#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:P08253	reactome:R-HSA-2089970	intact:EBI-1033518|uniprotkb:B2R6U1|uniprotkb:Q9UCJ8|ensembl:ENSP00000219070|uniprotkb:E9PE45|uniprotkb:B4DWH3	intact:EBI-2325312|matrixdb:MULT_3_human|reactome:R-HSA-2467139|reactome:R-HSA-2396132|reactome:R-HSA-2396423|reactome:R-HSA-2396135|reactome:R-HSA-2396296|reactome:R-HSA-2396322|reactome:R-HSA-2428941|reactome:R-HSA-2396033|reactome:R-HSA-2396048	psi-mi:mmp2_human(display_long)|uniprotkb:MMP2(gene name)|psi-mi:MMP2(display_short)|uniprotkb:CLG4A(gene name synonym)|uniprotkb:72 kDa gelatinase(gene name synonym)|uniprotkb:Matrix metalloproteinase-2(gene name synonym)|uniprotkb:Gelatinase A(gene name synonym)|uniprotkb:TBE-1(gene name synonym)	psi-mi:collagen_i_human(display_short)|psi-mi:R-HSA-2089970(display_long)|intact:Collagen type I trimer(complex recommended name)|intact:Type I collagen(complex synonym)|intact:"2xCOL1A1:COL1A2"(complex systematic name)	psi-mi:"MI:0411"(enzyme linked immunosorbent assay)	Mikhailova et al. (2012)	pubmed:23085623|imex:IM-20973	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0917"(matrixdb)	intact:EBI-6894395|imex:IM-20973-3	-	-	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)	refseq:NP_001289437.1|refseq:NP_001289438.1|refseq:NP_001289439.1|ensembl:ENSG00000087245(gene)|ensembl:ENST00000219070(transcript)|go:"GO:0001525"(angiogenesis)|go:"GO:0001666"(response to hypoxia)|go:"GO:0001955"(blood vessel maturation)|go:"GO:0001957"(intramembranous ossification)|go:"GO:0004175"(endopeptidase activity)|go:"GO:0004222"(metalloendopeptidase activity)|go:"GO:0004252"(serine-type endopeptidase activity)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0005634"(nucleus)|go:"GO:0005739"(mitochondrion)|go:"GO:0005886"(plasma membrane)|go:"GO:0006508"(proteolysis)|go:"GO:0007566"(embryo implantation)|go:"GO:0008237"(metallopeptidase activity)|go:"GO:0008270"(zinc ion binding)|go:"GO:0022617"(extracellular matrix disassembly)|go:"GO:0030017"(sarcomere)|go:"GO:0030198"(extracellular matrix organization)|go:"GO:0030574"(collagen catabolic process)|go:"GO:0034614"(cellular response to reactive oxygen species)|go:"GO:0035987"(endodermal cell differentiation)|go:"GO:0044267"(cellular protein metabolic process)|go:"GO:0048013"(ephrin receptor signaling pathway)|go:"GO:0048771"(tissue remodeling)|go:"GO:0060325"(face morphogenesis)|go:"GO:0060346"(bone trabecula formation)|go:"GO:0062023"(collagen-containing extracellular matrix)|go:"GO:0071230"(cellular response to amino acid stimulus)|go:"GO:0071492"(cellular response to UV-A)|go:"GO:1904645"(response to amyloid-beta)|go:"GO:1904707"(positive regulation of vascular associated smooth muscle cell proliferation)|interpro:IPR000562(Type II fibronectin, collagen-binding)|interpro:IPR000585(Hemopexin)|interpro:IPR001818(Peptidase M10A and M12B, matrixin and adamalysin)|interpro:IPR002477(Peptidoglycan binding-like)|interpro:IPR006026(Peptidase, metallopeptidases)|interpro:IPR013806(Kringle-like fold)|interpro:IPR018486|interpro:IPR018487|interpro:IPR021158|interpro:IPR021190|interpro:IPR024079|interpro:IPR028708|interpro:IPR033739|interpro:IPR036365|interpro:IPR036375|interpro:IPR036943|rcsb pdb:1CK7|rcsb pdb:1CXW|rcsb pdb:1EAK|rcsb pdb:1GEN|rcsb pdb:1GXD|rcsb pdb:1HOV|rcsb pdb:1J7M|rcsb pdb:1KS0|rcsb pdb:1QIB|rcsb pdb:1RTG|rcsb pdb:3AYU|reactome:R-HSA-1442490|reactome:R-HSA-1474228|reactome:R-HSA-1592389|reactome:R-HSA-381426|reactome:R-HSA-3928665|reactome:R-HSA-6785807|reactome:R-HSA-9009391|refseq:NP_001121363.1|refseq:NP_004521.1	pubmed:1916105(see-also)|pubmed:17876790(see-also)|complex portal:CPX-1650(complex-primary)|intact:EBI-25750246(exp-evidence)|go:"GO:0005584"(collagen type I trimer)|go:"GO:0005201"(extracellular matrix structural constituent)|go:"GO:0030199"(collagen fibril organization)|evidence ontology:"ECO:0000353"	-	-	curated-complex:Forms the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.