2","pred":"fma_id","subj":"T2","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A3","pred":"fma_id","subj":"T3","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A4","pred":"fma_id","subj":"T4","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A5","pred":"fma_id","subj":"T5","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A6","pred":"fma_id","subj":"T6","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A7","pred":"fma_id","subj":"T7","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A8","pred":"fma_id","subj":"T8","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A9","pred":"fma_id","subj":"T9","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A10","pred":"fma_id","subj":"T10","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

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"EnjuParser_T185"},{"id":"EnjuParser_R193","pred":"arg1Of","subj":"EnjuParser_T185","obj":"EnjuParser_T186"},{"id":"EnjuParser_R194","pred":"arg2Of","subj":"EnjuParser_T188","obj":"EnjuParser_T186"},{"id":"EnjuParser_R195","pred":"arg1Of","subj":"EnjuParser_T188","obj":"EnjuParser_T187"},{"id":"EnjuParser_R196","pred":"arg1Of","subj":"EnjuParser_T188","obj":"EnjuParser_T189"},{"id":"EnjuParser_R197","pred":"arg2Of","subj":"EnjuParser_T191","obj":"EnjuParser_T189"},{"id":"EnjuParser_R198","pred":"arg1Of","subj":"EnjuParser_T191","obj":"EnjuParser_T190"}],"namespaces":[{"prefix":"_base","uri":"http://kmcs.nii.ac.jp/enju/"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"GlyCosmos600-GlycoProteins","denotations":[{"id":"PD-GlycoProteins-B_T1","span":{"begin":782,"end":785},"obj":"http://purl.uniprot.org/uniprot/P06744"},{"id":"PD-GlycoProteins-B_T2","span":{"begin":1071,"end":1074},"obj":"http://purl.uniprot.org/uniprot/P06744"},{"id":"PD-GlycoProteins-B_T3","span":{"begin":107,"end":118},"obj":"https://acgg.asia/db/gpdb/id/GPDB0007235"},{"id":"PD-GlycoProteins-B_T4","span":{"begin":814,"end":825},"obj":"https://acgg.asia/db/gpdb/id/GPDB0007235"},{"id":"PD-GlycoProteins-B_T5","span":{"begin":107,"end":118},"obj":"https://acgg.asia/db/gpdb/id/GPDB0008541"},{"id":"PD-GlycoProteins-B_T6","span":{"begin":814,"end":825},"obj":"https://acgg.asia/db/gpdb/id/GPDB0008541"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":119},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":120,"end":318},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":319,"end":580},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":581,"end":890},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":891,"end":1110},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1111,"end":1236},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":119},"obj":"Sentence"},{"id":"T2","span":{"begin":120,"end":318},"obj":"Sentence"},{"id":"T3","span":{"begin":319,"end":580},"obj":"Sentence"},{"id":"T4","span":{"begin":581,"end":890},"obj":"Sentence"},{"id":"T5","span":{"begin":891,"end":1110},"obj":"Sentence"},{"id":"T6","span":{"begin":1111,"end":1236},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":782,"end":795},"obj":"http://rdf.glycoinfo.org/glycan/G00045MO"},{"id":"T2","span":{"begin":1071,"end":1083},"obj":"http://rdf.glycoinfo.org/glycan/G00045MO"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":566,"end":569},"obj":"http://www.glycoepitope.jp/epitopes/AN0622"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":36,"end":39},"obj":"\"http://rdf.glycoinfo.org/glycan/G69371PB\""},{"id":"GlycanIUPAC_T2","span":{"begin":224,"end":227},"obj":"\"http://rdf.glycoinfo.org/glycan/G69371PB\""},{"id":"GlycanIUPAC_T3","span":{"begin":443,"end":446},"obj":"\"http://rdf