#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:P02741-PRO_0000023526	matrixdb:MULT_82_human	intact:EBI-22033103	intact:EBI-6264901|reactome:R-HSA-173579|wwpdb:1PK6|wwpdb:2wnv|wwpdb:2jg8|wwpdb:2jg9|wwpdb:2wnu|reactome:R-HSA-173588	psi-mi:p02741-pro_0000023526(display_long)|uniprotkb:CRP(gene name)|psi-mi:CRP(display_short)|uniprotkb:PTX1(gene name synonym)	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)	Bíró et al. (2007)	pubmed:17244159|imex:IM-27413	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-22079081|imex:IM-27413-1	-	-	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-1395983(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:19|chain-seq-end:224	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:2, Table 1|comment:"Cr-mCRP (acylated and mutated monomeric CRP)  readily bound to immobilized C1q. In contrast, no interaction was detected under the same conditions using pentameric CRP."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	kd:0.28x10^-9(molar)	2019/09/04	2019/10/07	rogid:CvK4vTdUxXgEsFN2HKUWzPg5lx49606	-	-	false	protein modification:1-1|mutation:36-36,97-97|acylated residue:?-?	-	1	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P02741-PRO_0000023526	matrixdb:MULT_82_human	intact:EBI-22033103	intact:EBI-6264901|reactome:R-HSA-173579|wwpdb:1PK6|wwpdb:2wnv|wwpdb:2jg8|wwpdb:2jg9|wwpdb:2wnu|reactome:R-HSA-173588	psi-mi:p02741-pro_0000023526(display_long)|uniprotkb:CRP(gene name)|psi-mi:CRP(display_short)|uniprotkb:PTX1(gene name synonym)	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)	Bíró et al. (2007)	pubmed:17244159|imex:IM-27413	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-22079440|imex:IM-27413-9	-	-	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:0326"(protein)	psi-mi:"MI:1302"(stable complex)	intact:EBI-1395983(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:19|chain-seq-end:224	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:Table 2|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	kd:1.95x10^-9(molar)	2019/09/04	2019/10/07	rogid:CvK4vTdUxXgEsFN2HKUWzPg5lx49606	-	-	false	protein modification:1-1|mutation:36-36,97-97|acylated residue:?-?	sufficient binding region:?-?	1	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P02741	matrixdb:MULT_82_human	intact:EBI-1395983|uniprotkb:A8K078|uniprotkb:Q08AK3|uniprotkb:Q8WW75|uniprotkb:D3DVD9|uniprotkb:D3DVE0|ensembl:ENSP00000255030	intact:EBI-6264901|reactome:R-HSA-173579|wwpdb:1PK6|wwpdb:2wnv|wwpdb:2jg8|wwpdb:2jg9|wwpdb:2wnu|reactome:R-HSA-173588	psi-mi:crp_human(display_long)|uniprotkb:CRP(gene name)|psi-mi:CRP(display_short)|uniprotkb:PTX1(gene name synonym)	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)	Bíró et al. (2007)	pubmed:17244159|imex:IM-27413	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-22079480|imex:IM-27413-11	-	-	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:0326"(protein)	psi-mi:"MI:1302"(stable complex)	refseq:NP_000558.2|refseq:NP_001315986.1|refseq:NP_001315987.1|dip:DIP-39125N|ensembl:ENSG00000132693(gene)|ensembl:ENST00000255030(transcript)|go:"GO:0001849"(complement component C1q complex binding)|go:"GO:0005509"(calcium ion binding)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0006953"(acute-phase response)|go:"GO:0006954"(inflammatory response)|go:"GO:0006958"(complement activation, classical pathway)|go:"GO:0008228"(opsonization)|go:"GO:0010628"(positive regulation of gene expression)|go:"GO:0010745"(negative regulation of macrophage derived foam cell differentiation)|go:"GO:0010888"(negative regulation of lipid storage)|go:"GO:0030169"(low-density lipoprotein particle binding)|go:"GO:0032677"(regulation of interleukin-8 production)|go:"GO:0032930"(positive regulation of superoxide anion generation)|go:"GO:0032945"(negative regulation of mononuclear cell proliferation)|go:"GO:0033265"(choline