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Glycosmos6-MAT

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":135,"end":140},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"T2","span":{"begin":227,"end":232},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"T3","span":{"begin":1339,"end":1344},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"}],"text":"The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver.\nThe alpha- and beta-subunits of the hetero-dimeric glucosidase II complex from human liver were cloned and expressed in COS-1 cells. The 4106 bp full-length cDNA for the alpha-subunit contained a 2835 bp ORF encoding a 107 kDa polypeptide. The 2095 bp cDNA for the beta-subunit encodes a approximately 60 kDa protein in a continuous 1605 bp ORF. The alpha- and beta-subunits each contain two potential Asn-Xaa-Thr/Ser acceptor sites, with only one site in the alpha-subunit (Asn97) being glycosylated. Additional lambda-clones were isolated for each subunit containing in-frame insertions/deletions within the coding region, indicating alternative splicing. Analysis of different human tissues revealed approximately 4.4 kb and approximately 2.4 kb transcripts for alpha- and beta-subunit, respectively, consistent with their full-length cDNA. Coexpression of the alpha- and beta-subunits in COS-1 cells resulted in \u003e4-fold increase of glucosidase II activity. An inactive protein was obtained, however, after transfection with the alpha-subunit alone, showing that both subunits are essential for expression of active glucosidase II. The observation that the enzyme, previously purified from pig liver and lacking the beta-subunit, was catalytically active indicates that the beta-subunit is involved in alpha-subunit maturation rather than being required for enzymatic activity once the alpha-subunit has acquired its mature form. The alpha-subunit is expressed in COS-1 cells as an ER-located protein, whether inactive or part of a catalytically active complex. This suggests that ER-localization of the alpha-subunit, when associated with the dimeric enzyme complex, is mediated by the C-terminal HDEL-signal in the beta-subunit, whereas the apparently incompletely folded form of the inactive alpha-subunit could be retained in the ER by the putative \"glycoprotein-specific quality control machinery. \""}

GlycoBiology-FMA

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":135,"end":140},"obj":"FMAID:7197"},{"id":"_T2","span":{"begin":135,"end":140},"obj":"FMAID:93672"},{"id":"_T3","span":{"begin":227,"end":232},"obj":"FMAID:7197"},{"id":"_T4","span":{"begin":227,"end":232},"obj":"FMAID:93672"},{"id":"_T5","span":{"begin":268,"end":273},"obj":"FMAID:68646"},{"id":"_T6","span":{"begin":268,"end":273},"obj":"FMAID:169002"},{"id":"_T7","span":{"begin":451,"end":458},"obj":"FMAID:67257"},{"id":"_T8","span":{"begin":451,"end":458},"obj":"FMAID:165447"},{"id":"_T9","span":{"begin":655,"end":661},"obj":"FMAID:264773"},{"id":"_T10","span":{"begin":655,"end":661},"obj":"FMAID:242025"},{"id":"_T11","span":{"begin":828,"end":835},"obj":"FMAID:256050"},{"id":"_T12","span":{"begin":1040,"end":1045},"obj":"FMAID:169002"},{"id":"_T13","span":{"begin":1040,"end":1045},"obj":"FMAID:68646"},{"id":"_T14","span":{"begin":1115,"end":1122},"obj":"FMAID:165447"},{"id":"_T15","span":{"begin":1115,"end":1122},"obj":"FMAID:67257"},{"id":"_T16","span":{"begin":1339,"end":1344},"obj":"FMAID:93672"},{"id":"_T17","span":{"begin":1339,"end":1344},"obj":"FMAID:7197"},{"id":"_T18","span":{"begin":1615,"end":1620},"obj":"FMAID:68646"},{"id":"_T19","span":{"begin":1615,"end":1620},"obj":"FMAID:169002"},{"id":"_T20","span":{"begin":1638,"end":1645},"obj":"FMAID:165447"},{"id":"_T21","span":{"begin":1638,"end":1645},"obj":"FMAID:67257"},{"id":"_T22","span":{"begin":1999,"end":2011},"obj":"FMAID:167256"},{"id":"_T23","span":{"begin":1999,"end":2011},"obj":"FMAID:62925"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver.\nThe alpha- and beta-subunits of the hetero-dimeric glucosidase II complex from human liver were cloned and expressed in COS-1 cells. The 4106 bp full-length cDNA for the alpha-subunit contained a 2835 bp ORF encoding a 107 kDa polypeptide. The 2095 bp cDNA for the beta-subunit encodes a approximately 60 kDa protein in a continuous 1605 bp ORF. The alpha- and beta-subunits each contain two potential Asn-Xaa-Thr/Ser acceptor sites, with only one site in the alpha-subunit (Asn97) being glycosylated. Additional lambda-clones were isolated for each subunit containing in-frame insertions/deletions within the coding region, indicating alternative splicing. Analysis of different human tissues revealed approximately 4.4 kb and approximately 2.4 kb transcripts for alpha- and beta-subunit, respectively, consistent with their full-length cDNA. Coexpression of the alpha- and beta-subunits in COS-1 cells resulted in \u003e4-fold increase of glucosidase II activity. An inactive protein was obtained, however, after transfection with the alpha-subunit alone, showing that both subunits are essential for expression of active glucosidase II. The observation that the enzyme, previously purified from pig liver and lacking the beta-subunit, was catalytically active indicates that the beta-subunit is involved in alpha-subunit maturation rather than being required for enzymatic activity once the alpha-subunit has acquired its mature form. The alpha-subunit is expressed in COS-1 cells as an ER-located protein, whether inactive or part of a catalytically active complex. This suggests that ER-localization of the alpha-subunit, when associated with the dimeric enzyme complex, is mediated by the C-terminal HDEL-signal in the beta-subunit, whereas the apparently incompletely folded form of the inactive alpha-subunit could be retained in the ER by the putative \"glycoprotein-specific quality control machinery. \""}