|assembly:Heterotrimer|complex-properties:"Triple-helices consisting of about 1000 amino acids per chain forming a coiled coil structure. Each polypeptide forms a left-handed helix in which every third residue, glycine, comes into the center of the superhelix. Propeptides (telopeptides) at both ends of the molecular precursor undergo highly complex fibrillogenesis."	figure legend:Fig. 4, Table 1|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	kd:1.03x10^-9(molar)	2013/07/15	2016/06/28	rogid:s0IHoSkzT9GNfkkLZsVsV7cIf1g9606	-	intact-crc:BB4D0F923AF4F169	false	mutation decreasing interaction strength:252-252|mutation decreasing interaction strength:252-252,297-297|mutation decreasing interaction strength:252-252,368-368|mutation disrupting interaction strength:252-252,297-297,368-368|his tag:n-n|mutation decreasing interaction strength:297-297|mutation disrupting interaction strength:368-368|mutation decreasing interaction strength:368-368,297-297	-	-	-	psi-mi:"MI:0421"(identification by antibody)	psi-mi:"MI:0421"(identification by antibody)
uniprotkb:P08253	reactome:R-HSA-2089970	intact:EBI-1033518|uniprotkb:B2R6U1|uniprotkb:Q9UCJ8|ensembl:ENSP00000219070|uniprotkb:E9PE45|uniprotkb:B4DWH3	intact:EBI-2325312|matrixdb:MULT_3_human|reactome:R-HSA-2467139|reactome:R-HSA-2396132|reactome:R-HSA-2396423|reactome:R-HSA-2396135|reactome:R-HSA-2396296|reactome:R-HSA-2396322|reactome:R-HSA-2428941|reactome:R-HSA-2396033|reactome:R-HSA-2396048	psi-mi:mmp2_human(display_long)|uniprotkb:MMP2(gene name)|psi-mi:MMP2(display_short)|uniprotkb:CLG4A(gene name synonym)|uniprotkb:72 kDa gelatinase(gene name synonym)|uniprotkb:Matrix metalloproteinase-2(gene name synonym)|uniprotkb:Gelatinase A(gene name synonym)|uniprotkb:TBE-1(gene name synonym)	psi-mi:collagen_i_human(display_short)|psi-mi:R-HSA-2089970(display_long)|intact:Collagen type I trimer(complex recommended name)|intact:Type I collagen(complex synonym)|intact:"2xCOL1A1:COL1A2"(complex systematic name)	psi-mi:"MI:0512"(zymography)	Mikhailova et al. (2012)	pubmed:23085623|imex:IM-20973	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0570"(protein cleavage)	psi-mi:"MI:0917"(matrixdb)	intact:EBI-6894490|imex:IM-20973-4	-	-	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:1302"(stable complex)	refseq:NP_001289437.1|refseq:NP_001289438.1|refseq:NP_001289439.1|ensembl:ENSG00000087245(gene)|ensembl:ENST00000219070(transcript)|go:"GO:0001525"(angiogenesis)|go:"GO:0001666"(response to hypoxia)|go:"GO:0001955"(blood vessel maturation)|go:"GO:0001957"(intramembranous ossification)|go:"GO:0004175"(endopeptidase activity)|go:"GO:0004222"(metalloendopeptidase activity)|go:"GO:0004252"(serine-type endopeptidase activity)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0005634"(nucleus)|go:"GO:0005739"(mitochondrion)|go:"GO:0005886"(plasma membrane)|go:"GO:0006508"(proteolysis)|go:"GO:0007566"(embryo implantation)|go:"GO:0008237"(metallopeptidase