binding)|go:"GO:0042310"(vasoconstriction)|go:"GO:0042802"(identical protein binding)|go:"GO:0044793"(negative regulation by host of viral process)|go:"GO:0045087"(innate immune response)|go:"GO:0050750"(low-density lipoprotein particle receptor binding)|go:"GO:0050830"(defense response to Gram-positive bacterium)|interpro:IPR001759(Pentaxin)|interpro:IPR013320(Concanavalin A-like lectin/glucanase, subgroup)|interpro:IPR030476|mint:P02741|rcsb pdb:1B09|rcsb pdb:1CRV|rcsb pdb:1GNH|rcsb pdb:1LJ7|rcsb pdb:3L2Y|rcsb pdb:3PVN|rcsb pdb:3PVO|reactome:R-HSA-173623	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:Table 2-1/2|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	kd:1.45x10^-9(molar)	2019/09/04	2019/10/07	rogid:R7vKMSGKD4ETbUKVGL9IiL8jzjE9606	-	-	false	-	sufficient binding region:?-?	5	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P04003	uniprotkb:P02741-PRO_0000023526	intact:EBI-978348|ensembl:ENSP00000356037|uniprotkb:Q5VVQ8	intact:EBI-22033103	psi-mi:c4bpa_human(display_long)|uniprotkb:Proline-rich protein(gene name synonym)|uniprotkb:C4BPA(gene name)|psi-mi:C4BPA(display_short)|uniprotkb:C4BP(gene name synonym)	psi-mi:p02741-pro_0000023526(display_long)|uniprotkb:CRP(gene name)|psi-mi:CRP(display_short)|uniprotkb:PTX1(gene name synonym)	psi-mi:"MI:0107"(surface plasmon resonance)	Bíró et al. (2007)	pubmed:17244159|imex:IM-27413	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-22079983|imex:IM-27413-29	-	-	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:0326"(protein)	psi-mi:"MI:0326"(protein)	ensembl:ENSG00000123838(gene)|ensembl:ENST00000367070(transcript)|go:"GO:0003723"(RNA binding)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0005886"(plasma membrane)|go:"GO:0006958"(complement activation, classical pathway)|go:"GO:0009609"(response to symbiotic bacterium)|go:"GO:0045087"(innate immune response)|go:"GO:0045732"(positive regulation of protein catabolic process)|go:"GO:0045959"(negative regulation of complement activation, classical pathway)|go:"GO:0072562"(blood microparticle)|go:"GO:1903027"(regulation of opsonization)|interpro:IPR000436(Sushi/SCR/CCP)|interpro:IPR035976|interpro:IPR040514|rcsb pdb:2A55|rcsb pdb:4B0F|rcsb pdb:5HYP|rcsb pdb:5HYT|rcsb pdb:5HYU|rcsb pdb:5HZP|rcsb pdb:5I0Q|reactome:R-HSA-977606|refseq:NP_000706.1|refseq:XP_005273308.1|refseq:XP_005273309.1	intact:EBI-1395983(chain-parent)	-	-	chain-seq-start:19|chain-seq-end:224	figure legend:7, Table 4|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	kd:5.87x10^-9(molar)	2019/09/04	2019/11/04	rogid:S0F99wuDTalS4UCuYGWbiCgWlO09606	rogid:CvK4vTdUxXgEsFN2HKUWzPg5lx49606	rigid:w2Ef6yAZO0DSrn1fr5n8iWmZHVw	false	-	protein modification:1-1|mutation:36-36,97-97|acylated residue:?-?	7	1	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
chebi:"CHEBI:64482"	uniprotkb:P02741	intact:EBI-13642339	intact:EBI-1395983|uniprotkb:A8K078|uniprotkb:Q08AK3|uniprotkb:Q8WW75|uniprotkb:D3DVD9|uniprotkb:D3DVE0|ensembl:ENSP00000255030	psi-mi:phosphatidylcholine(display_short)|psi-mi:"CHEBI:64482"(display_long)|intact:1,2-diacyl-glycero-3-phosphocholine(synonym)|intact:"a phosphatidylcholine (0)"(synonym)|intact:"2,3-bis(acyloxy)propyl 2-(trimethylammonio)ethyl phosphate"(iupac name)	psi-mi:crp_human(display_long)|uniprotkb:CRP(gene name)|psi-mi:CRP(display_short)|uniprotkb:PTX1(gene name synonym)	psi-mi:"MI:0411"(enzyme linked immunosorbent assay)	Bíró et al. (2007)	pubmed:17244159|imex:IM-27413	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0915"(physical association)	psi-mi:"MI:0469"(IntAct)	intact:EBI-22079142|imex:IM-27413-21	-	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:0328"(small molecule)	psi-mi:"MI:0326"(protein)	-	refseq:NP_000558.2|refseq:NP_001315986.1|refseq:NP_001315987.1|dip:DIP-39125N|ensembl:ENSG00000132693(gene)|ensembl:ENST00000255030(transcript)|go:"GO:0001849"(complement