#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
matrixdb:MULT_82_human	uniprotkb:P09871	intact:EBI-6264901|reactome:R-HSA-173579|wwpdb:1PK6|wwpdb:2wnv|wwpdb:2jg8|wwpdb:2jg9|wwpdb:2wnu|reactome:R-HSA-173588	intact:EBI-2810045|uniprotkb:Q9UCU9|uniprotkb:Q9UCV3|uniprotkb:Q9UCU7|uniprotkb:Q9UCV5|uniprotkb:Q9UCV4|uniprotkb:Q9UCU8|uniprotkb:Q9UCV2|uniprotkb:Q9UCV1|uniprotkb:Q9UCV0|uniprotkb:Q9UM14|uniprotkb:D3DUT4|ensembl:ENSP00000328173|ensembl:ENSP00000354057|ensembl:ENSP00000385035	psi-mi:c1q_human(display_short)|psi-mi:MULT_82_human(display_long)|intact:Complement component C1q complex(complex recommended name)|intact:C1q(complex synonym)|intact:Complement 1q(complex synonym)|intact:C1QA-C1QB-C1QC complex(complex synonym)|intact:"6xC1QA:6xC1QB:6xC1QC"(complex systematic name)	psi-mi:c1s_human(display_long)|uniprotkb:C1S(gene name)|psi-mi:C1S(display_short)|uniprotkb:C1 esterase(gene name synonym)|uniprotkb:Complement component 1 subcomponent s(gene name synonym)	psi-mi:"MI:0107"(surface plasmon resonance)	Bally et al. (2018)	pubmed:30923526|imex:IM-27715	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0915"(physical association)	psi-mi:"MI:0469"(IntAct)	intact:EBI-25425994|imex:IM-27715-1	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0496"(bait)	psi-mi:"MI:0498"(prey)	psi-mi:"MI:1302"(stable complex)	psi-mi:"MI:0326"(protein)	go:"GO:0005509"(calcium ion binding)|go:"GO:0019865"(immunoglobulin binding)|efo:"MONDO:0013343"(see-also)|pubmed:28601358(see-also)|pubmed:22536204(see-also)|intact:EBI-6264878(exp-evidence)|evidence ontology:"ECO:0000353"|complex portal:CPX-1919(complex-primary)|go:"GO:0006958"(complement activation, classical pathway)|go:"GO:0005576"(extracellular region)|pubmed:20548024(see-also)|pubmed:29449492(see-also)|pubmed:18250442(see-also)|go:"GO:0062167"(complement component C1q complex)|pubmed:31165008(see-also)|pubmed:27914690(see-also)|pubmed:26489954(see-also)	refseq:NP_001725.1|refseq:NP_958850.1|ensembl:ENSG00000182326(gene)|ensembl:ENST00000328916(transcript)|ensembl:ENST00000360817(transcript)|ensembl:ENST00000406697(transcript)|go:"GO:0004252"(serine-type endopeptidase activity)|go:"GO:0005509"(calcium ion binding)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0006958"(complement activation, classical pathway)|go:"GO:0042802"(identical protein binding)|go:"GO:0045087"(innate immune response)|go:"GO:0072562"(blood microparticle)|interpro:IPR000152(Aspartic acid and asparagine hydroxylation site)|interpro:IPR000436(Sushi/SCR/CCP)|interpro:IPR000859(CUB)|interpro:IPR001254(Peptidase S1 and S6, chymotrypsin/Hap)|interpro:IPR001314(Peptidase S1A, chymotrypsin)|interpro:IPR001881(EGF-like calcium-binding)|interpro:IPR009003(Peptidase, trypsin-like serine and cysteine)|interpro:IPR018097|interpro:IPR033116|interpro:IPR035708|interpro:IPR035914|interpro:IPR035976|interpro:IPR043504|rcsb pdb:1ELV|rcsb pdb:1NZI|rcsb pdb:4J1Y|rcsb pdb:4LMF|rcsb pdb:4LOR|rcsb pdb:4LOS|rcsb pdb:4LOT|rcsb pdb:6F1C|rcsb pdb:6F1H|reactome:R-HSA-166663|reactome:R-HSA-173623|reactome:R-HSA-977606|refseq:NP_001333779.1|refseq:XP_005253817.1	-	disease:"Complement component C1q deficiency (C1QD) [MONDO:0013343]: a disorder caused by impaired activation of the complement classical pathway. It generally leads to severe immune complex disease with features of systemic lupus erythematosus and glomerulonephritis."