activity)|go:"GO:0008270"(zinc ion binding)|go:"GO:0022617"(extracellular matrix disassembly)|go:"GO:0030017"(sarcomere)|go:"GO:0030198"(extracellular matrix organization)|go:"GO:0030574"(collagen catabolic process)|go:"GO:0034614"(cellular response to reactive oxygen species)|go:"GO:0035987"(endodermal cell differentiation)|go:"GO:0044267"(cellular protein metabolic process)|go:"GO:0048013"(ephrin receptor signaling pathway)|go:"GO:0048771"(tissue remodeling)|go:"GO:0060325"(face morphogenesis)|go:"GO:0060346"(bone trabecula formation)|go:"GO:0062023"(collagen-containing extracellular matrix)|go:"GO:0071230"(cellular response to amino acid stimulus)|go:"GO:0071492"(cellular response to UV-A)|go:"GO:1904645"(response to amyloid-beta)|go:"GO:1904707"(positive regulation of vascular associated smooth muscle cell proliferation)|interpro:IPR000562(Type II fibronectin, collagen-binding)|interpro:IPR000585(Hemopexin)|interpro:IPR001818(Peptidase M10A and M12B, matrixin and adamalysin)|interpro:IPR002477(Peptidoglycan binding-like)|interpro:IPR006026(Peptidase, metallopeptidases)|interpro:IPR013806(Kringle-like fold)|interpro:IPR018486|interpro:IPR018487|interpro:IPR021158|interpro:IPR021190|interpro:IPR024079|interpro:IPR028708|interpro:IPR033739|interpro:IPR036365|interpro:IPR036375|interpro:IPR036943|rcsb pdb:1CK7|rcsb pdb:1CXW|rcsb pdb:1EAK|rcsb pdb:1GEN|rcsb pdb:1GXD|rcsb pdb:1HOV|rcsb pdb:1J7M|rcsb pdb:1KS0|rcsb pdb:1QIB|rcsb pdb:1RTG|rcsb pdb:3AYU|reactome:R-HSA-1442490|reactome:R-HSA-1474228|reactome:R-HSA-1592389|reactome:R-HSA-381426|reactome:R-HSA-3928665|reactome:R-HSA-6785807|reactome:R-HSA-9009391|refseq:NP_001121363.1|refseq:NP_004521.1	pubmed:1916105(see-also)|pubmed:17876790(see-also)|complex portal:CPX-1650(complex-primary)|intact:EBI-25750246(exp-evidence)|go:"GO:0005584"(collagen type I trimer)|go:"GO:0005201"(extracellular matrix structural constituent)|go:"GO:0030199"(collagen fibril organization)|evidence ontology:"ECO:0000353"	go:"GO:0004222"(metalloendopeptidase activity)|go:"GO:0030574"(collagen catabolic process)	-	curated-complex:Forms the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.|assembly:Heterotrimer|complex-properties:"Triple-helices consisting of about 1000 amino acids per chain forming a coiled coil structure. Each polypeptide forms a left-handed helix in which every third residue, glycine, comes into the center of the superhelix. Propeptides (telopeptides) at both ends of the molecular precursor undergo highly complex fibrillogenesis."	figure legend:5A, 5B|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2013/07/15	2016/06/28	rogid:s0IHoSkzT9GNfkkLZsVsV7cIf1g9606	-	intact-crc:EA9022320E177BD7	false	mutation decreasing interaction:297-297|mutation decreasing interaction:252-252|mutation decreasing interaction:368-368|mutation decreasing interaction:252-252,297-297|mutation decreasing interaction:297-297,368-368|his tag:n-n|mutation decreasing interaction:252-252,297-297,368-368|mutation decreasing interaction:252-252,368-368	-	-	-	psi-mi:"MI:0818"(molecular weight estimation by coomasie staining)	psi-mi:"MI:0818"(molecular weight estimation by coomasie staining)