.glycoinfo.org/glycan/G69371PB\""},{"id":"GlycanIUPAC_T4","span":{"begin":459,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G69371PB\""},{"id":"GlycanIUPAC_T5","span":{"begin":711,"end":714},"obj":"\"http://rdf.glycoinfo.org/glycan/G69371PB\""},{"id":"GlycanIUPAC_T6","span":{"begin":36,"end":39},"obj":"\"http://rdf.glycoinfo.org/glycan/G04439TG\""},{"id":"GlycanIUPAC_T7","span":{"begin":224,"end":227},"obj":"\"http://rdf.glycoinfo.org/glycan/G04439TG\""},{"id":"GlycanIUPAC_T8","span":{"begin":443,"end":446},"obj":"\"http://rdf.glycoinfo.org/glycan/G04439TG\""},{"id":"GlycanIUPAC_T9","span":{"begin":459,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G04439TG\""},{"id":"GlycanIUPAC_T10","span":{"begin":711,"end":714},"obj":"\"http://rdf.glycoinfo.org/glycan/G04439TG\""},{"id":"GlycanIUPAC_T11","span":{"begin":36,"end":39},"obj":"\"http://rdf.glycoinfo.org/glycan/G01418RR\""},{"id":"GlycanIUPAC_T12","span":{"begin":224,"end":227},"obj":"\"http://rdf.glycoinfo.org/glycan/G01418RR\""},{"id":"GlycanIUPAC_T13","span":{"begin":443,"end":446},"obj":"\"http://rdf.glycoinfo.org/glycan/G01418RR\""},{"id":"GlycanIUPAC_T14","span":{"begin":459,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G01418RR\""},{"id":"GlycanIUPAC_T15","span":{"begin":711,"end":714},"obj":"\"http://rdf.glycoinfo.org/glycan/G01418RR\""},{"id":"GlycanIUPAC_T16","span":{"begin":36,"end":39},"obj":"\"http://rdf.glycoinfo.org/glycan/G98605AX\""},{"id":"GlycanIUPAC_T17","span":{"begin":224,"end":227},"obj":"\"http://rdf.glycoinfo.org/glycan/G98605AX\""},{"id":"GlycanIUPAC_T18","span":{"begin":443,"end":446},"obj":"\"http://rdf.glycoinfo.org/glycan/G98605AX\""},{"id":"GlycanIUPAC_T19","span":{"begin":459,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G98605AX\""},{"id":"GlycanIUPAC_T20","span":{"begin":711,"end":714},"obj":"\"http://rdf.glycoinfo.org/glycan/G98605AX\""},{"id":"GlycanIUPAC_T21","span":{"begin":36,"end":39},"obj":"\"http://rdf.glycoinfo.org/glycan/G24282OK\""},{"id":"GlycanIUPAC_T22","span":{"begin":224,"end":227},"obj":"\"http://rdf.glycoinfo.org/glycan/G24282OK\""},{"id":"GlycanIUPAC_T23","span":{"begin":443,"end":446},"obj":"\"http://rdf.glycoinfo.org/glycan/G24282OK\""},{"id":"GlycanIUPAC_T24","span":{"begin":459,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G24282OK\""},{"id":"GlycanIUPAC_T25","span":{"begin":711,"end":714},"obj":"\"http://rdf.glycoinfo.org/glycan/G24282OK\""},{"id":"GlycanIUPAC_T26","span":{"begin":36,"end":39},"obj":"\"http://rdf.glycoinfo.org/glycan/G55879EK\""},{"id":"GlycanIUPAC_T27","span":{"begin":224,"end":227},"obj":"\"http://rdf.glycoinfo.org/glycan/G55879EK\""},{"id":"GlycanIUPAC_T28","span":{"begin":443,"end":446},"obj":"\"http://rdf.glycoinfo.org/glycan/G55879EK\""},{"id":"GlycanIUPAC_T29","span":{"begin":459,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G55879EK\""},{"id":"GlycanIUPAC_T30","span":{"begin":711,"end":714},"obj":"\"http://rdf.glycoinfo.org/glycan/G55879EK\""},{"id":"GlycanIUPAC_T31","span":{"begin":36,"end":39},"obj":"\"http://rdf.glycoinfo.org/glycan/G12116BQ\""},{"id":"GlycanIUPAC_T32","span":{"begin":224,"end":227},"obj":"\"http://rdf.glycoinfo.org/glycan/G12116BQ\""},{"id":"GlycanIUPAC_T33","span":{"begin":443,"end":446},"obj":"\"http://rdf.glycoinfo.org/glycan/G12116BQ\""},{"id":"GlycanIUPAC_T34","span":{"begin":459,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G12116BQ\""},{"id":"GlycanIUPAC_T35","span":{"begin":711,"end":714},"obj":"\"http://rdf.glycoinfo.org/glycan/G12116BQ\""},{"id":"GlycanIUPAC_T36","span":{"begin":36,"end":39},"obj":"\"http://rdf.glycoinfo.org/glycan/G54590PA\""},{"id":