#ID(s) interactor A	ID(s) interactor B	Alt. ID(s) interactor A	Alt. ID(s) interactor B	Alias(es) interactor A	Alias(es) interactor B	Interaction detection method(s)	Publication 1st author(s)	Publication Identifier(s)	Taxid interactor A	Taxid interactor B	Interaction type(s)	Source database(s)	Interaction identifier(s)	Confidence value(s)	Expansion method(s)	Biological role(s) interactor A	Biological role(s) interactor B	Experimental role(s) interactor A	Experimental role(s) interactor B	Type(s) interactor A	Type(s) interactor B	Xref(s) interactor A	Xref(s) interactor B	Interaction Xref(s)	Annotation(s) interactor A	Annotation(s) interactor B	Interaction annotation(s)	Host organism(s)	Interaction parameter(s)	Creation date	Update date	Checksum(s) interactor A	Checksum(s) interactor B	Interaction Checksum(s)	Negative	Feature(s) interactor A	Feature(s) interactor B	Stoichiometry(s) interactor A	Stoichiometry(s) interactor B	Identification method participant A	Identification method participant B
uniprotkb:P0DTD1-PRO_0000449628	uniprotkb:P0DTD1-PRO_0000449631	intact:EBI-25475880	intact:EBI-25475920	psi-mi:p0dtd1-pro_0000449628(display_long)|uniprotkb:rep(gene name)|psi-mi:rep(display_short)|uniprotkb:ORF1ab polyprotein(gene name synonym)|uniprotkb:1a-1b(orf name)	psi-mi:p0dtd1-pro_0000449631(display_long)|uniprotkb:rep(gene name)|psi-mi:rep(display_short)|uniprotkb:ORF1ab polyprotein(gene name synonym)|uniprotkb:1a-1b(orf name)	psi-mi:"MI:0114"(x-ray crystallography)	Moeller et al. (2021)	pubmed:33821277|imex:IM-28938	taxid:2697049(SARS-CoV-2)|taxid:2697049(SARS-CoV-2)	taxid:2697049(SARS-CoV-2)|taxid:2697049(SARS-CoV-2)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0469"(IntAct)	intact:EBI-26971334|pdbe:7MC5|imex:IM-28938-1|pdbe:7MC6	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	intact:EBI-25492095(chain-parent)|uniprotkb:P0DTD1(chain-parent)	intact:EBI-25492095(chain-parent)|uniprotkb:P0DTD1(chain-parent)	-	chain-seq-start:4254|chain-seq-end:4392	chain-seq-start:5926|chain-seq-end:6452	figure legend:Table 2|dataset:Virus - Publications including interactions involving viral proteins|dataset:Coronavirus - Interactions investigated in the context of Coronavirus|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:83333(ecoli)|taxid:83333("Escherichia coli (strain K12)")	-	2021/05/06	2021/05/06	rogid:L4eD+20oc1IdNFJ9By3H2uun6L02697049	rogid:LpGB5BQU5uhWK/60422jkiKHRL82697049	rigid:31XhqL6F4tfEjhLqU/s/PXVionw	false	-	sufficient binding region:3-289|mutation:191-191	-	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
intenz:3.1.13	intact:EBI-26973610	intact:EBI-25564924|intact:EBI-25492032|reactome:R-COV-9694688|wwpdb:7diy|wwpdb:7mc6|wwpdb:7mc5|wwpdb:7n0c|emdb:EMD-24103|wwpdb:7n0d|emdb:EMD-24104|wwpdb:7n0b|emdb:EMD-24102	-	psi-mi:nsp10-nsp14_sars2-1(display_short)|psi-mi:3.1.13(display_long)|intact:SARS-CoV-2 3'-5' exoribonuclease proof-reading complex(complex recommended name)|intact:"NSP10:NSP14"(complex systematic name)|intact:SARS-CoV-2 NSP14/NSP10 complex(complex synonym)	psi-mi:ls2u rna(display_short)|psi-mi:EBI-26973610(display_long)	psi-mi:"MI:0920"(ribonuclease assay)	Moeller et al. (2021)	pubmed:33821277|imex:IM-28938	taxid:2697049(SARS-CoV-2)|taxid:2697049(SARS-CoV-2)	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	psi-mi:"MI:0902"(rna cleavage)	psi-mi:"MI:0469"(IntAct)	intact:EBI-26973606|imex:IM-28938-2	-	-	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:1302"(stable complex)	psi-mi:"MI:0320"(ribonucleic acid)	go:"GO:0000175"(3'-5'-exoribonuclease activity)|go:"GO:0003725"(double-stranded RNA binding)|go:"GO:0039694"(viral RNA genome replication)|go:"GO:1905354"(exoribonuclease complex)|pubmed:31440227(see-also)|pubmed:29279395(see-also)|efo:"EFO:0000694"(see-also)|pubmed:32015508(see-also)|pubmed:31987001(see-also)|complex portal:CPX-5692(complex-primary)|evidence ontology:"ECO:0000353"|pubmed:33821277(see-also)|intact:EBI-26971334(exp-evidence)	-	go:"GO:0004532"(exoribonuclease activity)	curated-complex:"The SARS-CoV-2 coronavirus 3'-5' exoribonuclease complex which strictly targets double-stranded RNA and can selectively remove a mismatched ribonucleotide at the 3'-end of a dsRNA substrate. Formation of the NSP10-NSP14 complex strongly enhances the exonuclease activity of the bifunctional NSP14 and enhances the fidelity of RNA synthesis by correcting nucleotide incorporation errors made by the RNA-dependent RNA polymerase. May bind to, and act with the nsp7/nsp8/nsp12 polymerase complex (CPX-5742). Proof-reading exonuclease activity may explain why coronaviruses have the largest RNA genomes known to date. Complex formation does not appear to effect the C-terminal N7-methyltransferase activity of NSP14 involved in RNA cap modification."|disease:"Severe acute respiratory syndrome (SARS) [EFO:0000694]: A viral respiratory infection caused by the SARS coronavirus. It is transmitted through close person-to-person contact. It is manifested with high fever, headache, dry cough and myalgias. It may progress to pneumonia and cause death."