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":444,"end":458},"obj":"http://www.uniprot.org/uniprot/Q9H1W6"},{"id":"T2","span":{"begin":907,"end":930},"obj":"http://www.uniprot.org/uniprot/P06865"},{"id":"T3","span":{"begin":1627,"end":1629},"obj":"http://www.uniprot.org/uniprot/P03372"},{"id":"T4","span":{"begin":1726,"end":1728},"obj":"http://www.uniprot.org/uniprot/P03372"},{"id":"T5","span":{"begin":1979,"end":1981},"obj":"http://www.uniprot.org/uniprot/P03372"}],"text":"The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver.\nThe alpha- and beta-subunits of the hetero-dimeric glucosidase II complex from human liver were cloned and expressed in COS-1 cells. The 4106 bp full-length cDNA for the alpha-subunit contained a 2835 bp ORF encoding a 107 kDa polypeptide. The 2095 bp cDNA for the beta-subunit encodes a approximately 60 kDa protein in a continuous 1605 bp ORF. The alpha- and beta-subunits each contain two potential Asn-Xaa-Thr/Ser acceptor sites, with only one site in the alpha-subunit (Asn97) being glycosylated. Additional lambda-clones were isolated for each subunit containing in-frame insertions/deletions within the coding region, indicating alternative splicing. Analysis of different human tissues revealed approximately 4.4 kb and approximately 2.4 kb transcripts for alpha- and beta-subunit, respectively, consistent with their full-length cDNA. Coexpression of the alpha- and beta-subunits in COS-1 cells resulted in \u003e4-fold increase of glucosidase II activity. An inactive protein was obtained, however, after transfection with the alpha-subunit alone, showing that both subunits are essential for expression of active glucosidase II. The observation that the enzyme, previously purified from pig liver and lacking the beta-subunit, was catalytically active indicates that the beta-subunit is involved in alpha-subunit maturation rather than being required for enzymatic activity once the alpha-subunit has acquired its mature form. The alpha-subunit is expressed in COS-1 cells as an ER-located protein, whether inactive or part of a catalytically active complex. This suggests that ER-localization of the alpha-subunit, when associated with the dimeric enzyme complex, is mediated by the C-terminal HDEL-signal in the beta-subunit, whereas the apparently incompletely folded form of the inactive alpha-subunit could be retained in the ER by the putative \"glycoprotein-specific quality control machinery. \""}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":544,"end":547},"obj":"http://www.uniprot.org/uniprot/Q61024"},{"id":"T2","span":{"begin":1627,"end":1629},"obj":"http://www.uniprot.org/uniprot/P19785"},{"id":"T3","span":{"begin":1726,"end":1728},"obj":"http://www.uniprot.org/uniprot/P19785"},{"id":"T4","span":{"begin":1979,"end":1981},"obj":"http://www.uniprot.org/uniprot/P19785"}],"text":"The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver.\nThe alpha- and beta-subunits of the hetero-dimeric glucosidase II complex from human liver were cloned and expressed in COS-1 cells. The 4106 bp full-length cDNA for the alpha-subunit contained a 2835 bp ORF encoding a 107 kDa polypeptide. The 2095 bp cDNA for the beta-subunit encodes a approximately 60 kDa protein in a continuous 1605 bp ORF. The alpha- and beta-subunits each contain two potential Asn-Xaa-Thr/Ser acceptor sites, with only one site in the alpha-subunit (Asn97) being glycosylated. Additional lambda-clones were isolated for each subunit containing in-frame insertions/deletions within the coding region, indicating alternative splicing. Analysis of different human tissues revealed approximately 4.4 kb and approximately 2.4 kb transcripts for alpha- and beta-subunit, respectively, consistent with their full-length cDNA. Coexpression of the alpha- and beta-subunits in COS-1 cells resulted in \u003e4-fold increase of glucosidase II activity. An inactive protein was obtained, however, after transfection with the alpha-subunit alone, showing that both subunits are essential for expression of active glucosidase II. The observation that the enzyme, previously purified from pig liver and lacking the beta-subunit, was catalytically active indicates that the beta-subunit is involved in alpha-subunit maturation rather than being required for enzymatic activity once the alpha-subunit has acquired its mature form. The alpha-subunit is expressed in COS-1 cells as an ER-located protein, whether inactive or part of a catalytically active complex. This suggests that ER-localization of the alpha-subunit, when associated with the dimeric enzyme complex, is mediated by the C-terminal HDEL-signal in the beta-subunit, whereas the apparently incompletely folded form of the inactive alpha-subunit could be retained in the ER by the putative \"glycoprotein-specific quality control machinery. \""}

