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 |
| AKM30486.3 | AKM30491.1 | AB870_10810 | AB870_10840 | Hypothetical 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 M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.978 |
| AKM30486.3 | AKM30495.1 | AB870_10810 | AB870_10870 | Hypothetical 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-associated protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | 0.959 |
| AKM30486.3 | AKM31254.3 | AB870_10810 | AB870_15670 | Hypothetical 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.876 |
| AKM30486.3 | AKM32748.1 | AB870_10810 | AB870_10955 | Hypothetical 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 FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | 0.979 |
| AKM30486.3 | flgC | AB870_10810 | AB870_10950 | Hypothetical 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. | 0.972 |
| AKM30486.3 | flgJ | AB870_10810 | AB870_10915 | Hypothetical 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 rod assembly protein/muramidase FlgJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.893 |
| AKM30486.3 | fliE | AB870_10810 | AB870_10835 | Hypothetical 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 FlhB; Incomplete; partial on complete genome; missing stop; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.972 |
| AKM30486.3 | fliG | AB870_10810 | AB870_10845 | Hypothetical 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.977 |
| AKM30486.3 | fliM | AB870_10810 | AB870_10875 | Hypothetical 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.974 |
| AKM30491.1 | AKM30486.3 | AB870_10840 | AB870_10810 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | Hypothetical 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. | 0.978 |
| AKM30491.1 | AKM30495.1 | AB870_10840 | AB870_10870 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | Flagellar basal body-associated protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | 0.985 |
| AKM30491.1 | AKM31254.3 | AB870_10840 | AB870_15670 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.881 |
| AKM30491.1 | AKM32748.1 | AB870_10840 | AB870_10955 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | Flagellar basal body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | 0.995 |
| AKM30491.1 | flgC | AB870_10840 | AB870_10950 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 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. | 0.995 |
| AKM30491.1 | flgJ | AB870_10840 | AB870_10915 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | Flagellar rod assembly protein/muramidase FlgJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.985 |
| AKM30491.1 | fliE | AB870_10840 | AB870_10835 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | Flagellar biosynthesis protein FlhB; Incomplete; partial on complete genome; missing stop; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.992 |
| AKM30491.1 | fliG | AB870_10840 | AB870_10845 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | Flagellar motor switch protein FliG; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| AKM30491.1 | fliM | AB870_10840 | AB870_10875 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | Flagellar motor switch protein FliM; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.989 |
| AKM30495.1 | AKM30486.3 | AB870_10870 | AB870_10810 | Flagellar basal body-associated protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | Hypothetical 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. | 0.959 |
| AKM30495.1 | AKM30491.1 | AB870_10870 | AB870_10840 | Flagellar basal body-associated protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.985 |
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