uniprotkb:P08253	matrixdb:MULT_3_pig	intact:EBI-1033518|uniprotkb:B2R6U1|uniprotkb:Q9UCJ8|ensembl:ENSP00000219070|uniprotkb:E9PE45|uniprotkb:B4DWH3	intact:EBI-21181034	psi-mi:mmp2_human(display_long)|uniprotkb:MMP2(gene name)|psi-mi:MMP2(display_short)|uniprotkb:CLG4A(gene name synonym)|uniprotkb:72 kDa gelatinase(gene name synonym)|uniprotkb:Matrix metalloproteinase-2(gene name synonym)|uniprotkb:Gelatinase A(gene name synonym)|uniprotkb:TBE-1(gene name synonym)	psi-mi:collagen_i_pig(display_short)|psi-mi:MULT_3_pig(display_long)|intact:Collagen type I trimer(complex recommended name)|intact:Type I collagen(complex synonym)|intact:"2xCOL1A1:COL1A2"(complex systematic name)	psi-mi:"MI:0435"(protease assay)	Mikhailova et al. (2012)	pubmed:23085623|imex:IM-20973	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9823(pig)|taxid:9823("Sus scrofa (Pig)")	psi-mi:"MI:0570"(protein cleavage)	psi-mi:"MI:0917"(matrixdb)	intact:EBI-6894530|imex:IM-20973-6	-	-	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:1302"(stable complex)	refseq:NP_001289437.1|refseq:NP_001289438.1|refseq:NP_001289439.1|ensembl:ENSG00000087245(gene)|ensembl:ENST00000219070(transcript)|go:"GO:0001525"(angiogenesis)|go:"GO:0001666"(response to hypoxia)|go:"GO:0001955"(blood vessel maturation)|go:"GO:0001957"(intramembranous ossification)|go:"GO:0004175"(endopeptidase activity)|go:"GO:0004222"(metalloendopeptidase activity)|go:"GO:0004252"(serine-type endopeptidase activity)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0005634"(nucleus)|go:"GO:0005739"(mitochondrion)|go:"GO:0005886"(plasma membrane)|go:"GO:0006508"(proteolysis)|go:"GO:0007566"(embryo implantation)|go:"GO:0008237"(metallopeptidase activity)|go:"GO:0008270"(zinc ion binding)|go:"GO:0022617"(extracellular matrix disassembly)|go:"GO:0030017"(sarcomere)|go:"GO:0030198"(extracellular matrix organization)|go:"GO:0030574"(collagen catabolic process)|go:"GO:0034614"(cellular response to reactive oxygen species)|go:"GO:0035987"(endodermal cell differentiation)|go:"GO:0044267"(cellular protein metabolic process)|go:"GO:0048013"(ephrin receptor signaling pathway)|go:"GO:0048771"(tissue remodeling)|go:"GO:0060325"(face morphogenesis)|go:"GO:0060346"(bone trabecula formation)|go:"GO:0062023"(collagen-containing extracellular matrix)|go:"GO:0071230"(cellular response to amino acid stimulus)|go:"GO:0071492"(cellular response to UV-A)|go:"GO:1904645"(response to amyloid-beta)|go:"GO:1904707"(positive regulation of vascular associated smooth muscle cell proliferation)|interpro:IPR000562(Type II fibronectin, collagen-binding)|interpro:IPR000585(Hemopexin)|interpro:IPR001818(Peptidase M10A and M12B, matrixin and adamalysin)|interpro:IPR002477(Peptidoglycan binding-like)|interpro:IPR006026(Peptidase, metallopeptidases)|interpro:IPR013806(Kringle-like fold)|interpro:IPR018486|interpro:IPR018487|interpro:IPR021158|interpro:IPR021190|interpro:IPR024079|interpro:IPR028708|interpro:IPR033739|interpro:IPR036365|interpro:IPR036375|interpro:IPR036943|rcsb pdb:1CK7|rcsb pdb:1CXW|rcsb pdb:1EAK|rcsb pdb:1GEN|rcsb pdb:1GXD|rcsb pdb:1HOV|rcsb pdb:1J7M|rcsb pdb:1KS0|rcsb pdb:1QIB|rcsb pdb:1RTG|rcsb pdb:3AYU|reactome:R-HSA-1442490|reactome:R-HSA-1474228|reactome:R-HSA-1592389|reactome:R-HSA-381426|reactome:R-HSA-3928665|reactome:R-HSA-6785807|reactome:R-HSA-9009391|refseq:NP_001121363.1|refseq:NP_004521.1	pubmed:1916105(see-also)|go:"GO:0005201"(extracellular matrix structural constituent)|go:"GO:0005584"(collagen type I trimer)|pubmed:17876790(see-also)|go:"GO:0030199"(collagen fibril organization)|complex portal:CPX-4112(complex-primary)|evidence ontology:"ECO:0005547"	go:"GO:0030574"(collagen catabolic process)|go:"GO:0004222"(metalloendopeptidase activity)	-	curated-complex:Forms the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.