
PubMed:15537790
Annnotations
sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
TextSentencer_T1 | 0-114 | Sentence | denotes | Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins. |
TextSentencer_T2 | 115-292 | Sentence | denotes | In 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). |
TextSentencer_T3 | 293-502 | Sentence | denotes | 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. |
TextSentencer_T4 | 503-554 | Sentence | denotes | In humans there are a total of three EDEM homologs. |
TextSentencer_T5 | 555-708 | Sentence | denotes | The amino acid sequences of these proteins are different from other lectins but are closely related to the Class I mannosidases (family 47 glycosidases). |
TextSentencer_T6 | 709-822 | Sentence | denotes | In this study, we characterize one of the EDEM homologs from Homo sapiens, which we have termed EDEM2 (C20orf31). |
TextSentencer_T7 | 823-907 | Sentence | denotes | Using recombinantly generated EDEM2, no alpha-1,2 mannosidase activity was observed. |
TextSentencer_T8 | 908-1023 | Sentence | denotes | In HEK293 cells, recombinant EDEM2 is localized to the ER where it can associate with misfolded alpha1-antitrypsin. |
TextSentencer_T9 | 1024-1157 | Sentence | denotes | Overexpression of EDEM2 accelerates the degradation of misfolded alpha1-antitrypsin, indicating that the protein is involved in ERAD. |
T1 | 0-114 | Sentence | denotes | Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins. |
T2 | 115-292 | Sentence | denotes | In 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). |
T3 | 293-502 | Sentence | denotes | 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. |
T4 | 503-554 | Sentence | denotes | In humans there are a total of three EDEM homologs. |
T5 | 555-708 | Sentence | denotes | The amino acid sequences of these proteins are different from other lectins but are closely related to the Class I mannosidases (family 47 glycosidases). |
T6 | 709-822 | Sentence | denotes | In this study, we characterize one of the EDEM homologs from Homo sapiens, which we have termed EDEM2 (C20orf31). |
T7 | 823-907 | Sentence | denotes | Using recombinantly generated EDEM2, no alpha-1,2 mannosidase activity was observed. |
T8 | 908-1023 | Sentence | denotes | In HEK293 cells, recombinant EDEM2 is localized to the ER where it can associate with misfolded alpha1-antitrypsin. |
T9 | 1024-1157 | Sentence | denotes | Overexpression of EDEM2 accelerates the degradation of misfolded alpha1-antitrypsin, indicating that the protein is involved in ERAD. |
T1 | 0-114 | Sentence | denotes | Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins. |
T2 | 115-292 | Sentence | denotes | In 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). |
T3 | 293-502 | Sentence | denotes | 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. |
T4 | 503-554 | Sentence | denotes | In humans there are a total of three EDEM homologs. |
T5 | 555-708 | Sentence | denotes | The amino acid sequences of these proteins are different from other lectins but are closely related to the Class I mannosidases (family 47 glycosidases). |
T6 | 709-822 | Sentence | denotes | In this study, we characterize one of the EDEM homologs from Homo sapiens, which we have termed EDEM2 (C20orf31). |
T7 | 823-907 | Sentence | denotes | Using recombinantly generated EDEM2, no alpha-1,2 mannosidase activity was observed. |
T8 | 908-1023 | Sentence | denotes | In HEK293 cells, recombinant EDEM2 is localized to the ER where it can associate with misfolded alpha1-antitrypsin. |