|complex-properties:NSP10 forms a homododecamer in isolation. A flexible N-terminal domain of NSP14 forms the NSP10 docking site and induces conformational changes in the NSP14 that modulate the distance between the catalytic residues.	-	figure legend:4a|dataset:Virus - Publications including interactions involving viral proteins|dataset:Coronavirus - Interactions investigated in the context of Coronavirus|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2021/05/06	2021/08/17	-	-	-	false	sufficient binding region:1-289|mutation disrupting interaction rate:191-191|mutation decreasing interaction rate:9-9|mutation decreasing interaction rate:61-61|mutation decreasing interaction rate:139-139	fluorescein label:1-1	-	-	psi-mi:"MI:0866"(tag visualisation)	psi-mi:"MI:0866"(tag visualisation)
intact:EBI-26973632	intact:EBI-26973610	-	-	psi-mi:ls15a rna(display_short)|psi-mi:EBI-26973632(display_long)	psi-mi:ls2u rna(display_short)|psi-mi:EBI-26973610(display_long)	psi-mi:"MI:0920"(ribonuclease assay)	Moeller et al. (2021)	pubmed:33821277|imex:IM-28938	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	psi-mi:"MI:0902"(rna cleavage)	psi-mi:"MI:0469"(IntAct)	intact:EBI-26973626|imex:IM-28938-4	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0840"(stimulator)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0320"(ribonucleic acid)	psi-mi:"MI:0320"(ribonucleic acid)	-	-	go:"GO:0004532"(exoribonuclease activity)	-	-	figure legend:SF1|dataset:Virus - Publications including interactions involving viral proteins|dataset:Coronavirus - Interactions investigated in the context of Coronavirus|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2021/05/06	2021/08/23	-	-	-	false	-	fluorescein label:1-1	-	-	psi-mi:"MI:0866"(tag visualisation)	psi-mi:"MI:0866"(tag visualisation)
intact:EBI-26973632	reactome:R-COV-9682545	-	intact:EBI-25496027|wwpdb:5c8s|intenz:3.1.13|wwpdb:5c8t|wwpdb:5c8u|wwpdb:5nfy	psi-mi:ls15a rna(display_short)|psi-mi:EBI-26973632(display_long)	psi-mi:nsp10-nsp14_cvhsa(display_short)|psi-mi:R-COV-9682545(display_long)|intact:SARS-CoV 3'-5' exoribonuclease proof-reading complex(complex recommended name)|intact:"NSP10:NSP14"(complex systematic name)|intact:SARS-CoV NSP14/NSP10 complex(complex synonym)	psi-mi:"MI:0920"(ribonuclease assay)	Moeller et al. (2021)	pubmed:33821277|imex:IM-28938	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:694009(sars-cov)|taxid:694009(Human SARS coronavirus)	psi-mi:"MI:0902"(rna cleavage)	psi-mi:"MI:0469"(IntAct)	intact:EBI-26973626|imex:IM-28938-4	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0840"(stimulator)	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0320"(ribonucleic acid)	psi-mi:"MI:1302"(stable complex)	-	evidence ontology:"ECO:0000353"|efo:"EFO:0000694"(see-also)|pubmed:29279395(see-also)|pubmed:26159422(see-also)|complex portal:CPX-5707(complex-primary)|go:"GO:0000175"(3'-5'-exoribonuclease activity)|go:"GO:1905354"(exoribonuclease complex)|go:"GO:0003725"(double-stranded RNA binding)|go:"GO:0039694"(viral RNA genome replication)|pubmed:31440227(see-also)|intact:EBI-25499834(exp-evidence)|pubmed:18255185(see-also)	go:"GO:0004532"(exoribonuclease activity)	-	curated-complex:"The SARS-CoV coronavirus 3'-5' exoribonuclease complex which strictly targets double-stranded RNA and can also selectively remove a mismatched ribonucleotide at the 3'-end of a dsRNA substrate. Formation of the NSP10-NSP14 complex strongly enhances the exonuclease activity of the bifunctional NSP14 and enhances the fidelity of RNA synthesis by correcting nucleotide incorporation errors made by the RNA-dependent RNA polymerase. May bind to, and act with the nsp7/nsp8/nsp12 polymerase complex (CPX-5717). Proof-reading exonuclease activity may explain why coronaviruses have the largest RNA genomes known to date. Complex formation does not appear to effect the C-terminal N7-methyltransferase activity of NSP14 involved in RNA cap modification."|disease:"Severe acute respiratory syndrome (SARS) [EFO:0000694]: A viral respiratory infection caused by the SARS coronavirus. It is transmitted through close person-to-person contact. It is manifested with high fever, headache, dry cough and myalgias. It may progress to pneumonia and cause death."|complex-assembly:Heterodimer|complex-properties:NSP10 forms a homododecamer in isolation. A flexible N-terminal domain of NSP14 forms the NSP10 docking site and induces conformational changes in the NSP14 that modulate the distance between the catalytic residues.	figure legend:SF1|dataset:Virus - Publications including interactions involving viral proteins|dataset:Coronavirus - Interactions investigated in the context of Coronavirus|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2021/05/06	2021/08/23	-	-	-	false	-	sufficient binding region:1..1-287..287	-	-	psi-mi:"MI:0866"(tag visualisation)	psi-mi:"MI:0866"(tag visualisation)