|complex-properties:The complex comprises of six heterotrimeric collagen-like triple helices, formed from triplets of the A, B, and C chains, that associate in their N-terminal half to form a stalk, then diverge to form individual stems, each terminating in a C-terminal globular domain. Each of the six heterotrimeric globular heads or domains is made up of the globular domains from one A, one B, and one C chain, each of which in turn has its own ligand specificity. The six collagen-like stalks appear to be fibril-like and exist in the central region. The collagen-like region and the globular heads can independently interact with a multiplicity of biological structures including pathogen-associated and cell associated molecules, also each of the individual globular head domains is capable of independently interacting with specific ligands. Chains A and B are disulfide-linked whilst the C chain forms a disulfide bond with the C chain of the next strand.     Molecular weight 460 kDa.|curated-complex:"Recognition unit of the classical pathway of complement which associates with the Ca2+ - dependent C1r(2)-C1s(2) tetramer to form C1 (CPX-1920), the first component of the classical complement system. The complex's role in C1 is the recognition of immune complexes, or other molecules, which trigger the classical pathway of the complement system. Independent of complement activation C1q appears to have additional roles in homeostasis and cellular development, superoxide (O2-) production by neutrophils, blood coagulation and neurological synapse pruning."|complex-assembly:Heterooctadecamer	-	figure legend:Fig.2 A,B,C and Table 1|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	kd:6.36x10^-9 ~0.42(molar)	2020/02/14	2020/02/14	-	rogid:3zz5RwIqLyPO71zdCp5Vx7aVl+Y9606	-	false	mutation with no effect:198-198|mutation with no effect:202-202|flag tag:?-?	flag tag:c-c	-	2	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
matrixdb:MULT_82_human	uniprotkb:P00736	intact:EBI-6264901|reactome:R-HSA-173579|wwpdb:1PK6|wwpdb:2wnv|wwpdb:2jg8|wwpdb:2jg9|wwpdb:2wnu|reactome:R-HSA-173588	intact:EBI-3926504|uniprotkb:Q8J012|uniprotkb:Q68D77|uniprotkb:A6NJQ8	psi-mi:c1q_human(display_short)|psi-mi:MULT_82_human(display_long)|intact:Complement component C1q complex(complex recommended name)|intact:C1q(complex synonym)|intact:Complement 1q(complex synonym)|intact:C1QA-C1QB-C1QC complex(complex synonym)|intact:"6xC1QA:6xC1QB:6xC1QC"(complex systematic name)	psi-mi:c1r_human(display_long)|uniprotkb:C1R(gene name)|psi-mi:C1R(display_short)|uniprotkb:Complement component 1 subcomponent r(gene name synonym)	psi-mi:"MI:0107"(surface plasmon resonance)	Bally et al. (2018)	pubmed:30923526|imex:IM-27715	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0915"(physical association)	psi-mi:"MI:0469"(IntAct)	intact:EBI-25425994|imex:IM-27715-1	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0496"(bait)	psi-mi:"MI:0498"(prey)	psi-mi:"MI:1302"(stable complex)	psi-mi:"MI:0326"(protein)	go:"GO:0005509"(calcium ion binding)|go:"GO:0019865"(immunoglobulin binding)|efo:"MONDO:0013343"(see-also)|pubmed:28601358(see-also)|pubmed:22536204(see-also)|intact:EBI-6264878(exp-evidence)|evidence ontology:"ECO:0000353"|complex portal:CPX-1919(complex-primary)|go:"GO:0006958"(complement activation, classical pathway)|go:"GO:0005576"(extracellular region)|pubmed:20548024(see-also)|pubmed:29449492(see-also)|pubmed:18250442(see-also)|go:"GO:0062167"(complement component C1q complex)|pubmed:31165008(see-also)|pubmed:27914690(see-also)|pubmed:26489954(see-also)	interpro:IPR035914|interpro:IPR035976|rcsb pdb:6F1C|rcsb pdb:6F1D|rcsb pdb:6F1H|refseq:NP_001724.3|interpro:IPR000859(CUB)|interpro:IPR001881(EGF-like calcium-binding)|interpro:IPR018097|interpro:IPR009003(Peptidase, trypsin-like serine and cysteine)|interpro:IPR001254(Peptidase S1 and S6, chymotrypsin/Hap)|interpro:IPR001314(Peptidase