#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
intact:EBI-26976231	intact:EBI-26976238	refseq:NC_045512.2	refseq:NC_045512.2	psi-mi:3' utr_20-mer-rna primer(display_short)|psi-mi:EBI-26976231(display_long)	psi-mi:3' utr_40-mer-rna template(display_short)|psi-mi:EBI-26976238(display_long)	psi-mi:"MI:0920"(ribonuclease assay)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	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-26976210|imex:IM-28954-1	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0502"(enzyme target)	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:0008408"(3'-5' exonuclease activity)	comment:29870 - 29851 3' UTR	comment:residues 29831-29870 from 3' UTR	figure legend:1D|comment:The addition of nsp10 dramatically stimulates the nuclease activity of nsp14, forming a functional nuclease.|agonist:"Mg2+ (CHEBI:18420)"|agonist:"Mn2+ (CHEBI:29035)"|antagonist:"EDTA (CHEBI:42191)"|antagonist:"Zn2+ (CHEBI:29105)"|antagonist:"Ca2+ (CHEBI:29108)"|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)	-	2021/05/07	2021/05/18	-	-	-	false	sufficient binding region:?-?|fluorescein label:1-1	sufficient binding region:?-?	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
intact:EBI-26976231	uniprotkb:P0DTD1-PRO_0000449628	refseq:NC_045512.2	intact:EBI-25475880	psi-mi:3' utr_20-mer-rna primer(display_short)|psi-mi:EBI-26976231(display_long)	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:"MI:0920"(ribonuclease assay)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	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-26976210|imex:IM-28954-1	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0840"(stimulator)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0684"(ancillary)	psi-mi:"MI:0320"(ribonucleic acid)	psi-mi:"MI:0326"(protein)	-	intact:EBI-25492095(chain-parent)|uniprotkb:P0DTD1(chain-parent)	go:"GO:0008408"(3'-5' exonuclease activity)	comment:29870 - 29851 3' UTR	chain-seq-start:4254|chain-seq-end:4392	figure legend:1D|comment:The addition of nsp10 dramatically stimulates the nuclease activity of nsp14, forming a functional nuclease.|agonist:"Mg2+ (CHEBI:18420)"|agonist:"Mn2+ (CHEBI:29035)"|antagonist:"EDTA (CHEBI:42191)"|antagonist:"Zn2+ (CHEBI:29105)"|antagonist:"Ca2+ (CHEBI:29108)"|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)	-	2021/05/07	2021/05/18	-	rogid:L4eD+20oc1IdNFJ9By3H2uun6L02697049	-	false	sufficient binding region:?-?|fluorescein label:1-1	his tag:n-n	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
intact:EBI-26976231	uniprotkb:P0DTD1-PRO_0000449631	refseq:NC_045512.2	intact:EBI-25475920	psi-mi:3' utr_20-mer-rna primer(display_short)|psi-mi:EBI-26976231(display_long)	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:0920"(ribonuclease assay)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	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-26976210|imex:IM-28954-1	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0502"(enzyme target)	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:0326"(protein)	-	intact:EBI-25492095(chain-parent)|uniprotkb:P0DTD1(chain-parent)	go:"GO:0008408"(3'-5' exonuclease activity)	comment:29870 - 29851 3' UTR	chain-seq-start:5926|chain-seq-end:6452	figure legend:1D|comment:The addition of nsp10 dramatically stimulates the nuclease activity of nsp14, forming a functional nuclease.|agonist:"Mg2+ (CHEBI:18420)"|agonist:"Mn2+ (CHEBI:29035)"|antagonist:"EDTA (CHEBI:42191)"|antagonist:"Zn2+ (CHEBI:29105)"|antagonist:"Ca2+ (CHEBI:29108)"|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)	-	2021/05/07	2021/05/18	-	rogid:LpGB5BQU5uhWK/60422jkiKHRL82697049	-	false	sufficient binding region:?-?|fluorescein label:1-1	glutathione s tranferase tag:n-n	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