intact:EBI-26973632	intact:EBI-26973610	-	-	psi-mi:ls15a rna(display_short)|psi-mi:EBI-26973632(display_long)	psi-mi:ls2u rna(display_short)|psi-mi:EBI-26973610(display_long)	psi-mi:"MI:0920"(ribonuclease assay)	Moeller et al. (2021)	pubmed:33821277|imex:IM-28938	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	psi-mi:"MI:0902"(rna cleavage)	psi-mi:"MI:0469"(IntAct)	intact:EBI-26973635|imex:IM-28938-6	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0840"(stimulator)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0320"(ribonucleic acid)	psi-mi:"MI:0320"(ribonucleic acid)	-	-	go:"GO:0004532"(exoribonuclease activity)	-	-	figure legend:1a, 1b|comment:"More extensive degradation was observed when LS2U RNA was annealed to an unlabeled 40-nt template strand (LS15A_RNA) to generate a double-stranded (ds) RNA with a 20-nt 5'-overhang"|dataset:Virus - Publications including interactions involving viral proteins|dataset:Coronavirus - Interactions investigated in the context of Coronavirus|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2021/05/06	2021/08/23	-	-	-	false	mutation with no effect:21-21	fluorescein label:1-1	-	-	psi-mi:"MI:0866"(tag visualisation)	psi-mi:"MI:0866"(tag visualisation)
intact:EBI-26973632	intenz:3.1.13	-	intact:EBI-25564924|intact:EBI-25492032|reactome:R-COV-9694688|wwpdb:7diy|wwpdb:7mc6|wwpdb:7mc5|wwpdb:7n0c|emdb:EMD-24103|wwpdb:7n0d|emdb:EMD-24104|wwpdb:7n0b|emdb:EMD-24102	psi-mi:ls15a rna(display_short)|psi-mi:EBI-26973632(display_long)	psi-mi:nsp10-nsp14_sars2-1(display_short)|psi-mi:3.1.13(display_long)|intact:SARS-CoV-2 3'-5' exoribonuclease proof-reading complex(complex recommended name)|intact:"NSP10:NSP14"(complex systematic name)|intact:SARS-CoV-2 NSP14/NSP10 complex(complex synonym)	psi-mi:"MI:0920"(ribonuclease assay)	Moeller et al. (2021)	pubmed:33821277|imex:IM-28938	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:2697049(SARS-CoV-2)|taxid:2697049(SARS-CoV-2)	psi-mi:"MI:0902"(rna cleavage)	psi-mi:"MI:0469"(IntAct)	intact:EBI-26973635|imex:IM-28938-6	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0840"(stimulator)	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0320"(ribonucleic acid)	psi-mi:"MI:1302"(stable complex)	-	go:"GO:0000175"(3'-5'-exoribonuclease activity)|go:"GO:0003725"(double-stranded RNA binding)|go:"GO:0039694"(viral RNA genome replication)|go:"GO:1905354"(exoribonuclease complex)|pubmed:31440227(see-also)|pubmed:29279395(see-also)|efo:"EFO:0000694"(see-also)|pubmed:32015508(see-also)|pubmed:31987001(see-also)|complex portal:CPX-5692(complex-primary)|evidence ontology:"ECO:0000353"|pubmed:33821277(see-also)|intact:EBI-26971334(exp-evidence)	go:"GO:0004532"(exoribonuclease activity)	-	curated-complex:"The SARS-CoV-2 coronavirus 3'-5' exoribonuclease complex which strictly targets double-stranded RNA and can selectively remove a mismatched ribonucleotide at the 3'-end of a dsRNA substrate. Formation of the NSP10-NSP14 complex strongly enhances the exonuclease activity of the bifunctional NSP14 and enhances the fidelity of RNA synthesis by correcting nucleotide incorporation errors made by the RNA-dependent RNA polymerase. May bind to, and act with the nsp7/nsp8/nsp12 polymerase complex (CPX-5742). Proof-reading exonuclease activity may explain why coronaviruses have the largest RNA genomes known to date. Complex formation does not appear to effect the C-terminal N7-methyltransferase activity of NSP14 involved in RNA cap modification."|disease:"Severe acute respiratory syndrome (SARS) [EFO:0000694]: A viral respiratory infection caused by the SARS coronavirus. It is transmitted through close person-to-person contact. It is manifested with high fever, headache, dry cough and myalgias. It may progress to pneumonia and cause death."|complex-properties:NSP10 forms a homododecamer in isolation. A flexible N-terminal domain of NSP14 forms the NSP10 docking site and induces conformational changes in the NSP14 that modulate the distance between the catalytic residues.	figure legend:1a, 1b|comment:"More extensive degradation was observed when LS2U RNA was annealed to an unlabeled 40-nt template strand (LS15A_RNA) to generate a double-stranded (ds) RNA with a 20-nt 5'-overhang"|dataset:Virus - Publications including interactions involving viral proteins|dataset:Coronavirus - Interactions investigated in the context of Coronavirus|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2021/05/06	2021/08/23	-	-	-	false	mutation with no effect:21-21	sufficient binding region:1-289	-	-	psi-mi:"MI:0866"(tag visualisation)	psi-mi:"MI:0866"(tag visualisation)