S1A, chymotrypsin)|interpro:IPR000436(Sushi/SCR/CCP)|rcsb pdb:1APQ|rcsb pdb:1GPZ|rcsb pdb:1MD7|rcsb pdb:1MD8|rcsb pdb:2QY0|go:"GO:0004252"(serine-type endopeptidase activity)|go:"GO:0005509"(calcium ion binding)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0006955"(immune response)|go:"GO:0006958"(complement activation, classical pathway)|go:"GO:0008236"(serine-type peptidase activity)|go:"GO:0031638"(zymogen activation)|go:"GO:0042802"(identical protein binding)|go:"GO:0045087"(innate immune response)|go:"GO:0070062"(extracellular exosome)|go:"GO:0072562"(blood microparticle)|interpro:IPR033116|rcsb pdb:6F39|interpro:IPR000742(EGF-like, type 3)|reactome:R-HSA-166663|reactome:R-HSA-173623|reactome:R-HSA-977606|interpro:IPR035707|interpro:IPR043504	-	disease:"Complement component C1q deficiency (C1QD) [MONDO:0013343]: a disorder caused by impaired activation of the complement classical pathway. It generally leads to severe immune complex disease with features of systemic lupus erythematosus and glomerulonephritis."|complex-properties:The complex comprises of six heterotrimeric collagen-like triple helices, formed from triplets of the A, B, and C chains, that associate in their N-terminal half to form a stalk, then diverge to form individual stems, each terminating in a C-terminal globular domain. Each of the six heterotrimeric globular heads or domains is made up of the globular domains from one A, one B, and one C chain, each of which in turn has its own ligand specificity. The six collagen-like stalks appear to be fibril-like and exist in the central region. The collagen-like region and the globular heads can independently interact with a multiplicity of biological structures including pathogen-associated and cell associated molecules, also each of the individual globular head domains is capable of independently interacting with specific ligands. Chains A and B are disulfide-linked whilst the C chain forms a disulfide bond with the C chain of the next strand.     Molecular weight 460 kDa.|curated-complex:"Recognition unit of the classical pathway of complement which associates with the Ca2+ - dependent C1r(2)-C1s(2) tetramer to form C1 (CPX-1920), the first component of the classical complement system. The complex's role in C1 is the recognition of immune complexes, or other molecules, which trigger the classical pathway of the complement system. Independent of complement activation C1q appears to have additional roles in homeostasis and cellular development, superoxide (O2-) production by neutrophils, blood coagulation and neurological synapse pruning."|complex-assembly:Heterooctadecamer	-	figure legend:Fig.2 A,B,C and Table 1|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	kd:6.36x10^-9 ~0.42(molar)	2020/02/14	2020/02/14	-	rogid:7E+ASC6Hv3CoXdwfWEMwCtYALbw9606	-	false	mutation with no effect:198-198|mutation with no effect:202-202|flag tag:?-?	mutation:654-654|strep tag:c-c	-	2	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:O00187-PRO_0000027598	matrixdb:MULT_82_human	intact:EBI-25426044	intact:EBI-6264901|reactome:R-HSA-173579|wwpdb:1PK6|wwpdb:2wnv|wwpdb:2jg8|wwpdb:2jg9|wwpdb:2wnu|reactome:R-HSA-173588	psi-mi:o00187-pro_0000027598(display_long)|uniprotkb:MBL-associated serine protease 2(gene name synonym)|uniprotkb:Mannose-binding protein-associated serine protease 2(gene name synonym)|uniprotkb:MASP2(gene name)|psi-mi:MASP2(display_short)	psi-mi:c1q_human(display_short)|psi-mi:MULT_82_human(display_long)|intact:Complement component C1q complex(complex recommended name)|intact:C1q(complex synonym)|intact:Complement 1q(complex synonym)|intact:C1QA-C1QB-C1QC complex(complex