intact:EBI-26976231	intact:EBI-26976238	refseq:NC_045512.2	refseq:NC_045512.2	psi-mi:3' utr_20-mer-rna primer(display_short)|psi-mi:EBI-26976231(display_long)	psi-mi:3' utr_40-mer-rna template(display_short)|psi-mi:EBI-26976238(display_long)	psi-mi:"MI:0920"(ribonuclease assay)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	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-26976559|imex:IM-28954-5	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0502"(enzyme target)	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:0008408"(3'-5' exonuclease activity)	comment:29870 - 29851 3' UTR	comment:residues 29831-29870 from 3' UTR	figure legend:2A, 3A, 4A|agonist:"Mg2+ (CHEBI:18420)"|agonist:"Mn2+ (CHEBI:29035)"|antagonist:"EDTA (CHEBI:42191)"|antagonist:"Zn2+ (CHEBI:29105)"|antagonist:"Ca2+ (CHEBI:29108)"|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)	-	2021/05/07	2021/05/18	-	-	-	false	sufficient binding region:?-?|fluorescein label:1-1	sufficient binding region:?-?	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
intact:EBI-26976231	intenz:3.1.13	refseq:NC_045512.2	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:3' utr_20-mer-rna primer(display_short)|psi-mi:EBI-26976231(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)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	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-26976559|imex:IM-28954-5	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0502"(enzyme target)	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:0008408"(3'-5' exonuclease activity)	comment:29870 - 29851 3' UTR	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:2A, 3A, 4A|agonist:"Mg2+ (CHEBI:18420)"|agonist:"Mn2+ (CHEBI:29035)"|antagonist:"EDTA (CHEBI:42191)"|antagonist:"Zn2+ (CHEBI:29105)"|antagonist:"Ca2+ (CHEBI:29108)"|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)	-	2021/05/07	2021/05/18	-	-	-	false	sufficient binding region:?-?|fluorescein label:1-1	his tag:n-n|glutathione s tranferase tag:n-n	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
intact:EBI-26976231	intenz:3.1.13	refseq:NC_045512.2	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:3' utr_20-mer-rna primer(display_short)|psi-mi:EBI-26976231(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)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	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-26976583|imex:IM-28954-7	-	-	psi-mi:"MI:0502"(enzyme target)	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:0008408"(3'-5' exonuclease activity)	comment:29870 - 29851 3' UTR	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:3A|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)	-	2021/05/07	2021/05/18	-	-	-	false	sufficient binding region:?-?|fluorescein label:1-1	his tag:n-n|glutathione s tranferase tag:n-n	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
intact:EBI-26976231	intact:EBI-26976609	refseq:NC_045512.2	refseq:NC_045512.2	psi-mi:3' utr_20-mer-rna primer(display_short)|psi-mi:EBI-26976231(display_long)	psi-mi:3'-utr_40mer-dna template(display_short)|psi-mi:EBI-26976609(display_long)	psi-mi:"MI:0920"(ribonuclease assay)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	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-26976613|imex:IM-28954-9	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0502"(enzyme target)	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:0680"(single stranded deoxyribonucleic acid)	-	-	go:"GO:0008408"(3'-5' exonuclease activity)	comment:29870 - 29851 3' UTR	comment:29831 -29870	figure legend:3A|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)	-	2021/05/07	2021/05/18	-	-	-	false	sufficient binding region:?-?|fluorescein label:1-1	sufficient binding region:?-?	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