intenz:3.1.13	intact:EBI-27069181	intact:EBI-25564924|intact:EBI-25492032|reactome:R-COV-9694688|wwpdb:7diy|wwpdb:7mc6|wwpdb:7mc5|wwpdb:7n0c|emdb:EMD-24103|wwpdb:7n0d|emdb:EMD-24104|wwpdb:7n0b|emdb:EMD-24102	-	psi-mi:nsp10-nsp14_sars2-1(display_short)|psi-mi:3.1.13(display_long)|intact:SARS-CoV-2 3'-5' exoribonuclease proof-reading complex(complex recommended name)|intact:"NSP10:NSP14"(complex systematic name)|intact:SARS-CoV-2 NSP14/NSP10 complex(complex synonym)	psi-mi:poly a rna(display_short)|psi-mi:EBI-27069181(display_long)	psi-mi:"MI:0920"(ribonuclease assay)	Moeller et al. (2021)	pubmed:33821277|imex:IM-28938	taxid:2697049(SARS-CoV-2)|taxid:2697049(SARS-CoV-2)	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	psi-mi:"MI:0902"(rna cleavage)	psi-mi:"MI:0469"(IntAct)	intact:EBI-27069166|imex:IM-28938-7	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0684"(ancillary)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:1302"(stable complex)	psi-mi:"MI:0320"(ribonucleic acid)	go:"GO:0000175"(3'-5'-exoribonuclease activity)|go:"GO:0003725"(double-stranded RNA binding)|go:"GO:0039694"(viral RNA genome replication)|go:"GO:1905354"(exoribonuclease complex)|pubmed:31440227(see-also)|pubmed:29279395(see-also)|efo:"EFO:0000694"(see-also)|pubmed:32015508(see-also)|pubmed:31987001(see-also)|complex portal:CPX-5692(complex-primary)|evidence ontology:"ECO:0000353"|pubmed:33821277(see-also)|intact:EBI-26971334(exp-evidence)	-	go:"GO:0004532"(exoribonuclease activity)	curated-complex:"The SARS-CoV-2 coronavirus 3'-5' exoribonuclease complex which strictly targets double-stranded RNA and can selectively remove a mismatched ribonucleotide at the 3'-end of a dsRNA substrate. Formation of the NSP10-NSP14 complex strongly enhances the exonuclease activity of the bifunctional NSP14 and enhances the fidelity of RNA synthesis by correcting nucleotide incorporation errors made by the RNA-dependent RNA polymerase. May bind to, and act with the nsp7/nsp8/nsp12 polymerase complex (CPX-5742). Proof-reading exonuclease activity may explain why coronaviruses have the largest RNA genomes known to date. Complex formation does not appear to effect the C-terminal N7-methyltransferase activity of NSP14 involved in RNA cap modification."|disease:"Severe acute respiratory syndrome (SARS) [EFO:0000694]: A viral respiratory infection caused by the SARS coronavirus. It is transmitted through close person-to-person contact. It is manifested with high fever, headache, dry cough and myalgias. It may progress to pneumonia and cause death."|complex-properties:NSP10 forms a homododecamer in isolation. A flexible N-terminal domain of NSP14 forms the NSP10 docking site and induces conformational changes in the NSP14 that modulate the distance between the catalytic residues.	-	figure legend:1c|comment:A 20-nt poly-U RNA, which is less likely to adopt secondary structures did not serve as a substrate by itself but was degraded extensively when supplemented with a complementary 30-nt poly-A RNA|dataset:Virus - Publications including interactions involving viral proteins|dataset:Coronavirus - Interactions investigated in the context of Coronavirus|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2021/05/06	2021/08/23	-	-	-	false	mutation disrupting interaction rate:191-191|sufficient binding region:1-289	-	-	-	psi-mi:"MI:0866"(tag visualisation)	psi-mi:"MI:0866"(tag visualisation)
intenz:3.1.13	intact:EBI-27069153	intact:EBI-25564924|intact:EBI-25492032|reactome:R-COV-9694688|wwpdb:7diy|wwpdb:7mc6|wwpdb:7mc5|wwpdb:7n0c|emdb:EMD-24103|wwpdb:7n0d|emdb:EMD-24104|wwpdb:7n0b|emdb:EMD-24102	-	psi-mi:nsp10-nsp14_sars2-1(display_short)|psi-mi:3.1.13(display_long)|intact:SARS-CoV-2 3'-5' exoribonuclease proof-reading complex(complex recommended name)|intact:"NSP10:NSP14"(complex systematic name)|intact:SARS-CoV-2 NSP14/NSP10 complex(complex synonym)	psi-mi:poly u rna(display_short)|psi-mi:EBI-27069153(display_long)	psi-mi:"MI:0920"(ribonuclease assay)	Moeller et al. (2021)	pubmed:33821277|imex:IM-28938	taxid:2697049(SARS-CoV-2)|taxid:2697049(SARS-CoV-2)	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	psi-mi:"MI:0902"(rna cleavage)	psi-mi:"MI:0469"(IntAct)	intact:EBI-27069166|imex:IM-28938-7	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:1302"(stable complex)	psi-mi:"MI:0320"(ribonucleic acid)	go:"GO:0000175"(3'-5'-exoribonuclease activity)|go:"GO:0003725"(double-stranded RNA binding)|go:"GO:0039694"(viral RNA genome replication)|go:"GO:1905354"(exoribonuclease complex)|pubmed:31440227(see-also)|pubmed:29279395(see-also)|efo:"EFO:0000694"(see-also)|pubmed:32015508(see-also)|pubmed:31987001(see-also)|complex portal:CPX-5692(complex-primary)|evidence ontology:"ECO:0000353"|pubmed:33821277(see-also)|intact:EBI-26971334(exp-evidence)	-	go:"GO:0004532"(exoribonuclease activity)	curated-complex:"The SARS-CoV-2 coronavirus 3'-5' exoribonuclease complex which strictly targets double-stranded RNA and can selectively remove a mismatched ribonucleotide at the 3'-end of a dsRNA substrate. Formation of the NSP10-NSP14 complex strongly enhances the exonuclease activity of the bifunctional NSP14 and enhances the fidelity of RNA synthesis by correcting nucleotide incorporation errors made by the RNA-dependent RNA polymerase. May bind to, and act with the nsp7/nsp8/nsp12 polymerase complex (CPX-5742). Proof-reading exonuclease activity may explain why coronaviruses have the largest RNA genomes known to date. Complex formation does not appear to effect the C-terminal N7-methyltransferase activity of NSP14 involved in RNA cap modification."