node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
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 |
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 |
MMP20 | ACAN | ENSP00000260228 | ENSP00000387356 | 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 | 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 | 0.736 |
MMP20 | COL18A1 | ENSP00000260228 | ENSP00000347665 | 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 | collagen, type XVIII, alpha 1 | 0.909 |
MMP20 | LAMA3 | ENSP00000260228 | ENSP00000324532 | 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 | 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 | 0.901 |