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 |
| fliD | fliE | DR95_332 | DR95_323 | Flagellar hook-associated protein 2; 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. | fliE: flagellar hook-basal body complex protein FliE. | 0.962 |
| fliD | fliF | DR95_332 | DR95_322 | Flagellar hook-associated protein 2; 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. | 0.969 |
| fliD | fliG | DR95_332 | DR95_321 | Flagellar hook-associated protein 2; 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. | 0.964 |
| fliD | fliH | DR95_332 | DR95_320 | Flagellar hook-associated protein 2; 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 FliH family protein. | 0.988 |
| fliD | fliI | DR95_332 | DR95_319 | Flagellar hook-associated protein 2; 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. | fliI_clade1: flagellar protein export ATPase FliI. | 0.950 |
| fliD | fliJ | DR95_332 | DR95_318 | Flagellar hook-associated protein 2; 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 protein FliJ; Flagellar protein that affects chemotactic events. Belongs to the FliJ family. | 0.910 |
| fliD | fliK | DR95_332 | DR95_317 | Flagellar hook-associated protein 2; 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 FliK family protein. | 0.949 |
| fliD | fliL | DR95_332 | DR95_316 | Flagellar hook-associated protein 2; 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 basal body-associated FliL family protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | 0.927 |
| fliD | fliM | DR95_332 | DR95_315 | Flagellar hook-associated protein 2; 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. | 0.965 |
| fliD | fliN | DR95_332 | DR95_314 | Flagellar hook-associated protein 2; 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. | 0.932 |
| fliE | fliD | DR95_323 | DR95_332 | fliE: flagellar hook-basal body complex protein FliE. | Flagellar hook-associated protein 2; 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. | 0.962 |
| fliE | fliF | DR95_323 | DR95_322 | fliE: flagellar hook-basal body complex protein FliE. | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.992 |
| fliE | fliG | DR95_323 | DR95_321 | fliE: flagellar hook-basal body complex protein FliE. | 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. | 0.989 |
| fliE | fliH | DR95_323 | DR95_320 | fliE: flagellar hook-basal body complex protein FliE. | Flagellar assembly FliH family protein. | 0.984 |
| fliE | fliI | DR95_323 | DR95_319 | fliE: flagellar hook-basal body complex protein FliE. | fliI_clade1: flagellar protein export ATPase FliI. | 0.913 |
| fliE | fliJ | DR95_323 | DR95_318 | fliE: flagellar hook-basal body complex protein FliE. | Flagellar export protein FliJ; Flagellar protein that affects chemotactic events. Belongs to the FliJ family. | 0.963 |
| fliE | fliK | DR95_323 | DR95_317 | fliE: flagellar hook-basal body complex protein FliE. | Flagellar hook-length control FliK family protein. | 0.984 |
| fliE | fliL | DR95_323 | DR95_316 | fliE: flagellar hook-basal body complex protein FliE. | Flagellar basal body-associated FliL family protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | 0.968 |
| fliE | fliM | DR95_323 | DR95_315 | fliE: flagellar hook-basal body complex protein FliE. | 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. | 0.983 |
| fliE | fliN | DR95_323 | DR95_314 | fliE: flagellar hook-basal body complex protein FliE. | 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. | 0.919 |
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