intact:EBI-26976231	intenz:3.1.13	refseq:NC_045512.2	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:3' utr_20-mer-rna primer(display_short)|psi-mi:EBI-26976231(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)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	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-26976613|imex:IM-28954-9	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0502"(enzyme target)	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:0008408"(3'-5' exonuclease activity)	comment:29870 - 29851 3' UTR	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:3A|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)	-	2021/05/07	2021/05/18	-	-	-	false	sufficient binding region:?-?|fluorescein label:1-1	his tag:n-n|glutathione s tranferase tag:n-n	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
intact:EBI-26976231	intact:EBI-26976238	refseq:NC_045512.2	refseq:NC_045512.2	psi-mi:3' utr_20-mer-rna primer(display_short)|psi-mi:EBI-26976231(display_long)	psi-mi:3' utr_40-mer-rna template(display_short)|psi-mi:EBI-26976238(display_long)	psi-mi:"MI:0920"(ribonuclease assay)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	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-26976625|imex:IM-28954-11	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0502"(enzyme target)	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:0008408"(3'-5' exonuclease activity)	comment:29870 - 29851 3' UTR	comment:residues 29831-29870 from 3' UTR	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)	-	2021/05/07	2021/05/18	-	-	-	false	sufficient binding region:?-?|fluorescein label:1-1	sufficient binding region:?-?	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
intact:EBI-26976231	intenz:3.1.13	refseq:NC_045512.2	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:3' utr_20-mer-rna primer(display_short)|psi-mi:EBI-26976231(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)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	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-26976625|imex:IM-28954-11	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0502"(enzyme target)	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:0008408"(3'-5' exonuclease activity)	comment:29870 - 29851 3' UTR	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)	-	2021/05/07	2021/05/18	-	-	-	false	sufficient binding region:?-?|fluorescein label:1-1	his tag:n-n|glutathione s tranferase tag:n-n	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
intact:EBI-26976231	wwpdb:7ctt	refseq:NC_045512.2	intact:EBI-25564960|wwpdb:6xqb|emdb:EMD-22288|wwpdb:6M71|wwpdb:7btf|emdb:EMD-30178|emdb:EMD-30127|intenz:2.7.7.48|wwpdb:7bv2|emdb:EMD-30210|wwpdb:7bv1|emdb:EMD-30209|wwpdb:6x2g|wwpdb:7bw4|emdb:EMD-30226|wwpdb:7l1f|emdb:EMD-23109|wwpdb:6yyt|emdb:EMD-11007|wwpdb:7c2k|emdb:EMD-30275|wwpdb:7bzf|emdb:EMD-30252|reactome:R-COV-9691364|wwpdb:7aap|emdb:EMD-11692|wwpdb:7d4f|emdb:EMD-30572|emdb:EMD-23009|wwpdb:7krp|wwpdb:7b3b|emdb:EMD-11993|wwpdb:7b3c|emdb:EMD-11994|wwpdb:7b3d|emdb:EMD-11995|rhea:"RHEA:21248"|wwpdb:7ozv|emdb:EMD-13138|wwpdb:7ozu|emdb:EMD-13135|wwpdb:7oyg|emdb:EMD-13116	psi-mi:3' utr_20-mer-rna primer(display_short)|psi-mi:EBI-26976231(display_long)	psi-mi:nsp7-nsp8-nsp12_sars2(display_short)|psi-mi:7ctt(display_long)|intact:SARS-CoV-2 polymerase complex(complex recommended name)|intact:"NSP7:2xNSP8:NSP12"(complex systematic name)|intact:replication-transcription complex(complex synonym)|intact:replication and transcription complex(complex synonym)|intact:RTC(complex synonym)|intact:central RTC(complex synonym)|intact:C-RTC(complex synonym)|intact:holo-RdRp complex(complex synonym)|intact:holo-RNA-dependent RNA polymerase complex(complex synonym)	psi-mi:"MI:0920"(ribonuclease assay)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	