| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Ctsg | Elane | ENSMUSP00000015583 | ENSMUSP00000038925 | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | Neutrophil elastase; Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity). Capable of killing E.coli; probably digests outer membrane protein A (ompA) in E.coli ; Belongs to the peptidase S1 family. Elastase subfamily. | 0.997 |
| Ctsg | Ltf | ENSMUSP00000015583 | ENSMUSP00000035077 | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | Lactotransferrin; Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites. | 0.995 |
| Ctsg | Mpo | ENSMUSP00000015583 | ENSMUSP00000020779 | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | Myeloperoxidase heavy chain; Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity; Belongs to the peroxidase family. XPO subfamily. | 0.999 |
| Ctsg | Prtn3 | ENSMUSP00000015583 | ENSMUSP00000006679 | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | Myeloblastin; Serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro). By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration. May play a role in neutrophil transendothelial migration, probably when associated with CD177; Belongs to the peptidase S1 family. Elastase subfamily. | 0.994 |
| Ctsg | Serpina1a | ENSMUSP00000015583 | ENSMUSP00000072652 | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | Alpha-1-antitrypsin 1-1; Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Belongs to the serpin family. | 0.594 |
| Ctsg | Serpina1b | ENSMUSP00000015583 | ENSMUSP00000139941 | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | Alpha-1-antitrypsin 1-2; Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Belongs to the serpin family. | 0.593 |
| Ctsg | Serpina1c | ENSMUSP00000015583 | ENSMUSP00000073695 | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | Alpha-1-antitrypsin 1-3; Inhibitor of serine proteases. Can inhibit trypsin and chymotrypsin; relatively ineffective against elastase. Belongs to the serpin family. | 0.560 |
| Ctsg | Serpina1d | ENSMUSP00000015583 | ENSMUSP00000077909 | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | Alpha-1-antitrypsin 1-4; Inhibitor of serine proteases. Can inhibit trypsin and chymotrypsin; relatively ineffective against elastase. Belongs to the serpin family. | 0.568 |
| Ctsg | Serpina1e | ENSMUSP00000015583 | ENSMUSP00000113606 | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | Alpha-1-antitrypsin 1-5; Does not inhibit elastase or chymotrypsin. No target protease has been identified to date; Belongs to the serpin family. | 0.591 |
| Ctsg | Slpi | ENSMUSP00000015583 | ENSMUSP00000104992 | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | Antileukoproteinase; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. Modulates the innate immune response after bacterial infection. Contributes to regulate the inflammatory and immune responses to the intracellular parasite L.major. Down-regulates responses to bacterial lipopolysaccharide (LPS). Plays a role in regulating the activation of NF-kappa-B and inflammatory responses. Has antimicrobial activity against mycobacteria, but not against salmonella. Contributes to normal resistance against infection by M.tuberculosis. R [...] | 0.746 |
| Elane | Ctsg | ENSMUSP00000038925 | ENSMUSP00000015583 | Neutrophil elastase; Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity). Capable of killing E.coli; probably digests outer membrane protein A (ompA) in E.coli ; Belongs to the peptidase S1 family. Elastase subfamily. | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | 0.997 |
| Elane | Ltf | ENSMUSP00000038925 | ENSMUSP00000035077 | Neutrophil elastase; Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity). Capable of killing E.coli; probably digests outer membrane protein A (ompA) in E.coli ; Belongs to the peptidase S1 family. Elastase subfamily. | Lactotransferrin; Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites. | 0.992 |
| Elane | Mpo | ENSMUSP00000038925 | ENSMUSP00000020779 | Neutrophil elastase; Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity). Capable of killing E.coli; probably digests outer membrane protein A (ompA) in E.coli ; Belongs to the peptidase S1 family. Elastase subfamily. | Myeloperoxidase heavy chain; Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity; Belongs to the peroxidase family. XPO subfamily. | 0.999 |
| Elane | Prtn3 | ENSMUSP00000038925 | ENSMUSP00000006679 | Neutrophil elastase; Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity). Capable of killing E.coli; probably digests outer membrane protein A (ompA) in E.coli ; Belongs to the peptidase S1 family. Elastase subfamily. | Myeloblastin; Serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro). By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration. May play a role in neutrophil transendothelial migration, probably when associated with CD177; Belongs to the peptidase S1 family. Elastase subfamily. | 0.986 |
| Elane | Serpina1a | ENSMUSP00000038925 | ENSMUSP00000072652 | Neutrophil elastase; Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity). Capable of killing E.coli; probably digests outer membrane protein A (ompA) in E.coli ; Belongs to the peptidase S1 family. Elastase subfamily. | Alpha-1-antitrypsin 1-1; Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Belongs to the serpin family. | 0.980 |
| Elane | Serpina1b | ENSMUSP00000038925 | ENSMUSP00000139941 | Neutrophil elastase; Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity). Capable of killing E.coli; probably digests outer membrane protein A (ompA) in E.coli ; Belongs to the peptidase S1 family. Elastase subfamily. | Alpha-1-antitrypsin 1-2; Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Belongs to the serpin family. | 0.973 |
| Elane | Serpina1c | ENSMUSP00000038925 | ENSMUSP00000073695 | Neutrophil elastase; Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity). Capable of killing E.coli; probably digests outer membrane protein A (ompA) in E.coli ; Belongs to the peptidase S1 family. Elastase subfamily. | Alpha-1-antitrypsin 1-3; Inhibitor of serine proteases. Can inhibit trypsin and chymotrypsin; relatively ineffective against elastase. Belongs to the serpin family. | 0.971 |
| Elane | Serpina1d | ENSMUSP00000038925 | ENSMUSP00000077909 | Neutrophil elastase; Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity). Capable of killing E.coli; probably digests outer membrane protein A (ompA) in E.coli ; Belongs to the peptidase S1 family. Elastase subfamily. | Alpha-1-antitrypsin 1-4; Inhibitor of serine proteases. Can inhibit trypsin and chymotrypsin; relatively ineffective against elastase. Belongs to the serpin family. | 0.970 |
| Elane | Serpina1e | ENSMUSP00000038925 | ENSMUSP00000113606 | Neutrophil elastase; Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity). Capable of killing E.coli; probably digests outer membrane protein A (ompA) in E.coli ; Belongs to the peptidase S1 family. Elastase subfamily. | Alpha-1-antitrypsin 1-5; Does not inhibit elastase or chymotrypsin. No target protease has been identified to date; Belongs to the serpin family. | 0.973 |
| Elane | Slpi | ENSMUSP00000038925 | ENSMUSP00000104992 | Neutrophil elastase; Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity). Capable of killing E.coli; probably digests outer membrane protein A (ompA) in E.coli ; Belongs to the peptidase S1 family. Elastase subfamily. | Antileukoproteinase; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. Modulates the innate immune response after bacterial infection. Contributes to regulate the inflammatory and immune responses to the intracellular parasite L.major. Down-regulates responses to bacterial lipopolysaccharide (LPS). Plays a role in regulating the activation of NF-kappa-B and inflammatory responses. Has antimicrobial activity against mycobacteria, but not against salmonella. Contributes to normal resistance against infection by M.tuberculosis. R [...] | 0.942 |