component C1q complex binding)|go:"GO:0005509"(calcium ion binding)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0006953"(acute-phase response)|go:"GO:0006954"(inflammatory response)|go:"GO:0006958"(complement activation, classical pathway)|go:"GO:0008228"(opsonization)|go:"GO:0010628"(positive regulation of gene expression)|go:"GO:0010745"(negative regulation of macrophage derived foam cell differentiation)|go:"GO:0010888"(negative regulation of lipid storage)|go:"GO:0030169"(low-density lipoprotein particle binding)|go:"GO:0032677"(regulation of interleukin-8 production)|go:"GO:0032930"(positive regulation of superoxide anion generation)|go:"GO:0032945"(negative regulation of mononuclear cell proliferation)|go:"GO:0033265"(choline binding)|go:"GO:0042310"(vasoconstriction)|go:"GO:0042802"(identical protein binding)|go:"GO:0044793"(negative regulation by host of viral process)|go:"GO:0045087"(innate immune response)|go:"GO:0050750"(low-density lipoprotein particle receptor binding)|go:"GO:0050830"(defense response to Gram-positive bacterium)|interpro:IPR001759(Pentaxin)|interpro:IPR013320(Concanavalin A-like lectin/glucanase, subgroup)|interpro:IPR030476|mint:P02741|rcsb pdb:1B09|rcsb pdb:1CRV|rcsb pdb:1GNH|rcsb pdb:1LJ7|rcsb pdb:3L2Y|rcsb pdb:3PVN|rcsb pdb:3PVO|reactome:R-HSA-173623	-	-	-	figure legend:3b|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/09/04	2019/10/07	-	rogid:R7vKMSGKD4ETbUKVGL9IiL8jzjE9606	-	false	-	-	-	5	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
chebi:"CHEBI:64482"	matrixdb:MULT_82_human	intact:EBI-13642339	intact:EBI-6264901|reactome:R-HSA-173579|wwpdb:1PK6|wwpdb:2wnv|wwpdb:2jg8|wwpdb:2jg9|wwpdb:2wnu|reactome:R-HSA-173588	psi-mi:phosphatidylcholine(display_short)|psi-mi:"CHEBI:64482"(display_long)|intact:1,2-diacyl-glycero-3-phosphocholine(synonym)|intact:"a phosphatidylcholine (0)"(synonym)|intact:"2,3-bis(acyloxy)propyl 2-(trimethylammonio)ethyl phosphate"(iupac name)	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:0411"(enzyme linked immunosorbent assay)	Bíró et al. (2007)	pubmed:17244159|imex:IM-27413	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0915"(physical association)	psi-mi:"MI:0469"(IntAct)	intact:EBI-22079142|imex:IM-27413-21	-	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:0328"(small molecule)	psi-mi:"MI:1302"(stable complex)	-	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:3b|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/09/04	2019/10/07	-	-	-	false	-	-	-	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
chebi:"CHEBI:64482"	matrixdb:MULT_82_human	intact:EBI-13642339	intact:EBI-6264901|reactome:R-HSA-173579|wwpdb:1PK6|wwpdb:2wnv|wwpdb:2jg8|wwpdb:2jg9|wwpdb:2wnu|reactome:R-HSA-173588	psi-mi:phosphatidylcholine(display_short)|psi-mi:"CHEBI:64482"(display_long)|intact:1,2-diacyl-glycero-3-phosphocholine(synonym)|intact:"a phosphatidylcholine (0)"(synonym)|intact:"2,3-bis(acyloxy)propyl 2-(trimethylammonio)ethyl phosphate"(iupac name)	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:0411"(enzyme linked immunosorbent assay)	Bíró et al. (2007)	pubmed:17244159|imex:IM-27413	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0915"(physical association)	psi-mi:"MI:0469"(IntAct)	intact:EBI-22079161|imex:IM-27413-3	-	-	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:0328"(small molecule)	psi-mi:"MI:1302"(stable complex)	-	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:3b-2|comment:Some binding of C1q  to PC-KLH was seen in the absence of  polymeric CRP.