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-26976625|imex:IM-28954-11	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0586"(inhibitor)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0320"(ribonucleic acid)	psi-mi:"MI:1302"(stable complex)	-	intact:EBI-25506373(exp-evidence)|pubmed:32277040(see-also)|go:"GO:0003968"(RNA-directed 5'-3' RNA polymerase activity)|go:"GO:0003725"(double-stranded RNA binding)|go:"GO:0039694"(viral RNA genome replication)|efo:"EFO:0000694"(see-also)|pubmed:16228002(see-also)|go:"GO:0031381"(viral RNA-directed RNA polymerase complex)|pubmed:19875418(see-also)|pubmed:31138817(see-also)|pubmed:31987001(see-also)|pubmed:18255185(see-also)|complex portal:CPX-5742(complex-primary)|pubmed:32015508(see-also)|evidence ontology:"ECO:0000353"	go:"GO:0008408"(3'-5' exonuclease activity)	comment:29870 - 29851 3' UTR	curated-complex:"RNA-directed 5'-3' RNA polymerase of the SARS-CoV-2 coronavirus which consists of the main polymerase protein NSP12 and a stoichiometric variant of the primase complex (CPX-5690). Extends partially double-stranded RNA templates and is probably also required for transcription initiation, though the mechanism for this has yet to be determined. Complex formation enhances dsRNA binding of the individual protomers."|complex-assembly:Heterotetramer|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:"Primase complex without polymerase has a different stoichiometry (8:8). NSP12 possesses conserved motifs involved in template binding, NTP binding, and polymerization that assume a structure resembling a cupped “right hand”. The NSP7-NSP8 heterodimer binds to the index finger loop and may facilitates the interaction of NSP12 with additional components of the RNA synthesis machinery. The second NSP8 molecule binds close to the RNA template-binding channel."	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)	-	2021/05/07	2021/05/18	-	-	-	false	sufficient binding region:?-?|fluorescein label:1-1	his tag:c-c|his tag:n-n|his tag:n-n|his tag:n-n	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
intact:EBI-26976848	intact:EBI-26976238	refseq:NC_045512.2	refseq:NC_045512.2	psi-mi:3' utr_21-mer-rna primer(display_short)|psi-mi:EBI-26976848(display_long)	psi-mi:3' utr_40-mer-rna template(display_short)|psi-mi:EBI-26976238(display_long)	psi-mi:"MI:0920"(ribonuclease assay)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	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-26976863|imex:IM-28954-15	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0502"(enzyme target)	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:0008408"(3'-5' exonuclease activity)	comment:"29870 - 29851 3' UTR plus 3-prime extra \"A\""	comment:residues 29831-29870 from 3' UTR	figure legend:4C Lane 9|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)	-	2021/05/07	2021/05/19	-	-	-	false	sufficient binding region:?-?|fluorescein label:1-1	sufficient binding region:?-?	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
intact:EBI-26976848	intenz:3.1.13	refseq:NC_045512.2	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:3' utr_21-mer-rna primer(display_short)|psi-mi:EBI-26976848(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)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	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-26976863|imex:IM-28954-15	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0502"(enzyme target)	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:0008408"(3'-5' exonuclease activity)	comment:"29870 - 29851 3' UTR plus 3-prime extra \"A\""	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:4C Lane 9|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)	-	2021/05/07	2021/05/19	-	-	-	false	sufficient binding region:?-?|fluorescein label:1-1	his tag:n-n|glutathione s tranferase tag:n-n	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