|assembly:Heterotrimer|complex-properties:"Triple-helices consisting of about 1000 amino acids per chain forming a coiled coil structure. Each polypeptide forms a left-handed helix in which every third residue, glycine, comes into the center of the superhelix. Propeptides (telopeptides) at both ends of the molecular precursor undergo highly complex fibrillogenesis."|curation request:Sylvie Ricard-Blum, MatrixDB|comment:"Pig collagen I was heat-denatured (gelatin)"	figure legend:Table 2|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2013/07/15	2019/02/07	rogid:s0IHoSkzT9GNfkkLZsVsV7cIf1g9606	-	intact-crc:14F72FC7850B3978	false	mutation decreasing interaction:297-297|mutation:252-252,297-297|mutation decreasing interaction:252-252|mutation decreasing interaction:252-252,297-297,368-368|mutation decreasing interaction:297-297,368-368|mutation decreasing interaction:252-252,368-368|his tag:n-n|mutation decreasing interaction:368-368	fluorescein label:?-?	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
uniprotkb:P08253	intact:EBI-6894566	intact:EBI-1033518|uniprotkb:B2R6U1|uniprotkb:Q9UCJ8|ensembl:ENSP00000219070|uniprotkb:E9PE45|uniprotkb:B4DWH3	-	psi-mi:mmp2_human(display_long)|uniprotkb:MMP2(gene name)|psi-mi:MMP2(display_short)|uniprotkb:CLG4A(gene name synonym)|uniprotkb:72 kDa gelatinase(gene name synonym)|uniprotkb:Matrix metalloproteinase-2(gene name synonym)|uniprotkb:Gelatinase A(gene name synonym)|uniprotkb:TBE-1(gene name synonym)	psi-mi:nff-1(display_short)|psi-mi:EBI-6894566(display_long)	psi-mi:"MI:0435"(protease assay)	Mikhailova et al. (2012)	pubmed:23085623|imex:IM-20973	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	psi-mi:"MI:0570"(protein cleavage)	psi-mi:"MI:0917"(matrixdb)	intact:EBI-6894561|imex:IM-20973-1	-	-	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0327"(peptide)	refseq:NP_001289437.1|refseq:NP_001289438.1|refseq:NP_001289439.1|ensembl:ENSG00000087245(gene)|ensembl:ENST00000219070(transcript)|go:"GO:0001525"(angiogenesis)|go:"GO:0001666"(response to hypoxia)|go:"GO:0001955"(blood vessel maturation)|go:"GO:0001957"(intramembranous ossification)|go:"GO:0004175"(endopeptidase activity)|go:"GO:0004222"(metalloendopeptidase activity)|go:"GO:0004252"(serine-type endopeptidase activity)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0005634"(nucleus)|go:"GO:0005739"(mitochondrion)|go:"GO:0005886"(plasma membrane)|go:"GO:0006508"(proteolysis)|go:"GO:0007566"(embryo implantation)|go:"GO:0008237"(metallopeptidase activity)|go:"GO:0008270"(zinc ion binding)|go:"GO:0022617"(extracellular matrix disassembly)|go:"GO:0030017"(sarcomere)|go:"GO:0030198"(extracellular matrix organization)|go:"GO:0030574"(collagen catabolic process)|go:"GO:0034614"(cellular response to reactive oxygen species)|go:"GO:0035987"(endodermal cell differentiation)|go:"GO:0044267"(cellular protein metabolic process)|go:"GO:0048013"(ephrin receptor signaling pathway)|go:"GO:0048771"(tissue remodeling)|go:"GO:0060325"(face morphogenesis)|go:"GO:0060346"(bone trabecula formation)|go:"GO:0062023"(collagen-containing extracellular matrix)|go:"GO:0071230"(cellular response to amino acid stimulus)|go:"GO:0071492"(cellular response to UV-A)|go:"GO:1904645"(response to amyloid-beta)|go:"GO:1904707"(positive regulation of vascular associated smooth muscle cell