| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| A2m | Ahsg | ENSMUSP00000032203 | ENSMUSP00000023583 | Alpha-2-macroglobulin-P; 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 [...] | Alpha-2-HS-glycoprotein; Probably involved in differentiation; Belongs to the fetuin family | 0.945 |
| A2m | Alb | ENSMUSP00000032203 | ENSMUSP00000031314 | Alpha-2-macroglobulin-P; 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 [...] | Serum albumin; Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc; Belongs to the ALB/AFP/VDB family | 0.963 |
| A2m | Elane | ENSMUSP00000032203 | ENSMUSP00000038925 | Alpha-2-macroglobulin-P; 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 [...] | Neutrophil elastase; Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity) | 0.476 |
| A2m | Plg | ENSMUSP00000032203 | ENSMUSP00000014578 | Alpha-2-macroglobulin-P; 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 [...] | Plasminogen; 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 invasion may be modulated b [...] | 0.953 |
| A2m | Serpina3n | ENSMUSP00000032203 | ENSMUSP00000021506 | Alpha-2-macroglobulin-P; 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 [...] | Serine (or cysteine) peptidase inhibitor, clade A, member 3N | 0.950 |
| A2m | Serping1 | ENSMUSP00000032203 | ENSMUSP00000023994 | Alpha-2-macroglobulin-P; 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 [...] | Plasma protease C1 inhibitor; Activation of the C1 complex is under control of the C1- inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. May inhibit chymotrypsin and kallikrein | 0.956 |
| A2m | Timp1 | ENSMUSP00000032203 | ENSMUSP00000009530 | Alpha-2-macroglobulin-P; 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 [...] | Metalloproteinase inhibitor 1; Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14 (By similarity). Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling; Belongs to the protease inhibitor I35 [...] | 0.938 |
| A2m | Ttr | ENSMUSP00000032203 | ENSMUSP00000074783 | Alpha-2-macroglobulin-P; 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 [...] | Transthyretin; Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain | 0.626 |
| Ahsg | A2m | ENSMUSP00000023583 | ENSMUSP00000032203 | Alpha-2-HS-glycoprotein; Probably involved in differentiation; Belongs to the fetuin family | Alpha-2-macroglobulin-P; 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 [...] | 0.945 |
| Ahsg | Alb | ENSMUSP00000023583 | ENSMUSP00000031314 | Alpha-2-HS-glycoprotein; Probably involved in differentiation; Belongs to the fetuin family | Serum albumin; Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc; Belongs to the ALB/AFP/VDB family | 0.996 |
| Ahsg | C3 | ENSMUSP00000023583 | ENSMUSP00000024988 | Alpha-2-HS-glycoprotein; Probably involved in differentiation; Belongs to the fetuin family | Complement C3; C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates | 0.961 |
| Ahsg | Plg | ENSMUSP00000023583 | ENSMUSP00000014578 | Alpha-2-HS-glycoprotein; Probably involved in differentiation; Belongs to the fetuin family | Plasminogen; 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 invasion may be modulated b [...] | 0.979 |
| Ahsg | Serpina3n | ENSMUSP00000023583 | ENSMUSP00000021506 | Alpha-2-HS-glycoprotein; Probably involved in differentiation; Belongs to the fetuin family | Serine (or cysteine) peptidase inhibitor, clade A, member 3N | 0.952 |
| Ahsg | Serping1 | ENSMUSP00000023583 | ENSMUSP00000023994 | Alpha-2-HS-glycoprotein; Probably involved in differentiation; Belongs to the fetuin family | Plasma protease C1 inhibitor; Activation of the C1 complex is under control of the C1- inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. May inhibit chymotrypsin and kallikrein | 0.927 |
| Ahsg | Timp1 | ENSMUSP00000023583 | ENSMUSP00000009530 | Alpha-2-HS-glycoprotein; Probably involved in differentiation; Belongs to the fetuin family | Metalloproteinase inhibitor 1; Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14 (By similarity). Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling; Belongs to the protease inhibitor I35 [...] | 0.915 |
| Ahsg | Ttr | ENSMUSP00000023583 | ENSMUSP00000074783 | Alpha-2-HS-glycoprotein; Probably involved in differentiation; Belongs to the fetuin family | Transthyretin; Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain | 0.826 |
| Alb | A2m | ENSMUSP00000031314 | ENSMUSP00000032203 | Serum albumin; Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc; Belongs to the ALB/AFP/VDB family | Alpha-2-macroglobulin-P; 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 [...] | 0.963 |
| Alb | Ahsg | ENSMUSP00000031314 | ENSMUSP00000023583 | Serum albumin; Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc; Belongs to the ALB/AFP/VDB family | Alpha-2-HS-glycoprotein; Probably involved in differentiation; Belongs to the fetuin family | 0.996 |
| Alb | C3 | ENSMUSP00000031314 | ENSMUSP00000024988 | Serum albumin; Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc; Belongs to the ALB/AFP/VDB family | Complement C3; C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates | 0.968 |
| Alb | Ctsg | ENSMUSP00000031314 | ENSMUSP00000015583 | Serum albumin; Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc; Belongs to the ALB/AFP/VDB family | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis | 0.408 |