intact:EBI-26976231	wwpdb:7ctt	refseq:NC_045512.2	intact:EBI-25564960|wwpdb:6xqb|emdb:EMD-22288|wwpdb:6M71|wwpdb:7btf|emdb:EMD-30178|emdb:EMD-30127|intenz:2.7.7.48|wwpdb:7bv2|emdb:EMD-30210|wwpdb:7bv1|emdb:EMD-30209|wwpdb:6x2g|wwpdb:7bw4|emdb:EMD-30226|wwpdb:7l1f|emdb:EMD-23109|wwpdb:6yyt|emdb:EMD-11007|wwpdb:7c2k|emdb:EMD-30275|wwpdb:7bzf|emdb:EMD-30252|reactome:R-COV-9691364|wwpdb:7aap|emdb:EMD-11692|wwpdb:7d4f|emdb:EMD-30572|emdb:EMD-23009|wwpdb:7krp|wwpdb:7b3b|emdb:EMD-11993|wwpdb:7b3c|emdb:EMD-11994|wwpdb:7b3d|emdb:EMD-11995|rhea:"RHEA:21248"|wwpdb:7ozv|emdb:EMD-13138|wwpdb:7ozu|emdb:EMD-13135|wwpdb:7oyg|emdb:EMD-13116	psi-mi:3' utr_20-mer-rna primer(display_short)|psi-mi:EBI-26976231(display_long)	psi-mi:nsp7-nsp8-nsp12_sars2(display_short)|psi-mi:7ctt(display_long)|intact:SARS-CoV-2 polymerase complex(complex recommended name)|intact:"NSP7:2xNSP8:NSP12"(complex systematic name)|intact:replication-transcription complex(complex synonym)|intact:replication and transcription complex(complex synonym)|intact:RTC(complex synonym)|intact:central RTC(complex synonym)|intact:C-RTC(complex synonym)|intact:holo-RdRp complex(complex synonym)|intact:holo-RNA-dependent RNA polymerase complex(complex synonym)	psi-mi:"MI:0700"(rna directed rna polymerase assay)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:2697049(SARS-CoV-2)|taxid:2697049(SARS-CoV-2)	psi-mi:"MI:0987"(rna strand elongation)	psi-mi:"MI:0469"(IntAct)	intact:EBI-26976538|imex:IM-28954-3	-	-	psi-mi:"MI:0502"(enzyme target)	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)	-	intact:EBI-25506373(exp-evidence)|pubmed:32277040(see-also)|go:"GO:0003968"(RNA-directed 5'-3' RNA polymerase activity)|go:"GO:0003725"(double-stranded RNA binding)|go:"GO:0039694"(viral RNA genome replication)|efo:"EFO:0000694"(see-also)|pubmed:16228002(see-also)|go:"GO:0031381"(viral RNA-directed RNA polymerase complex)|pubmed:19875418(see-also)|pubmed:31138817(see-also)|pubmed:31987001(see-also)|pubmed:18255185(see-also)|complex portal:CPX-5742(complex-primary)|pubmed:32015508(see-also)|evidence ontology:"ECO:0000353"	go:"GO:0003968"(RNA-directed 5'-3' RNA polymerase activity)	comment:29870 - 29851 3' UTR	curated-complex:"RNA-directed 5'-3' RNA polymerase of the SARS-CoV-2 coronavirus which consists of the main polymerase protein NSP12 and a stoichiometric variant of the primase complex (CPX-5690). Extends partially double-stranded RNA templates and is probably also required for transcription initiation, though the mechanism for this has yet to be determined. Complex formation enhances dsRNA binding of the individual protomers."|complex-assembly:Heterotetramer|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:"Primase complex without polymerase has a different stoichiometry (8:8). NSP12 possesses conserved motifs involved in template binding, NTP binding, and polymerization that assume a structure resembling a cupped “right hand”. The NSP7-NSP8 heterodimer binds to the index finger loop and may facilitates the interaction of NSP12 with additional components of the RNA synthesis machinery. The second NSP8 molecule binds close to the RNA template-binding channel."	figure legend:2B, 4B lane 2.|agonist:"Mg2+ (CHEBI:18420)"|agonist:"Mn2+ (CHEBI:29035)"|antagonist:"EDTA (CHEBI:42191)"|antagonist:"Zn2+ (CHEBI:29105)"|agonist:"Ca2+ (CHEBI:29108)"|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)	-	2021/05/07	2021/05/18	-	-	-	false	sufficient binding region:?-?|fluorescein label:1-1	his tag:c-c|his tag:n-n|his tag:n-n|his tag:n-n	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