proliferation)|interpro:IPR000562(Type II fibronectin, collagen-binding)|interpro:IPR000585(Hemopexin)|interpro:IPR001818(Peptidase M10A and M12B, matrixin and adamalysin)|interpro:IPR002477(Peptidoglycan binding-like)|interpro:IPR006026(Peptidase, metallopeptidases)|interpro:IPR013806(Kringle-like fold)|interpro:IPR018486|interpro:IPR018487|interpro:IPR021158|interpro:IPR021190|interpro:IPR024079|interpro:IPR028708|interpro:IPR033739|interpro:IPR036365|interpro:IPR036375|interpro:IPR036943|rcsb pdb:1CK7|rcsb pdb:1CXW|rcsb pdb:1EAK|rcsb pdb:1GEN|rcsb pdb:1GXD|rcsb pdb:1HOV|rcsb pdb:1J7M|rcsb pdb:1KS0|rcsb pdb:1QIB|rcsb pdb:1RTG|rcsb pdb:3AYU|reactome:R-HSA-1442490|reactome:R-HSA-1474228|reactome:R-HSA-1592389|reactome:R-HSA-381426|reactome:R-HSA-3928665|reactome:R-HSA-6785807|reactome:R-HSA-9009391|refseq:NP_001121363.1|refseq:NP_004521.1	-	go:"GO:0004222"(metalloendopeptidase activity)|go:"GO:0030574"(collagen catabolic process)	-	-	figure legend:Table 2|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2013/07/15	2014/10/16	rogid:s0IHoSkzT9GNfkkLZsVsV7cIf1g9606	rogid:oEiKjGU1bLVsfIhpvbxvG+1JTXo-2	intact-crc:452CEC9D7087FF60|rigid:yxDfjSDKAebLG+KNqTW8lZymOU8	false	his tag:n-n	fluorescent dye label:n-n	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
uniprotkb:P08253	intact:EBI-6894609	intact:EBI-1033518|uniprotkb:B2R6U1|uniprotkb:Q9UCJ8|ensembl:ENSP00000219070|uniprotkb:E9PE45|uniprotkb:B4DWH3	-	psi-mi:mmp2_human(display_long)|uniprotkb:MMP2(gene name)|psi-mi:MMP2(display_short)|uniprotkb:CLG4A(gene name synonym)|uniprotkb:72 kDa gelatinase(gene name synonym)|uniprotkb:Matrix metalloproteinase-2(gene name synonym)|uniprotkb:Gelatinase A(gene name synonym)|uniprotkb:TBE-1(gene name synonym)	psi-mi:fthp-15(display_short)|psi-mi:EBI-6894609(display_long)	psi-mi:"MI:0435"(protease assay)	Mikhailova et al. (2012)	pubmed:23085623|imex:IM-20973	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	psi-mi:"MI:0570"(protein cleavage)	psi-mi:"MI:0917"(matrixdb)	intact:EBI-6894611|imex:IM-20973-2	-	-	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0327"(peptide)	refseq:NP_001289437.1|refseq:NP_001289438.1|refseq:NP_001289439.1|ensembl:ENSG00000087245(gene)|ensembl:ENST00000219070(transcript)|go:"GO:0001525"(angiogenesis)|go:"GO:0001666"(response to hypoxia)|go:"GO:0001955"(blood vessel maturation)|go:"GO:0001957"(intramembranous ossification)|go:"GO:0004175"(endopeptidase activity)|go:"GO:0004222"(metalloendopeptidase activity)|go:"GO:0004252"(serine-type endopeptidase activity)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0005634"(nucleus)|go:"GO:0005739"(mitochondrion)|go:"GO:0005886"(plasma membrane)|go:"GO:0006508"(proteolysis)|go:"GO:0007566"(embryo implantation)|go:"GO:0008237"(metallopeptidase activity)|go:"GO:0008270"(zinc ion binding)|go:"GO:0022617"(extracellular matrix disassembly)|go:"GO:0030017"(sarcomere)|go:"GO:0030198"(extracellular matrix organization)|go:"GO:0030574"(collagen catabolic process)|go:"GO:0034614"(cellular response to reactive oxygen species)|go:"GO:0035987"(endodermal cell differentiation)|go:"GO:0044267"(cellular protein metabolic process)|go:"GO:0048013"(ephrin receptor signaling pathway)|go:"GO:0048771"(tissue remodeling)|go:"GO:0060325"(face morphogenesis)|go:"GO:0060346"(bone trabecula formation)|go:"GO:0062023"(collagen-containing extracellular matrix)|go:"GO:0071230"(cellular response to amino acid stimulus)|go:"GO:0071492"(cellular response