node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
A2M | CELA1 | ENSP00000323929 | ENSP00000293636 | 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 [...] | chymotrypsin-like elastase family, member 1; Acts upon elastin | 0.576 |
A2M | SERPINA1 | ENSP00000323929 | ENSP00000348068 | 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 [...] | serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1 | 0.948 |
A2M | SERPINA3 | ENSP00000323929 | ENSP00000376793 | 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 [...] | serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3 | 0.499 |
CELA1 | A2M | ENSP00000293636 | ENSP00000323929 | chymotrypsin-like elastase family, member 1; Acts upon elastin | 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 [...] | 0.576 |
CELA1 | CSN2 | ENSP00000293636 | ENSP00000341030 | chymotrypsin-like elastase family, member 1; Acts upon elastin | casein beta; Important role in determination of the surface properties of the casein micelles | 0.576 |
CELA1 | LPA | ENSP00000293636 | ENSP00000321334 | chymotrypsin-like elastase family, member 1; Acts upon elastin | lipoprotein, Lp(a); Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330 | 0.580 |
CELA1 | PI3 | ENSP00000293636 | ENSP00000243924 | chymotrypsin-like elastase family, member 1; Acts upon elastin | peptidase inhibitor 3, skin-derived; Neutrophil and pancreatic elastase-specific inhibitor of skin. It may prevent elastase-mediated tissue proteolysis | 0.576 |
CELA1 | SERPINA1 | ENSP00000293636 | ENSP00000348068 | chymotrypsin-like elastase family, member 1; Acts upon elastin | serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1 | 0.617 |
CELA1 | SERPINA3 | ENSP00000293636 | ENSP00000376793 | chymotrypsin-like elastase family, member 1; Acts upon elastin | serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3 | 0.610 |
CSN2 | CELA1 | ENSP00000341030 | ENSP00000293636 | casein beta; Important role in determination of the surface properties of the casein micelles | chymotrypsin-like elastase family, member 1; Acts upon elastin | 0.576 |
LPA | CELA1 | ENSP00000321334 | ENSP00000293636 | lipoprotein, Lp(a); Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330 | chymotrypsin-like elastase family, member 1; Acts upon elastin | 0.580 |
PI3 | CELA1 | ENSP00000243924 | ENSP00000293636 | peptidase inhibitor 3, skin-derived; Neutrophil and pancreatic elastase-specific inhibitor of skin. It may prevent elastase-mediated tissue proteolysis | chymotrypsin-like elastase family, member 1; Acts upon elastin | 0.576 |
PI3 | SERPINA1 | ENSP00000243924 | ENSP00000348068 | peptidase inhibitor 3, skin-derived; Neutrophil and pancreatic elastase-specific inhibitor of skin. It may prevent elastase-mediated tissue proteolysis | serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1 | 0.472 |
SERPINA1 | A2M | ENSP00000348068 | ENSP00000323929 | serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1 | 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 [...] | 0.948 |
SERPINA1 | CELA1 | ENSP00000348068 | ENSP00000293636 | serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1 | chymotrypsin-like elastase family, member 1; Acts upon elastin | 0.617 |
SERPINA1 | PI3 | ENSP00000348068 | ENSP00000243924 | serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1 | peptidase inhibitor 3, skin-derived; Neutrophil and pancreatic elastase-specific inhibitor of skin. It may prevent elastase-mediated tissue proteolysis | 0.472 |
SERPINA3 | A2M | ENSP00000376793 | ENSP00000323929 | serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3 | 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 [...] | 0.499 |
SERPINA3 | CELA1 | ENSP00000376793 | ENSP00000293636 | serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3 | chymotrypsin-like elastase family, member 1; Acts upon elastin | 0.610 |