PubMed:10764837 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":101},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":102,"end":372},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":373,"end":673},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":674,"end":918},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":919,"end":1046},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1047,"end":1180},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1181,"end":1310},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1311,"end":1470},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":101},"obj":"Sentence"},{"id":"T2","span":{"begin":102,"end":372},"obj":"Sentence"},{"id":"T3","span":{"begin":373,"end":673},"obj":"Sentence"},{"id":"T4","span":{"begin":674,"end":918},"obj":"Sentence"},{"id":"T5","span":{"begin":919,"end":1046},"obj":"Sentence"},{"id":"T6","span":{"begin":1047,"end":1180},"obj":"Sentence"},{"id":"T7","span":{"begin":1181,"end":1310},"obj":"Sentence"},{"id":"T8","span":{"begin":1311,"end":1470},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":101},"obj":"Sentence"},{"id":"T2","span":{"begin":102,"end":372},"obj":"Sentence"},{"id":"T3","span":{"begin":373,"end":673},"obj":"Sentence"},{"id":"T4","span":{"begin":674,"end":918},"obj":"Sentence"},{"id":"T5","span":{"begin":919,"end":1046},"obj":"Sentence"},{"id":"T6","span":{"begin":1047,"end":1180},"obj":"Sentence"},{"id":"T7","span":{"begin":1181,"end":1310},"obj":"Sentence"},{"id":"T8","span":{"begin":1311,"end":1470},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit.\nRecent purification and cDNA cloning of the endoplasmic reticulum processing enzyme glucosidase II have revealed that it is composed of two soluble proteins: a catalytic alpha-subunit and a beta-subunit of unknown function, both of which are highly conserved in mammals. Since the beta-subunit, which contains a C-terminal His-Asp-Glu-Leu (HDEL) motif, may function to link the catalytic subunit to the KDEL receptor as a retrieval mechanism, we sought to map the regions of the mouse beta-subunit protein responsible for mediating the association with the alpha-subunit. By screening a panel of recombinant beta-subunit glutathione S-transferase fusion proteins for the ability to precipitate glucosidase II activity, we have identified two non-overlapping interaction domains (ID1 and ID2) within the beta-subunit. ID1 encompasses 118 amino acids at the N-terminus of the mature polypeptide, spanning the cysteine-rich element in this region. ID2, located near the C-terminus, is contained within amino acids 273-400, a region occupied in part by a stretch of acidic residues. Variable usage of 7 alternatively spliced amino acids within ID2 was found not to influence the association of the two sub-units. We theorize that the catalytic subunit of glucosidase II binds synergistically to ID1 and ID2, explaining the high associative stability of the enzyme complex."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":146,"end":157},"obj":"FMAID:66856"},{"id":"_T2","span":{"begin":146,"end":157},"obj":"FMAID:165003"},{"id":"_T3","span":{"begin":146,"end":167},"obj":"FMAID:63842"},{"id":"_T4","span":{"begin":146,"end":167},"obj":"FMAID:66897"},{"id":"_T5","span":{"begin":146,"end":167},"obj":"FMAID:165027"},{"id":"_T6","span":{"begin":146,"end":167},"obj":"FMAID:66898"},{"id":"_T7","span":{"begin":146,"end":167},"obj":"FMAID:210679"},{"id":"_T8","span":{"begin":146,"end":167},"obj":"FMAID:165142"},{"id":"_T9","span":{"begin":146,"end":167},"obj":"FMAID:80351"},{"id":"_T10","span":{"begin":146,"end":167},"obj":"FMAID:188464"},{"id":"_T11","span":{"begin":146,"end":167},"obj":"FMAID:165026"},{"id":"_T12","span":{"begin":146,"end":167},"obj":"FMAID:162308"},{"id":"_T13","span":{"begin":146,"end":167},"obj":"FMAID:212510"},{"id":"_T14","span":{"begin":146,"end":167},"obj":"FMAID:67429"},{"id":"_T15","span":{"begin":146,"end":167},"obj":"FMAID:165250"},{"id":"_T16","span":{"begin":146,"end":167},"obj":"FMAID:199093"},{"id":"_T17","span":{"begin":146,"end":167},"obj":"FMAID:211269"},{"id":"_T18","span