GlycoBiology-NCBITAXON

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":60,"end":78},"obj":"http://purl.obolibrary.org/obo/GO_0003824"},{"id":"T2","span":{"begin":1379,"end":1399},"obj":"http://purl.obolibrary.org/obo/GO_0003824"},{"id":"T3","span":{"begin":1677,"end":1697},"obj":"http://purl.obolibrary.org/obo/GO_0003824"},{"id":"T4","span":{"begin":113,"end":123},"obj":"http://purl.obolibrary.org/obo/GO_0008177"},{"id":"T5","span":{"begin":205,"end":215},"obj":"http://purl.obolibrary.org/obo/GO_0008177"},{"id":"T6","span":{"begin":630,"end":642},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T7","span":{"begin":790,"end":798},"obj":"http://purl.obolibrary.org/obo/GO_0045292"},{"id":"T8","span":{"begin":891,"end":902},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T9","span":{"begin":1078,"end":1101},"obj":"http://purl.obolibrary.org/obo/GO_0033919"},{"id":"T10","span":{"begin":1254,"end":1275},"obj":"http://purl.obolibrary.org/obo/GO_0033919"},{"id":"T11","span":{"begin":1254,"end":1272},"obj":"http://purl.obolibrary.org/obo/GO_0015926"},{"id":"T12","span":{"begin":1627,"end":1645},"obj":"http://purl.obolibrary.org/obo/GO_0035437"},{"id":"T13","span":{"begin":1726,"end":1741},"obj":"http://purl.obolibrary.org/obo/GO_0051643"},{"id":"T14","span":{"begin":1729,"end":1741},"obj":"http://purl.obolibrary.org/obo/GO_0051179"},{"id":"T15","span":{"begin":1848,"end":1854},"obj":"http://purl.obolibrary.org/obo/GO_0023052"}],"text":"The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver.\nThe alpha- and beta-subunits of the hetero-dimeric glucosidase II complex from human liver were cloned and expressed in COS-1 cells. The 4106 bp full-length cDNA for the alpha-subunit contained a 2835 bp ORF encoding a 107 kDa polypeptide. The 2095 bp cDNA for the beta-subunit encodes a approximately 60 kDa protein in a continuous 1605 bp ORF. The alpha- and beta-subunits each contain two potential Asn-Xaa-Thr/Ser acceptor sites, with only one site in the alpha-subunit (Asn97) being glycosylated. Additional lambda-clones were isolated for each subunit containing in-frame insertions/deletions within the coding region, indicating alternative splicing. Analysis of different human tissues revealed approximately 4.4 kb and approximately 2.4 kb transcripts for alpha- and beta-subunit, respectively, consistent with their full-length cDNA. Coexpression of the alpha- and beta-subunits in COS-1 cells resulted in \u003e4-fold increase of glucosidase II activity. An inactive protein was obtained, however, after transfection with the alpha-subunit alone, showing that both subunits are essential for expression of active glucosidase II. The observation that the enzyme, previously purified from pig liver and lacking the beta-subunit, was catalytically active indicates that the beta-subunit is involved in alpha-subunit maturation rather than being required for enzymatic activity once the alpha-subunit has acquired its mature form. The alpha-subunit is expressed in COS-1 cells as an ER-located protein, whether inactive or part of a catalytically active complex. This suggests that ER-localization of the alpha-subunit, when associated with the dimeric enzyme complex, is mediated by the C-terminal HDEL-signal in the beta-subunit, whereas