synonym)|intact:"6xC1QA:6xC1QB:6xC1QC"(complex systematic name)	psi-mi:"MI:0107"(surface plasmon resonance)	Bally et al. (2018)	pubmed:30923526|imex:IM-27715	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0469"(IntAct)	intact:EBI-25426018|imex:IM-27715-3	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0498"(prey)	psi-mi:"MI:0496"(bait)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:1302"(stable complex)	intact:EBI-7965040(chain-parent)	go:"GO:0005509"(calcium ion binding)|go:"GO:0019865"(immunoglobulin binding)|efo:"MONDO:0013343"(see-also)|pubmed:28601358(see-also)|pubmed:22536204(see-also)|intact:EBI-6264878(exp-evidence)|evidence ontology:"ECO:0000353"|complex portal:CPX-1919(complex-primary)|go:"GO:0006958"(complement activation, classical pathway)|go:"GO:0005576"(extracellular region)|pubmed:20548024(see-also)|pubmed:29449492(see-also)|pubmed:18250442(see-also)|go:"GO:0062167"(complement component C1q complex)|pubmed:31165008(see-also)|pubmed:27914690(see-also)|pubmed:26489954(see-also)	-	chain-seq-start:16|chain-seq-end:686	disease:"Complement component C1q deficiency (C1QD) [MONDO:0013343]: a disorder caused by impaired activation of the complement classical pathway. It generally leads to severe immune complex disease with features of systemic lupus erythematosus and glomerulonephritis."|complex-properties:The complex comprises of six heterotrimeric collagen-like triple helices, formed from triplets of the A, B, and C chains, that associate in their N-terminal half to form a stalk, then diverge to form individual stems, each terminating in a C-terminal globular domain. Each of the six heterotrimeric globular heads or domains is made up of the globular domains from one A, one B, and one C chain, each of which in turn has its own ligand specificity. The six collagen-like stalks appear to be fibril-like and exist in the central region. The collagen-like region and the globular heads can independently interact with a multiplicity of biological structures including pathogen-associated and cell associated molecules, also each of the individual globular head domains is capable of independently interacting with specific ligands. Chains A and B are disulfide-linked whilst the C chain forms a disulfide bond with the C chain of the next strand.     Molecular weight 460 kDa.|curated-complex:"Recognition unit of the classical pathway of complement which associates with the Ca2+ - dependent C1r(2)-C1s(2) tetramer to form C1 (CPX-1920), the first component of the classical complement system. The complex's role in C1 is the recognition of immune complexes, or other molecules, which trigger the classical pathway of the complement system. Independent of complement activation C1q appears to have additional roles in homeostasis and cellular development, superoxide (O2-) production by neutrophils, blood coagulation and neurological synapse pruning."|complex-assembly:Heterooctadecamer	figure legend:Fig.2 D,E,F and Table 1|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	kd:5.04x10^-9 ~0.03(molar)	2020/02/14	2020/02/14	rogid:ITPqelOnS4bMzlrC0mxhSvS8DYg9606	-	-	false	mutation:618-618|his tag:c-c|v5 tag:c-c	mutation with no effect:222-223|mutation with no effect:135-136|flag tag:?-?	