"GlycanIUPAC_T37","span":{"begin":224,"end":227},"obj":"\"http://rdf.glycoinfo.org/glycan/G54590PA\""},{"id":"GlycanIUPAC_T38","span":{"begin":443,"end":446},"obj":"\"http://rdf.glycoinfo.org/glycan/G54590PA\""},{"id":"GlycanIUPAC_T39","span":{"begin":459,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G54590PA\""},{"id":"GlycanIUPAC_T40","span":{"begin":711,"end":714},"obj":"\"http://rdf.glycoinfo.org/glycan/G54590PA\""},{"id":"GlycanIUPAC_T41","span":{"begin":36,"end":39},"obj":"\"http://rdf.glycoinfo.org/glycan/G31652HG\""},{"id":"GlycanIUPAC_T42","span":{"begin":224,"end":227},"obj":"\"http://rdf.glycoinfo.org/glycan/G31652HG\""},{"id":"GlycanIUPAC_T43","span":{"begin":443,"end":446},"obj":"\"http://rdf.glycoinfo.org/glycan/G31652HG\""},{"id":"GlycanIUPAC_T44","span":{"begin":459,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G31652HG\""},{"id":"GlycanIUPAC_T45","span":{"begin":711,"end":714},"obj":"\"http://rdf.glycoinfo.org/glycan/G31652HG\""},{"id":"GlycanIUPAC_T46","span":{"begin":36,"end":39},"obj":"\"http://rdf.glyco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AC_T777","span":{"begin":224,"end":227},"obj":"\"http://rdf.glycoinfo.org/glycan/G36146RU\""},{"id":"GlycanIUPAC_T778","span":{"begin":443,"end":446},"obj":"\"http://rdf.glycoinfo.org/glycan/G36146RU\""},{"id":"GlycanIUPAC_T779","span":{"begin":459,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G36146RU\""},{"id":"GlycanIUPAC_T780","span":{"begin":711,"end":714},"obj":"\"http://rdf.glycoinfo.org/glycan/G36146RU\""},{"id":"GlycanIUPAC_T781","span":{"begin":36,"end":39},"obj":"\"http://rdf.glycoinfo.org/glycan/G23944RZ\""},{"id":"GlycanIUPAC_T782","span":{"begin":224,"end":227},"obj":"\"http://rdf.glycoinfo.org/glycan/G23944RZ\""},{"id":"GlycanIUPAC_T783","span":{"begin":443,"end":446},"obj":"\"http://rdf.glycoinfo.org/glycan/G23944RZ\""},{"id":"GlycanIUPAC_T784","span":{"begin":459,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G23944RZ\""},{"id":"GlycanIUPAC_T785","span":{"begin":711,"end":714},"obj":"\"http://rdf.glycoinfo.org/glycan/G23944RZ\""},{"id":"GlycanIUPAC_T786","span":{"begin":36,"end":39},"obj":"\"http://rdf.glycoinfo.org/glycan/G67041BN\""},{"id":"GlycanIUPAC_T787","span":{"begin":224,"end":227},"obj":"\"http://rdf.glycoinfo.org/glycan/G67041BN\""},{"id":"GlycanIUPAC_T788","span":{"begin":443,"end":446},"obj":"\"http://rdf.glycoinfo.org/glycan/G67041BN\""},{"id":"GlycanIUPAC_T789","span":{"begin":459,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G67041BN\""},{"id":"GlycanIUPAC_T790","span":{"begin":711,"end":714},"obj":"\"http://rdf.glycoinfo.org/glycan/G67041BN\""},{"id":"GlycanIUPAC_T791","span":{"begin":36,"end":39},"obj":"\"http://rdf.glycoinfo.org/glycan/G95408HX\""},{"id":"GlycanIUPAC_T792","span":{"begin":224,"end":227},"obj":"\"http://rdf.glycoinfo.org/glycan/G95408HX\""},{"id":"GlycanIUPAC_T793","span":{"begin":443,"end":446},"obj":"\"http://rdf.glycoinfo.org/glycan/G95408HX\""},{"id":"GlycanIUPAC_T794","span":{"begin":459,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G95408HX\""},{"id":"GlycanIUPAC_T795","span":{"begin":711,"end":714},"obj":"\"http://rdf.glycoinfo.org/glycan/G95408HX\""},{"id":"GlycanIUPAC_T796","span":{"begin":36,"end":39},"obj":"\"http://rdf.glycoinfo.org/glycan/G31094CC\""},{"id":"GlycanIUPAC_T797","span":{"begin":224,"end":227},"obj":"\"http://rdf.glycoinfo.org/glycan/G31094CC\""},{"id":"GlycanIUPAC_T798","span":{"begin":443,"end":446},"obj":"\"http://rdf.glycoinfo.org/glycan/G31094CC\""},{"id":"GlycanIUPAC_T799","span":{"begin":459,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G31094CC\""},{"id":"