Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... 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 annotated functions of the network proteins
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Bpi | Ctsc | ENSMUSP00000067837 | ENSMUSP00000032779 | 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 | Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function | 0.905 |
| 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 | 0.959 |
| 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) | 0.958 |
| 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; 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 | 0.959 |
| Bpi | Serpina3a | ENSMUSP00000067837 | ENSMUSP00000140024 | 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 | Serine (or cysteine) peptidase inhibitor, clade A, member 3A; Belongs to the serpin family | 0.900 |
| Bpi | Serpina3b | ENSMUSP00000067837 | ENSMUSP00000082127 | 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 | Serine (or cysteine) peptidase inhibitor, clade A, member 3B | 0.900 |
| Bpi | Serpina3f | ENSMUSP00000067837 | ENSMUSP00000113945 | 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 | Serine (or cysteine) peptidase inhibitor, clade A, member 3F; Belongs to the serpin family | 0.900 |
| Bpi | Serpina3i | ENSMUSP00000067837 | ENSMUSP00000105584 | 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 | Serine (or cysteine) peptidase inhibitor, clade A, member 3I; Belongs to the serpin family | 0.900 |
| Bpi | Serpina3n | ENSMUSP00000067837 | ENSMUSP00000021506 | 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 | Serine (or cysteine) peptidase inhibitor, clade A, member 3N | 0.900 |
| Ctsc | Bpi | ENSMUSP00000032779 | ENSMUSP00000067837 | Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function | 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 | 0.905 |
| Ctsc | Ctsg | ENSMUSP00000032779 | ENSMUSP00000015583 | Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis | 0.966 |
| Ctsc | Elane | ENSMUSP00000032779 | ENSMUSP00000038925 | Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function | Neutrophil elastase; Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity) | 0.956 |
| Ctsc | Mpo | ENSMUSP00000032779 | ENSMUSP00000020779 | Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function | Myeloperoxidase; 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 | 0.921 |
| Ctsc | Serpina3a | ENSMUSP00000032779 | ENSMUSP00000140024 | Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function | Serine (or cysteine) peptidase inhibitor, clade A, member 3A; Belongs to the serpin family | 0.929 |
| Ctsc | Serpina3b | ENSMUSP00000032779 | ENSMUSP00000082127 | Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function | Serine (or cysteine) peptidase inhibitor, clade A, member 3B | 0.929 |
| Ctsc | Serpina3f | ENSMUSP00000032779 | ENSMUSP00000113945 | Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function | Serine (or cysteine) peptidase inhibitor, clade A, member 3F; Belongs to the serpin family | 0.930 |
| Ctsc | Serpina3i | ENSMUSP00000032779 | ENSMUSP00000105584 | Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function | Serine (or cysteine) peptidase inhibitor, clade A, member 3I; Belongs to the serpin family | 0.929 |
| Ctsc | Serpina3n | ENSMUSP00000032779 | ENSMUSP00000021506 | Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function | Serine (or cysteine) peptidase inhibitor, clade A, member 3N | 0.929 |
| 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 | 0.959 |
| Ctsg | Ctsc | ENSMUSP00000015583 | ENSMUSP00000032779 | Cathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis | Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function | 0.966 |
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