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 |
| STY0012 | fliC | gene:17584067 | gene:17586075 | DnaK protein (heat shock protein 70); Acts as a chaperone. | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.496 |
| STY0012 | sipD | gene:17584067 | gene:17586900 | DnaK protein (heat shock protein 70); Acts as a chaperone. | Pathogenicity island 1 effector protein; Required for translocation of effector proteins via the type III secretion system SPI-1, which is essential for an efficient bacterial internalization. Probably acts by modulating the secretion of SipA, SipB, and SipC (By similarity). | 0.410 |
| fliC | STY0012 | gene:17586075 | gene:17584067 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | DnaK protein (heat shock protein 70); Acts as a chaperone. | 0.496 |
| fliC | sipA | gene:17586075 | gene:17586899 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Pathogenicity island 1 effector protein (function unknown); Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F- actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization (By similarity). Belongs to the SipA/IpaA family. | 0.578 |
| fliC | sipB | gene:17586075 | gene:17586902 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Pathogenicity island 1 effector protein; Required for entry into the host cell through presentation or delivery of SipC at the host cell plasma membrane. Along with SipC, is necessary for the transfer of other effector proteins into the host cell. Induces macrophage apoptosis either by binding and activating the proapoptotic enzyme caspase-1 (caspase-1 dependent), resulting in the release of interleukin-1 beta active form, or by disrupting mitochondria and inducing autophagy (caspase-1 independent). The former is dependent of its membrane-fusion activity. The SipBC complex, in associat [...] | 0.502 |
| fliC | sipC | gene:17586075 | gene:17586901 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Pathogenicity island 1 effector protein; Actin-binding protein that interferes with host cell actin cytoskeleton. Nucleates actin polymerization and condensates actin filaments into cables (bundling). SipA potenciates SipC activity and both are required for an efficient bacterial internalization by the host cell (By similarity). | 0.568 |
| fliC | sipD | gene:17586075 | gene:17586900 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Pathogenicity island 1 effector protein; Required for translocation of effector proteins via the type III secretion system SPI-1, which is essential for an efficient bacterial internalization. Probably acts by modulating the secretion of SipA, SipB, and SipC (By similarity). | 0.423 |
| sigD | sipA | gene:17585096 | gene:17586899 | Cell invasion protein; Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns 3-P and prevents the transition of PtdIns 3-P to PtdIns 3,5-P2. It is one of the known effectors injected by Salmonella into the host cell and is required for invasion and for an efficient generation and maintenance of Salmonella-containing vacuole (SVC). Alteration of the phosphoinositide composition of the plasma membrane causes membrane ruffling and actin cytoskeleton rearrangements. The persistence of PtdIns 3-P diverts the SCV from the endocytic pathway resulting in enlarged vesicl [...] | Pathogenicity island 1 effector protein (function unknown); Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F- actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization (By similarity). Belongs to the SipA/IpaA family. | 0.999 |
| sigD | sipB | gene:17585096 | gene:17586902 | Cell invasion protein; Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns 3-P and prevents the transition of PtdIns 3-P to PtdIns 3,5-P2. It is one of the known effectors injected by Salmonella into the host cell and is required for invasion and for an efficient generation and maintenance of Salmonella-containing vacuole (SVC). Alteration of the phosphoinositide composition of the plasma membrane causes membrane ruffling and actin cytoskeleton rearrangements. The persistence of PtdIns 3-P diverts the SCV from the endocytic pathway resulting in enlarged vesicl [...] | Pathogenicity island 1 effector protein; Required for entry into the host cell through presentation or delivery of SipC at the host cell plasma membrane. Along with SipC, is necessary for the transfer of other effector proteins into the host cell. Induces macrophage apoptosis either by binding and activating the proapoptotic enzyme caspase-1 (caspase-1 dependent), resulting in the release of interleukin-1 beta active form, or by disrupting mitochondria and inducing autophagy (caspase-1 independent). The former is dependent of its membrane-fusion activity. The SipBC complex, in associat [...] | 0.998 |
| sigD | sipC | gene:17585096 | gene:17586901 | Cell invasion protein; Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns 3-P and prevents the transition of PtdIns 3-P to PtdIns 3,5-P2. It is one of the known effectors injected by Salmonella into the host cell and is required for invasion and for an efficient generation and maintenance of Salmonella-containing vacuole (SVC). Alteration of the phosphoinositide composition of the plasma membrane causes membrane ruffling and actin cytoskeleton rearrangements. The persistence of PtdIns 3-P diverts the SCV from the endocytic pathway resulting in enlarged vesicl [...] | Pathogenicity island 1 effector protein; Actin-binding protein that interferes with host cell actin cytoskeleton. Nucleates actin polymerization and condensates actin filaments into cables (bundling). SipA potenciates SipC activity and both are required for an efficient bacterial internalization by the host cell (By similarity). | 0.998 |
| sigD | sipD | gene:17585096 | gene:17586900 | Cell invasion protein; Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns 3-P and prevents the transition of PtdIns 3-P to PtdIns 3,5-P2. It is one of the known effectors injected by Salmonella into the host cell and is required for invasion and for an efficient generation and maintenance of Salmonella-containing vacuole (SVC). Alteration of the phosphoinositide composition of the plasma membrane causes membrane ruffling and actin cytoskeleton rearrangements. The persistence of PtdIns 3-P diverts the SCV from the endocytic pathway resulting in enlarged vesicl [...] | Pathogenicity island 1 effector protein; Required for translocation of effector proteins via the type III secretion system SPI-1, which is essential for an efficient bacterial internalization. Probably acts by modulating the secretion of SipA, SipB, and SipC (By similarity). | 0.991 |
| sipA | fliC | gene:17586899 | gene:17586075 | Pathogenicity island 1 effector protein (function unknown); Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F- actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization (By similarity). Belongs to the SipA/IpaA family. | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.578 |