|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/09/04	2019/10/07	-	-	-	false	-	-	-	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P02741-PRO_0000023526	matrixdb:MULT_82_human	intact:EBI-22033103	intact:EBI-6264901|reactome:R-HSA-173579|wwpdb:1PK6|wwpdb:2wnv|wwpdb:2jg8|wwpdb:2jg9|wwpdb:2wnu|reactome:R-HSA-173588	psi-mi:p02741-pro_0000023526(display_long)|uniprotkb:CRP(gene name)|psi-mi:CRP(display_short)|uniprotkb:PTX1(gene name synonym)	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:0411"(enzyme linked immunosorbent assay)	Bíró et al. (2007)	pubmed:17244159|imex:IM-27413	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-22079282|imex:IM-27413-5	-	-	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)	intact:EBI-1395983(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:19|chain-seq-end:224	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:3, 4|comment:"Cr-mCRP (acylated and mutated monomeric CRP)  readily bound to immobilized C1q. In contrast, no interaction was detected under the same conditions using pentameric CRP."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/09/04	2019/11/04	rogid:CvK4vTdUxXgEsFN2HKUWzPg5lx49606	-	-	false	protein modification:1-1|mutation:36-36,97-97|acylated residue:?-?	-	1	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
matrixdb:MULT_82_human	matrixdb:MULT_82_human	intact:EBI-6264901|reactome:R-HSA-173579|wwpdb:1PK6|wwpdb:2wnv|wwpdb:2jg8|wwpdb:2jg9|wwpdb:2wnu|reactome:R-HSA-173588	intact:EBI-6264901|reactome:R-HSA-173579|wwpdb:1PK6|wwpdb:2wnv|wwpdb:2jg8|wwpdb:2jg9|wwpdb:2wnu|reactome:R-HSA-173588	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: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:0411"(enzyme linked immunosorbent assay)	Bíró et al. (2007)	pubmed:17244159|imex:IM-27413	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-22079335|imex:IM-27413-7	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0941"(competitor)	psi-mi:"MI:0496"(bait)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:1302"(stable complex)	psi-mi:"MI:1302"(stable complex)	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)	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	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:4|comment:"Fragments corresponding to the globular head regions of C1q (C1q GR) also competed for binding to CRP."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/09/04	2019/11/04	-	-	-	false	-	sufficient binding region:?-?	-	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
matrixdb:MULT_82_human	uniprotkb:P02741-PRO_0000023526	intact:EBI-6264901|reactome:R-HSA-173579|wwpdb:1PK6|wwpdb:2wnv|wwpdb:2jg8|wwpdb:2jg9|wwpdb:2wnu|reactome:R-HSA-173588	intact:EBI-22033103	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:p02741-pro_0000023526(display_long)|uniprotkb:CRP(gene name)|psi-mi:CRP(display_short)|uniprotkb:PTX1(gene name synonym)	psi-mi:"MI:0411"(enzyme linked immunosorbent assay)	Bíró et al. (2007)	pubmed:17244159|imex:IM-27413	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-22079335|imex:IM-27413-7	-	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)	intact:EBI-1395983(chain-parent)	-	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	chain-seq-start:19|chain-seq-end:224	figure legend:4|comment:"Fragments corresponding to the globular head regions of C1q (C1q GR) also competed for binding to CRP."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/09/04	2019/11/04	-	rogid:CvK4vTdUxXgEsFN2HKUWzPg5lx49606	-	false	-	protein modification:1-1|mutation:36-36,97-97|acylated residue:?-?	-	1	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P02741	matrixdb:MULT_82_human	intact:EBI-1395983|uniprotkb:A8K078|uniprotkb:Q08AK3|uniprotkb:Q8WW75|uniprotkb:D3DVD9|uniprotkb:D3DVE0|ensembl:ENSP00000255030	intact:EBI-6264901|reactome:R-HSA-173579|wwpdb:1PK6|wwpdb:2wnv|wwpdb:2jg8|wwpdb:2jg9|wwpdb:2wnu|reactome:R-HSA-173588	psi-mi:crp_human(display_long)|uniprotkb:CRP(gene name)|psi-mi:CRP(display_short)|uniprotkb:PTX1(gene name synonym)	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:0411"(enzyme linked immunosorbent assay)	Bíró et al. (2007)	pubmed:17244159|imex:IM-27413	