node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Bpi | Ctsg | ENSMUSP00000067837 | ENSMUSP00000015583 | Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family. | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | 0.771 |
Bpi | Elane | ENSMUSP00000067837 | ENSMUSP00000038925 | Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family. | 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. | 0.663 |
Bpi | Ltf | ENSMUSP00000067837 | ENSMUSP00000035077 | Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family. | 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. | 0.719 |
Bpi | Mpo | ENSMUSP00000067837 | ENSMUSP00000020779 | Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family. | 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. | 0.914 |
Bpi | Prtn3 | ENSMUSP00000067837 | ENSMUSP00000006679 | Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family. | 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. | 0.594 |
Ces1d | Mpo | ENSMUSP00000034172 | ENSMUSP00000020779 | Carboxylesterase 1D; Major lipase in white adipose tissue. Involved in the metabolism of xenobiotics and of natural substrates. Hydrolyzes triacylglycerols and monoacylglycerols, with a preference for monoacylglycerols. The susceptibility of the substrate increases with decreasing acyl chain length of the fatty acid moiety. Catalyzes the synthesis of fatty acid ethyl esters. | 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. | 0.910 |
Ctsg | Bpi | ENSMUSP00000015583 | ENSMUSP00000067837 | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family. | 0.771 |
Ctsg | Ctss | ENSMUSP00000015583 | ENSMUSP00000015667 | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | 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; Belongs to the peptidase C1 family. | 0.671 |
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 | Mmp9 | ENSMUSP00000015583 | ENSMUSP00000017881 | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | Matrix metalloproteinase-9; Could play a role in bone osteoclastic resorption. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments (By similarity). Belongs to the peptidase M10A family. | 0.990 |
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 | Ms4a3 | ENSMUSP00000015583 | ENSMUSP00000108608 | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | Membrane-spanning 4-domains subfamily A member 3; Hematopoietic modulator for the G1-S cell cycle transition. Modulates the level of phosphorylation of cyclin-dependent kinase 2 (CDK2) through its direct binding to cyclin-dependent kinase inhibitor 3 (CDKN3/KAP) (By similarity). | 0.838 |
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 |
Ctss | Ctsg | ENSMUSP00000015667 | ENSMUSP00000015583 | 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; Belongs to the peptidase C1 family. | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | 0.671 |
Ctss | Elane | ENSMUSP00000015667 | ENSMUSP00000038925 | 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; Belongs to the peptidase C1 family. | 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. | 0.817 |
Ctss | Ltf | ENSMUSP00000015667 | ENSMUSP00000035077 | 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; Belongs to the peptidase C1 family. | 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. | 0.666 |
Ctss | Mmp9 | ENSMUSP00000015667 | ENSMUSP00000017881 | 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; Belongs to the peptidase C1 family. | Matrix metalloproteinase-9; Could play a role in bone osteoclastic resorption. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments (By similarity). Belongs to the peptidase M10A family. | 0.819 |
Ctss | Mpo | ENSMUSP00000015667 | ENSMUSP00000020779 | 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; Belongs to the peptidase C1 family. | 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. | 0.953 |
Ctss | Prtn3 | ENSMUSP00000015667 | ENSMUSP00000006679 | 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; Belongs to the peptidase C1 family. | 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. | 0.548 |