the apparently incompletely folded form of the inactive alpha-subunit could be retained in the ER by the putative \"glycoprotein-specific quality control machinery. \""}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":101,"end":123},"obj":"http://purl.obolibrary.org/obo/GO_0017177"},{"id":"T2","span":{"begin":193,"end":215},"obj":"http://purl.obolibrary.org/obo/GO_0017177"},{"id":"T3","span":{"begin":268,"end":273},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":1040,"end":1045},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":1615,"end":1620},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T6","span":{"begin":556,"end":559},"obj":"http://purl.obolibrary.org/obo/GO_0005790"},{"id":"T7","span":{"begin":1627,"end":1629},"obj":"http://purl.obolibrary.org/obo/GO_0005783"},{"id":"T8","span":{"begin":1726,"end":1728},"obj":"http://purl.obolibrary.org/obo/GO_0005783"},{"id":"T9","span":{"begin":1979,"end":1981},"obj":"http://purl.obolibrary.org/obo/GO_0005783"},{"id":"T10","span":{"begin":1797,"end":1811},"obj":"http://purl.obolibrary.org/obo/GO_1902494"},{"id":"T11","span":{"begin":1804,"end":1824},"obj":"http://purl.obolibrary.org/obo/GO_0016592"},{"id":"T12","span":{"begin":1804,"end":1833},"obj":"http://purl.obolibrary.org/obo/GO_0070847"}],"text":"The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver.\nThe alpha- and beta-subunits of the hetero-dimeric glucosidase II complex from human liver were cloned and expressed in COS-1 cells. The 4106 bp full-length cDNA for the alpha-subunit contained a 2835 bp ORF encoding a 107 kDa polypeptide. The 2095 bp cDNA for the beta-subunit encodes a approximately 60 kDa protein in a continuous 1605 bp ORF. The alpha- and beta-subunits each contain two potential Asn-Xaa-Thr/Ser acceptor sites, with only one site in the alpha-subunit (Asn97) being glycosylated. Additional lambda-clones were isolated for each subunit containing in-frame insertions/deletions within the coding region, indicating alternative splicing. Analysis of different human tissues revealed approximately 4.4 kb and approximately 2.4 kb transcripts for alpha- and beta-subunit, respectively, consistent with their full-length cDNA. Coexpression of the alpha- and beta-subunits in COS-1 cells resulted in \u003e4-fold increase of glucosidase II activity. An inactive protein was obtained, however, after transfection with the alpha-subunit alone, showing that both subunits are essential for expression of active glucosidase II. The observation that the enzyme, previously purified from pig liver and lacking the beta-subunit, was catalytically active indicates that the beta-subunit is involved in alpha-subunit maturation rather than being required for enzymatic activity once the alpha-subunit has acquired its mature form. The alpha-subunit is expressed in COS-1 cells as an ER-located protein, whether inactive or part of a catalytically active complex. This suggests that ER-localization of the alpha-subunit, when associated with the dimeric enzyme complex, is mediated by the C-terminal HDEL-signal in the beta-subunit, whereas the apparently incompletely folded form of the inactive alpha-subunit could be retained in the ER by the putative \"glycoprotein-specific quality control machinery. \""}