intact:EBI-26976848	intact:EBI-26976238	refseq:NC_045512.2	refseq:NC_045512.2	psi-mi:3' utr_21-mer-rna primer(display_short)|psi-mi:EBI-26976848(display_long)	psi-mi:3' utr_40-mer-rna template(display_short)|psi-mi:EBI-26976238(display_long)	psi-mi:"MI:0415"(enzymatic study)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	psi-mi:"MI:0987"(rna strand elongation)	psi-mi:"MI:0469"(IntAct)	intact:EBI-26976825|imex:IM-28954-13	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0502"(enzyme target)	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:0008408"(3'-5' exonuclease activity)|go:"GO:0003968"(RNA-directed 5'-3' RNA polymerase activity)	comment:"29870 - 29851 3' UTR plus 3-prime extra \"A\""	comment:residues 29831-29870 from 3' UTR	figure legend:4 B/C|antagonist:"EDTA (CHEBI:64755)"|agonist:"Mg2+ (CHEBI:18420)"|antagonist:"Ca2+ (CHEBI:29108)"|comment:"The addition of RTC partially protects the dsRNA from degradation by nsp14-nsp10.  The RTC cannot extend this primer due to the A:A mismatch at the 3′ end of the primer. However, when SARS-CoV-2 nsp14-nsp10 is added to reactions, the full-length extension product (40-mer) starts to be detected."|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)	-	2021/05/07	2021/05/20	-	-	-	false	sufficient binding region:?-?|fluorescein label:1-1	sufficient binding region:?-?	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
intact:EBI-26976848	intenz:3.1.13	refseq:NC_045512.2	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:3' utr_21-mer-rna primer(display_short)|psi-mi:EBI-26976848(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:0415"(enzymatic study)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:2697049(SARS-CoV-2)|taxid:2697049(SARS-CoV-2)	psi-mi:"MI:0987"(rna strand elongation)	psi-mi:"MI:0469"(IntAct)	intact:EBI-26976825|imex:IM-28954-13	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:1343"(enzyme regulator)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0684"(ancillary)	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:0008408"(3'-5' exonuclease activity)|go:"GO:0003968"(RNA-directed 5'-3' RNA polymerase activity)	comment:"29870 - 29851 3' UTR plus 3-prime extra \"A\""	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:4 B/C|antagonist:"EDTA (CHEBI:64755)"|agonist:"Mg2+ (CHEBI:18420)"|antagonist:"Ca2+ (CHEBI:29108)"|comment:"The addition of RTC partially protects the dsRNA from degradation by nsp14-nsp10.  The RTC cannot extend this primer due to the A:A mismatch at the 3′ end of the primer. However, when SARS-CoV-2 nsp14-nsp10 is added to reactions, the full-length extension product (40-mer) starts to be detected."|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)	-	2021/05/07	2021/05/20	-	-	-	false	sufficient binding region:?-?|fluorescein label:1-1	his tag:n-n|glutathione s tranferase tag:n-n	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
intact:EBI-26976848	wwpdb:7ctt	refseq:NC_045512.2	intact:EBI-25564960|wwpdb:6xqb|emdb:EMD-22288|wwpdb:6M71|wwpdb:7btf|emdb:EMD-30178|emdb:EMD-30127|intenz:2.7.7.48|wwpdb:7bv2|emdb:EMD-30210|wwpdb:7bv1|emdb:EMD-30209|wwpdb:6x2g|wwpdb:7bw4|emdb:EMD-30226|wwpdb:7l1f|emdb:EMD-23109|wwpdb:6yyt|emdb:EMD-11007|wwpdb:7c2k|emdb:EMD-30275|wwpdb:7bzf|emdb:EMD-30252|reactome:R-COV-9691364|wwpdb:7aap|emdb:EMD-11692|wwpdb:7d4f|emdb:EMD-30572|emdb:EMD-23009|wwpdb:7krp|wwpdb:7b3b|emdb:EMD-11993|wwpdb:7b3c|emdb:EMD-11994|wwpdb:7b3d|emdb:EMD-11995|rhea:"RHEA:21248"|wwpdb:7ozv|emdb:EMD-13138|wwpdb:7ozu|emdb:EMD-13135|wwpdb:7oyg|emdb:EMD-13116	psi-mi:3' utr_21-mer-rna primer(display_short)|psi-mi:EBI-26976848(display_long)	psi-mi:nsp7-nsp8-nsp12_sars2(display_short)|psi-mi:7ctt(display_long)|intact:SARS-CoV-2 polymerase complex(complex recommended name)|intact:"NSP7:2xNSP8:NSP12"(complex systematic name)|intact:replication-transcription complex(complex synonym)|intact:replication and transcription complex(complex synonym)|intact:RTC(complex synonym)|intact:central RTC(complex synonym)|intact:C-RTC(complex