2	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P26022	matrixdb:MULT_82_human	intact:EBI-11574553|uniprotkb:B2R6T6|uniprotkb:Q38M82|ensembl:ENSP00000295927	intact:EBI-6264901|reactome:R-HSA-173579|wwpdb:1PK6|wwpdb:2wnv|wwpdb:2jg8|wwpdb:2jg9|wwpdb:2wnu|reactome:R-HSA-173588	psi-mi:ptx3_human(display_long)|uniprotkb:Pentaxin-related protein PTX3(gene name synonym)|uniprotkb:TNFAIP5(gene name synonym)|uniprotkb:TSG14(gene name synonym)|uniprotkb:Tumor necrosis factor alpha-induced protein 5(gene name synonym)|uniprotkb:Tumor necrosis factor-inducible gene 14 protein(gene name synonym)|uniprotkb:PTX3(gene name)|psi-mi:PTX3(display_short)	psi-mi:c1q_human(display_short)|psi-mi:MULT_82_human(display_long)|intact:Complement component C1q complex(complex recommended name)|intact:C1q(complex synonym)|intact:Complement 1q(complex synonym)|intact:C1QA-C1QB-C1QC complex(complex synonym)|intact:"6xC1QA:6xC1QB:6xC1QC"(complex systematic name)	psi-mi:"MI:0107"(surface plasmon resonance)	Bally et al. (2018)	pubmed:30923526|imex:IM-27715	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0469"(IntAct)	intact:EBI-25426378|imex:IM-27715-5	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0498"(prey)	psi-mi:"MI:0496"(bait)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:1302"(stable complex)	refseq:NP_002843.2|ensembl:ENSG00000163661(gene)|ensembl:ENST00000295927(transcript)|go:"GO:0001550"(ovarian cumulus expansion)|go:"GO:0001849"(complement component C1q complex binding)|go:"GO:0001872"("(1->3)-beta-D-glucan binding")|go:"GO:0001878"(response to yeast)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0006954"(inflammatory response)|go:"GO:0008228"(opsonization)|go:"GO:0030198"(extracellular matrix organization)|go:"GO:0031012"(extracellular matrix)|go:"GO:0035580"(specific granule lumen)|go:"GO:0042802"(identical protein binding)|go:"GO:0044793"(negative regulation by host of viral process)|go:"GO:0044869"(negative regulation by host of viral exo-alpha-sialidase activity)|go:"GO:0044871"(negative regulation by host of viral glycoprotein metabolic process)|go:"GO:0045087"(innate immune response)|go:"GO:0045429"(positive regulation of nitric oxide biosynthetic process)|go:"GO:0046597"(negative regulation of viral entry into host cell)|go:"GO:0046790"(virion binding)|go:"GO:0050766"(positive regulation of phagocytosis)|go:"GO:1903016"(negative regulation of exo-alpha-sialidase activity)|go:"GO:1903019"(negative regulation of glycoprotein metabolic process)|go:"GO:1904724"(tertiary granule lumen)|interpro:IPR001759(Pentaxin)|interpro:IPR006558(LamG-like jellyroll fold)|interpro:IPR013320(Concanavalin A-like lectin/glucanase, subgroup)|interpro:IPR030476|interpro:IPR042837|reactome:R-HSA-6798695	go:"GO:0005509"(calcium ion binding)|go:"GO:0019865"(immunoglobulin binding)|efo:"MONDO:0013343"(see-also)|pubmed:28601358(see-also)|pubmed:22536204(see-also)|intact:EBI-6264878(exp-evidence)|evidence ontology:"ECO:0000353"|complex portal:CPX-1919(complex-primary)|go:"GO:0006958"(complement activation, classical pathway)|go:"GO:0005576"(extracellular region)|pubmed:20548024(see-also)|pubmed:29449492(see-also)|pubmed:18250442(see-also)|go:"GO:0062167"(complement component C1q complex)|pubmed:31165008(see-also)|pubmed:27914690(see-also)|pubmed:26489954(see-also)	-	-	disease:"Complement component C1q deficiency (C1QD) [MONDO:0013343]: a disorder caused by impaired activation of the complement classical pathway. It generally leads to severe immune complex disease with features of systemic lupus erythematosus and glomerulonephritis."|complex-properties:The complex comprises of six heterotrimeric collagen-like triple helices, formed from triplets of the A, B, and C chains, that associate in their N-terminal half to form a stalk, then diverge to form individual stems, each terminating in a C-terminal globular domain. Each of the six heterotrimeric globular heads or domains is made up of the globular domains from one A, one B, and one C chain, each of which in turn has its own ligand specificity. The six collagen-like stalks appear to be fibril-like and exist in the central region. The collagen-like region and the globular heads can independently interact with a multiplicity of biological structures including pathogen-associated and cell associated molecules, also each of the individual globular head domains is capable of independently interacting with specific ligands. Chains A and B are disulfide-linked whilst the C chain forms a disulfide bond with the C chain of the next strand.     