|disease:"Severe acute respiratory syndrome (SARS) [EFO:0000694]: A viral respiratory infection caused by the SARS coronavirus. It is transmitted through close person-to-person contact. It is manifested with high fever, headache, dry cough and myalgias. It may progress to pneumonia and cause death."|complex-properties:NSP10 forms a homododecamer in isolation. A flexible N-terminal domain of NSP14 forms the NSP10 docking site and induces conformational changes in the NSP14 that modulate the distance between the catalytic residues.	-	figure legend:1c|comment:A 20-nt poly-U RNA, which is less likely to adopt secondary structures did not serve as a substrate by itself but was degraded extensively when supplemented with a complementary 30-nt poly-A RNA|dataset:Virus - Publications including interactions involving viral proteins|dataset:Coronavirus - Interactions investigated in the context of Coronavirus|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2021/05/06	2021/08/23	-	-	-	false	mutation disrupting interaction rate:191-191|sufficient binding region:1-289	fluorescein label:1-1	-	-	psi-mi:"MI:0866"(tag visualisation)	psi-mi:"MI:0866"(tag visualisation)
reactome:R-COV-9682545	intact:EBI-27069181	intact:EBI-25496027|wwpdb:5c8s|intenz:3.1.13|wwpdb:5c8t|wwpdb:5c8u|wwpdb:5nfy	-	psi-mi:nsp10-nsp14_cvhsa(display_short)|psi-mi:R-COV-9682545(display_long)|intact:SARS-CoV 3'-5' exoribonuclease proof-reading complex(complex recommended name)|intact:"NSP10:NSP14"(complex systematic name)|intact:SARS-CoV NSP14/NSP10 complex(complex synonym)	psi-mi:poly a rna(display_short)|psi-mi:EBI-27069181(display_long)	psi-mi:"MI:0920"(ribonuclease assay)	Moeller et al. (2021)	pubmed:33821277|imex:IM-28938	taxid:694009(sars-cov)|taxid:694009(Human SARS coronavirus)	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	psi-mi:"MI:0902"(rna cleavage)	psi-mi:"MI:0469"(IntAct)	intact:EBI-27069216|imex:IM-28938-9	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0684"(ancillary)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:1302"(stable complex)	psi-mi:"MI:0320"(ribonucleic acid)	evidence ontology:"ECO:0000353"|efo:"EFO:0000694"(see-also)|pubmed:29279395(see-also)|pubmed:26159422(see-also)|complex portal:CPX-5707(complex-primary)|go:"GO:0000175"(3'-5'-exoribonuclease activity)|go:"GO:1905354"(exoribonuclease complex)|go:"GO:0003725"(double-stranded RNA binding)|go:"GO:0039694"(viral RNA genome replication)|pubmed:31440227(see-also)|intact:EBI-25499834(exp-evidence)|pubmed:18255185(see-also)	-	go:"GO:0004532"(exoribonuclease activity)	curated-complex:"The SARS-CoV coronavirus 3'-5' exoribonuclease complex which strictly targets double-stranded RNA and can also selectively remove a mismatched ribonucleotide at the 3'-end of a dsRNA substrate. Formation of the NSP10-NSP14 complex strongly enhances the exonuclease activity of the bifunctional NSP14 and enhances the fidelity of RNA synthesis by correcting nucleotide incorporation errors made by the RNA-dependent RNA polymerase. May bind to, and act with the nsp7/nsp8/nsp12 polymerase complex (CPX-5717). Proof-reading exonuclease activity may explain why coronaviruses have the largest RNA genomes known to date. Complex formation does not appear to effect the C-terminal N7-methyltransferase activity of NSP14 involved in RNA cap modification."|disease:"Severe acute respiratory syndrome (SARS) [EFO:0000694]: A viral respiratory infection caused by the SARS coronavirus. It is transmitted through close person-to-person contact. It is manifested with high fever, headache, dry cough and myalgias. It may progress to pneumonia and cause death."|complex-assembly:Heterodimer|complex-properties:NSP10 forms a homododecamer in isolation. A flexible N-terminal domain of NSP14 forms the NSP10 docking site and induces conformational changes in the NSP14 that modulate the distance between the catalytic residues.	-	figure legend:1c|comment:A 20-nt poly-U RNA, which is less likely to adopt secondary structures did not serve as a substrate by itself but was degraded extensively when supplemented with a complementary 30-nt poly-A RNA|dataset:Virus - Publications including interactions involving viral proteins|dataset:Coronavirus - Interactions investigated in the context of Coronavirus|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2021/05/06	2021/08/23	-	-	-	false	sufficient binding region:1..1-287..287	-	-	-	psi-mi:"MI:0866"(tag visualisation)	psi-mi:"MI:0866"(tag visualisation)