to UV-A)|go:"GO:1904645"(response to amyloid-beta)|go:"GO:1904707"(positive regulation of vascular associated smooth muscle cell proliferation)|interpro:IPR000562(Type II fibronectin, collagen-binding)|interpro:IPR000585(Hemopexin)|interpro:IPR001818(Peptidase M10A and M12B, matrixin and adamalysin)|interpro:IPR002477(Peptidoglycan binding-like)|interpro:IPR006026(Peptidase, metallopeptidases)|interpro:IPR013806(Kringle-like fold)|interpro:IPR018486|interpro:IPR018487|interpro:IPR021158|interpro:IPR021190|interpro:IPR024079|interpro:IPR028708|interpro:IPR033739|interpro:IPR036365|interpro:IPR036375|interpro:IPR036943|rcsb pdb:1CK7|rcsb pdb:1CXW|rcsb pdb:1EAK|rcsb pdb:1GEN|rcsb pdb:1GXD|rcsb pdb:1HOV|rcsb pdb:1J7M|rcsb pdb:1KS0|rcsb pdb:1QIB|rcsb pdb:1RTG|rcsb pdb:3AYU|reactome:R-HSA-1442490|reactome:R-HSA-1474228|reactome:R-HSA-1592389|reactome:R-HSA-381426|reactome:R-HSA-3928665|reactome:R-HSA-6785807|reactome:R-HSA-9009391|refseq:NP_001121363.1|refseq:NP_004521.1	-	go:"GO:0004222"(metalloendopeptidase activity)|go:"GO:0030574"(collagen catabolic process)	-	comment:fTHP-15 is a triple-helical peptide substrate	figure legend:Table 3|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2013/07/15	2014/10/16	rogid:s0IHoSkzT9GNfkkLZsVsV7cIf1g9606	rogid:LIMxDxxY8MmcDgEk2Re7OLbtxLs-2	intact-crc:DB547591DEE9DF55|rigid:ZzunNMrSJLKJgCMjqlW5iomwYYs	false	mutation disrupting interaction strength:297-297,368-368|his tag:n-n|mutation decreasing interaction strength:368-368|mutation decreasing interaction strength:252-252,368-368|mutation decreasing interaction strength:252-252,297-297,368-368	fluorescent dye label:18-18	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
uniprotkb:P08253	reactome:R-HSA-2089970	intact:EBI-1033518|uniprotkb:B2R6U1|uniprotkb:Q9UCJ8|ensembl:ENSP00000219070|uniprotkb:E9PE45|uniprotkb:B4DWH3	intact:EBI-2325312|matrixdb:MULT_3_human|reactome:R-HSA-2467139|reactome:R-HSA-2396132|reactome:R-HSA-2396423|reactome:R-HSA-2396135|reactome:R-HSA-2396296|reactome:R-HSA-2396322|reactome:R-HSA-2428941|reactome:R-HSA-2396033|reactome:R-HSA-2396048	psi-mi:mmp2_human(display_long)|uniprotkb:MMP2(gene name)|psi-mi:MMP2(display_short)|uniprotkb:CLG4A(gene name synonym)|uniprotkb:72 kDa gelatinase(gene name synonym)|uniprotkb:Matrix metalloproteinase-2(gene name synonym)|uniprotkb:Gelatinase A(gene name synonym)|uniprotkb:TBE-1(gene name synonym)	psi-mi:collagen_i_human(display_short)|psi-mi:R-HSA-2089970(display_long)|intact:Collagen type I trimer(complex recommended name)|intact:Type I collagen(complex synonym)|intact:"2xCOL1A1:COL1A2"(complex systematic name)	psi-mi:"MI:0435"(protease assay)	Mikhailova et al. (2012)	pubmed:23085623|imex:IM-20973	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0570"(protein cleavage)	psi-mi:"MI:0917"(matrixdb)	intact:EBI-6894581|imex:IM-20973-5	-	-	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:1302"(stable complex)	refseq:NP_001289437.1|refseq:NP_001289438.1|refseq:NP_001289439.1|ensembl:ENSG00000087245(gene)|ensembl:ENST00000219070(transcript)|go:"GO:0001525"(angiogenesis)|go:"GO:0001666"(response to hypoxia)|go:"GO:0001955"(blood vessel maturation)|go:"GO:0001957"(intramembranous ossification)|go:"GO:0004175"(endopeptidase activity)|go:"GO:0004222"(metalloendopeptidase activity)|go:"GO:0004252"(serine-type endopeptidase activity)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0005634"(nucleus)|go:"GO:0005739"(mitochondrion)|go:"GO:0005886"(plasma