GlycanIUPAC_T800","span":{"begin":711,"end":714},"obj":"\"http://rdf.glycoinfo.org/glycan/G31094CC\""},{"id":"GlycanIUPAC_T801","span":{"begin":36,"end":39},"obj":"\"http://rdf.glycoinfo.org/glycan/G99598GU\""},{"id":"GlycanIUPAC_T802","span":{"begin":224,"end":227},"obj":"\"http://rdf.glycoinfo.org/glycan/G99598GU\""},{"id":"GlycanIUPAC_T803","span":{"begin":443,"end":446},"obj":"\"http://rdf.glycoinfo.org/glycan/G99598GU\""},{"id":"GlycanIUPAC_T804","span":{"begin":459,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G99598GU\""},{"id":"GlycanIUPAC_T805","span":{"begin":711,"end":714},"obj":"\"http://rdf.glycoinfo.org/glycan/G99598GU\""},{"id":"GlycanIUPAC_T806","span":{"begin":36,"end":39},"obj":"\"http://rdf.glycoinfo.org/glycan/G94072IC\""},{"id":"GlycanIUPAC_T807","span":{"begin":224,"end":227},"obj":"\"http://rdf.glycoinfo.org/glycan/G94072IC\""},{"id":"GlycanIUPAC_T808","span":{"begin":443,"end":446},"obj":"\"http://rdf.glycoinfo.org/glycan/G94072IC\""},{"id":"GlycanIUPAC_T809","span":{"begin":459,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G94072IC\""},{"id":"GlycanIUPAC_T810","span":{"begin":711,"end":714},"obj":"\"http://rdf.glycoinfo.org/glycan/G94072IC\""},{"id":"GlycanIUPAC_T811","span":{"begin":36,"end":39},"obj":"\"http://rdf.glycoinfo.org/glycan/G09523ZS\""},{"id":"GlycanIUPAC_T812","span":{"begin":224,"end":227},"obj":"\"http://rdf.glycoinfo.org/glycan/G09523ZS\""},{"id":"GlycanIUPAC_T813","span":{"begin":443,"end":446},"obj":"\"http://rdf.glycoinfo.org/glycan/G09523ZS\""},{"id":"GlycanIUPAC_T814","span":{"begin":459,"end":462},"obj":"\"http://rdf.glycoinfo.org/glycan/G09523ZS\""},{"id":"GlycanIUPAC_T815","span":{"begin":711,"end":714},"obj":"\"http://rdf.glycoinfo.org/glycan/G09523ZS\""}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":919,"end":932},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0003006"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":919,"end":932},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005072"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":913,"end":918},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":98,"end":106},"obj":"Body_part"},{"id":"T4","span":{"begin":805,"end":813},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A3","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A5","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A6","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"}],"text":"Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase.\nIn vitro transcription/translation studies with model proteins have shown that glycosylation of Asn-Xaa-Thr sequons is reduced when the sequon is within 60 residues of the C-terminus of the protein. We have previously shown that in living cells N-glycosylation of the prion protein (PrP) is also abolished when its Asn-Ile-Thr and Asn-Phe-Thr sequons are less than 60 residues from the C-terminus (Walmsley and Hooper [2003] Biochemical Journal, 370, 351-355). To investigate whether sequon distance to the C-terminus is a general determinant of N-glycosylation in living cells, Asn-Ile/Phe-Thr sequons were introduced into another glycosylphosphatidylinositol (GPI) anchored protein, membrane dipeptidase (MDP), at similar distances from the C-terminus as those in PrP. When expressed in the human neuroblastoma SH-SY5Y cell line, the introduced sequons were fully N-glycosylated even when they were less than 60 residues from the C-terminus in both GPI-anchored and secreted forms of MDP. These data demonstrate that the utilization of sequons in some proteins is independent of their distance from the C-terminus."}