reactome:R-COV-9682545	intact:EBI-27069153	intact:EBI-25496027|wwpdb:5c8s|intenz:3.1.13|wwpdb:5c8t|wwpdb:5c8u|wwpdb:5nfy	-	psi-mi:nsp10-nsp14_cvhsa(display_short)|psi-mi:R-COV-9682545(display_long)|intact:SARS-CoV 3'-5' exoribonuclease proof-reading complex(complex recommended name)|intact:"NSP10:NSP14"(complex systematic name)|intact:SARS-CoV NSP14/NSP10 complex(complex synonym)	psi-mi:poly u rna(display_short)|psi-mi:EBI-27069153(display_long)	psi-mi:"MI:0920"(ribonuclease assay)	Moeller et al. (2021)	pubmed:33821277|imex:IM-28938	taxid:694009(sars-cov)|taxid:694009(Human SARS coronavirus)	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	psi-mi:"MI:0902"(rna cleavage)	psi-mi:"MI:0469"(IntAct)	intact:EBI-27069216|imex:IM-28938-9	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:1302"(stable complex)	psi-mi:"MI:0320"(ribonucleic acid)	evidence ontology:"ECO:0000353"|efo:"EFO:0000694"(see-also)|pubmed:29279395(see-also)|pubmed:26159422(see-also)|complex portal:CPX-5707(complex-primary)|go:"GO:0000175"(3'-5'-exoribonuclease activity)|go:"GO:1905354"(exoribonuclease complex)|go:"GO:0003725"(double-stranded RNA binding)|go:"GO:0039694"(viral RNA genome replication)|pubmed:31440227(see-also)|intact:EBI-25499834(exp-evidence)|pubmed:18255185(see-also)	-	go:"GO:0004532"(exoribonuclease activity)	curated-complex:"The SARS-CoV coronavirus 3'-5' exoribonuclease complex which strictly targets double-stranded RNA and can also selectively remove a mismatched ribonucleotide at the 3'-end of a dsRNA substrate. Formation of the NSP10-NSP14 complex strongly enhances the exonuclease activity of the bifunctional NSP14 and enhances the fidelity of RNA synthesis by correcting nucleotide incorporation errors made by the RNA-dependent RNA polymerase. May bind to, and act with the nsp7/nsp8/nsp12 polymerase complex (CPX-5717). Proof-reading exonuclease activity may explain why coronaviruses have the largest RNA genomes known to date. Complex formation does not appear to effect the C-terminal N7-methyltransferase activity of NSP14 involved in RNA cap modification."|disease:"Severe acute respiratory syndrome (SARS) [EFO:0000694]: A viral respiratory infection caused by the SARS coronavirus. It is transmitted through close person-to-person contact. It is manifested with high fever, headache, dry cough and myalgias. It may progress to pneumonia and cause death."|complex-assembly:Heterodimer|complex-properties:NSP10 forms a homododecamer in isolation. A flexible N-terminal domain of NSP14 forms the NSP10 docking site and induces conformational changes in the NSP14 that modulate the distance between the catalytic residues.	-	figure legend:1c|comment:A 20-nt poly-U RNA, which is less likely to adopt secondary structures did not serve as a substrate by itself but was degraded extensively when supplemented with a complementary 30-nt poly-A RNA|dataset:Virus - Publications including interactions involving viral proteins|dataset:Coronavirus - Interactions investigated in the context of Coronavirus|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2021/05/06	2021/08/23	-	-	-	false	sufficient binding region:1..1-287..287	fluorescein label:1-1	-	-	psi-mi:"MI:0866"(tag visualisation)	psi-mi:"MI:0866"(tag visualisation)
intenz:3.1.13	intact:EBI-26973610	intact:EBI-25564924|intact:EBI-25492032|reactome:R-COV-9694688|wwpdb:7diy|wwpdb:7mc6|wwpdb:7mc5|wwpdb:7n0c|emdb:EMD-24103|wwpdb:7n0d|emdb:EMD-24104|wwpdb:7n0b|emdb:EMD-24102	-	psi-mi:nsp10-nsp14_sars2-1(display_short)|psi-mi:3.1.13(display_long)|intact:SARS-CoV-2 3'-5' exoribonuclease proof-reading complex(complex recommended name)|intact:"NSP10:NSP14"(complex systematic name)|intact:SARS-CoV-2 NSP14/NSP10 complex(complex synonym)	psi-mi:ls2u rna(display_short)|psi-mi:EBI-26973610(display_long)	psi-mi:"MI:0920"(ribonuclease assay)	Moeller et al. (2021)	pubmed:33821277|imex:IM-28938	taxid:2697049(SARS-CoV-2)|taxid:2697049(SARS-CoV-2)	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	psi-mi:"MI:0902"(rna cleavage)	psi-mi:"MI:0469"(IntAct)	intact:EBI-27069276|imex:IM-28938-11	-	-	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:1302"(stable complex)	psi-mi:"MI:0320"(ribonucleic acid)	go:"GO:0000175"(3'-5'-exoribonuclease activity)|go:"GO:0003725"(double-stranded RNA binding)|go:"GO:0039694"(viral RNA genome replication)|go:"GO:1905354"(exoribonuclease complex)|pubmed:31440227(see-also)|pubmed:29279395(see-also)|efo:"EFO:0000694"(see-also)|pubmed:32015508(see-also)|pubmed:31987001(see-also)|complex portal:CPX-5692(complex-primary)|evidence ontology:"ECO:0000353"|pubmed:33821277(see-also)|intact:EBI-26971334(exp-evidence)	-	go:"GO:0004532"(exoribonuclease activity)	curated-complex:"The SARS-CoV-2 coronavirus 3'-5' exoribonuclease complex which strictly targets double-stranded RNA and can selectively remove a mismatched ribonucleotide at the 3'-end of a dsRNA substrate. Formation of the NSP10-NSP14 complex strongly enhances the exonuclease activity of the bifunctional NSP14 and enhances the fidelity of RNA synthesis by correcting nucleotide incorporation errors made by the RNA-dependent RNA polymerase. May bind to, and act with the nsp7/nsp8/nsp12 polymerase complex (CPX-5742). Proof-reading exonuclease activity may explain why coronaviruses have the largest RNA genomes known to date. Complex formation does not appear to effect the C-terminal N7-methyltransferase activity of NSP14 involved in RNA cap modification."