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 protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| APG18648.1 | APG19363.1 | A3780_14145 | A3780_18035 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Flagellar cap 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. | 0.934 |
| APG18648.1 | flgC | A3780_14145 | A3780_08690 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | With FlgF and B makes up the proximal portion of the flagellar basal body rod; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.906 |
| APG18648.1 | flgC-2 | A3780_14145 | A3780_18160 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | With FlgF and B makes up the proximal portion of the flagellar basal body rod; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.911 |
| APG18648.1 | flgJ-2 | A3780_14145 | A3780_18125 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Flagellar rod assembly protein/muramidase FlgJ; Flagellum-specific muramidase which hydrolyzes the peptidoglycan layer to assemble the rod structure in the periplasmic space; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.926 |
| APG18648.1 | flgK-2 | A3780_14145 | A3780_18120 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Flagellar biosynthesis protein FlgK; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.908 |
| APG18648.1 | fliD | A3780_14145 | A3780_14165 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Flagellar cap 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. | 0.948 |
| APG18648.1 | fliG | A3780_14145 | A3780_14210 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 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. | 0.905 |
| APG18648.1 | fliG-2 | A3780_14145 | A3780_17975 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 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. | 0.906 |
| APG18648.1 | fliS | A3780_14145 | A3780_14170 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Flagellar protein FliS; Flagellin specific chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.979 |
| APG18648.1 | fliS-2 | A3780_14145 | A3780_18030 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Flagellar protein FliS; Flagellin specific chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.951 |
| APG19363.1 | APG18648.1 | A3780_18035 | A3780_14145 | Flagellar cap 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; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.934 |
| APG19363.1 | flgC | A3780_18035 | A3780_08690 | Flagellar cap 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. | With FlgF and B makes up the proximal portion of the flagellar basal body rod; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.931 |
| APG19363.1 | flgC-2 | A3780_18035 | A3780_18160 | Flagellar cap 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. | With FlgF and B makes up the proximal portion of the flagellar basal body rod; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.935 |
| APG19363.1 | flgJ-2 | A3780_18035 | A3780_18125 | Flagellar cap 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; Flagellum-specific muramidase which hydrolyzes the peptidoglycan layer to assemble the rod structure in the periplasmic space; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.860 |
| APG19363.1 | flgK-2 | A3780_18035 | A3780_18120 | Flagellar cap 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. | 0.960 |
| APG19363.1 | fliD | A3780_18035 | A3780_14165 | Flagellar cap 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 cap 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. | 0.918 |
| APG19363.1 | fliG | A3780_18035 | A3780_14210 | Flagellar cap 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. | 0.947 |
| APG19363.1 | fliG-2 | A3780_18035 | A3780_17975 | Flagellar cap 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. | 0.947 |
| APG19363.1 | fliS | A3780_18035 | A3780_14170 | Flagellar cap 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. | 0.976 |
| APG19363.1 | fliS-2 | A3780_18035 | A3780_18030 | Flagellar cap 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. | 0.983 |
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