Molecular weight 460 kDa.|curated-complex:"Recognition unit of the classical pathway of complement which associates with the Ca2+ - dependent C1r(2)-C1s(2) tetramer to form C1 (CPX-1920), the first component of the classical complement system. The complex's role in C1 is the recognition of immune complexes, or other molecules, which trigger the classical pathway of the complement system. Independent of complement activation C1q appears to have additional roles in homeostasis and cellular development, superoxide (O2-) production by neutrophils, blood coagulation and neurological synapse pruning."|complex-assembly:Heterooctadecamer	figure legend:Fig.3 A-E and Table 2|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	kd:5.65x10^-9 ~0.82(molar)	2020/02/14	2020/02/14	rogid:E2p0QaxS5/8mpgyOghoPCB+WHx09606	-	-	false	variant:48-48(rs3816527)	mutation decreasing interaction strength:222-223|mutation disrupting interaction strength:135-136|flag tag:?-?|mutation decreasing interaction strength:198-198|mutation disrupting interaction strength:202-202	2	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
matrixdb:MULT_82_human	uniprotkb:P26022	intact:EBI-6264901|reactome:R-HSA-173579|wwpdb:1PK6|wwpdb:2wnv|wwpdb:2jg8|wwpdb:2jg9|wwpdb:2wnu|reactome:R-HSA-173588	intact:EBI-11574553|uniprotkb:B2R6T6|uniprotkb:Q38M82|ensembl:ENSP00000295927	psi-mi:c1q_human(display_short)|psi-mi:MULT_82_human(display_long)|intact:Complement component C1q complex(complex recommended name)|intact:C1q(complex synonym)|intact:Complement 1q(complex synonym)|intact:C1QA-C1QB-C1QC complex(complex synonym)|intact:"6xC1QA:6xC1QB:6xC1QC"(complex systematic name)	psi-mi:ptx3_human(display_long)|uniprotkb:Pentaxin-related protein PTX3(gene name synonym)|uniprotkb:TNFAIP5(gene name synonym)|uniprotkb:TSG14(gene name synonym)|uniprotkb:Tumor necrosis factor alpha-induced protein 5(gene name synonym)|uniprotkb:Tumor necrosis factor-inducible gene 14 protein(gene name synonym)|uniprotkb:PTX3(gene name)|psi-mi:PTX3(display_short)	psi-mi:"MI:0892"(solid phase assay)	Bally et al. (2018)	pubmed:30923526|imex:IM-27715	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0469"(IntAct)	intact:EBI-25426479|imex:IM-27715-7	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0496"(bait)	psi-mi:"MI:0498"(prey)	psi-mi:"MI:1302"(stable complex)	psi-mi:"MI:0326"(protein)	go:"GO:0005509"(calcium ion binding)|go:"GO:0019865"(immunoglobulin binding)|efo:"MONDO:0013343"(see-also)|pubmed:28601358(see-also)|pubmed:22536204(see-also)|intact:EBI-6264878(exp-evidence)|evidence ontology:"ECO:0000353"|complex portal:CPX-1919(complex-primary)|go:"GO:0006958"(complement activation, classical pathway)|go:"GO:0005576"(extracellular region)|pubmed:20548024(see-also)|pubmed:29449492(see-also)|pubmed:18250442(see-also)|go:"GO:0062167"(complement component C1q complex)|pubmed:31165008(see-also)|pubmed:27914690(see-also)|pubmed:26489954(see-also)	refseq:NP_002843.2|ensembl:ENSG00000163661(gene)|ensembl:ENST00000295927(transcript)|go:"GO:0001550"(ovarian cumulus expansion)|go:"GO:0001849"(complement component C1q complex binding)|go:"GO:0001872"("(1->3)-beta-D-glucan binding")|go:"GO:0001878"(response