|disease:"Severe acute respiratory syndrome (SARS) [EFO:0000694]: A viral respiratory infection caused by the SARS coronavirus. It is transmitted through close person-to-person contact. It is manifested with high fever, headache, dry cough and myalgias. It may progress to pneumonia and cause death."|complex-properties:NSP10 forms a homododecamer in isolation. A flexible N-terminal domain of NSP14 forms the NSP10 docking site and induces conformational changes in the NSP14 that modulate the distance between the catalytic residues.	-	figure legend:1a, 1b|dataset:Virus - Publications including interactions involving viral proteins|dataset:Coronavirus - Interactions investigated in the context of Coronavirus|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2021/05/06	2021/08/17	-	-	-	false	sufficient binding region:1-289	fluorescein label:1-1	-	-	psi-mi:"MI:0866"(tag visualisation)	psi-mi:"MI:0866"(tag visualisation)
intact:EBI-26973632	intact:EBI-26973610	-	-	psi-mi:ls15a rna(display_short)|psi-mi:EBI-26973632(display_long)	psi-mi:ls2u rna(display_short)|psi-mi:EBI-26973610(display_long)	psi-mi:"MI:0920"(ribonuclease assay)	Moeller et al. (2021)	pubmed:33821277|imex:IM-28938	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	psi-mi:"MI:0902"(rna cleavage)	psi-mi:"MI:0469"(IntAct)	intact:EBI-27069293|imex:IM-28938-13	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0840"(stimulator)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0320"(ribonucleic acid)	psi-mi:"MI:0320"(ribonucleic acid)	-	-	go:"GO:0004532"(exoribonuclease activity)	-	-	figure legend:SF1, 4b|comment:"More extensive degradation was observed when LS2U RNA was annealed to an unlabeled 40-nt template strand (LS15A_RNA) to generate a double-stranded (ds) RNA with a 20-nt 5'-overhang"|dataset:Virus - Publications including interactions involving viral proteins|dataset:Coronavirus - Interactions investigated in the context of Coronavirus|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2021/05/06	2021/08/23	-	-	-	false	-	fluorescein label:1-1	-	-	psi-mi:"MI:0866"(tag visualisation)	psi-mi:"MI:0866"(tag visualisation)
intact:EBI-26973632	intenz:3.1.13	-	intact:EBI-25564924|intact:EBI-25492032|reactome:R-COV-9694688|wwpdb:7diy|wwpdb:7mc6|wwpdb:7mc5|wwpdb:7n0c|emdb:EMD-24103|wwpdb:7n0d|emdb:EMD-24104|wwpdb:7n0b|emdb:EMD-24102	psi-mi:ls15a rna(display_short)|psi-mi:EBI-26973632(display_long)	psi-mi:nsp10-nsp14_sars2-1(display_short)|psi-mi:3.1.13(display_long)|intact:SARS-CoV-2 3'-5' exoribonuclease proof-reading complex(complex recommended name)|intact:"NSP10:NSP14"(complex systematic name)|intact:SARS-CoV-2 NSP14/NSP10 complex(complex synonym)	psi-mi:"MI:0920"(ribonuclease assay)	Moeller et al. (2021)	pubmed:33821277|imex:IM-28938	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:2697049(SARS-CoV-2)|taxid:2697049(SARS-CoV-2)	psi-mi:"MI:0902"(rna cleavage)	psi-mi:"MI:0469"(IntAct)	intact:EBI-27069293|imex:IM-28938-13	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0840"(stimulator)	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0320"(ribonucleic acid)	psi-mi:"MI:1302"(stable complex)	-	go:"GO:0000175"(3'-5'-exoribonuclease activity)|go:"GO:0003725"(double-stranded RNA binding)|go:"GO:0039694"(viral RNA genome replication)|go:"GO:1905354"(exoribonuclease complex)|pubmed:31440227(see-also)|pubmed:29279395(see-also)|efo:"EFO:0000694"(see-also)|pubmed:32015508(see-also)|pubmed:31987001(see-also)|complex portal:CPX-5692(complex-primary)|evidence ontology:"ECO:0000353"|pubmed:33821277(see-also)|intact:EBI-26971334(exp-evidence)	go:"GO:0004532"(exoribonuclease activity)	-	curated-complex:"The SARS-CoV-2 coronavirus 3'-5' exoribonuclease complex which strictly targets double-stranded RNA and can selectively remove a mismatched ribonucleotide at the 3'-end of a dsRNA substrate. Formation of the NSP10-NSP14 complex strongly enhances the exonuclease activity of the bifunctional NSP14 and enhances the fidelity of RNA synthesis by correcting nucleotide incorporation errors made by the RNA-dependent RNA polymerase. May bind to, and act with the nsp7/nsp8/nsp12 polymerase complex (CPX-5742). Proof-reading exonuclease activity may explain why coronaviruses have the largest RNA genomes known to date. Complex formation does not appear to effect the C-terminal N7-methyltransferase activity of NSP14 involved in RNA cap modification."|disease:"Severe acute respiratory syndrome (SARS) [EFO:0000694]: A viral respiratory infection caused by the SARS coronavirus. It is transmitted through close person-to-person contact. It is manifested with high fever, headache, dry cough and myalgias. It may progress to pneumonia and cause death."|complex-properties:NSP10 forms a homododecamer in isolation. A flexible N-terminal domain of NSP14 forms the NSP10 docking site and induces conformational changes in the NSP14 that modulate the distance between the catalytic residues.	figure legend:SF1, 4b|comment:"More extensive degradation was observed when LS2U RNA was annealed to an unlabeled 40-nt template strand (LS15A_RNA) to generate a double-stranded (ds) RNA with a 20-nt 5'-overhang"|dataset:Virus - Publications including interactions involving viral proteins|dataset:Coronavirus - Interactions investigated in the context of Coronavirus|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2021/05/06	2021/08/23	-	-	-	false	-	sufficient binding region:1-289|mutation disrupting interaction rate:191-191|mutation decreasing interaction rate:9-9|mutation decreasing interaction rate:61-61|mutation decreasing interaction rate:139-139	-	-	psi-mi:"MI:0866"(tag visualisation)	psi-mi:"MI:0866"(tag visualisation)
