node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CTSB | CTSL1 | ENSP00000342070 | ENSP00000345344 | cathepsin B; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis | cathepsin L1; Important for the overall degradation of proteins in lysosomes | 0.700 |
CTSB | SLPI | ENSP00000342070 | ENSP00000342082 | cathepsin B; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis | secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues | 0.702 |
CTSL1 | CTSB | ENSP00000345344 | ENSP00000342070 | cathepsin L1; Important for the overall degradation of proteins in lysosomes | cathepsin B; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis | 0.700 |
CTSL1 | CTSS | ENSP00000345344 | ENSP00000357981 | cathepsin L1; Important for the overall degradation of proteins in lysosomes | cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N | 0.905 |
CTSL1 | SLPI | ENSP00000345344 | ENSP00000342082 | cathepsin L1; Important for the overall degradation of proteins in lysosomes | secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues | 0.590 |
CTSS | CTSL1 | ENSP00000357981 | ENSP00000345344 | cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N | cathepsin L1; Important for the overall degradation of proteins in lysosomes | 0.905 |
CTSS | SLPI | ENSP00000357981 | ENSP00000342082 | cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N | secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues | 0.717 |
ELANE | GRN | ENSP00000263621 | ENSP00000053867 | elastase, neutrophil expressed; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis | granulin | 0.677 |
ELANE | SLPI | ENSP00000263621 | ENSP00000342082 | elastase, neutrophil expressed; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis | secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues | 0.972 |
GRN | ELANE | ENSP00000053867 | ENSP00000263621 | granulin | elastase, neutrophil expressed; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis | 0.677 |
GRN | SLPI | ENSP00000053867 | ENSP00000342082 | granulin | secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues | 0.963 |
KLK3 | SLPI | ENSP00000314151 | ENSP00000342082 | kallikrein-related peptidase 3; Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum | secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues | 0.602 |
PLSCR1 | SLPI | ENSP00000345494 | ENSP00000342082 | phospholipid scramblase 1; May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system | secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues | 0.620 |
SLPI | CTSB | ENSP00000342082 | ENSP00000342070 | secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues | cathepsin B; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis | 0.702 |
SLPI | CTSL1 | ENSP00000342082 | ENSP00000345344 | secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues | cathepsin L1; Important for the overall degradation of proteins in lysosomes | 0.590 |
SLPI | CTSS | ENSP00000342082 | ENSP00000357981 | secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues | cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N | 0.717 |
SLPI | ELANE | ENSP00000342082 | ENSP00000263621 | secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues | elastase, neutrophil expressed; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis | 0.972 |
SLPI | GRN | ENSP00000342082 | ENSP00000053867 | secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues | granulin | 0.963 |
SLPI | KLK3 | ENSP00000342082 | ENSP00000314151 | secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues | kallikrein-related peptidase 3; Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum | 0.602 |
SLPI | PLSCR1 | ENSP00000342082 | ENSP00000345494 | secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues | phospholipid scramblase 1; May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system | 0.620 |