":{"begin":146,"end":167},"obj":"FMAID:210694"},{"id":"_T19","span":{"begin":146,"end":167},"obj":"FMAID:165144"},{"id":"_T20","span":{"begin":146,"end":167},"obj":"FMAID:67438"},{"id":"_T21","span":{"begin":146,"end":167},"obj":"FMAID:165141"},{"id":"_T22","span":{"begin":146,"end":167},"obj":"FMAID:67434"},{"id":"_T23","span":{"begin":158,"end":167},"obj":"FMAID:94520"},{"id":"_T24","span":{"begin":158,"end":167},"obj":"FMAID:7646"},{"id":"_T25","span":{"begin":250,"end":258},"obj":"FMAID:165447"},{"id":"_T26","span":{"begin":250,"end":258},"obj":"FMAID:67257"},{"id":"_T27","span":{"begin":558,"end":561},"obj":"FMAID:90078"},{"id":"_T28","span":{"begin":600,"end":607},"obj":"FMAID:67257"},{"id":"_T29","span":{"begin":600,"end":607},"obj":"FMAID:165447"},{"id":"_T30","span":{"begin":756,"end":764},"obj":"FMAID:165447"},{"id":"_T31","span":{"begin":756,"end":764},"obj":"FMAID:67257"},{"id":"_T32","span":{"begin":939,"end":950},"obj":"FMAID:196728"},{"id":"_T33","span":{"begin":939,"end":950},"obj":"FMAID:82739"},{"id":"_T34","span":{"begin":1009,"end":1017},"obj":"FMAID:196740"},{"id":"_T35","span":{"begin":1009,"end":1017},"obj":"FMAID:82751"},{"id":"_T36","span":{"begin":1101,"end":1112},"obj":"FMAID:196728"},{"id":"_T37","span":{"begin":1101,"end":1112},"obj":"FMAID:82739"},{"id":"_T38","span":{"begin":1223,"end":1234},"obj":"FMAID:82739"},{"id":"_T39","span":{"begin":1223,"end":1234},"obj":"FMAID:196728"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit.\nRecent purification and cDNA cloning of the endoplasmic reticulum processing enzyme glucosidase II have revealed that it is composed of two soluble proteins: a catalytic alpha-subunit and a beta-subunit of unknown function, both of which are highly conserved in mammals. Since the beta-subunit, which contains a C-terminal His-Asp-Glu-Leu (HDEL) motif, may function to link the catalytic subunit to the KDEL receptor as a retrieval mechanism, we sought to map the regions of the mouse beta-subunit protein responsible for mediating the association with the alpha-subunit. By screening a panel of recombinant beta-subunit glutathione S-transferase fusion proteins for the ability to precipitate glucosidase II activity, we have identified two non-overlapping interaction domains (ID1 and ID2) within the beta-subunit. ID1 encompasses 118 amino acids at the N-terminus of the mature polypeptide, spanning the cysteine-rich element in this region. ID2, located near the C-terminus, is contained within amino acids 273-400, a region occupied in part by a stretch of acidic residues. Variable usage of 7 alternatively spliced amino acids within ID2 was found not to influence the association of the two sub-units. We theorize that the catalytic subunit of glucosidase II binds synergistically to ID1 and ID2, explaining the high associative stability of the enzyme complex."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":28,"end":58},"obj":"http://www.uniprot.org/uniprot/P14314"},{"id":"T2","span":{"begin":272,"end":296},"obj":"http://www.uniprot.org/uniprot/P06865"},{"id":"T3","span":{"begin":723,"end":748},"obj":"http://www.uniprot.org/uniprot/O60760"},{"id":"T4","span":{"begin":723,"end":748},"obj":"http://www.uniprot.org/uniprot/Q7RTV2"},{"id":"T5","span":{"begin":723,"end":748},"obj":"http://www.uniprot.org/uniprot/P09211"},{"id":"T6","span":{"begin":723,"end":748},"obj":"http://www.uniprot.org/uniprot/P08263"},{"id":"T7","span":{"begin":723,"end":748},"obj":"http://www.uniprot.org/uniprot/Q16772"},{"id":"T8","span":{"begin":723,"end":748},"obj":"http://www.uniprot.org/uniprot/O15217"},{"id":"T9","span":{"begin":723,"end":748},"obj":"http://www.uniprot.org/uniprot/P09210"},{"id":"T10","span":{"begin":737,"end":748},"obj":"http://www.uniprot.org/uniprot/Q99484"},{"id":"T11","span":{"begin":881,"end":884},"obj":"http://www.uniprot.org/uniprot/Q5TE67"},{"id":"T12","span":{"begin":919,"end":922},"obj":"http://www.uniprot.org/uniprot/Q5TE67"},{"id":"T13","span":{"begin":1393,"end":1396},"obj":"http://www.uniprot.org/uniprot/Q5TE67"},{"id":"T14","span":{"begin":889,"end":892},"obj":"http://www.uniprot.org/uniprot/Q02363"},{"id":"T15","span":{"begin":1047,"end":1050},"obj":"http://www.uniprot.org/uniprot/Q02363"},{"id":"T16","span":{"begin":1242,"end":1245},"obj":"http://www.uniprot.org/uniprot/Q02363"},{"id":"T17","span":{"begin":1401,"end":1404},"obj":"http://www.uniprot.org/uniprot/Q02363"}],"text":"Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit.\nRecent purification and cDNA cloning of the endoplasmic reticulum processing enzyme glucosidase II have revealed that it is composed of two soluble proteins: a catalytic alpha-subunit and a beta-subunit of unknown function, both of which are highly conserved in mammals. Since the beta-subunit, which contains a C-terminal His-Asp-Glu-Leu (HDEL) motif, may function to link the catalytic subunit to the KDEL receptor as a retrieval mechanism, we sought to map the regions of the mouse beta-subunit protein responsible for mediating the association with the alpha-subunit. By screening a panel of recombinant beta-subunit glutathione S-transferase fusion proteins for the ability to precipitate glucosidase II activity, we have identified two non-overlapping interaction domains (ID1 and ID2) within the beta-subunit. ID1 encompasses 118 amino acids at the N-terminus of the mature polypeptide, spanning the cysteine-rich element in this region. ID2, located near the C-terminus, is contained within amino acids 273-400, a region occupied in part by a stretch of acidic residues. Variable usage of 7 alternatively spliced amino acids within ID2 was found not to influence the association of the two sub-units. We theorize that the catalytic subunit of glucosidase II binds synergistically to ID1 and ID2, explaining the high associative stability of the enzyme complex."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":28,"end":58},"obj":"http://www.uniprot.org/uniprot/O08795"},{"id":"T2","span":{"begin":723,"end":748},"obj":"http://www.uniprot.org/uniprot/Q9JHF7"},{"id":"T3","span":{"begin":737,"end":748},"obj":"http://www.uniprot.org/uniprot/P38649"}],"text":"Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit.\nRecent purification and cDNA cloning of the endoplasmic reticulum processing enzyme glucosidase II have revealed that it is composed of two soluble proteins: a catalytic alpha-subunit and a beta-subunit of unknown function, both of which are highly conserved in mammals. Since the beta-subunit, which contains a C-terminal His-Asp-Glu-Leu (HDEL) motif, may function to link the catalytic subunit to the KDEL receptor as a retrieval mechanism, we sought to map the regions of the mouse beta-subunit protein responsible for mediating the association with the alpha-subunit. By screening a panel of recombinant beta-subunit glutathione S-transferase fusion proteins for the ability to precipitate glucosidase II activity, we have identified two non-overlapping interaction domains (ID1 and ID2) within the beta-subunit. ID1 encompasses 118 amino acids at the N-terminus of the mature polypeptide, spanning the cysteine-rich element in this region. ID2, located near the C-terminus, is contained within amino acids 273-400, a region occupied in part by a stretch of acidic residues. Variable usage of 7 alternatively spliced amino acids within ID2 was found not to influence the association of the two sub-units. We theorize that the catalytic subunit of glucosidase II binds synergistically to ID1 and ID2, explaining the high associative stability of the enzyme complex."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":28,"end":32},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T2","span":{"begin":28,"end":32},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T3","span":{"begin":292,"end":296},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T4","span":{"begin":292,"end":296},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T5","span":{"begin":364,"end":371},"obj":"http://purl.bioontology.org/ontology/STY/T015"},{"id":"T6","span":{"begin":383,"end":387},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T7","span":{"begin":383,"end":387},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