to yeast)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0006954"(inflammatory response)|go:"GO:0008228"(opsonization)|go:"GO:0030198"(extracellular matrix organization)|go:"GO:0031012"(extracellular matrix)|go:"GO:0035580"(specific granule lumen)|go:"GO:0042802"(identical protein binding)|go:"GO:0044793"(negative regulation by host of viral process)|go:"GO:0044869"(negative regulation by host of viral exo-alpha-sialidase activity)|go:"GO:0044871"(negative regulation by host of viral glycoprotein metabolic process)|go:"GO:0045087"(innate immune response)|go:"GO:0045429"(positive regulation of nitric oxide biosynthetic process)|go:"GO:0046597"(negative regulation of viral entry into host cell)|go:"GO:0046790"(virion binding)|go:"GO:0050766"(positive regulation of phagocytosis)|go:"GO:1903016"(negative regulation of exo-alpha-sialidase activity)|go:"GO:1903019"(negative regulation of glycoprotein metabolic process)|go:"GO:1904724"(tertiary granule lumen)|interpro:IPR001759(Pentaxin)|interpro:IPR006558(LamG-like jellyroll fold)|interpro:IPR013320(Concanavalin A-like lectin/glucanase, subgroup)|interpro:IPR030476|interpro:IPR042837|reactome:R-HSA-6798695	-	disease:"Complement component C1q deficiency (C1QD) [MONDO:0013343]: a disorder caused by impaired activation of the complement classical pathway. It generally leads to severe immune complex disease with features of systemic lupus erythematosus and glomerulonephritis."|complex-properties:The complex comprises of six heterotrimeric collagen-like triple helices, formed from triplets of the A, B, and C chains, that associate in their N-terminal half to form a stalk, then diverge to form individual stems, each terminating in a C-terminal globular domain. Each of the six heterotrimeric globular heads or domains is made up of the globular domains from one A, one B, and one C chain, each of which in turn has its own ligand specificity. The six collagen-like stalks appear to be fibril-like and exist in the central region. The collagen-like region and the globular heads can independently interact with a multiplicity of biological structures including pathogen-associated and cell associated molecules, also each of the individual globular head domains is capable of independently interacting with specific ligands. Chains A and B are disulfide-linked whilst the C chain forms a disulfide bond with the C chain of the next strand.     Molecular weight 460 kDa.|curated-complex:"Recognition unit of the classical pathway of complement which associates with the Ca2+ - dependent C1r(2)-C1s(2) tetramer to form C1 (CPX-1920), the first component of the classical complement system. The complex's role in C1 is the recognition of immune complexes, or other molecules, which trigger the classical pathway of the complement system. Independent of complement activation C1q appears to have additional roles in homeostasis and cellular development, superoxide (O2-) production by neutrophils, blood coagulation and neurological synapse pruning."|complex-assembly:Heterooctadecamer	-	figure legend:Fig. 5D|comment:"In this regard, when assayed in solid phase binding experiments, the D48 and A48 alleles had comparable binding to plastic-immobilized C1q at each applied concentration (Figure 5D), indicating that in the described experimental conditions the p.D48A polymorphism does not affect the interaction of PTX3 with C1q."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2020/02/14	2020/02/14	-	rogid:E2p0QaxS5/8mpgyOghoPCB+WHx09606	-	false	-	mutation with no effect:48-48(r3816527)	-	-	psi-mi:"MI:0421"(identification by antibody)	psi-mi:"MI:0421"(identification by antibody)