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-22079331|imex:IM-27413-23	-	-	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_000558.2|refseq:NP_001315986.1|refseq:NP_001315987.1|dip:DIP-39125N|ensembl:ENSG00000132693(gene)|ensembl:ENST00000255030(transcript)|go:"GO:0001849"(complement component C1q complex binding)|go:"GO:0005509"(calcium ion binding)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0006953"(acute-phase response)|go:"GO:0006954"(inflammatory response)|go:"GO:0006958"(complement activation, classical pathway)|go:"GO:0008228"(opsonization)|go:"GO:0010628"(positive regulation of gene expression)|go:"GO:0010745"(negative regulation of macrophage derived foam cell differentiation)|go:"GO:0010888"(negative regulation of lipid storage)|go:"GO:0030169"(low-density lipoprotein particle binding)|go:"GO:0032677"(regulation of interleukin-8 production)|go:"GO:0032930"(positive regulation of superoxide anion generation)|go:"GO:0032945"(negative regulation of mononuclear cell proliferation)|go:"GO:0033265"(choline binding)|go:"GO:0042310"(vasoconstriction)|go:"GO:0042802"(identical protein binding)|go:"GO:0044793"(negative regulation by host of viral process)|go:"GO:0045087"(innate immune response)|go:"GO:0050750"(low-density lipoprotein particle receptor binding)|go:"GO:0050830"(defense response to Gram-positive bacterium)|interpro:IPR001759(Pentaxin)|interpro:IPR013320(Concanavalin A-like lectin/glucanase, subgroup)|interpro:IPR030476|mint:P02741|rcsb pdb:1B09|rcsb pdb:1CRV|rcsb pdb:1GNH|rcsb pdb:1LJ7|rcsb pdb:3L2Y|rcsb pdb:3PVN|rcsb pdb:3PVO|reactome:R-HSA-173623	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:3|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/09/04	2019/10/07	rogid:R7vKMSGKD4ETbUKVGL9IiL8jzjE9606	-	-	false	-	-	1	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P02741-PRO_0000023526	uniprotkb:P08603	intact:EBI-22033103	intact:EBI-1223708|uniprotkb:A5PL14|uniprotkb:Q2TAZ5|uniprotkb:P78435|uniprotkb:Q14570|uniprotkb:Q38G77|uniprotkb:Q5TFM3|uniprotkb:Q8N708|uniprotkb:Q9NU86|ensembl:ENSP00000356399	psi-mi:p02741-pro_0000023526(display_long)|uniprotkb:CRP(gene name)|psi-mi:CRP(display_short)|uniprotkb:PTX1(gene name synonym)	psi-mi:cfah_human(display_long)|uniprotkb:CFH(gene name)|psi-mi:CFH(display_short)|uniprotkb:HF(gene name synonym)|uniprotkb:HF1(gene name synonym)|uniprotkb:HF2(gene name synonym)|uniprotkb:H factor 1(gene name synonym)	psi-mi:"MI:0411"(enzyme linked immunosorbent assay)	Bíró et al. (2007)	pubmed:17244159|imex:IM-27413	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-22079913|imex:IM-27413-13	-	-	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:0326"(protein)	psi-mi:"MI:0326"(protein)	intact:EBI-1395983(chain-parent)	refseq:NP_000177.2|dip:DIP-38303N|ensembl:ENSG00000000971(gene)|ensembl:ENST00000367429(transcript)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0006956"(complement activation)|go:"GO:0006957"(complement activation, alternative pathway)|go:"GO:0008201"(heparin binding)|go:"GO:0030449"(regulation of complement activation)|go:"GO:0042802"(identical protein binding)|go:"GO:0043395"(heparan sulfate proteoglycan binding)|go:"GO:0070062"(extracellular exosome)|go:"GO:0072562"(blood microparticle)|go:"GO:1903659"(regulation of complement-dependent cytotoxicity)|interpro:IPR000436(Sushi/SCR/CCP)|interpro:IPR035976|mint:P08603|rcsb pdb:1FHC|rcsb pdb:1HAQ|rcsb pdb:1HCC|rcsb pdb:1HFH|rcsb pdb:1HFI|rcsb pdb:1KOV|rcsb pdb:2QFH|rcsb pdb:2RLP|rcsb pdb:2RLQ|rcsb pdb:2UWN|rcsb pdb:2V8E|rcsb pdb:2W80|rcsb pdb:2BZM|rcsb pdb:2G7I|rcsb pdb:2W81|rcsb pdb:2WII|rcsb pdb:2XQW|rcsb pdb:3GAU|rcsb pdb:3GAV|rcsb pdb:3GAW|rcsb pdb:3KXV|rcsb pdb:3KZJ|rcsb pdb:3OXU|rcsb pdb:3R62|rcsb pdb:3RJ3|rcsb pdb:3SW0|rcsb pdb:4AYD|rcsb pdb:4AYE|rcsb pdb:4AYI|rcsb pdb:4AYM|rcsb pdb:4B2R|rcsb pdb:4B2S|rcsb pdb:2IC4|rcsb pdb:2JGW|rcsb pdb:2JGX|rcsb pdb:4J38|rcsb pdb:4K12|rcsb pdb:4ONT|rcsb pdb:4ZH1|rcsb pdb:5NBQ|rcsb pdb:5O32|rcsb pdb:5O35|rcsb pdb:2KMS|rcsb pdb:2QFG|rcsb pdb:5WTB|rcsb pdb:6ATG|reactome:R-HSA-977606	-	chain-seq-start:19|chain-seq-end:224	-	figure legend:5A, 8|comment:Preincubation of immobilized Cr-mCRP with C1q had no significant effect on subsequent binding of FH or C4BP.