membrane)|go:"GO:0006508"(proteolysis)|go:"GO:0007566"(embryo implantation)|go:"GO:0008237"(metallopeptidase activity)|go:"GO:0008270"(zinc ion binding)|go:"GO:0022617"(extracellular matrix disassembly)|go:"GO:0030017"(sarcomere)|go:"GO:0030198"(extracellular matrix organization)|go:"GO:0030574"(collagen catabolic process)|go:"GO:0034614"(cellular response to reactive oxygen species)|go:"GO:0035987"(endodermal cell differentiation)|go:"GO:0044267"(cellular protein metabolic process)|go:"GO:0048013"(ephrin receptor signaling pathway)|go:"GO:0048771"(tissue remodeling)|go:"GO:0060325"(face morphogenesis)|go:"GO:0060346"(bone trabecula formation)|go:"GO:0062023"(collagen-containing extracellular matrix)|go:"GO:0071230"(cellular response to amino acid stimulus)|go:"GO:0071492"(cellular response to UV-A)|go:"GO:1904645"(response to amyloid-beta)|go:"GO:1904707"(positive regulation of vascular associated smooth muscle cell proliferation)|interpro:IPR000562(Type II fibronectin, collagen-binding)|interpro:IPR000585(Hemopexin)|interpro:IPR001818(Peptidase M10A and M12B, matrixin and adamalysin)|interpro:IPR002477(Peptidoglycan binding-like)|interpro:IPR006026(Peptidase, metallopeptidases)|interpro:IPR013806(Kringle-like fold)|interpro:IPR018486|interpro:IPR018487|interpro:IPR021158|interpro:IPR021190|interpro:IPR024079|interpro:IPR028708|interpro:IPR033739|interpro:IPR036365|interpro:IPR036375|interpro:IPR036943|rcsb pdb:1CK7|rcsb pdb:1CXW|rcsb pdb:1EAK|rcsb pdb:1GEN|rcsb pdb:1GXD|rcsb pdb:1HOV|rcsb pdb:1J7M|rcsb pdb:1KS0|rcsb pdb:1QIB|rcsb pdb:1RTG|rcsb pdb:3AYU|reactome:R-HSA-1442490|reactome:R-HSA-1474228|reactome:R-HSA-1592389|reactome:R-HSA-381426|reactome:R-HSA-3928665|reactome:R-HSA-6785807|reactome:R-HSA-9009391|refseq:NP_001121363.1|refseq:NP_004521.1	pubmed:1916105(see-also)|pubmed:17876790(see-also)|complex portal:CPX-1650(complex-primary)|intact:EBI-25750246(exp-evidence)|go:"GO:0005584"(collagen type I trimer)|go:"GO:0005201"(extracellular matrix structural constituent)|go:"GO:0030199"(collagen fibril organization)|evidence ontology:"ECO:0000353"	go:"GO:0030574"(collagen catabolic process)|go:"GO:0004222"(metalloendopeptidase activity)	comment:"For all MMP-2 WT and variants substitution of residues in the type I collagen binding sites in general impacted the hydrolysis of the α1(I) chain more than the α2(I) chain (Fig. 6B, D)."	curated-complex:Forms the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.|assembly:Heterotrimer|complex-properties:"Triple-helices consisting of about 1000 amino acids per chain forming a coiled coil structure. Each polypeptide forms a left-handed helix in which every third residue, glycine, comes into the center of the superhelix. Propeptides (telopeptides) at both ends of the molecular precursor undergo highly complex fibrillogenesis."	figure legend:6|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2013/07/15	2016/06/28	rogid:s0IHoSkzT9GNfkkLZsVsV7cIf1g9606	-	intact-crc:71F877B37C7291C8	false	mutation decreasing interaction:252-252|mutation decreasing interaction:297-297,368-368|mutation decreasing interaction:252-252,297-297,368-368|his tag:n-n|mutation decreasing interaction:297-297|mutation decreasing interaction:368-368|mutation decreasing interaction:252-252,297-297|mutation decreasing interaction:252-252,368-368	biotin tag:?-?	-	-	psi-mi:"MI:0705"(anti tag western blot)	psi-mi:"MI:0705"(anti tag western blot)