UBERON-AE

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":135,"end":140},"obj":"http://purl.obolibrary.org/obo/UBERON_0002107"},{"id":"T2","span":{"begin":227,"end":232},"obj":"http://purl.obolibrary.org/obo/UBERON_0002107"},{"id":"T3","span":{"begin":1339,"end":1344},"obj":"http://purl.obolibrary.org/obo/UBERON_0002107"},{"id":"T4","span":{"begin":828,"end":835},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"}],"text":"The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver.\nThe alpha- and beta-subunits of the hetero-dimeric glucosidase II complex from human liver were cloned and expressed in COS-1 cells. The 4106 bp full-length cDNA for the alpha-subunit contained a 2835 bp ORF encoding a 107 kDa polypeptide. The 2095 bp cDNA for the beta-subunit encodes a approximately 60 kDa protein in a continuous 1605 bp ORF. The alpha- and beta-subunits each contain two potential Asn-Xaa-Thr/Ser acceptor sites, with only one site in the alpha-subunit (Asn97) being glycosylated. Additional lambda-clones were isolated for each subunit containing in-frame insertions/deletions within the coding region, indicating alternative splicing. Analysis of different human tissues revealed approximately 4.4 kb and approximately 2.4 kb transcripts for alpha- and beta-subunit, respectively, consistent with their full-length cDNA. Coexpression of the alpha- and beta-subunits in COS-1 cells resulted in \u003e4-fold increase of glucosidase II activity. An inactive protein was obtained, however, after transfection with the alpha-subunit alone, showing that both subunits are essential for expression of active glucosidase II. The observation that the enzyme, previously purified from pig liver and lacking the beta-subunit, was catalytically active indicates that the beta-subunit is involved in alpha-subunit maturation rather than being required for enzymatic activity once the alpha-subunit has acquired its mature form. The alpha-subunit is expressed in COS-1 cells as an ER-located protein, whether inactive or part of a catalytically active complex. This suggests that ER-localization of the alpha-subunit, when associated with the dimeric enzyme complex, is mediated by the C-terminal HDEL-signal in the beta-subunit, whereas the apparently incompletely folded form of the inactive alpha-subunit could be retained in the ER by the putative \"glycoprotein-specific quality control machinery. \""}

EDAM-topics

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":129,"end":134},"obj":"http://edamontology.org/topic_2815"},{"id":"T2","span":{"begin":221,"end":226},"obj":"http://edamontology.org/topic_2815"},{"id":"T3","span":{"begin":299,"end":303},"obj":"http://edamontology.org/topic_3512"},{"id":"T4","span":{"begin":394,"end":398},"obj":"http://edamontology.org/topic_3512"},{"id":"T5","span":{"begin":451,"end":458},"obj":"http://edamontology.org/topic_0078"},{"id":"T6","span":{"begin":778,"end":798},"obj":"http://edamontology.org/topic_3320"},{"id":"T7","span":{"begin":822,"end":827},"obj":"http://edamontology.org/topic_2815"},{"id":"T8","span":{"begin":891,"end":902},"obj":"http://edamontology.org/topic_3512"},{"id":"T9","span":{"begin":891,"end":902},"obj":"http://edamontology.org/topic_3308"},{"id":"T10","span":{"begin":891,"end":902},"obj":"http://edamontology.org/topic_0203"},{"id":"T11","span":{"begin":891,"end":902},"obj":"http://edamontology.org/topic_0110"},{"id":"T12","span":{"begin":891,"end":906},"obj":"http://edamontology.org/topic_0749"},{"id":"T13","span":{"begin":980,"end":984},"obj":"http://edamontology.org/topic_3512"},{"id":"T14","span":{"begin":1115,"end":1122},"obj":"http://edamontology.org/topic_0078"},{"id":"T15","span":{"begin":1638,"end":1645},"obj":"http://edamontology.org/topic_0078"},{"id":"T16","span":{"begin":1834,"end":1842},"obj":"http://edamontology.org/topic_0749"}],"text":"The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver.\nThe alpha- and beta-subunits of the hetero-dimeric glucosidase II complex from human liver were cloned and expressed in COS-1 cells. The 4106 bp full-length cDNA for the alpha-subunit contained a 2835 bp ORF encoding a 107 kDa polypeptide. The 2095 bp cDNA for the beta-subunit encodes a approximately 60 kDa protein in a continuous 1605 bp ORF. The alpha- and beta-subunits each contain two potential Asn-Xaa-Thr/Ser acceptor sites, with only one site in the alpha-subunit (Asn97) being glycosylated. Additional lambda-clones were isolated for each subunit containing in-frame insertions/deletions within the coding region, indicating alternative splicing. Analysis of different human tissues revealed approximately 4.4 kb and approximately 2.4 kb transcripts for alpha- and beta-subunit, respectively, consistent with their full-length cDNA. Coexpression of the alpha- and beta-subunits in COS-1 cells resulted in \u003e4-fold increase of glucosidase II activity. An inactive protein was obtained, however, after transfection with the alpha-subunit alone, showing that both subunits are essential for expression of active glucosidase II. The observation that the enzyme, previously purified from pig liver and lacking the beta-subunit, was catalytically active indicates that the beta-subunit is involved in alpha-subunit maturation rather than being required for enzymatic activity once the alpha-subunit has acquired its mature form. The alpha-subunit is expressed in COS-1 cells as an ER-located protein, whether inactive or part of a catalytically active complex. This suggests that ER-localization of the alpha-subunit, when associated with the dimeric enzyme complex, is mediated by the C-terminal HDEL-signal in the beta-subunit, whereas the apparently incompletely folded form of the inactive alpha-subunit could be retained in the ER by the putative \"glycoprotein-specific quality control machinery. \""}

