| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CHD1L | SPOCK1 | ENSP00000358262 | ENSP00000282223 | chromodomain helicase DNA binding protein 1-like | sparc/osteonectin, cwcv and kazal-like domains proteoglycan (testican) 1; May play a role in cell-cell and cell-matrix interactions. May contribute to various neuronal mechanisms in the central nervous system | 0.891 |
| FSD1L | SPOCK1 | ENSP00000417492 | ENSP00000282223 | fibronectin type III and SPRY domain containing 1-like | sparc/osteonectin, cwcv and kazal-like domains proteoglycan (testican) 1; May play a role in cell-cell and cell-matrix interactions. May contribute to various neuronal mechanisms in the central nervous system | 0.536 |
| FSD1L | TMEM38B | ENSP00000417492 | ENSP00000363824 | fibronectin type III and SPRY domain containing 1-like | transmembrane protein 38B; Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores (By similarity) | 0.739 |
| FST | SPARC | ENSP00000256759 | ENSP00000231061 | follistatin; Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH) | secreted protein, acidic, cysteine-rich (osteonectin); Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity | 0.477 |
| FST | SPOCK1 | ENSP00000256759 | ENSP00000282223 | follistatin; Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH) | sparc/osteonectin, cwcv and kazal-like domains proteoglycan (testican) 1; May play a role in cell-cell and cell-matrix interactions. May contribute to various neuronal mechanisms in the central nervous system | 0.607 |
| MMP14 | MMP16 | ENSP00000308208 | ENSP00000286614 | matrix metallopeptidase 14 (membrane-inserted); Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15 | matrix metallopeptidase 16 (membrane-inserted); Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells | 0.903 |
| MMP14 | MMP2 | ENSP00000308208 | ENSP00000219070 | matrix metallopeptidase 14 (membrane-inserted); Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15 | matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative s [...] | 0.968 |
| MMP14 | SPARC | ENSP00000308208 | ENSP00000231061 | matrix metallopeptidase 14 (membrane-inserted); Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15 | secreted protein, acidic, cysteine-rich (osteonectin); Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity | 0.400 |
| MMP14 | SPOCK1 | ENSP00000308208 | ENSP00000282223 | matrix metallopeptidase 14 (membrane-inserted); Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15 | sparc/osteonectin, cwcv and kazal-like domains proteoglycan (testican) 1; May play a role in cell-cell and cell-matrix interactions. May contribute to various neuronal mechanisms in the central nervous system | 0.736 |
| MMP16 | MMP14 | ENSP00000286614 | ENSP00000308208 | matrix metallopeptidase 16 (membrane-inserted); Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells | matrix metallopeptidase 14 (membrane-inserted); Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15 | 0.903 |
| MMP16 | SPOCK1 | ENSP00000286614 | ENSP00000282223 | matrix metallopeptidase 16 (membrane-inserted); Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells | sparc/osteonectin, cwcv and kazal-like domains proteoglycan (testican) 1; May play a role in cell-cell and cell-matrix interactions. May contribute to various neuronal mechanisms in the central nervous system | 0.681 |
| MMP2 | MMP14 | ENSP00000219070 | ENSP00000308208 | matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative s [...] | matrix metallopeptidase 14 (membrane-inserted); Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15 | 0.968 |
| MMP2 | SPARC | ENSP00000219070 | ENSP00000231061 | matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative s [...] | secreted protein, acidic, cysteine-rich (osteonectin); Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity | 0.588 |
| MMP2 | SPOCK1 | ENSP00000219070 | ENSP00000282223 | matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative s [...] | sparc/osteonectin, cwcv and kazal-like domains proteoglycan (testican) 1; May play a role in cell-cell and cell-matrix interactions. May contribute to various neuronal mechanisms in the central nervous system | 0.689 |
| MMP3 | SPARC | ENSP00000299855 | ENSP00000231061 | matrix metallopeptidase 3 (stromelysin 1, progelatinase); Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase | secreted protein, acidic, cysteine-rich (osteonectin); Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity | 0.421 |
| MMP3 | SPOCK1 | ENSP00000299855 | ENSP00000282223 | matrix metallopeptidase 3 (stromelysin 1, progelatinase); Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase | sparc/osteonectin, cwcv and kazal-like domains proteoglycan (testican) 1; May play a role in cell-cell and cell-matrix interactions. May contribute to various neuronal mechanisms in the central nervous system | 0.594 |
| SPARC | FST | ENSP00000231061 | ENSP00000256759 | secreted protein, acidic, cysteine-rich (osteonectin); Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity | follistatin; Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH) | 0.477 |
| SPARC | MMP14 | ENSP00000231061 | ENSP00000308208 | secreted protein, acidic, cysteine-rich (osteonectin); Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity | matrix metallopeptidase 14 (membrane-inserted); Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15 | 0.400 |
| SPARC | MMP2 | ENSP00000231061 | ENSP00000219070 | secreted protein, acidic, cysteine-rich (osteonectin); Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity | matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative s [...] | 0.588 |
| SPARC | MMP3 | ENSP00000231061 | ENSP00000299855 | secreted protein, acidic, cysteine-rich (osteonectin); Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity | matrix metallopeptidase 3 (stromelysin 1, progelatinase); Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase | 0.421 |
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