|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/09/04	2019/11/04	rogid:CvK4vTdUxXgEsFN2HKUWzPg5lx49606	rogid:1mjo+AJLIQnEsMFqsGsmUFbfUxk9606	rigid:j7J02aEiR5U4XuCFyVHXAsvVUos	false	protein modification:1-1|mutation:36-36,97-97|acylated residue:?-?	-	1	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P02741-PRO_0000023526	uniprotkb:P08603	intact:EBI-22033103	intact:EBI-1223708|uniprotkb:A5PL14|uniprotkb:Q2TAZ5|uniprotkb:P78435|uniprotkb:Q14570|uniprotkb:Q38G77|uniprotkb:Q5TFM3|uniprotkb:Q8N708|uniprotkb:Q9NU86|ensembl:ENSP00000356399	psi-mi:p02741-pro_0000023526(display_long)|uniprotkb:CRP(gene name)|psi-mi:CRP(display_short)|uniprotkb:PTX1(gene name synonym)	psi-mi:cfah_human(display_long)|uniprotkb:CFH(gene name)|psi-mi:CFH(display_short)|uniprotkb:HF(gene name synonym)|uniprotkb:HF1(gene name synonym)|uniprotkb:HF2(gene name synonym)|uniprotkb:H factor 1(gene name synonym)	psi-mi:"MI:0411"(enzyme linked immunosorbent assay)	Bíró et al. (2007)	pubmed:17244159|imex:IM-27413	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-22079926|imex:IM-27413-25	-	-	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:0326"(protein)	psi-mi:"MI:0326"(protein)	intact:EBI-1395983(chain-parent)	refseq:NP_000177.2|dip:DIP-38303N|ensembl:ENSG00000000971(gene)|ensembl:ENST00000367429(transcript)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0006956"(complement activation)|go:"GO:0006957"(complement activation, alternative pathway)|go:"GO:0008201"(heparin binding)|go:"GO:0030449"(regulation of complement activation)|go:"GO:0042802"(identical protein binding)|go:"GO:0043395"(heparan sulfate proteoglycan binding)|go:"GO:0070062"(extracellular exosome)|go:"GO:0072562"(blood microparticle)|go:"GO:1903659"(regulation of complement-dependent cytotoxicity)|interpro:IPR000436(Sushi/SCR/CCP)|interpro:IPR035976|mint:P08603|rcsb pdb:1FHC|rcsb pdb:1HAQ|rcsb pdb:1HCC|rcsb pdb:1HFH|rcsb pdb:1HFI|rcsb pdb:1KOV|rcsb pdb:2QFH|rcsb pdb:2RLP|rcsb pdb:2RLQ|rcsb pdb:2UWN|rcsb pdb:2V8E|rcsb pdb:2W80|rcsb pdb:2BZM|rcsb pdb:2G7I|rcsb pdb:2W81|rcsb pdb:2WII|rcsb pdb:2XQW|rcsb pdb:3GAU|rcsb pdb:3GAV|rcsb pdb:3GAW|rcsb pdb:3KXV|rcsb pdb:3KZJ|rcsb pdb:3OXU|rcsb pdb:3R62|rcsb pdb:3RJ3|rcsb pdb:3SW0|rcsb pdb:4AYD|rcsb pdb:4AYE|rcsb pdb:4AYI|rcsb pdb:4AYM|rcsb pdb:4B2R|rcsb pdb:4B2S|rcsb pdb:2IC4|rcsb pdb:2JGW|rcsb pdb:2JGX|rcsb pdb:4J38|rcsb pdb:4K12|rcsb pdb:4ONT|rcsb pdb:4ZH1|rcsb pdb:5NBQ|rcsb pdb:5O32|rcsb pdb:5O35|rcsb pdb:2KMS|rcsb pdb:2QFG|rcsb pdb:5WTB|rcsb pdb:6ATG|reactome:R-HSA-977606	-	chain-seq-start:19|chain-seq-end:224	-	figure legend:5A-2|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/09/04	2019/11/04	rogid:CvK4vTdUxXgEsFN2HKUWzPg5lx49606	rogid:1mjo+AJLIQnEsMFqsGsmUFbfUxk9606	rigid:j7J02aEiR5U4XuCFyVHXAsvVUos	false	-	-	1	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P02741-PRO_0000023526	uniprotkb:P08603	intact:EBI-22033103	intact:EBI-1223708|uniprotkb:A5PL14|uniprotkb:Q2TAZ5|uniprotkb:P78435|uniprotkb:Q14570|uniprotkb:Q38G77|uniprotkb:Q5TFM3|uniprotkb:Q8N708|uniprotkb:Q9NU86|ensembl:ENSP00000356399	psi-mi:p02741-pro_0000023526(display_long)|uniprotkb:CRP(gene name)|psi-mi:CRP(display_short)|uniprotkb:PTX1(gene name synonym)	psi-mi:cfah_human(display_long)|uniprotkb:CFH(gene name)|psi-mi:CFH(display_short)|uniprotkb:HF(gene name synonym)|uniprotkb:HF1(gene name synonym)|uniprotkb:HF2(gene name synonym)|uniprotkb:H factor 1(gene name synonym)	psi-mi:"MI:0411"(enzyme linked immunosorbent assay)	Bíró et al. (2007)	pubmed:17244159|imex:IM-27413	