PubMed:15537790 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":114},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":115,"end":292},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":293,"end":502},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":503,"end":554},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":555,"end":708},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":709,"end":822},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":823,"end":907},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":908,"end":1023},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1024,"end":1157},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":114},"obj":"Sentence"},{"id":"T2","span":{"begin":115,"end":292},"obj":"Sentence"},{"id":"T3","span":{"begin":293,"end":502},"obj":"Sentence"},{"id":"T4","span":{"begin":503,"end":554},"obj":"Sentence"},{"id":"T5","span":{"begin":555,"end":708},"obj":"Sentence"},{"id":"T6","span":{"begin":709,"end":822},"obj":"Sentence"},{"id":"T7","span":{"begin":823,"end":907},"obj":"Sentence"},{"id":"T8","span":{"begin":908,"end":1023},"obj":"Sentence"},{"id":"T9","span":{"begin":1024,"end":1157},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":114},"obj":"Sentence"},{"id":"T2","span":{"begin":115,"end":292},"obj":"Sentence"},{"id":"T3","span":{"begin":293,"end":502},"obj":"Sentence"},{"id":"T4","span":{"begin":503,"end":554},"obj":"Sentence"},{"id":"T5","span":{"begin":555,"end":708},"obj":"Sentence"},{"id":"T6","span":{"begin":709,"end":822},"obj":"Sentence"},{"id":"T7","span":{"begin":823,"end":907},"obj":"Sentence"},{"id":"T8","span":{"begin":908,"end":1023},"obj":"Sentence"},{"id":"T9","span":{"begin":1024,"end":1157},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins.\nIn the endoplasmic reticulum (ER), misfolded proteins are retrotranslocated to the cytosol and degraded by the proteasome in a process known as ER-associated degradation (ERAD). Early in this pathway, a proposed lumenal ER lectin, EDEM, recognizes misfolded glycoproteins in the ER, disengages the nascent molecules from the folding pathway, and facilitates their targeting for disposal. In humans there are a total of three EDEM homologs. The amino acid sequences of these proteins are different from other lectins but are closely related to the Class I mannosidases (family 47 glycosidases). In this study, we characterize one of the EDEM homologs from Homo sapiens, which we have termed EDEM2 (C20orf31). Using recombinantly generated EDEM2, no alpha-1,2 mannosidase activity was observed. In HEK293 cells, recombinant EDEM2 is localized to the ER where it can associate with misfolded alpha1-antitrypsin. Overexpression of EDEM2 accelerates the degradation of misfolded alpha1-antitrypsin, indicating that the protein is involved in ERAD."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":6,"end":11},"obj":"http://www.uniprot.org/uniprot/Q9NVE6"},{"id":"T2","span":{"begin":805,"end":810},"obj":"http://www.uniprot.org/uniprot/Q9NVE6"},{"id":"T3","span":{"begin":853,"end":858},"obj":"http://www.uniprot.org/uniprot/Q9NVE6"},{"id":"T4","span":{"begin":937,"end":942},"obj":"http://www.uniprot.org/uniprot/Q9NVE6"},{"id":"T5","span":{"begin":812,"end":820},"obj":"http://www.uniprot.org/uniprot/Q9NVE6"},{"id":"T6","span":{"begin":71,"end":73},"obj":"http://www.uniprot.org/uniprot/P03372"},{"id":"T7","span":{"begin":145,"end":147},"obj":"http://www.uniprot.org/uniprot/P03372"},{"id":"T8","span":{"begin":259,"end":261},"obj":"http://www.uniprot.org/uniprot/P03372"},{"id":"T9","span":{"begin":335,"end":337},"obj":"http://www.uniprot.org/uniprot/P03372"},{"id":"T10","span":{"begin":394,"end":396},"obj":"http://www.uniprot.org/uniprot/P03372"},{"id":"T11","span":{"begin":963,"end":965},"obj":"http://www.uniprot.org/uniprot/P03372"},{"id":"T12","span":{"begin":335,"end":344},"obj":"http://www.uniprot.org/uniprot/Q96DZ1"},{"id":"T13","span":{"begin":346,"end":350},"obj":"http://www.uniprot.org/uniprot/Q92611"},{"id":"T14","span":{"begin":540,"end":544},"obj":"http://www.uniprot.org/uniprot/Q92611"},{"id":"T15","span":{"begin":751,"end":755},"obj":"http://www.uniprot.org/uniprot/Q92611"},{"id":"T16","span":{"begin":863,"end":884},"obj":"http://www.uniprot.org/uniprot/O60476"},{"id":"T17","span":{"begin":863,"end":884},"obj":"http://www.uniprot.org/uniprot/Q9UKM7"},{"id":"T18","span":{"begin":863,"end":884},"obj":"http://www.uniprot.org/uniprot/Q9BZQ6"},{"id":"T19","span":{"begin":863,"end":884},"obj":"http://www.uniprot.org/uniprot/Q5SRI9"},{"id":"T20","span":{"begin":863,"end":884},"obj":"http://www.uniprot.org/uniprot/Q9NR34"},{"id":"T21","span":{"begin":863,"end":884},"obj":"http://www.uniprot.org/uniprot/P33908"}],"text":"Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins.\nIn the endoplasmic reticulum (ER), misfolded proteins are retrotranslocated to the cytosol and degraded by the proteasome in a process known as ER-associated degradation (ERAD). Early in this pathway, a proposed lumenal ER lectin, EDEM, recognizes misfolded glycoproteins in the ER, disengages the nascent molecules from the folding pathway, and facilitates their targeting for disposal. In humans there are a total of three EDEM homologs. The amino acid sequences of these proteins are different from other lectins but are closely related to the Class I mannosidases (family 47 glycosidases). In this study, we characterize one of the EDEM homologs from Homo sapiens, which we have termed EDEM2 (C20orf31). Using recombinantly generated EDEM2, no alpha-1,2 mannosidase activity was observed. In HEK293 cells, recombinant EDEM2 is localized to the ER where it can associate with misfolded alpha1-antitrypsin. Overexpression of EDEM2 accelerates the degradation of misfolded alpha1-antitrypsin, indicating that the protein is involved in ERAD."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":71,"end":73},"obj":"http://www.uniprot.org/uniprot/P19785"},{"id":"T2","span":{"begin":145,"end":147},"obj":"http://www.uniprot.org/uniprot/P19785"},{"id":"T3","span":{"begin":259,"end":261},"obj":"http://www.uniprot.org/uniprot/P19785"},{"id":"T4","span":{"begin":335,"end":337},"obj":"http://www.uniprot.org/uniprot/P19785"},{"id":"T5","span":{"begin":394,"end":396},"obj":"http://www.uniprot.org/uniprot/P19785"},{"id":"T6","span":{"begin":963,"end":965},"obj":"http://www.uniprot.org/uniprot/P19785"},{"id":"T7","span":{"begin":335,"end":344},"obj":"http://www.uniprot.org/uniprot/Q8VEH8"}],"text":"Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins.\nIn the endoplasmic reticulum (ER), misfolded proteins are retrotranslocated to the cytosol and degraded by the proteasome in a process known as ER-associated degradation (ERAD). Early in this pathway, a proposed lumenal ER lectin, EDEM, recognizes misfolded glycoproteins in the ER, disengages the nascent molecules from the folding pathway, and facilitates their targeting for disposal. In humans there are a total of three EDEM homologs. The amino acid sequences of these proteins are different from other lectins but are closely related to the Class I mannosidases (family 47 glycosidases). In this study, we characterize one of the EDEM homologs from Homo sapiens, which we have termed EDEM2 (C20orf31). Using recombinantly generated EDEM2, no alpha-1,2 mannosidase activity was observed. In HEK293 cells, recombinant EDEM2 is localized to the ER where it can associate with misfolded alpha1-antitrypsin. Overexpression of EDEM2 accelerates the degradation of misfolded alpha1-antitrypsin, indicating that the protein is involved in ERAD."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":559,"end":579},"obj":"http://purl.bioontology.org/ontology/STY/T087"},{"id":"T2","span":{"begin":647,"end":654},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/353209"},{"id":"T3","span":{"begin":770,"end":774},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/9605"},{"id":"T4","span":{"begin":770,"end":782},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/9606"},{"id":"T5","span":{"begin":798,"end":804},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/62951"},{"id":"T6","span":{"begin":918,"end":923},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins.\nIn the endoplasmic reticulum (ER), misfolded proteins are retrotranslocated to the cytosol and degraded by the proteasome in a process known as ER-associated degradation (ERAD). Early in this pathway, a proposed lumenal ER lectin, EDEM, recognizes misfolded glycoproteins in the ER, disengages the nascent molecules from the folding pathway, and facilitates their targeting for disposal. In humans there are a total of three EDEM homologs. The amino acid sequences of these proteins are different from other lectins but are closely related to the Class I mannosidases (family 47 glycosidases). In this study, we characterize one of the EDEM homologs from Homo sapiens, which we have termed EDEM2 (C20orf31). Using recombinantly generated EDEM2, no alpha-1,2 mannosidase activity was observed. In HEK293 cells, recombinant EDEM2 is localized to the ER where it can associate with misfolded alpha1-antitrypsin. Overexpression of EDEM2 accelerates the degradation of misfolded alpha1-antitrypsin, indicating that the protein is involved in ERAD."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":74,"end":113},"obj":"http://purl.obolibrary.org/obo/GO_0097466"},{"id":"T2","span":{"begin":85,"end":96},"obj":"http://purl.obolibrary.org/obo/GO_0009056"},{"id":"T3","span":{"begin":273,"end":284},"obj":"http://purl.obolibrary.org/obo/GO_0009056"},{"id":"T4","span":{"begin":210,"end":218},"obj":"http://purl.obolibrary.org/obo/GO_0009056"},{"id":"T5","span":{"begin":85,"end":113},"obj":"http://purl.obolibrary.org/obo/GO_0006516"},{"id":"T6","span":{"begin":210,"end":236},"obj":"http://purl.obolibrary.org/obo/GO_1903009"},{"id":"T7","span":{"begin":226,"end":249},"obj":"http://purl.obolibrary.org/obo/GO_0043161"},{"id":"T8","span":{"begin":286,"end":290},"obj":"http://purl.obolibrary.org/obo/GO_0030433"},{"id":"T9","span":{"begin":1152,"end":1156},"obj":"http://purl.obolibrary.org/obo/GO_0030433"},{"id":"T10","span":{"begin":668,"end":682},"obj":"http://purl.obolibrary.org/obo/GO_0004571"},{"id":"T11","span":{"begin":863,"end":884},"obj":"http://purl.obolibrary.org/obo/GO_0004559"},{"id":"T12","span":{"begin":863,"end":884},"obj":"http://purl.obolibrary.org/obo/GO_0004571"},{"id":"T13","span":{"begin":863,"end":893},"obj":"http://purl.obolibrary.org/obo/GO_0004559"},{"id":"T14","span":{"begin":873,"end":893},"obj":"http://purl.obolibrary.org/obo/GO_0015923"},{"id":"T15","span":{"begin":946,"end":955},"obj":"http://purl.obolibrary.org/obo/GO_0051179"},{"id":"T16","span":{"begin":946,"end":965},"obj":"http://purl.obolibrary.org/obo/GO_0051643"}],"text":"Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins.\nIn the endoplasmic reticulum (ER), misfolded proteins are retrotranslocated to the cytosol and degraded by the proteasome in a process known as ER-associated degradation (ERAD). Early in this pathway, a proposed lumenal ER lectin, EDEM, recognizes misfolded glycoproteins in the ER, disengages the nascent molecules from the folding pathway, and facilitates their targeting for disposal. In humans there are a total of three EDEM homologs. The amino acid sequences of these proteins are different from other lectins but are closely related to the Class I mannosidases (family 47 glycosidases). In this study, we characterize one of the EDEM homologs from Homo sapiens, which we have termed EDEM2 (C20orf31). Using recombinantly generated EDEM2, no alpha-1,2 mannosidase activity was observed. In HEK293 cells, recombinant EDEM2 is localized to the ER where it can associate with misfolded alpha1-antitrypsin. Overexpression of EDEM2 accelerates the degradation of misfolded alpha1-antitrypsin, indicating that the protein is involved in ERAD."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":71,"end":73},"obj":"http://purl.obolibrary.org/obo/GO_0005783"},{"id":"T2","span":{"begin":145,"end":147},"obj":"http://purl.obolibrary.org/obo/GO_0005783"},{"id":"T3","span":{"begin":259,"end":261},"obj":"http://purl.obolibrary.org/obo/GO_0005783"},{"id":"T4","span":{"begin":335,"end":337},"obj":"http://purl.obolibrary.org/obo/GO_0005783"},{"id":"T5","span":{"begin":394,"end":396},"obj":"http://purl.obolibrary.org/obo/GO_0005783"},{"id":"T6","span":{"begin":963,"end":965},"obj":"http://purl.obolibrary.org/obo/GO_0005783"},{"id":"T7","span":{"begin":122,"end":143},"obj":"http://purl.obolibrary.org/obo/GO_0005783"},{"id":"T8","span":{"begin":198,"end":205},"obj":"http://purl.obolibrary.org/obo/GO_0005829"},{"id":"T9","span":{"begin":226,"end":236},"obj":"http://purl.obolibrary.org/obo/GO_0000502"},{"id":"T10","span":{"begin":327,"end":337},"obj":"http://purl.obolibrary.org/obo/GO_0005788"},{"id":"T11","span":{"begin":918,"end":923},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins.\nIn the endoplasmic reticulum (ER), misfolded proteins are retrotranslocated to the cytosol and degraded by the proteasome in a process known as ER-associated degradation (ERAD). Early in this pathway, a proposed lumenal ER lectin, EDEM, recognizes misfolded glycoproteins in the ER, disengages the nascent molecules from the folding pathway, and facilitates their targeting for disposal. In humans there are a total of three EDEM homologs. The amino acid sequences of these proteins are different from other lectins but are closely related to the Class I mannosidases (family 47 glycosidases). In this study, we characterize one of the EDEM homologs from Homo sapiens, which we have termed EDEM2 (C20orf31). Using recombinantly generated EDEM2, no alpha-1,2 mannosidase activity was observed. In HEK293 cells, recombinant EDEM2 is localized to the ER where it can associate with misfolded alpha1-antitrypsin. Overexpression of EDEM2 accelerates the degradation of misfolded alpha1-antitrypsin, indicating that the protein is involved in ERAD."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":0,"end":5},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":770,"end":782},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"}],"text":"Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins.\nIn the endoplasmic reticulum (ER), misfolded proteins are retrotranslocated to the cytosol and degraded by the proteasome in a process known as ER-associated degradation (ERAD). Early in this pathway, a proposed lumenal ER lectin, EDEM, recognizes misfolded glycoproteins in the ER, disengages the nascent molecules from the folding pathway, and facilitates their targeting for disposal. In humans there are a total of three EDEM homologs. The amino acid sequences of these proteins are different from other lectins but are closely related to the Class I mannosidases (family 47 glycosidases). In this study, we characterize one of the EDEM homologs from Homo sapiens, which we have termed EDEM2 (C20orf31). Using recombinantly generated EDEM2, no alpha-1,2 mannosidase activity was observed. In HEK293 cells, recombinant EDEM2 is localized to the ER where it can associate with misfolded alpha1-antitrypsin. Overexpression of EDEM2 accelerates the degradation of misfolded alpha1-antitrypsin, indicating that the protein is involved in ERAD."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":134,"end":143},"obj":"Body_part"},{"id":"T2","span":{"begin":198,"end":205},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0007361"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/GO_0005829"}],"text":"Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins.\nIn the endoplasmic reticulum (ER), misfolded proteins are retrotranslocated to the cytosol and degraded by the proteasome in a process known as ER-associated degradation (ERAD). Early in this pathway, a proposed lumenal ER lectin, EDEM, recognizes misfolded glycoproteins in the ER, disengages the nascent molecules from the folding pathway, and facilitates their targeting for disposal. In humans there are a total of three EDEM homologs. The amino acid sequences of these proteins are different from other lectins but are closely related to the Class I mannosidases (family 47 glycosidases). In this study, we characterize one of the EDEM homologs from Homo sapiens, which we have termed EDEM2 (C20orf31). Using recombinantly generated EDEM2, no alpha-1,2 mannosidase activity was observed. In HEK293 cells, recombinant EDEM2 is localized to the ER where it can associate with misfolded alpha1-antitrypsin. Overexpression of EDEM2 accelerates the degradation of misfolded alpha1-antitrypsin, indicating that the protein is involved in ERAD."}