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 |
| AMF98646.1 | AMG00239.1 | AL538_13495 | AL538_21315 | Flagellin; Structural flagella protein; Vibrio contains multiple flagellin genes usually localized into two region on the chromosome, flaAC and flaCEDB in V. cholerae, flaFBA and flaCDE in V. parahemolyticus; FlaA is sigma 54 dependent and essential for motility in V.cholerae but not in V. parahaemolyticus; 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. | 0.884 |
| AMF98646.1 | FlgL | AL538_13495 | AL538_21080 | Flagellin; Structural flagella protein; Vibrio contains multiple flagellin genes usually localized into two region on the chromosome, flaAC and flaCEDB in V. cholerae, flaFBA and flaCDE in V. parahemolyticus; FlaA is sigma 54 dependent and essential for motility in V.cholerae but not in V. parahaemolyticus; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar biosynthesis protein FlgL; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.882 |
| AMF98646.1 | FliS | AL538_13495 | AL538_21310 | Flagellin; Structural flagella protein; Vibrio contains multiple flagellin genes usually localized into two region on the chromosome, flaAC and flaCEDB in V. cholerae, flaFBA and flaCDE in V. parahemolyticus; FlaA is sigma 54 dependent and essential for motility in V.cholerae but not in V. parahaemolyticus; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar protein FliS; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.917 |
| AMF98646.1 | flgC | AL538_13495 | AL538_13440 | Flagellin; Structural flagella protein; Vibrio contains multiple flagellin genes usually localized into two region on the chromosome, flaAC and flaCEDB in V. cholerae, flaFBA and flaCDE in V. parahemolyticus; FlaA is sigma 54 dependent and essential for motility in V.cholerae but not in V. parahaemolyticus; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar basal-body rod protein FlgC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the flagella basal body rod proteins family. | 0.887 |
| AMF98646.1 | flgC-2 | AL538_13495 | AL538_21035 | Flagellin; Structural flagella protein; Vibrio contains multiple flagellin genes usually localized into two region on the chromosome, flaAC and flaCEDB in V. cholerae, flaFBA and flaCDE in V. parahemolyticus; FlaA is sigma 54 dependent and essential for motility in V.cholerae but not in V. parahaemolyticus; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar basal-body rod protein FlgC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the flagella basal body rod proteins family. | 0.868 |
| AMF98646.1 | flgE-2 | AL538_13495 | AL538_13450 | Flagellin; Structural flagella protein; Vibrio contains multiple flagellin genes usually localized into two region on the chromosome, flaAC and flaCEDB in V. cholerae, flaFBA and flaCDE in V. parahemolyticus; FlaA is sigma 54 dependent and essential for motility in V.cholerae but not in V. parahaemolyticus; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar biosynthesis protein FlgE; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.867 |
| AMF98646.1 | flgK-2 | AL538_13495 | AL538_21075 | Flagellin; Structural flagella protein; Vibrio contains multiple flagellin genes usually localized into two region on the chromosome, flaAC and flaCEDB in V. cholerae, flaFBA and flaCDE in V. parahemolyticus; FlaA is sigma 54 dependent and essential for motility in V.cholerae but not in V. parahaemolyticus; 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. | 0.893 |
| AMF98646.1 | fliG | AL538_13495 | AL538_21390 | Flagellin; Structural flagella protein; Vibrio contains multiple flagellin genes usually localized into two region on the chromosome, flaAC and flaCEDB in V. cholerae, flaFBA and flaCDE in V. parahemolyticus; FlaA is sigma 54 dependent and essential for motility in V.cholerae but not in V. parahaemolyticus; Derived by automated computational analysis using gene prediction method: Protein Homology. | One of three proteins involved in switching the direction of the flagellar rotation; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.882 |
| AMF98646.1 | fliG-2 | AL538_13495 | AL538_05110 | Flagellin; Structural flagella protein; Vibrio contains multiple flagellin genes usually localized into two region on the chromosome, flaAC and flaCEDB in V. cholerae, flaFBA and flaCDE in V. parahemolyticus; FlaA is sigma 54 dependent and essential for motility in V.cholerae but not in V. parahaemolyticus; 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. | 0.875 |
| AMF98646.1 | fliS | AL538_13495 | AL538_05140 | Flagellin; Structural flagella protein; Vibrio contains multiple flagellin genes usually localized into two region on the chromosome, flaAC and flaCEDB in V. cholerae, flaFBA and flaCDE in V. parahemolyticus; FlaA is sigma 54 dependent and essential for motility in V.cholerae but not in V. parahaemolyticus; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar protein FliS; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.955 |
| AMG00239.1 | AMF98646.1 | AL538_21315 | AL538_13495 | 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; Vibrio contains multiple flagellin genes usually localized into two region on the chromosome, flaAC and flaCEDB in V. cholerae, flaFBA and flaCDE in V. parahemolyticus; FlaA is sigma 54 dependent and essential for motility in V.cholerae but not in V. parahaemolyticus; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.884 |
| AMG00239.1 | FlgL | AL538_21315 | AL538_21080 | 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.952 |
| AMG00239.1 | FliS | AL538_21315 | AL538_21310 | 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.989 |
| AMG00239.1 | flgC | AL538_21315 | AL538_13440 | 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 basal-body rod protein FlgC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the flagella basal body rod proteins family. | 0.925 |
| AMG00239.1 | flgC-2 | AL538_21315 | AL538_21035 | 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 basal-body rod protein FlgC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the flagella basal body rod proteins family. | 0.936 |
| AMG00239.1 | flgE-2 | AL538_21315 | AL538_13450 | 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 FlgE; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.919 |
| AMG00239.1 | flgK-2 | AL538_21315 | AL538_21075 | 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. | 0.964 |
| AMG00239.1 | fliG | AL538_21315 | AL538_21390 | 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. | One of three proteins involved in switching the direction of the flagellar rotation; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.942 |
| AMG00239.1 | fliG-2 | AL538_21315 | AL538_05110 | 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 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. | 0.903 |
| AMG00239.1 | fliS | AL538_21315 | AL538_05140 | 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.953 |
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