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-22079938|imex:IM-27413-15	-	-	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:0326"(protein)	intact:EBI-1395983(chain-parent)	refseq:NP_000177.2|dip:DIP-38303N|ensembl:ENSG00000000971(gene)|ensembl:ENST00000367429(transcript)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0006956"(complement activation)|go:"GO:0006957"(complement activation, alternative pathway)|go:"GO:0008201"(heparin binding)|go:"GO:0030449"(regulation of complement activation)|go:"GO:0042802"(identical protein binding)|go:"GO:0043395"(heparan sulfate proteoglycan binding)|go:"GO:0070062"(extracellular exosome)|go:"GO:0072562"(blood microparticle)|go:"GO:1903659"(regulation of complement-dependent cytotoxicity)|interpro:IPR000436(Sushi/SCR/CCP)|interpro:IPR035976|mint:P08603|rcsb pdb:1FHC|rcsb pdb:1HAQ|rcsb pdb:1HCC|rcsb pdb:1HFH|rcsb pdb:1HFI|rcsb pdb:1KOV|rcsb pdb:2QFH|rcsb pdb:2RLP|rcsb pdb:2RLQ|rcsb pdb:2UWN|rcsb pdb:2V8E|rcsb pdb:2W80|rcsb pdb:2BZM|rcsb pdb:2G7I|rcsb pdb:2W81|rcsb pdb:2WII|rcsb pdb:2XQW|rcsb pdb:3GAU|rcsb pdb:3GAV|rcsb pdb:3GAW|rcsb pdb:3KXV|rcsb pdb:3KZJ|rcsb pdb:3OXU|rcsb pdb:3R62|rcsb pdb:3RJ3|rcsb pdb:3SW0|rcsb pdb:4AYD|rcsb pdb:4AYE|rcsb pdb:4AYI|rcsb pdb:4AYM|rcsb pdb:4B2R|rcsb pdb:4B2S|rcsb pdb:2IC4|rcsb pdb:2JGW|rcsb pdb:2JGX|rcsb pdb:4J38|rcsb pdb:4K12|rcsb pdb:4ONT|rcsb pdb:4ZH1|rcsb pdb:5NBQ|rcsb pdb:5O32|rcsb pdb:5O35|rcsb pdb:2KMS|rcsb pdb:2QFG|rcsb pdb:5WTB|rcsb pdb:6ATG|reactome:R-HSA-977606	-	chain-seq-start:19|chain-seq-end:224	-	figure legend:5B|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/09/04	2019/11/04	rogid:CvK4vTdUxXgEsFN2HKUWzPg5lx49606	rogid:1mjo+AJLIQnEsMFqsGsmUFbfUxk9606	rigid:j7J02aEiR5U4XuCFyVHXAsvVUos	false	protein modification:1-1|mutation:36-36,97-97|acylated residue:?-?	-	1	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P04003	uniprotkb:P02741-PRO_0000023526	intact:EBI-978348|ensembl:ENSP00000356037|uniprotkb:Q5VVQ8	intact:EBI-22033103	psi-mi:c4bpa_human(display_long)|uniprotkb:Proline-rich protein(gene name synonym)|uniprotkb:C4BPA(gene name)|psi-mi:C4BPA(display_short)|uniprotkb:C4BP(gene name synonym)	psi-mi:p02741-pro_0000023526(display_long)|uniprotkb:CRP(gene name)|psi-mi:CRP(display_short)|uniprotkb:PTX1(gene name synonym)	psi-mi:"MI:0411"(enzyme linked immunosorbent assay)	Bíró et al. (2007)	pubmed:17244159|imex:IM-27413	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-22079954|imex:IM-27413-17	-	-	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:0326"(protein)	ensembl:ENSG00000123838(gene)|ensembl:ENST00000367070(transcript)|go:"GO:0003723"(RNA binding)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0005886"(plasma membrane)|go:"GO:0006958"(complement activation, classical pathway)|go:"GO:0009609"(response to symbiotic bacterium)|go:"GO:0045087"(innate immune response)|go:"GO:0045732"(positive regulation of protein catabolic process)|go:"GO:0045959"(negative regulation of complement activation, classical pathway)|go:"GO:0072562"(blood microparticle)|go:"GO:1903027"(regulation of opsonization)|interpro:IPR000436(Sushi/SCR/CCP)|interpro:IPR035976|interpro:IPR040514|rcsb pdb:2A55|rcsb pdb:4B0F|rcsb pdb:5HYP|rcsb pdb:5HYT|rcsb pdb:5HYU|rcsb pdb:5HZP|rcsb pdb:5I0Q|reactome:R-HSA-977606|refseq:NP_000706.1|refseq:XP_005273308.1|refseq:XP_005273309.1	intact:EBI-1395983(chain-parent)	-	-	chain-seq-start:19|chain-seq-end:224	figure legend:6A,8|comment:Preincubation of immobilized Cr-mCRP with C1q had no significant effect on subsequent binding of FH or C4BP.|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/09/04	2019/11/04	rogid:S0F99wuDTalS4UCuYGWbiCgWlO09606	rogid:CvK4vTdUxXgEsFN2HKUWzPg5lx49606	rigid:w2Ef6yAZO0DSrn1fr5n8iWmZHVw	false	-	protein modification:1-1|mutation:36-36,97-97|acylated residue:?-?	