synonym)|intact:holo-RdRp complex(complex synonym)|intact:holo-RNA-dependent RNA polymerase complex(complex synonym)	psi-mi:"MI:0415"(enzymatic study)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:2697049(SARS-CoV-2)|taxid:2697049(SARS-CoV-2)	psi-mi:"MI:0987"(rna strand elongation)	psi-mi:"MI:0469"(IntAct)	intact:EBI-26976825|imex:IM-28954-13	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0502"(enzyme target)	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)	-	intact:EBI-25506373(exp-evidence)|pubmed:32277040(see-also)|go:"GO:0003968"(RNA-directed 5'-3' RNA polymerase activity)|go:"GO:0003725"(double-stranded RNA binding)|go:"GO:0039694"(viral RNA genome replication)|efo:"EFO:0000694"(see-also)|pubmed:16228002(see-also)|go:"GO:0031381"(viral RNA-directed RNA polymerase complex)|pubmed:19875418(see-also)|pubmed:31138817(see-also)|pubmed:31987001(see-also)|pubmed:18255185(see-also)|complex portal:CPX-5742(complex-primary)|pubmed:32015508(see-also)|evidence ontology:"ECO:0000353"	go:"GO:0008408"(3'-5' exonuclease activity)|go:"GO:0003968"(RNA-directed 5'-3' RNA polymerase activity)	comment:"29870 - 29851 3' UTR plus 3-prime extra \"A\""	curated-complex:"RNA-directed 5'-3' RNA polymerase of the SARS-CoV-2 coronavirus which consists of the main polymerase protein NSP12 and a stoichiometric variant of the primase complex (CPX-5690). Extends partially double-stranded RNA templates and is probably also required for transcription initiation, though the mechanism for this has yet to be determined. Complex formation enhances dsRNA binding of the individual protomers."|complex-assembly:Heterotetramer|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:"Primase complex without polymerase has a different stoichiometry (8:8). NSP12 possesses conserved motifs involved in template binding, NTP binding, and polymerization that assume a structure resembling a cupped “right hand”. The NSP7-NSP8 heterodimer binds to the index finger loop and may facilitates the interaction of NSP12 with additional components of the RNA synthesis machinery. The second NSP8 molecule binds close to the RNA template-binding channel."	figure legend:4 B/C|antagonist:"EDTA (CHEBI:64755)"|agonist:"Mg2+ (CHEBI:18420)"|antagonist:"Ca2+ (CHEBI:29108)"|comment:"The addition of RTC partially protects the dsRNA from degradation by nsp14-nsp10.  The RTC cannot extend this primer due to the A:A mismatch at the 3′ end of the primer. However, when SARS-CoV-2 nsp14-nsp10 is added to reactions, the full-length extension product (40-mer) starts to be detected."|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)	-	2021/05/07	2021/05/20	-	-	-	false	sufficient binding region:?-?|fluorescein label:1-1	his tag:c-c|his tag:n-n|his tag:n-n|his tag:n-n	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
uniprotkb:P0DTD1-PRO_0000449631	uniprotkb:P0DTD1-PRO_0000449631	intact:EBI-25475920	intact:EBI-25475920	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: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:0071"(molecular sieving)	Ma et al. (2021)	imex:IM-28954|pubmed:33933612	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-26976907|imex:IM-28954-17	-	-	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:5926|chain-seq-end:6452	chain-seq-start:5926|chain-seq-end:6452	figure legend:Supplementary figure 4|comment:GST-nsp14 appears to be in equilibrium between different oligomeric states with the dimeric form as the predominant  species.|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)")	-	2021/05/07	2021/05/24	rogid:LpGB5BQU5uhWK/60422jkiKHRL82697049	rogid:LpGB5BQU5uhWK/60422jkiKHRL82697049	rigid:/9SW8MKmr6mltemVnyruKeq75HA	false	glutathione s tranferase tag:n-n	glutathione s tranferase tag:n-n	2	0	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)