EDAM-DFO

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":451,"end":458},"obj":"http://edamontology.org/data_1467"},{"id":"T2","span":{"begin":451,"end":458},"obj":"http://edamontology.org/format_1208"},{"id":"T3","span":{"begin":752,"end":765},"obj":"http://edamontology.org/data_1313"},{"id":"T4","span":{"begin":790,"end":808},"obj":"http://edamontology.org/operation_2499"},{"id":"T5","span":{"begin":800,"end":808},"obj":"http://edamontology.org/operation_2945"},{"id":"T6","span":{"begin":1115,"end":1122},"obj":"http://edamontology.org/format_1208"},{"id":"T7","span":{"begin":1115,"end":1122},"obj":"http://edamontology.org/data_1467"},{"id":"T8","span":{"begin":1638,"end":1645},"obj":"http://edamontology.org/data_1467"},{"id":"T9","span":{"begin":1638,"end":1645},"obj":"http://edamontology.org/format_1208"},{"id":"T10","span":{"begin":2021,"end":2036},"obj":"http://edamontology.org/operation_2428"}],"text":"The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver.\nThe alpha- and beta-subunits of the hetero-dimeric glucosidase II complex from human liver were cloned and expressed in COS-1 cells. The 4106 bp full-length cDNA for the alpha-subunit contained a 2835 bp ORF encoding a 107 kDa polypeptide. The 2095 bp cDNA for the beta-subunit encodes a approximately 60 kDa protein in a continuous 1605 bp ORF. The alpha- and beta-subunits each contain two potential Asn-Xaa-Thr/Ser acceptor sites, with only one site in the alpha-subunit (Asn97) being glycosylated. Additional lambda-clones were isolated for each subunit containing in-frame insertions/deletions within the coding region, indicating alternative splicing. Analysis of different human tissues revealed approximately 4.4 kb and approximately 2.4 kb transcripts for alpha- and beta-subunit, respectively, consistent with their full-length cDNA. Coexpression of the alpha- and beta-subunits in COS-1 cells resulted in \u003e4-fold increase of glucosidase II activity. An inactive protein was obtained, however, after transfection with the alpha-subunit alone, showing that both subunits are essential for expression of active glucosidase II. The observation that the enzyme, previously purified from pig liver and lacking the beta-subunit, was catalytically active indicates that the beta-subunit is involved in alpha-subunit maturation rather than being required for enzymatic activity once the alpha-subunit has acquired its mature form. The alpha-subunit is expressed in COS-1 cells as an ER-located protein, whether inactive or part of a catalytically active complex. This suggests that ER-localization of the alpha-subunit, when associated with the dimeric enzyme complex, is mediated by the C-terminal HDEL-signal in the beta-subunit, whereas the apparently incompletely folded form of the inactive alpha-subunit could be retained in the ER by the putative \"glycoprotein-specific quality control machinery. \""}

GlycoBiology-MAT

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":135,"end":140},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"T2","span":{"begin":227,"end":232},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"T3","span":{"begin":1339,"end":1344},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"}],"text":"The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver.\nThe alpha- and beta-subunits of the hetero-dimeric glucosidase II complex from human liver were cloned and expressed in COS-1 cells. The 4106 bp full-length cDNA for the alpha-subunit contained a 2835 bp ORF encoding a 107 kDa polypeptide. The 2095 bp cDNA for the beta-subunit encodes a approximately 60 kDa protein in a continuous 1605 bp ORF. The alpha- and beta-subunits each contain two potential Asn-Xaa-Thr/Ser acceptor sites, with only one site in the alpha-subunit (Asn97) being glycosylated. Additional lambda-clones were isolated for each subunit containing in-frame insertions/deletions within the coding region, indicating alternative splicing. Analysis of different human tissues revealed approximately 4.4 kb and approximately 2.4 kb transcripts for alpha- and beta-subunit, respectively, consistent with their full-length cDNA. Coexpression of the alpha- and beta-subunits in COS-1 cells resulted in \u003e4-fold increase of glucosidase II activity. An inactive protein was obtained, however, after transfection with the alpha-subunit alone, showing that both subunits are essential for expression of active glucosidase II. The observation that the enzyme, previously purified from pig liver and lacking the beta-subunit, was catalytically active indicates that the beta-subunit is involved in alpha-subunit maturation rather than being required for enzymatic activity once the alpha-subunit has acquired its mature form. The alpha-subunit is expressed in COS-1 cells as an ER-located protein, whether inactive or part of a catalytically active complex. This suggests that ER-localization of the alpha-subunit, when associated with the dimeric enzyme complex, is mediated by the C-terminal HDEL-signal in the beta-subunit, whereas the apparently incompletely folded form of the inactive alpha-subunit could be retained in the ER by the putative \"glycoprotein-specific quality control machinery. \""}

