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 |
| AMG69666.1 | AMG69667.1 | AL531_04530 | AL531_04535 | Flagellar hook-associated protein; 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. | Flagellin; Structural flagella protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.965 |
| AMG69666.1 | flgB | AL531_04530 | AL531_04350 | Flagellar hook-associated protein; 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 protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | 0.971 |
| AMG69666.1 | flgK | AL531_04530 | AL531_04395 | Flagellar hook-associated protein; 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 protein FlgK; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.974 |
| AMG69666.1 | flgL | AL531_04530 | AL531_04400 | Flagellar hook-associated protein; 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 protein FlgL; With FlgK acts as a hook filament junction protein to join the flagellar filament to the hook; Yersinia, Vibrio parahaemolyticus, Bradyrhizobium and other organisms have 2 copies of this and other flagellar genes; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.977 |
| AMG69666.1 | fliF | AL531_04530 | AL531_04475 | Flagellar hook-associated protein; 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 MS-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.971 |
| AMG69666.1 | fliG | AL531_04530 | AL531_04470 | Flagellar hook-associated protein; 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 G; 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. | 0.969 |
| AMG69666.1 | fliH | AL531_04530 | AL531_04465 | Flagellar hook-associated protein; 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 H; Binds to and inhibits the function of flagella specific ATPase FliI; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.966 |
| AMG69666.1 | fliM | AL531_04530 | AL531_04440 | Flagellar hook-associated protein; 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. | 0.970 |
| AMG69666.1 | fliS | AL531_04530 | AL531_04525 | Flagellar hook-associated protein; 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 protein FliS; Flagellin specific chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.995 |
| AMG69666.1 | fliT | AL531_04530 | AL531_04520 | Flagellar hook-associated protein; 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 protein FliT; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.988 |
| AMG69667.1 | AMG69666.1 | AL531_04535 | AL531_04530 | Flagellin; Structural flagella protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar hook-associated protein; 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. | 0.965 |
| AMG69667.1 | flgB | AL531_04535 | AL531_04350 | Flagellin; Structural flagella protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar biosynthesis protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | 0.936 |
| AMG69667.1 | flgK | AL531_04535 | AL531_04395 | Flagellin; Structural flagella protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar biosynthesis protein FlgK; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.934 |
| AMG69667.1 | flgL | AL531_04535 | AL531_04400 | Flagellin; Structural flagella protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar biosynthesis protein FlgL; With FlgK acts as a hook filament junction protein to join the flagellar filament to the hook; Yersinia, Vibrio parahaemolyticus, Bradyrhizobium and other organisms have 2 copies of this and other flagellar genes; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.926 |
| AMG69667.1 | fliF | AL531_04535 | AL531_04475 | Flagellin; Structural flagella protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar MS-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.899 |
| AMG69667.1 | fliG | AL531_04535 | AL531_04470 | Flagellin; Structural flagella protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar motor switch protein G; 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. | 0.932 |
| AMG69667.1 | fliH | AL531_04535 | AL531_04465 | Flagellin; Structural flagella protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar assembly protein H; Binds to and inhibits the function of flagella specific ATPase FliI; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.613 |
| AMG69667.1 | fliM | AL531_04535 | AL531_04440 | Flagellin; Structural flagella protein; 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. | 0.917 |
| AMG69667.1 | fliS | AL531_04535 | AL531_04525 | Flagellin; Structural flagella protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar protein FliS; Flagellin specific chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.987 |
| AMG69667.1 | fliT | AL531_04535 | AL531_04520 | Flagellin; Structural flagella protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar protein FliT; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.612 |
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