T9 | 1024-1157 | Sentence | denotes | Overexpression of EDEM2 accelerates the degradation of misfolded alpha1-antitrypsin, indicating that the protein is involved in ERAD. |
uniprot-human
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 6-11 | http://www.uniprot.org/uniprot/Q9NVE6 | denotes | EDEM2 |
T2 | 805-810 | http://www.uniprot.org/uniprot/Q9NVE6 | denotes | EDEM2 |
T3 | 853-858 | http://www.uniprot.org/uniprot/Q9NVE6 | denotes | EDEM2 |
T4 | 937-942 | http://www.uniprot.org/uniprot/Q9NVE6 | denotes | EDEM2 |
T5 | 812-820 | http://www.uniprot.org/uniprot/Q9NVE6 | denotes | C20orf31 |
T6 | 71-73 | http://www.uniprot.org/uniprot/P03372 | denotes | ER |
T7 | 145-147 | http://www.uniprot.org/uniprot/P03372 | denotes | ER |
T8 | 259-261 | http://www.uniprot.org/uniprot/P03372 | denotes | ER |
T9 | 335-337 | http://www.uniprot.org/uniprot/P03372 | denotes | ER |
T10 | 394-396 | http://www.uniprot.org/uniprot/P03372 | denotes | ER |
T11 | 963-965 | http://www.uniprot.org/uniprot/P03372 | denotes | ER |
T12 | 335-344 | http://www.uniprot.org/uniprot/Q96DZ1 | denotes | ER lectin |
T13 | 346-350 | http://www.uniprot.org/uniprot/Q92611 | denotes | EDEM |
T14 | 540-544 | http://www.uniprot.org/uniprot/Q92611 | denotes | EDEM |
T15 | 751-755 | http://www.uniprot.org/uniprot/Q92611 | denotes | EDEM |
T16 | 863-884 | http://www.uniprot.org/uniprot/O60476 | denotes | alpha-1,2 mannosidase |
T17 | 863-884 | http://www.uniprot.org/uniprot/Q9UKM7 | denotes | alpha-1,2 mannosidase |
T18 | 863-884 | http://www.uniprot.org/uniprot/Q9BZQ6 | denotes | alpha-1,2 mannosidase |
T19 | 863-884 | http://www.uniprot.org/uniprot/Q5SRI9 | denotes | alpha-1,2 mannosidase |
T20 | 863-884 | http://www.uniprot.org/uniprot/Q9NR34 | denotes | alpha-1,2 mannosidase |
T21 | 863-884 | http://www.uniprot.org/uniprot/P33908 | denotes | alpha-1,2 mannosidase |
uniprot-mouse
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 71-73 | http://www.uniprot.org/uniprot/P19785 | denotes | ER |
T2 | 145-147 | http://www.uniprot.org/uniprot/P19785 | denotes | ER |
T3 | 259-261 | http://www.uniprot.org/uniprot/P19785 | denotes | ER |
T4 | 335-337 | http://www.uniprot.org/uniprot/P19785 | denotes | ER |
T5 | 394-396 | http://www.uniprot.org/uniprot/P19785 | denotes | ER |
T6 | 963-965 | http://www.uniprot.org/uniprot/P19785 | denotes | ER |
T7 | 335-344 | http://www.uniprot.org/uniprot/Q8VEH8 | denotes | ER lectin |
GlycoBiology-NCBITAXON
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 559-579 | http://purl.bioontology.org/ontology/STY/T087 | denotes | amino acid sequences |
T2 | 647-654 | http://purl.bioontology.org/ontology/NCBITAXON/353209 | denotes | related |
T3 | 770-774 | http://purl.bioontology.org/ontology/NCBITAXON/9605 | denotes | Homo |
T4 | 770-782 | http://purl.bioontology.org/ontology/NCBITAXON/9606 | denotes | Homo sapiens |
T5 | 798-804 | http://purl.bioontology.org/ontology/NCBITAXON/62951 | denotes | termed |
T6 | 918-923 | http://purl.bioontology.org/ontology/STY/T025 | denotes | cells |
GO-BP
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 74-113 | http://purl.obolibrary.org/obo/GO_0097466 | denotes | associated degradation of glycoproteins |
T2 | 85-96 | http://purl.obolibrary.org/obo/GO_0009056 | denotes | degradation |
T3 | 273-284 | http://purl.obolibrary.org/obo/GO_0009056 | denotes | degradation |
T4 | 210-218 | http://purl.obolibrary.org/obo/GO_0009056 | denotes | degraded |
T5 | 85-113 | http://purl.obolibrary.org/obo/GO_0006516 | denotes | degradation of glycoproteins |
T6 | 210-236 | http://purl.obolibrary.org/obo/GO_1903009 | denotes | degraded by the proteasome |
T7 | 226-249 | http://purl.obolibrary.org/obo/GO_0043161 | denotes | proteasome in a process |
