node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
A2M | TIMP1 | ENSP00000323929 | ENSP00000218388 | alpha-2-macroglobulin; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the co [...] | TIMP metallopeptidase inhibitor 1; Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Also mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13 and MMP-16. Does not act on MMP-14 | 0.930 |
ACAN | MMP20 | ENSP00000387356 | ENSP00000260228 | aggrecan; This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region | matrix metallopeptidase 20; Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix- aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation | 0.736 |
ACAN | TIMP1 | ENSP00000387356 | ENSP00000218388 | aggrecan; This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region | TIMP metallopeptidase inhibitor 1; Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Also mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13 and MMP-16. Does not act on MMP-14 | 0.645 |
ACAN | TIMP2 | ENSP00000387356 | ENSP00000262768 | aggrecan; This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region | TIMP metallopeptidase inhibitor 2; Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19 | 0.520 |
ACAN | TIMP3 | ENSP00000387356 | ENSP00000266085 | aggrecan; This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region | TIMP metallopeptidase inhibitor 3; Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15 | 0.569 |
COL15A1 | COL18A1 | ENSP00000364140 | ENSP00000347665 | collagen, type XV, alpha 1; Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle | collagen, type XVIII, alpha 1 | 0.930 |
COL18A1 | COL15A1 | ENSP00000347665 | ENSP00000364140 | collagen, type XVIII, alpha 1 | collagen, type XV, alpha 1; Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle | 0.930 |
COL18A1 | MMP20 | ENSP00000347665 | ENSP00000260228 | collagen, type XVIII, alpha 1 | matrix metallopeptidase 20; Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix- aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation | 0.909 |
COL18A1 | TIMP1 | ENSP00000347665 | ENSP00000218388 | collagen, type XVIII, alpha 1 | TIMP metallopeptidase inhibitor 1; Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Also mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13 and MMP-16. Does not act on MMP-14 | 0.565 |
COL18A1 | TIMP2 | ENSP00000347665 | ENSP00000262768 | collagen, type XVIII, alpha 1 | TIMP metallopeptidase inhibitor 2; Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19 | 0.562 |
COL18A1 | TIMP3 | ENSP00000347665 | ENSP00000266085 | collagen, type XVIII, alpha 1 | TIMP metallopeptidase inhibitor 3; Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15 | 0.450 |
LAMA3 | LAMB3 | ENSP00000324532 | ENSP00000348384 | laminin, alpha 3; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components | laminin, beta 3; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components | 0.976 |
LAMA3 | LAMC2 | ENSP00000324532 | ENSP00000264144 | laminin, alpha 3; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components | laminin, gamma 2; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ladsin exerts cell- scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells | 0.931 |
LAMA3 | MMP20 | ENSP00000324532 | ENSP00000260228 | laminin, alpha 3; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components | matrix metallopeptidase 20; Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix- aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation | 0.901 |
LAMB3 | LAMA3 | ENSP00000348384 | ENSP00000324532 | laminin, beta 3; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components | laminin, alpha 3; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components | 0.976 |
LAMB3 | LAMC2 | ENSP00000348384 | ENSP00000264144 | laminin, beta 3; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components | laminin, gamma 2; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ladsin exerts cell- scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells | 0.969 |
LAMB3 | MMP20 | ENSP00000348384 | ENSP00000260228 | laminin, beta 3; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components | matrix metallopeptidase 20; Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix- aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation | 0.907 |
LAMC2 | LAMA3 | ENSP00000264144 | ENSP00000324532 | laminin, gamma 2; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ladsin exerts cell- scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells | laminin, alpha 3; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components | 0.931 |
LAMC2 | LAMB3 | ENSP00000264144 | ENSP00000348384 | laminin, gamma 2; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ladsin exerts cell- scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells | laminin, beta 3; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components | 0.969 |
LAMC2 | MMP20 | ENSP00000264144 | ENSP00000260228 | laminin, gamma 2; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ladsin exerts cell- scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells | matrix metallopeptidase 20; Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix- aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation | 0.900 |