T8","span":{"begin":534,"end":543},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/127244"},{"id":"T9","span":{"begin":587,"end":591},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T10","span":{"begin":587,"end":591},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T11","span":{"begin":710,"end":714},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T12","span":{"begin":710,"end":714},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T13","span":{"begin":844,"end":847},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/604139"},{"id":"T14","span":{"begin":905,"end":909},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T15","span":{"begin":905,"end":909},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T16","span":{"begin":1374,"end":1389},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/2753"},{"id":"T17","span":{"begin":1374,"end":1389},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/649776"},{"id":"T18","span":{"begin":1374,"end":1389},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/649775"}],"text":"Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit.\nRecent purification and cDNA cloning of the endoplasmic reticulum processing enzyme glucosidase II have revealed that it is composed of two soluble proteins: a catalytic alpha-subunit and a beta-subunit of unknown function, both of which are highly conserved in mammals. Since the beta-subunit, which contains a C-terminal His-Asp-Glu-Leu (HDEL) motif, may function to link the catalytic subunit to the KDEL receptor as a retrieval mechanism, we sought to map the regions of the mouse beta-subunit protein responsible for mediating the association with the alpha-subunit. By screening a panel of recombinant beta-subunit glutathione S-transferase fusion proteins for the ability to precipitate glucosidase II activity, we have identified two non-overlapping interaction domains (ID1 and ID2) within the beta-subunit. ID1 encompasses 118 amino acids at the N-terminus of the mature polypeptide, spanning the cysteine-rich element in this region. ID2, located near the C-terminus, is contained within amino acids 273-400, a region occupied in part by a stretch of acidic residues. Variable usage of 7 alternatively spliced amino acids within ID2 was found not to influence the association of the two sub-units. We theorize that the catalytic subunit of glucosidase II binds synergistically to ID1 and ID2, explaining the high associative stability of the enzyme complex."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":796,"end":819},"obj":"http://purl.obolibrary.org/obo/GO_0033919"},{"id":"T2","span":{"begin":1215,"end":1222},"obj":"http://purl.obolibrary.org/obo/GO_0045292"}],"text":"Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit.\nRecent purification and cDNA cloning of the endoplasmic reticulum processing enzyme glucosidase II have revealed that it is composed of two soluble proteins: a catalytic alpha-subunit and a beta-subunit of unknown function, both of which are highly conserved in mammals. Since the beta-subunit, which contains a C-terminal His-Asp-Glu-Leu (HDEL) motif, may function to link the catalytic subunit to the KDEL receptor as a retrieval mechanism, we sought to map the regions of the mouse beta-subunit protein responsible for mediating the association with the alpha-subunit. By screening a panel of recombinant beta-subunit glutathione S-transferase fusion proteins for the ability to precipitate glucosidase II activity, we have identified two non-overlapping interaction domains (ID1 and ID2) within the beta-subunit. ID1 encompasses 118 amino acids at the N-terminus of the mature polypeptide, spanning the cysteine-rich element in this region. ID2, located near the C-terminus, is contained within amino acids 273-400, a region occupied in part by a stretch of acidic residues. Variable usage of 7 alternatively spliced amino acids within ID2 was found not to influence the association of the two sub-units. We theorize that the catalytic subunit of glucosidase II binds synergistically to ID1 and ID2, explaining the high associative stability of the enzyme complex."