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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DSJ_11940 | DSJ_12400 | DSJ_11940 | DSJ_12400 | Flagellar hook-length control protein FliK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar filament capping protein FliD; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | 0.906 |
| DSJ_11940 | fliF | DSJ_11940 | DSJ_11965 | Flagellar hook-length control protein FliK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.994 |
| DSJ_11940 | fliG | DSJ_11940 | DSJ_11960 | Flagellar hook-length control protein FliK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar motor switch protein FliG; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | 0.990 |
| DSJ_11940 | fliH | DSJ_11940 | DSJ_11955 | Flagellar hook-length control protein FliK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar assembly protein FliH; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.993 |
| DSJ_11940 | fliI | DSJ_11940 | DSJ_11950 | Flagellar hook-length control protein FliK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellum-specific ATP synthase FliI; Involved in type III protein export during flagellum assembly; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.984 |
| DSJ_11940 | fliJ | DSJ_11940 | DSJ_11945 | Flagellar hook-length control protein FliK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar biosynthesis chaperone FliJ; Flagellar protein that affects chemotactic events. Belongs to the FliJ family. | 0.994 |
| DSJ_11940 | fliM | DSJ_11940 | DSJ_11930 | Flagellar hook-length control protein FliK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar motor switch protein FliM; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | 0.990 |
| DSJ_11940 | fliN | DSJ_11940 | DSJ_11925 | Flagellar hook-length control protein FliK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar motor switch protein FliN; FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Belongs to the FliN/MopA/SpaO family. | 0.978 |
| DSJ_11940 | fliP | DSJ_11940 | DSJ_11915 | Flagellar hook-length control protein FliK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar biosynthetic protein FliP; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. | 0.939 |
| DSJ_11940 | fliS | DSJ_11940 | DSJ_12395 | Flagellar hook-length control protein FliK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar export chaperone FliS; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.913 |
| DSJ_12400 | DSJ_11940 | DSJ_12400 | DSJ_11940 | Flagellar filament capping protein FliD; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Flagellar hook-length control protein FliK; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.906 |
| DSJ_12400 | fliF | DSJ_12400 | DSJ_11965 | Flagellar filament capping protein FliD; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.975 |
| DSJ_12400 | fliG | DSJ_12400 | DSJ_11960 | Flagellar filament capping protein FliD; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Flagellar motor switch protein FliG; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | 0.970 |
| DSJ_12400 | fliH | DSJ_12400 | DSJ_11955 | Flagellar filament capping protein FliD; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Flagellar assembly protein FliH; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.978 |
| DSJ_12400 | fliI | DSJ_12400 | DSJ_11950 | Flagellar filament capping protein FliD; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Flagellum-specific ATP synthase FliI; Involved in type III protein export during flagellum assembly; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.983 |
| DSJ_12400 | fliJ | DSJ_12400 | DSJ_11945 | Flagellar filament capping protein FliD; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Flagellar biosynthesis chaperone FliJ; Flagellar protein that affects chemotactic events. Belongs to the FliJ family. | 0.889 |
| DSJ_12400 | fliM | DSJ_12400 | DSJ_11930 | Flagellar filament capping protein FliD; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Flagellar motor switch protein FliM; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | 0.978 |
| DSJ_12400 | fliN | DSJ_12400 | DSJ_11925 | Flagellar filament capping protein FliD; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Flagellar motor switch protein FliN; FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Belongs to the FliN/MopA/SpaO family. | 0.964 |
| DSJ_12400 | fliP | DSJ_12400 | DSJ_11915 | Flagellar filament capping protein FliD; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Flagellar biosynthetic protein FliP; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. | 0.828 |
| DSJ_12400 | fliS | DSJ_12400 | DSJ_12395 | Flagellar filament capping protein FliD; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | Flagellar export chaperone FliS; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.997 |
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