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 |
| fliC | prgH | STM1959 | STM2874 | Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Cell invasion protein; Required for invasion of epithelial cells. | 0.672 |
| fliC | sipA | STM1959 | STM2882 | Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Cell invasion protein; 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. In vitro, forms a complex with host cell protein T-plastin increasing actin bundling. It inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. Also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments; [...] | 0.891 |
| invG | prgH | STM2898 | STM2874 | Outer membrane invasion protein; Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells. Forms a ring-shaped multimeric structure with an apparent central pore in the outer membrane. | Cell invasion protein; Required for invasion of epithelial cells. | 0.999 |
| invG | prgK | STM2898 | STM2871 | Outer membrane invasion protein; Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells. Forms a ring-shaped multimeric structure with an apparent central pore in the outer membrane. | Cell invasion protein; Required for invasion of epithelial cells. Could be involved in protein secretion; Belongs to the YscJ lipoprotein family. | 0.999 |
| invG | sipA | STM2898 | STM2882 | Outer membrane invasion protein; Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells. Forms a ring-shaped multimeric structure with an apparent central pore in the outer membrane. | Cell invasion protein; 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. In vitro, forms a complex with host cell protein T-plastin increasing actin bundling. It inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. Also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments; [...] | 0.993 |
| prgH | fliC | STM2874 | STM1959 | Cell invasion protein; Required for invasion of epithelial cells. | Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.672 |
| prgH | invG | STM2874 | STM2898 | Cell invasion protein; Required for invasion of epithelial cells. | Outer membrane invasion protein; Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells. Forms a ring-shaped multimeric structure with an apparent central pore in the outer membrane. | 0.999 |
| prgH | prgK | STM2874 | STM2871 | Cell invasion protein; Required for invasion of epithelial cells. | Cell invasion protein; Required for invasion of epithelial cells. Could be involved in protein secretion; Belongs to the YscJ lipoprotein family. | 0.999 |
| prgH | sipA | STM2874 | STM2882 | Cell invasion protein; Required for invasion of epithelial cells. | Cell invasion protein; 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. In vitro, forms a complex with host cell protein T-plastin increasing actin bundling. It inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. Also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments; [...] | 0.993 |
| prgK | invG | STM2871 | STM2898 | Cell invasion protein; Required for invasion of epithelial cells. Could be involved in protein secretion; Belongs to the YscJ lipoprotein family. | Outer membrane invasion protein; Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells. Forms a ring-shaped multimeric structure with an apparent central pore in the outer membrane. | 0.999 |
| prgK | prgH | STM2871 | STM2874 | Cell invasion protein; Required for invasion of epithelial cells. Could be involved in protein secretion; Belongs to the YscJ lipoprotein family. | Cell invasion protein; Required for invasion of epithelial cells. | 0.999 |
| prgK | sipA | STM2871 | STM2882 | Cell invasion protein; Required for invasion of epithelial cells. Could be involved in protein secretion; Belongs to the YscJ lipoprotein family. | Cell invasion protein; 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. In vitro, forms a complex with host cell protein T-plastin increasing actin bundling. It inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. Also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments; [...] | 0.941 |
| sipA | fliC | STM2882 | STM1959 | Cell invasion protein; 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. In vitro, forms a complex with host cell protein T-plastin increasing actin bundling. It inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. Also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments; [...] | Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.891 |
| sipA | invG | STM2882 | STM2898 | Cell invasion protein; 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. In vitro, forms a complex with host cell protein T-plastin increasing actin bundling. It inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. Also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments; [...] | Outer membrane invasion protein; Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells. Forms a ring-shaped multimeric structure with an apparent central pore in the outer membrane. | 0.993 |
| sipA | prgH | STM2882 | STM2874 | Cell invasion protein; 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. In vitro, forms a complex with host cell protein T-plastin increasing actin bundling. It inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. Also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments; [...] | Cell invasion protein; Required for invasion of epithelial cells. | 0.993 |
| sipA | prgK | STM2882 | STM2871 | Cell invasion protein; 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. In vitro, forms a complex with host cell protein T-plastin increasing actin bundling. It inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. Also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments; [...] | Cell invasion protein; Required for invasion of epithelial cells. Could be involved in protein secretion; Belongs to the YscJ lipoprotein family. | 0.941 |