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":1368,"end":1373},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T2","span":{"begin":1368,"end":1373},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T3","span":{"begin":1368,"end":1373},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T4","span":{"begin":1368,"end":1373},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit.\nRecent purification and cDNA cloning of the endoplasmic reticulum processing enzyme glucosidase II have revealed that it is composed of two soluble proteins: a catalytic alpha-subunit and a beta-subunit of unknown function, both of which are highly conserved in mammals. Since the beta-subunit, which contains a C-terminal His-Asp-Glu-Leu (HDEL) motif, may function to link the catalytic subunit to the KDEL receptor as a retrieval mechanism, we sought to map the regions of the mouse beta-subunit protein responsible for mediating the association with the alpha-subunit. By screening a panel of recombinant beta-subunit glutathione S-transferase fusion proteins for the ability to precipitate glucosidase II activity, we have identified two non-overlapping interaction domains (ID1 and ID2) within the beta-subunit. ID1 encompasses 118 amino acids at the N-terminus of the mature polypeptide, spanning the cysteine-rich element in this region. ID2, located near the C-terminus, is contained within amino acids 273-400, a region occupied in part by a stretch of acidic residues. Variable usage of 7 alternatively spliced amino acids within ID2 was found not to influence the association of the two sub-units. We theorize that the catalytic subunit of glucosidase II binds synergistically to ID1 and ID2, explaining the high associative stability of the enzyme complex."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":146,"end":167},"obj":"http://purl.obolibrary.org/obo/GO_0005783"},{"id":"T2","span":{"begin":1455,"end":1469},"obj":"http://purl.obolibrary.org/obo/GO_1902494"}],"text":"Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit.\nRecent purification and cDNA cloning of the endoplasmic reticulum processing enzyme glucosidase II have revealed that it is composed of two soluble proteins: a catalytic alpha-subunit and a beta-subunit of unknown function, both of which are highly conserved in mammals. Since the beta-subunit, which contains a C-terminal His-Asp-Glu-Leu (HDEL) motif, may function to link the catalytic subunit to the KDEL receptor as a retrieval mechanism, we sought to map the regions of the mouse beta-subunit protein responsible for mediating the association with the alpha-subunit. By screening a panel of recombinant beta-subunit glutathione S-transferase fusion proteins for the ability to precipitate glucosidase II activity, we have identified two non-overlapping interaction domains (ID1 and ID2) within the beta-subunit. ID1 encompasses 118 amino acids at the N-terminus of the mature polypeptide, spanning the cysteine-rich element in this region. ID2, located near the C-terminus, is contained within amino acids 273-400, a region occupied in part by a stretch of acidic residues. Variable usage of 7 alternatively spliced amino acids within ID2 was found not to influence the association of the two sub-units. We theorize that the catalytic subunit of glucosidase II binds synergistically to ID1 and ID2, explaining the high associative stability of the enzyme complex."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":59,"end":67},"obj":"http://edamontology.org/topic_0602"},{"id":"T2","span":{"begin":126,"end":130},"obj":"http://edamontology.org/topic_3512"},{"id":"T3","span":{"begin":146,"end":167},"obj":"http://edamontology.org/topic_0616"},{"id":"T4","span":{"begin":250,"end":258},"obj":"http://edamontology.org/topic_0078"},{"id":"T5","span":{"begin":364,"end":371},"obj":"http://edamontology.org/topic_3048"},{"id":"T6","span":{"begin":416,"end":424},"obj":"http://edamontology.org/topic_0749"},{"id":"T7","span":{"begin":448,"end":453},"obj":"http://edamontology.org/topic_0158"},{"id":"T8","span":{"begin":558,"end":