T8 | 286-290 | http://purl.obolibrary.org/obo/GO_0030433 | denotes | ERAD |
T9 | 1152-1156 | http://purl.obolibrary.org/obo/GO_0030433 | denotes | ERAD |
T10 | 668-682 | http://purl.obolibrary.org/obo/GO_0004571 | denotes | I mannosidases |
T11 | 863-884 | http://purl.obolibrary.org/obo/GO_0004559 | denotes | alpha-1,2 mannosidase |
T12 | 863-884 | http://purl.obolibrary.org/obo/GO_0004571 | denotes | alpha-1,2 mannosidase |
T13 | 863-893 | http://purl.obolibrary.org/obo/GO_0004559 | denotes | alpha-1,2 mannosidase activity |
T14 | 873-893 | http://purl.obolibrary.org/obo/GO_0015923 | denotes | mannosidase activity |
T15 | 946-955 | http://purl.obolibrary.org/obo/GO_0051179 | denotes | localized |
T16 | 946-965 | http://purl.obolibrary.org/obo/GO_0051643 | denotes | localized to the ER |
GO-CC
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 71-73 | http://purl.obolibrary.org/obo/GO_0005783 | denotes | ER |
T2 | 145-147 | http://purl.obolibrary.org/obo/GO_0005783 | denotes | ER |
T3 | 259-261 | http://purl.obolibrary.org/obo/GO_0005783 | denotes | ER |
T4 | 335-337 | http://purl.obolibrary.org/obo/GO_0005783 | denotes | ER |
T5 | 394-396 | http://purl.obolibrary.org/obo/GO_0005783 | denotes | ER |
T6 | 963-965 | http://purl.obolibrary.org/obo/GO_0005783 | denotes | ER |
T7 | 122-143 | http://purl.obolibrary.org/obo/GO_0005783 | denotes | endoplasmic reticulum |
T8 | 198-205 | http://purl.obolibrary.org/obo/GO_0005829 | denotes | cytosol |
T9 | 226-236 | http://purl.obolibrary.org/obo/GO_0000502 | denotes | proteasome |
T10 | 327-337 | http://purl.obolibrary.org/obo/GO_0005788 | denotes | lumenal ER |
T11 | 918-923 | http://purl.obolibrary.org/obo/GO_0005623 | denotes | cells |
Lectin-Jamboree
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 338-344 | lectin | denotes | lectin |
T2 | 623-630 | lectin | denotes | lectins |
Lectin-Jamboree-Sentence
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 0-114 | Sentence | denotes | Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins. |
T2 | 115-292 | Sentence | denotes | In 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). |
T3 | 293-502 | Sentence | denotes | 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. |
T4 | 503-554 | Sentence | denotes | In humans there are a total of three EDEM homologs. |
T5 | 555-708 | Sentence | denotes | The amino acid sequences of these proteins are different from other lectins but are closely related to the Class I mannosidases (family 47 glycosidases). |
T6 | 709-822 | Sentence | denotes | In this study, we characterize one of the EDEM homologs from Homo sapiens, which we have termed EDEM2 (C20orf31). |
T7 | 823-907 | Sentence | denotes | Using recombinantly generated EDEM2, no alpha-1,2 mannosidase activity was observed. |
T8 | 908-1023 | Sentence | denotes | In HEK293 cells, recombinant EDEM2 is localized to the ER where it can associate with misfolded alpha1-antitrypsin. |
T9 | 1024-1157 | Sentence | denotes | Overexpression of EDEM2 accelerates the degradation of misfolded alpha1-antitrypsin, indicating that the protein is involved in ERAD. |
NCBITAXON
Id | Subject | Object | Predicate | Lexical cue | db_id |
---|---|---|---|---|---|
T1 | 0-5 | OrganismTaxon | denotes | Human | 9606 |
T2 | 770-782 | OrganismTaxon | denotes | Homo sapiens | 9606 |
Anatomy-UBERON
Id | Subject | Object | Predicate | Lexical cue | uberon_id |
---|---|---|---|---|---|
T1 | 134-143 | Body_part | denotes | reticulum | http://purl.obolibrary.org/obo/UBERON_0007361 |
T2 | 198-205 | Body_part | denotes | cytosol | http://purl.obolibrary.org/obo/GO_0005829 |