-	1	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P04003	uniprotkb:P02741-PRO_0000023526	intact:EBI-978348|ensembl:ENSP00000356037|uniprotkb:Q5VVQ8	intact:EBI-22033103	psi-mi:c4bpa_human(display_long)|uniprotkb:Proline-rich protein(gene name synonym)|uniprotkb:C4BPA(gene name)|psi-mi:C4BPA(display_short)|uniprotkb:C4BP(gene name synonym)	psi-mi:p02741-pro_0000023526(display_long)|uniprotkb:CRP(gene name)|psi-mi:CRP(display_short)|uniprotkb:PTX1(gene name synonym)	psi-mi:"MI:0411"(enzyme linked immunosorbent assay)	Bíró et al. (2007)	pubmed:17244159|imex:IM-27413	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-22079966|imex:IM-27413-27	-	-	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:0326"(protein)	ensembl:ENSG00000123838(gene)|ensembl:ENST00000367070(transcript)|go:"GO:0003723"(RNA binding)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0005886"(plasma membrane)|go:"GO:0006958"(complement activation, classical pathway)|go:"GO:0009609"(response to symbiotic bacterium)|go:"GO:0045087"(innate immune response)|go:"GO:0045732"(positive regulation of protein catabolic process)|go:"GO:0045959"(negative regulation of complement activation, classical pathway)|go:"GO:0072562"(blood microparticle)|go:"GO:1903027"(regulation of opsonization)|interpro:IPR000436(Sushi/SCR/CCP)|interpro:IPR035976|interpro:IPR040514|rcsb pdb:2A55|rcsb pdb:4B0F|rcsb pdb:5HYP|rcsb pdb:5HYT|rcsb pdb:5HYU|rcsb pdb:5HZP|rcsb pdb:5I0Q|reactome:R-HSA-977606|refseq:NP_000706.1|refseq:XP_005273308.1|refseq:XP_005273309.1	intact:EBI-1395983(chain-parent)	-	-	chain-seq-start:19|chain-seq-end:224	figure legend:6A-2|comment:Weak binding was seen. Some binding was also seen at higher concentrations of C4BP with pentameric CRP , structurally  modified by direct attachment to the ELISA plate.|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/09/04	2019/11/04	rogid:S0F99wuDTalS4UCuYGWbiCgWlO09606	rogid:CvK4vTdUxXgEsFN2HKUWzPg5lx49606	rigid:w2Ef6yAZO0DSrn1fr5n8iWmZHVw	false	-	-	-	1	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P02741-PRO_0000023526	uniprotkb:P04003	intact:EBI-22033103	intact:EBI-978348|ensembl:ENSP00000356037|uniprotkb:Q5VVQ8	psi-mi:p02741-pro_0000023526(display_long)|uniprotkb:CRP(gene name)|psi-mi:CRP(display_short)|uniprotkb:PTX1(gene name synonym)	psi-mi:c4bpa_human(display_long)|uniprotkb:Proline-rich protein(gene name synonym)|uniprotkb:C4BPA(gene name)|psi-mi:C4BPA(display_short)|uniprotkb:C4BP(gene name synonym)	psi-mi:"MI:0411"(enzyme linked immunosorbent assay)	Bíró et al. (2007)	pubmed:17244159|imex:IM-27413	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-22079972|imex:IM-27413-19	-	-	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:0326"(protein)	intact:EBI-1395983(chain-parent)	ensembl:ENSG00000123838(gene)|ensembl:ENST00000367070(transcript)|go:"GO:0003723"(RNA binding)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0005886"(plasma membrane)|go:"GO:0006958"(complement activation, classical pathway)|go:"GO:0009609"(response to symbiotic bacterium)|go:"GO:0045087"(innate immune response)|go:"GO:0045732"(positive regulation of protein catabolic process)|go:"GO:0045959"(negative regulation of complement activation, classical pathway)|go:"GO:0072562"(blood microparticle)|go:"GO:1903027"(regulation of opsonization)|interpro:IPR000436(Sushi/SCR/CCP)|interpro:IPR035976|interpro:IPR040514|rcsb pdb:2A55|rcsb pdb:4B0F|rcsb pdb:5HYP|rcsb pdb:5HYT|rcsb pdb:5HYU|rcsb pdb:5HZP|rcsb pdb:5I0Q|reactome:R-HSA-977606|refseq:NP_000706.1|refseq:XP_005273308.1|refseq:XP_005273309.1	-	chain-seq-start:19|chain-seq-end:224	-	figure legend:6B|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/09/04	2019/11/04	rogid:CvK4vTdUxXgEsFN2HKUWzPg5lx49606	rogid:S0F99wuDTalS4UCuYGWbiCgWlO09606	rigid:w2Ef6yAZO0DSrn1fr5n8iWmZHVw	false	protein modification:1-1|mutation:36-36,97-97|acylated residue:?-?	-	1	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)