561},"obj":"http://edamontology.org/topic_0102"},{"id":"T9","span":{"begin":600,"end":607},"obj":"http://edamontology.org/topic_0078"},{"id":"T10","span":{"begin":756,"end":764},"obj":"http://edamontology.org/topic_0078"},{"id":"T11","span":{"begin":860,"end":871},"obj":"http://edamontology.org/topic_0602"},{"id":"T12","span":{"begin":939,"end":950},"obj":"http://edamontology.org/topic_0154"},{"id":"T13","span":{"begin":1101,"end":1112},"obj":"http://edamontology.org/topic_0154"},{"id":"T14","span":{"begin":1201,"end":1222},"obj":"http://edamontology.org/topic_3320"},{"id":"T15","span":{"begin":1223,"end":1234},"obj":"http://edamontology.org/topic_0154"}],"text":"Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit.\nRecent purification and cDNA cloning of the endoplasmic reticulum processing enzyme glucosidase II have revealed that it is composed of two soluble proteins: a catalytic alpha-subunit and a beta-subunit of unknown function, both of which are highly conserved in mammals. Since the beta-subunit, which contains a C-terminal His-Asp-Glu-Leu (HDEL) motif, may function to link the catalytic subunit to the KDEL receptor as a retrieval mechanism, we sought to map the regions of the mouse beta-subunit protein responsible for mediating the association with the alpha-subunit. By screening a panel of recombinant beta-subunit glutathione S-transferase fusion proteins for the ability to precipitate glucosidase II activity, we have identified two non-overlapping interaction domains (ID1 and ID2) within the beta-subunit. ID1 encompasses 118 amino acids at the N-terminus of the mature polypeptide, spanning the cysteine-rich element in this region. ID2, located near the C-terminus, is contained within amino acids 273-400, a region occupied in part by a stretch of acidic residues. Variable usage of 7 alternatively spliced amino acids within ID2 was found not to influence the association of the two sub-units. We theorize that the catalytic subunit of glucosidase II binds synergistically to ID1 and ID2, explaining the high associative stability of the enzyme complex."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":168,"end":178},"obj":"http://edamontology.org/operation_0004"},{"id":"T2","span":{"begin":168,"end":178},"obj":"http://edamontology.org/operation_2409"},{"id":"T3","span":{"begin":250,"end":258},"obj":"http://edamontology.org/data_1467"},{"id":"T4","span":{"begin":250,"end":258},"obj":"http://edamontology.org/format_1208"},{"id":"T5","span":{"begin":524,"end":533},"obj":"http://edamontology.org/operation_2422"},{"id":"T6","span":{"begin":558,"end":561},"obj":"http://edamontology.org/format_3285"},{"id":"T7","span":{"begin":558,"end":561},"obj":"http://edamontology.org/data_1274"},{"id":"T8","span":{"begin":558,"end":561},"obj":"http://edamontology.org/operation_2429"},{"id":"T9","span":{"begin":600,"end":607},"obj":"http://edamontology.org/format_1208"},{"id":"T10","span":{"begin":600,"end":607},"obj":"http://edamontology.org/data_1467"},{"id":"T11","span":{"begin":756,"end":764},"obj":"http://edamontology.org/data_1467"},{"id":"T12","span":{"begin":756,"end":764},"obj":"http://edamontology.org/format_1208"},{"id":"T13","span":{"begin":829,"end":839},"obj":"http://edamontology.org/data_2611"},{"id":"T14","span":{"begin":829,"end":839},"obj":"http://edamontology.org/data_0842"},{"id":"T15","span":{"begin":939,"end":953},"obj":"http://edamontology.org/data_0894"},{"id":"T16","span":{"begin":1171,"end":1179},"obj":"http://edamontology.org/data_1756"}],"text":"Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit.\nRecent purification and cDNA cloning of the endoplasmic reticulum processing enzyme glucosidase II have revealed that it is composed of two soluble proteins: a catalytic alpha-subunit and a beta-subunit of unknown function, both of which are highly conserved in mammals. Since the beta-subunit, which contains a C-terminal His-Asp-Glu-Leu (HDEL) motif, may function to link the catalytic subunit to the KDEL receptor as a retrieval mechanism, we sought to map the regions of the mouse beta-subunit protein responsible for mediating the association with the alpha-subunit. By screening a panel of recombinant beta-subunit glutathione S-transferase fusion proteins for the ability to precipitate glucosidase II activity, we have identified two non-overlapping interaction domains (ID1 and ID2) within the beta-subunit. ID1 encompasses 118 amino acids at the N-terminus of the mature polypeptide, spanning the cysteine-rich element in this region. ID2, located near the C-terminus, is contained within amino acids 273-400, a region occupied in part by a stretch of acidic residues. Variable usage of 7 alternatively spliced amino acids within ID2 was found not to influence the association of the two sub-units. We theorize that the catalytic subunit of glucosidase II binds synergistically to ID1 and ID2, explaining the high associative stability of the enzyme complex."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":935,"end":938},"obj":"http://www.glycoepitope.jp/epitopes/AN0571"}],"text":"Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit.\nRecent purification and cDNA cloning of the endoplasmic reticulum processing enzyme glucosidase II have revealed that it is composed of two soluble proteins: a catalytic alpha-subunit and a beta-subunit of unknown function, both of which are highly conserved in mammals. Since the beta-subunit, which contains a C-terminal His-Asp-Glu-Leu (HDEL) motif, may function to link the catalytic subunit to the KDEL receptor as a retrieval mechanism, we sought to map the regions of the mouse beta-subunit protein responsible for mediating the association with the alpha-subunit. By screening a panel of recombinant beta-subunit glutathione S-transferase fusion proteins for the ability to precipitate glucosidase II activity, we have identified two non-overlapping interaction domains (ID1 and ID2) within the beta-subunit. ID1 encompasses 118 amino acids at the N-terminus of the mature polypeptide, spanning the cysteine-rich element in this region. ID2, located near the C-terminus, is contained within amino acids 273-400, a region occupied in part by a stretch of acidic residues. Variable usage of 7 alternatively spliced amino acids within ID2 was found not to influence the association of the two sub-units. We theorize that the catalytic subunit of glucosidase II binds synergistically to ID1 and ID2, explaining the high associative stability of the enzyme complex."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":844,"end":847},"obj":"\"http://rdf.glycoinfo.org/glycan/G02780QX\""},{"id":"GlycanIUPAC_T2","span":{"begin":844,"end":847},"obj":"\"http://rdf.glycoinfo.org/glycan/G18425DX\""},{"id":"GlycanIUPAC_T3","span":{"begin":844,"end":847},"obj":"\"http://rdf.glycoinfo.org/glycan/G18630JE\""},{"id":"GlycanIUPAC_T4","span":{"begin":844,"end":847},"obj":"\"http://rdf.glycoinfo.org/glycan/G01004IT\""},{"id":"GlycanIUPAC_T5","span":{"begin":844,"end":847},"obj":"\"http://rdf.glycoinfo.org/glycan/G87301QZ\""},{"id":"GlycanIUPAC_T6","span":{"begin":844,"end":847},"obj":"\"http://rdf.glycoinfo.org/glycan/G39790GW\""},{"id":"GlycanIUPAC_T7","span":{"begin":844,"end":847},"obj":"\"http://rdf.glycoinfo.org/glycan/G42928BB\""},{"id":"GlycanIUPAC_T8","span":{"begin":844,"end":847},"obj":"\"http://rdf.glycoinfo.org/glycan/G51134HC\""},{"id":"GlycanIUPAC_T9","span":{"begin":844,"end":847},"obj":"\"http://rdf.glycoinfo.org/glycan/G68183GR\""},{"id":"GlycanIUPAC_T10","span":{"begin":844,"end":847},"obj":"\"http://rdf.glycoinfo.org/glycan/G46883FA\""},{"id":"GlycanIUPAC_T11","span":{"begin":844,"end":847},"obj":"\"http://rdf.glycoinfo.org/glycan/G54702VY\""}],"text":"Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit.\nRecent purification and cDNA cloning of the endoplasmic reticulum processing enzyme glucosidase II have revealed that it is composed of two soluble proteins: a catalytic alpha-subunit and a beta-subunit of unknown function, both of which are highly conserved in mammals. Since the beta-subunit, which contains a C-terminal His-Asp-Glu-Leu (HDEL) motif, may function to link the catalytic subunit to the KDEL receptor as a retrieval mechanism, we sought to map the regions of the mouse beta-subunit protein responsible for mediating the association with the alpha-subunit. By screening a panel of recombinant beta-subunit glutathione S-transferase fusion proteins for the ability to precipitate glucosidase II activity, we have identified two non-overlapping interaction domains (ID1 and ID2) within the beta-subunit. ID1 encompasses 118 amino acids at the N-terminus of the mature polypeptide, spanning the cysteine-rich element in this region. ID2, located near the C-terminus, is contained within amino acids 273-400, a region occupied in part by a stretch of acidic residues. Variable usage of 7 alternatively spliced amino acids within ID2 was found not to influence the association of the two sub-units. We theorize that the catalytic subunit of glucosidase II binds synergistically to ID1 and ID2, explaining the high associative stability of the enzyme complex."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":581,"end":586},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10088"},{"id":"A2","pred":"db_id","subj":"T1","obj":"10090"}],"text":"Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit.\nRecent purification and cDNA cloning of the endoplasmic reticulum processing enzyme glucosidase II have revealed that it is composed of two soluble proteins: a catalytic alpha-subunit and a beta-subunit of unknown function, both of which are highly conserved in mammals. Since the beta-subunit, which contains a C-terminal His-Asp-Glu-Leu (HDEL) motif, may function to link the catalytic subunit to the KDEL receptor as a retrieval mechanism, we sought to map the regions of the mouse beta-subunit protein responsible for mediating the association with the alpha-subunit. By screening a panel of recombinant beta-subunit glutathione S-transferase fusion proteins for the ability to precipitate glucosidase II activity, we have identified two non-overlapping interaction domains (ID1 and ID2) within the beta-subunit. ID1 encompasses 118 amino acids at the N-terminus of the mature polypeptide, spanning the cysteine-rich element in this region. ID2, located near the C-terminus, is contained within amino acids 273-400, a region occupied in part by a stretch of acidic residues. Variable usage of 7 alternatively spliced amino acids within ID2 was found not to influence the association of the two sub-units. We theorize that the catalytic subunit of glucosidase II binds synergistically to ID1 and ID2, explaining the high associative stability of the enzyme complex."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":158,"end":167},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0007361"}],"text":"Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit.\nRecent purification and cDNA cloning of the endoplasmic reticulum processing enzyme glucosidase II have revealed that it is composed of two soluble proteins: a catalytic alpha-subunit and a beta-subunit of unknown function, both of which are highly conserved in mammals. Since the beta-subunit, which contains a C-terminal His-Asp-Glu-Leu (HDEL) motif, may function to link the catalytic subunit to the KDEL receptor as a retrieval mechanism, we sought to map the regions of the mouse beta-subunit protein responsible for mediating the association with the alpha-subunit. By screening a panel of recombinant beta-subunit glutathione S-transferase fusion proteins for the ability to precipitate glucosidase II activity, we have identified two non-overlapping interaction domains (ID1 and ID2) within the beta-subunit. ID1 encompasses 118 amino acids at the N-terminus of the mature polypeptide, spanning the cysteine-rich element in this region. ID2, located near the C-terminus, is contained within amino acids 273-400, a region occupied in part by a stretch of acidic residues. Variable usage of 7 alternatively spliced amino acids within ID2 was found not to influence the association of the two sub-units. We theorize that the catalytic subunit of glucosidase II binds synergistically to ID1 and ID2, explaining the high associative stability of the enzyme complex."}