GlyTouCan-IUPAC

performance-test

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":828,"end":835},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":135,"end":140},"obj":"http://purl.obolibrary.org/obo/UBERON_0002107"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":227,"end":232},"obj":"http://purl.obolibrary.org/obo/UBERON_0002107"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":1339,"end":1344},"obj":"http://purl.obolibrary.org/obo/UBERON_0002107"}],"text":"The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver.\nThe alpha- and beta-subunits of the hetero-dimeric glucosidase II complex from human liver were cloned and expressed in COS-1 cells. The 4106 bp full-length cDNA for the alpha-subunit contained a 2835 bp ORF encoding a 107 kDa polypeptide. The 2095 bp cDNA for the beta-subunit encodes a approximately 60 kDa protein in a continuous 1605 bp ORF. The alpha- and beta-subunits each contain two potential Asn-Xaa-Thr/Ser acceptor sites, with only one site in the alpha-subunit (Asn97) being glycosylated. Additional lambda-clones were isolated for each subunit containing in-frame insertions/deletions within the coding region, indicating alternative splicing. Analysis of different human tissues revealed approximately 4.4 kb and approximately 2.4 kb transcripts for alpha- and beta-subunit, respectively, consistent with their full-length cDNA. Coexpression of the alpha- and beta-subunits in COS-1 cells resulted in \u003e4-fold increase of glucosidase II activity. An inactive protein was obtained, however, after transfection with the alpha-subunit alone, showing that both subunits are essential for expression of active glucosidase II. The observation that the enzyme, previously purified from pig liver and lacking the beta-subunit, was catalytically active indicates that the beta-subunit is involved in alpha-subunit maturation rather than being required for enzymatic activity once the alpha-subunit has acquired its mature form. The alpha-subunit is expressed in COS-1 cells as an ER-located protein, whether inactive or part of a catalytically active complex. This suggests that ER-localization of the alpha-subunit, when associated with the dimeric enzyme complex, is mediated by the C-terminal HDEL-signal in the beta-subunit, whereas the apparently incompletely folded form of the inactive alpha-subunit could be retained in the ER by the putative \"glycoprotein-specific quality control machinery. \""}

