Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Bpi | Bpifa1 | ENSMUSP00000067837 | ENSMUSP00000028985 | 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. | BPI fold-containing family A member 1; Lipid-binding protein which shows high specificity for the surfactant phospholipid dipalmitoylphosphatidylcholine (DPPC) (By similarity). Plays a role in the innate immune responses of the upper airways. Reduces the surface tension in secretions from airway epithelia and inhibits the formation of biofilm by pathogenic Gram-negative bacteria, such as P.aeruginosa and K.pneumoniae. Negatively regulates proteolytic cleavage of SCNN1G, an event that is required for activation of the epithelial sodium channel (ENaC), and thereby contributes to airway s [...] | 0.679 |
| 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 | Lbp | ENSMUSP00000067837 | ENSMUSP00000016168 | 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. | Lipopolysaccharide-binding protein; Plays a role in the innate immune response. Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria. Acts as an affinity enhancer for CD14, facilitating its association with LPS (By similarity). Promotes the release of cytokines in response to bacterial lipopolysaccharide. | 0.779 |
| 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 | Mptx2 | ENSMUSP00000067837 | ENSMUSP00000106855 | 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. | Pentaxin. | 0.523 |
| Bpi | Pglyrp1 | ENSMUSP00000067837 | ENSMUSP00000032573 | 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. | Peptidoglycan recognition protein 1; Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram-negative bacteria. Involved in innate immunity. May function in intracellular killing of bacteria. The soluble form triggers apoptosis in vitro. Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. | 0.504 |
| 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 |
| Bpi | Slamf9 | ENSMUSP00000067837 | ENSMUSP00000027830 | 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. | SLAM family member 9; May play a role in the immune response. | 0.510 |
| Bpifa1 | Bpi | ENSMUSP00000028985 | ENSMUSP00000067837 | BPI fold-containing family A member 1; Lipid-binding protein which shows high specificity for the surfactant phospholipid dipalmitoylphosphatidylcholine (DPPC) (By similarity). Plays a role in the innate immune responses of the upper airways. Reduces the surface tension in secretions from airway epithelia and inhibits the formation of biofilm by pathogenic Gram-negative bacteria, such as P.aeruginosa and K.pneumoniae. Negatively regulates proteolytic cleavage of SCNN1G, an event that is required for activation of the epithelial sodium channel (ENaC), and thereby contributes to airway s [...] | 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. | 0.679 |
| Bpifa1 | Lbp | ENSMUSP00000028985 | ENSMUSP00000016168 | BPI fold-containing family A member 1; Lipid-binding protein which shows high specificity for the surfactant phospholipid dipalmitoylphosphatidylcholine (DPPC) (By similarity). Plays a role in the innate immune responses of the upper airways. Reduces the surface tension in secretions from airway epithelia and inhibits the formation of biofilm by pathogenic Gram-negative bacteria, such as P.aeruginosa and K.pneumoniae. Negatively regulates proteolytic cleavage of SCNN1G, an event that is required for activation of the epithelial sodium channel (ENaC), and thereby contributes to airway s [...] | Lipopolysaccharide-binding protein; Plays a role in the innate immune response. Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria. Acts as an affinity enhancer for CD14, facilitating its association with LPS (By similarity). Promotes the release of cytokines in response to bacterial lipopolysaccharide. | 0.537 |
| Bpifa1 | Ltf | ENSMUSP00000028985 | ENSMUSP00000035077 | BPI fold-containing family A member 1; Lipid-binding protein which shows high specificity for the surfactant phospholipid dipalmitoylphosphatidylcholine (DPPC) (By similarity). Plays a role in the innate immune responses of the upper airways. Reduces the surface tension in secretions from airway epithelia and inhibits the formation of biofilm by pathogenic Gram-negative bacteria, such as P.aeruginosa and K.pneumoniae. Negatively regulates proteolytic cleavage of SCNN1G, an event that is required for activation of the epithelial sodium channel (ENaC), and thereby contributes to airway s [...] | 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. | 0.728 |
| 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 | 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 | Mptx2 | ENSMUSP00000015583 | ENSMUSP00000106855 | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | Pentaxin. | 0.540 |
| Ctsg | Pglyrp1 | ENSMUSP00000015583 | ENSMUSP00000032573 | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. | Peptidoglycan recognition protein 1; Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram-negative bacteria. Involved in innate immunity. May function in intracellular killing of bacteria. The soluble form triggers apoptosis in vitro. Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. | 0.614 |
| 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 |
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