| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| A2M | CR201_G0003904 | ENSPPYP00000004847 | ENSPPYP00000019144 | 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 [...] | RAET1G isoform 1. | 0.459 |
| A2M | KLRF1 | ENSPPYP00000004847 | ENSPPYP00000004857 | 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 [...] | Killer cell lectin like receptor F1. | 0.689 |
| A2M | LOC100434525 | ENSPPYP00000004847 | ENSPPYP00000019147 | 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 [...] | RAET1L isoform 1. | 0.622 |
| A2M | RAET1E | ENSPPYP00000004847 | ENSPPYP00000019143 | 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 [...] | RAET1E isoform 1. | 0.646 |
| CLEC2A | KLRF1 | ENSPPYP00000004860 | ENSPPYP00000004857 | CLEC2A isoform 2. | Killer cell lectin like receptor F1. | 0.631 |
| CLEC2D | KLRF1 | ENSPPYP00000004852 | ENSPPYP00000004857 | C-type lectin domain family 2 member D. | Killer cell lectin like receptor F1. | 0.583 |
| CR201_G0003904 | A2M | ENSPPYP00000019144 | ENSPPYP00000004847 | RAET1G isoform 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 [...] | 0.459 |
| CR201_G0003904 | KLRF1 | ENSPPYP00000019144 | ENSPPYP00000004857 | RAET1G isoform 1. | Killer cell lectin like receptor F1. | 0.695 |
| CR201_G0003904 | LOC100434525 | ENSPPYP00000019144 | ENSPPYP00000019147 | RAET1G isoform 1. | RAET1L isoform 1. | 0.901 |
| CR201_G0003904 | RAET1E | ENSPPYP00000019144 | ENSPPYP00000019143 | RAET1G isoform 1. | RAET1E isoform 1. | 0.926 |
| KLRD1 | KLRF1 | ENSPPYP00000004870 | ENSPPYP00000004857 | KLRD1 isoform 1. | Killer cell lectin like receptor F1. | 0.603 |
| KLRF1 | A2M | ENSPPYP00000004857 | ENSPPYP00000004847 | Killer cell lectin like receptor F1. | 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 [...] | 0.689 |
| KLRF1 | CLEC2A | ENSPPYP00000004857 | ENSPPYP00000004860 | Killer cell lectin like receptor F1. | CLEC2A isoform 2. | 0.631 |
| KLRF1 | CLEC2D | ENSPPYP00000004857 | ENSPPYP00000004852 | Killer cell lectin like receptor F1. | C-type lectin domain family 2 member D. | 0.583 |
| KLRF1 | CR201_G0003904 | ENSPPYP00000004857 | ENSPPYP00000019144 | Killer cell lectin like receptor F1. | RAET1G isoform 1. | 0.695 |
| KLRF1 | KLRD1 | ENSPPYP00000004857 | ENSPPYP00000004870 | Killer cell lectin like receptor F1. | KLRD1 isoform 1. | 0.603 |
| KLRF1 | LOC100171566 | ENSPPYP00000004857 | ENSPPYP00000004854 | Killer cell lectin like receptor F1. | C-type lectin domain family 2 member H. | 0.583 |
| KLRF1 | LOC100434525 | ENSPPYP00000004857 | ENSPPYP00000019147 | Killer cell lectin like receptor F1. | RAET1L isoform 1. | 0.810 |
| KLRF1 | RAET1E | ENSPPYP00000004857 | ENSPPYP00000019143 | Killer cell lectin like receptor F1. | RAET1E isoform 1. | 0.861 |
| KLRF1 | REEP6 | ENSPPYP00000004857 | ENSPPYP00000010461 | Killer cell lectin like receptor F1. | Receptor accessory protein 6. | 0.621 |