| sipA | sigD | gene:17586899 | gene:17585096 | Pathogenicity island 1 effector protein (function unknown); Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F- actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization (By similarity). Belongs to the SipA/IpaA family. | Cell invasion protein; Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns 3-P and prevents the transition of PtdIns 3-P to PtdIns 3,5-P2. It is one of the known effectors injected by Salmonella into the host cell and is required for invasion and for an efficient generation and maintenance of Salmonella-containing vacuole (SVC). Alteration of the phosphoinositide composition of the plasma membrane causes membrane ruffling and actin cytoskeleton rearrangements. The persistence of PtdIns 3-P diverts the SCV from the endocytic pathway resulting in enlarged vesicl [...] | 0.999 |
| sipA | sipB | gene:17586899 | gene:17586902 | Pathogenicity island 1 effector protein (function unknown); Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F- actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization (By similarity). Belongs to the SipA/IpaA family. | Pathogenicity island 1 effector protein; Required for entry into the host cell through presentation or delivery of SipC at the host cell plasma membrane. Along with SipC, is necessary for the transfer of other effector proteins into the host cell. Induces macrophage apoptosis either by binding and activating the proapoptotic enzyme caspase-1 (caspase-1 dependent), resulting in the release of interleukin-1 beta active form, or by disrupting mitochondria and inducing autophagy (caspase-1 independent). The former is dependent of its membrane-fusion activity. The SipBC complex, in associat [...] | 0.999 |
| sipA | sipC | gene:17586899 | gene:17586901 | Pathogenicity island 1 effector protein (function unknown); Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F- actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization (By similarity). Belongs to the SipA/IpaA family. | Pathogenicity island 1 effector protein; Actin-binding protein that interferes with host cell actin cytoskeleton. Nucleates actin polymerization and condensates actin filaments into cables (bundling). SipA potenciates SipC activity and both are required for an efficient bacterial internalization by the host cell (By similarity). | 0.999 |
| sipA | sipD | gene:17586899 | gene:17586900 | Pathogenicity island 1 effector protein (function unknown); Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F- actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization (By similarity). Belongs to the SipA/IpaA family. | Pathogenicity island 1 effector protein; Required for translocation of effector proteins via the type III secretion system SPI-1, which is essential for an efficient bacterial internalization. Probably acts by modulating the secretion of SipA, SipB, and SipC (By similarity). | 0.999 |
| sipB | fliC | gene:17586902 | gene:17586075 | Pathogenicity island 1 effector protein; Required for entry into the host cell through presentation or delivery of SipC at the host cell plasma membrane. Along with SipC, is necessary for the transfer of other effector proteins into the host cell. Induces macrophage apoptosis either by binding and activating the proapoptotic enzyme caspase-1 (caspase-1 dependent), resulting in the release of interleukin-1 beta active form, or by disrupting mitochondria and inducing autophagy (caspase-1 independent). The former is dependent of its membrane-fusion activity. The SipBC complex, in associat [...] | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.502 |
| sipB | sigD | gene:17586902 | gene:17585096 | Pathogenicity island 1 effector protein; Required for entry into the host cell through presentation or delivery of SipC at the host cell plasma membrane. Along with SipC, is necessary for the transfer of other effector proteins into the host cell. Induces macrophage apoptosis either by binding and activating the proapoptotic enzyme caspase-1 (caspase-1 dependent), resulting in the release of interleukin-1 beta active form, or by disrupting mitochondria and inducing autophagy (caspase-1 independent). The former is dependent of its membrane-fusion activity. The SipBC complex, in associat [...] | Cell invasion protein; Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns 3-P and prevents the transition of PtdIns 3-P to PtdIns 3,5-P2. It is one of the known effectors injected by Salmonella into the host cell and is required for invasion and for an efficient generation and maintenance of Salmonella-containing vacuole (SVC). Alteration of the phosphoinositide composition of the plasma membrane causes membrane ruffling and actin cytoskeleton rearrangements. The persistence of PtdIns 3-P diverts the SCV from the endocytic pathway resulting in enlarged vesicl [...] | 0.998 |
| sipB | sipA | gene:17586902 | gene:17586899 | Pathogenicity island 1 effector protein; Required for entry into the host cell through presentation or delivery of SipC at the host cell plasma membrane. Along with SipC, is necessary for the transfer of other effector proteins into the host cell. Induces macrophage apoptosis either by binding and activating the proapoptotic enzyme caspase-1 (caspase-1 dependent), resulting in the release of interleukin-1 beta active form, or by disrupting mitochondria and inducing autophagy (caspase-1 independent). The former is dependent of its membrane-fusion activity. The SipBC complex, in associat [...] | Pathogenicity island 1 effector protein (function unknown); Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F- actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization (By similarity). Belongs to the SipA/IpaA family. | 0.999 |
| sipB | sipC | gene:17586902 | gene:17586901 | Pathogenicity island 1 effector protein; Required for entry into the host cell through presentation or delivery of SipC at the host cell plasma membrane. Along with SipC, is necessary for the transfer of other effector proteins into the host cell. Induces macrophage apoptosis either by binding and activating the proapoptotic enzyme caspase-1 (caspase-1 dependent), resulting in the release of interleukin-1 beta active form, or by disrupting mitochondria and inducing autophagy (caspase-1 independent). The former is dependent of its membrane-fusion activity. The SipBC complex, in associat [...] | Pathogenicity island 1 effector protein; Actin-binding protein that interferes with host cell actin cytoskeleton. Nucleates actin polymerization and condensates actin filaments into cables (bundling). SipA potenciates SipC activity and both are required for an efficient bacterial internalization by the host cell (By similarity). | 0.999 |
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