intact:EBI-27071150	intact:EBI-26973610	-	-	psi-mi:ls15_dna(display_short)|psi-mi:EBI-27071150(display_long)	psi-mi:ls2u rna(display_short)|psi-mi:EBI-26973610(display_long)	psi-mi:"MI:0920"(ribonuclease assay)	Moeller et al. (2021)	pubmed:33821277|imex:IM-28938	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	psi-mi:"MI:0902"(rna cleavage)	psi-mi:"MI:0469"(IntAct)	intact:EBI-27071141|imex:IM-28938-14	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0680"(single stranded deoxyribonucleic acid)	psi-mi:"MI:0320"(ribonucleic acid)	-	-	go:"GO:0004532"(exoribonuclease activity)	-	-	figure legend:1a, 1b,  Lane 5|comment:"When DNA was used as the template strand (LS15_DNA; Table 1) to generate an RNA/DNA heteroduplex substrate,  activity was observed but weaker than for dsRNA."|dataset:Virus - Publications including interactions involving viral proteins|dataset:Coronavirus - Interactions investigated in the context of Coronavirus|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2021/05/06	2021/08/23	-	-	-	false	-	fluorescein label:1-1	-	-	psi-mi:"MI:0866"(tag visualisation)	psi-mi:"MI:0866"(tag visualisation)
intact:EBI-27071150	intenz:3.1.13	-	intact:EBI-25564924|intact:EBI-25492032|reactome:R-COV-9694688|wwpdb:7diy|wwpdb:7mc6|wwpdb:7mc5|wwpdb:7n0c|emdb:EMD-24103|wwpdb:7n0d|emdb:EMD-24104|wwpdb:7n0b|emdb:EMD-24102	psi-mi:ls15_dna(display_short)|psi-mi:EBI-27071150(display_long)	psi-mi:nsp10-nsp14_sars2-1(display_short)|psi-mi:3.1.13(display_long)|intact:SARS-CoV-2 3'-5' exoribonuclease proof-reading complex(complex recommended name)|intact:"NSP10:NSP14"(complex systematic name)|intact:SARS-CoV-2 NSP14/NSP10 complex(complex synonym)	psi-mi:"MI:0920"(ribonuclease assay)	Moeller et al. (2021)	pubmed:33821277|imex:IM-28938	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:2697049(SARS-CoV-2)|taxid:2697049(SARS-CoV-2)	psi-mi:"MI:0902"(rna cleavage)	psi-mi:"MI:0469"(IntAct)	intact:EBI-27071141|imex:IM-28938-14	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0680"(single stranded deoxyribonucleic acid)	psi-mi:"MI:1302"(stable complex)	-	go:"GO:0000175"(3'-5'-exoribonuclease activity)|go:"GO:0003725"(double-stranded RNA binding)|go:"GO:0039694"(viral RNA genome replication)|go:"GO:1905354"(exoribonuclease complex)|pubmed:31440227(see-also)|pubmed:29279395(see-also)|efo:"EFO:0000694"(see-also)|pubmed:32015508(see-also)|pubmed:31987001(see-also)|complex portal:CPX-5692(complex-primary)|evidence ontology:"ECO:0000353"|pubmed:33821277(see-also)|intact:EBI-26971334(exp-evidence)	go:"GO:0004532"(exoribonuclease activity)	-	curated-complex:"The SARS-CoV-2 coronavirus 3'-5' exoribonuclease complex which strictly targets double-stranded RNA and can selectively remove a mismatched ribonucleotide at the 3'-end of a dsRNA substrate. Formation of the NSP10-NSP14 complex strongly enhances the exonuclease activity of the bifunctional NSP14 and enhances the fidelity of RNA synthesis by correcting nucleotide incorporation errors made by the RNA-dependent RNA polymerase. May bind to, and act with the nsp7/nsp8/nsp12 polymerase complex (CPX-5742). Proof-reading exonuclease activity may explain why coronaviruses have the largest RNA genomes known to date. Complex formation does not appear to effect the C-terminal N7-methyltransferase activity of NSP14 involved in RNA cap modification."|disease:"Severe acute respiratory syndrome (SARS) [EFO:0000694]: A viral respiratory infection caused by the SARS coronavirus. It is transmitted through close person-to-person contact. It is manifested with high fever, headache, dry cough and myalgias. It may progress to pneumonia and cause death."|complex-properties:NSP10 forms a homododecamer in isolation. A flexible N-terminal domain of NSP14 forms the NSP10 docking site and induces conformational changes in the NSP14 that modulate the distance between the catalytic residues.	figure legend:1a, 1b,  Lane 5|comment:"When DNA was used as the template strand (LS15_DNA; Table 1) to generate an RNA/DNA heteroduplex substrate,  activity was observed but weaker than for dsRNA."|dataset:Virus - Publications including interactions involving viral proteins|dataset:Coronavirus - Interactions investigated in the context of Coronavirus|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2021/05/06	2021/08/23	-	-	-	false	-	sufficient binding region:1-289	-	-	psi-mi:"MI:0866"(tag visualisation)	psi-mi:"MI:0866"(tag visualisation)