Anatomy-MAT

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":135,"end":140},"obj":"Body_part"},{"id":"T2","span":{"begin":227,"end":232},"obj":"Body_part"},{"id":"T3","span":{"begin":1339,"end":1344},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000097"}],"text":"The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver.\nThe alpha- and beta-subunits of the hetero-dimeric glucosidase II complex from human liver were cloned and expressed in COS-1 cells. The 4106 bp full-length cDNA for the alpha-subunit contained a 2835 bp ORF encoding a 107 kDa polypeptide. The 2095 bp cDNA for the beta-subunit encodes a approximately 60 kDa protein in a continuous 1605 bp ORF. The alpha- and beta-subunits each contain two potential Asn-Xaa-Thr/Ser acceptor sites, with only one site in the alpha-subunit (Asn97) being glycosylated. Additional lambda-clones were isolated for each subunit containing in-frame insertions/deletions within the coding region, indicating alternative splicing. Analysis of different human tissues revealed approximately 4.4 kb and approximately 2.4 kb transcripts for alpha- and beta-subunit, respectively, consistent with their full-length cDNA. Coexpression of the alpha- and beta-subunits in COS-1 cells resulted in \u003e4-fold increase of glucosidase II activity. An inactive protein was obtained, however, after transfection with the alpha-subunit alone, showing that both subunits are essential for expression of active glucosidase II. The observation that the enzyme, previously purified from pig liver and lacking the beta-subunit, was catalytically active indicates that the beta-subunit is involved in alpha-subunit maturation rather than being required for enzymatic activity once the alpha-subunit has acquired its mature form. The alpha-subunit is expressed in COS-1 cells as an ER-located protein, whether inactive or part of a catalytically active complex. This suggests that ER-localization of the alpha-subunit, when associated with the dimeric enzyme complex, is mediated by the C-terminal HDEL-signal in the beta-subunit, whereas the apparently incompletely folded form of the inactive alpha-subunit could be retained in the ER by the putative \"glycoprotein-specific quality control machinery. \""}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":129,"end":134},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":221,"end":226},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":822,"end":827},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"}],"text":"The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver.\nThe alpha- and beta-subunits of the hetero-dimeric glucosidase II complex from human liver were cloned and expressed in COS-1 cells. The 4106 bp full-length cDNA for the alpha-subunit contained a 2835 bp ORF encoding a 107 kDa polypeptide. The 2095 bp cDNA for the beta-subunit encodes a approximately 60 kDa protein in a continuous 1605 bp ORF. The alpha- and beta-subunits each contain two potential Asn-Xaa-Thr/Ser acceptor sites, with only one site in the alpha-subunit (Asn97) being glycosylated. Additional lambda-clones were isolated for each subunit containing in-frame insertions/deletions within the coding region, indicating alternative splicing. Analysis of different human tissues revealed approximately 4.4 kb and approximately 2.4 kb transcripts for alpha- and beta-subunit, respectively, consistent with their full-length cDNA. Coexpression of the alpha- and beta-subunits in COS-1 cells resulted in \u003e4-fold increase of glucosidase II activity. An inactive protein was obtained, however, after transfection with the alpha-subunit alone, showing that both subunits are essential for expression of active glucosidase II. The observation that the enzyme, previously purified from pig liver and lacking the beta-subunit, was catalytically active indicates that the beta-subunit is involved in alpha-subunit maturation rather than being required for enzymatic activity once the alpha-subunit has acquired its mature form. The alpha-subunit is expressed in COS-1 cells as an ER-located protein, whether inactive or part of a catalytically active complex. This suggests that ER-localization of the alpha-subunit, when associated with the dimeric enzyme complex, is mediated by the C-terminal HDEL-signal in the beta-subunit, whereas the apparently incompletely folded form of the inactive alpha-subunit could be retained in the ER by the putative \"glycoprotein-specific quality control machinery. \""}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":135,"end":140},"obj":"Body_part"},{"id":"T2","span":{"begin":227,"end":232},"obj":"Body_part"},{"id":"T3","span":{"begin":655,"end":661},"obj":"Body_part"},{"id":"T4","span":{"begin":1339,"end":1344},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002107"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002107"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0013424"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0002107"}],"text":"The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver.\nThe alpha- and beta-subunits of the hetero-dimeric glucosidase II complex from human liver were cloned and expressed in COS-1 cells. The 4106 bp full-length cDNA for the alpha-subunit contained a 2835 bp ORF encoding a 107 kDa polypeptide. The 2095 bp cDNA for the beta-subunit encodes a approximately 60 kDa protein in a continuous 1605 bp ORF. The alpha- and beta-subunits each contain two potential Asn-Xaa-Thr/Ser acceptor sites, with only one site in the alpha-subunit (Asn97) being glycosylated. Additional lambda-clones were isolated for each subunit containing in-frame insertions/deletions within the coding region, indicating alternative splicing. Analysis of different human tissues revealed approximately 4.4 kb and approximately 2.4 kb transcripts for alpha- and beta-subunit, respectively, consistent with their full-length cDNA. Coexpression of the alpha- and beta-subunits in COS-1 cells resulted in \u003e4-fold increase of glucosidase II activity. An inactive protein was obtained, however, after transfection with the alpha-subunit alone, showing that both subunits are essential for expression of active glucosidase II. The observation that the enzyme, previously purified from pig liver and lacking the beta-subunit, was catalytically active indicates that the beta-subunit is involved in alpha-subunit maturation rather than being required for enzymatic activity once the alpha-subunit has acquired its mature form. The alpha-subunit is expressed in COS-1 cells as an ER-located protein, whether inactive or part of a catalytically active complex. This suggests that ER-localization of the alpha-subunit, when associated with the dimeric enzyme complex, is mediated by the C-terminal HDEL-signal in the beta-subunit, whereas the apparently incompletely folded form of the inactive alpha-subunit could be retained in the ER by the putative \"glycoprotein-specific quality control machinery. \""}