| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Ctsb | Plat | ENSMUSP00000006235 | ENSMUSP00000033941 | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family. | Tissue-type plasminogen activator chain A; Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events; Belongs to the peptidase S1 family. | 0.727 |
| Ctsb | Plau | ENSMUSP00000006235 | ENSMUSP00000022368 | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family. | Urokinase-type plasminogen activator short chain A; Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin; Belongs to the peptidase S1 family. | 0.808 |
| Ctsb | Plg | ENSMUSP00000006235 | ENSMUSP00000014578 | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family. | Plasmin heavy chain A, short form; Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invas [...] | 0.533 |
| Ctsb | Serpinb6a | ENSMUSP00000006235 | ENSMUSP00000017188 | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family. | Serpin B6; Inhibitor of cathepsin G, kallikrein-8 and thrombin. May play an important role in the inner ear in the protection against leakage of lysosomal content during stress. May be involved in the regulation of serine proteinases present in the brain or extravasated from the blood. | 0.705 |
| Ctsb | Serpinb6b | ENSMUSP00000006235 | ENSMUSP00000105922 | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family. | Serine (Or cysteine) peptidase inhibitor, clade B, member 6B; Belongs to the serpin family. | 0.692 |
| Ctsb | Serpinb6c | ENSMUSP00000006235 | ENSMUSP00000127619 | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family. | Serine (or cysteine) peptidase inhibitor, clade B, member 6c; Belongs to the serpin family. | 0.692 |
| Ctsb | Serpinb6e | ENSMUSP00000006235 | ENSMUSP00000105904 | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family. | Serine (or cysteine) peptidase inhibitor, clade B, member 6e; Belongs to the serpin family. | 0.672 |
| Ctsb | Serpine1 | ENSMUSP00000006235 | ENSMUSP00000039586 | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family. | Plasminogen activator inhibitor 1; Serine protease inhibitor. Inhibits TMPRSS7. Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase- type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots. As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading. Acts as a regulator of cell migration, independently of its role as protease inhibitor. It is required for stimulation of keratinocyte migration during cutaneous injury repair (B [...] | 0.936 |
| Ctsb | Vtn | ENSMUSP00000006235 | ENSMUSP00000017488 | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family. | Vitronectin; Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway. | 0.935 |
| Plat | Ctsb | ENSMUSP00000033941 | ENSMUSP00000006235 | Tissue-type plasminogen activator chain A; Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events; Belongs to the peptidase S1 family. | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family. | 0.727 |
| Plat | Plau | ENSMUSP00000033941 | ENSMUSP00000022368 | Tissue-type plasminogen activator chain A; Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events; Belongs to the peptidase S1 family. | Urokinase-type plasminogen activator short chain A; Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin; Belongs to the peptidase S1 family. | 0.944 |
| Plat | Plg | ENSMUSP00000033941 | ENSMUSP00000014578 | Tissue-type plasminogen activator chain A; Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events; Belongs to the peptidase S1 family. | Plasmin heavy chain A, short form; Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invas [...] | 0.996 |
| Plat | Serpinb6a | ENSMUSP00000033941 | ENSMUSP00000017188 | Tissue-type plasminogen activator chain A; Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events; Belongs to the peptidase S1 family. | Serpin B6; Inhibitor of cathepsin G, kallikrein-8 and thrombin. May play an important role in the inner ear in the protection against leakage of lysosomal content during stress. May be involved in the regulation of serine proteinases present in the brain or extravasated from the blood. | 0.945 |
| Plat | Serpinb6b | ENSMUSP00000033941 | ENSMUSP00000105922 | Tissue-type plasminogen activator chain A; Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events; Belongs to the peptidase S1 family. | Serine (Or cysteine) peptidase inhibitor, clade B, member 6B; Belongs to the serpin family. | 0.945 |
| Plat | Serpinb6c | ENSMUSP00000033941 | ENSMUSP00000127619 | Tissue-type plasminogen activator chain A; Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events; Belongs to the peptidase S1 family. | Serine (or cysteine) peptidase inhibitor, clade B, member 6c; Belongs to the serpin family. | 0.942 |
| Plat | Serpinb6e | ENSMUSP00000033941 | ENSMUSP00000105904 | Tissue-type plasminogen activator chain A; Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events; Belongs to the peptidase S1 family. | Serine (or cysteine) peptidase inhibitor, clade B, member 6e; Belongs to the serpin family. | 0.941 |
| Plat | Serpine1 | ENSMUSP00000033941 | ENSMUSP00000039586 | Tissue-type plasminogen activator chain A; Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events; Belongs to the peptidase S1 family. | Plasminogen activator inhibitor 1; Serine protease inhibitor. Inhibits TMPRSS7. Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase- type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots. As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading. Acts as a regulator of cell migration, independently of its role as protease inhibitor. It is required for stimulation of keratinocyte migration during cutaneous injury repair (B [...] | 0.999 |
| Plat | Serpine2 | ENSMUSP00000033941 | ENSMUSP00000027467 | Tissue-type plasminogen activator chain A; Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events; Belongs to the peptidase S1 family. | Glia-derived nexin; Serine protease inhibitor with activity toward thrombin, trypsin, and urokinase. Promotes neurite extension by inhibiting thrombin. Binds heparin. | 0.992 |
| Plat | Vtn | ENSMUSP00000033941 | ENSMUSP00000017488 | Tissue-type plasminogen activator chain A; Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events; Belongs to the peptidase S1 family. | Vitronectin; Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway. | 0.814 |
| Plau | Ctsb | ENSMUSP00000022368 | ENSMUSP00000006235 | Urokinase-type plasminogen activator short chain A; Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin; Belongs to the peptidase S1 family. | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family. | 0.808 |
