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 |
| ALX95613.1 | ALX95640.1 | AV650_19580 | AV650_19730 | Flagellar hook 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. | Flagellar biosynthesis anti-sigma factor FlgM; Regulates the flagellar specific sigma28 transcription factor; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.912 |
| ALX95613.1 | flgB | AV650_19580 | AV650_19720 | Flagellar hook 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. | Flagellar biosynthesis protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | 0.974 |
| ALX95613.1 | flgC | AV650_19580 | AV650_19715 | Flagellar hook 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. | Flagellar basal-body rod protein FlgC; 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. | 0.978 |
| ALX95613.1 | flgD | AV650_19580 | AV650_19710 | Flagellar hook 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. | Flagellar basal body rod modification protein; Required for flagellar hook formation. May act as a scaffolding protein. | 0.976 |
| ALX95613.1 | flgE | AV650_19580 | AV650_19705 | Flagellar hook 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. | FlgF, with FlgB and C, makes up the proximal portion of the flagellar basal body rod; frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.974 |
| ALX95613.1 | flgK | AV650_19580 | AV650_19675 | Flagellar hook 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. | Flagellar biosynthesis protein FlgK; With FlgL acts as a hook filament junction protein to join the flagellar filament to the hook; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.985 |
| ALX95613.1 | fliA | AV650_19580 | AV650_19570 | Flagellar hook 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. | Flagellar biosynthesis sigma factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes; Belongs to the sigma-70 factor family. FliA subfamily. | 0.954 |
| ALX95613.1 | fliG | AV650_19580 | AV650_19610 | Flagellar hook 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. | 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. | 0.973 |
| ALX95613.1 | fliM | AV650_19580 | AV650_19640 | Flagellar hook 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. | 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. | 0.984 |
| ALX95613.1 | fliN | AV650_19580 | AV650_19645 | Flagellar hook 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. | 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. | 0.971 |
| ALX95640.1 | ALX95613.1 | AV650_19730 | AV650_19580 | Flagellar biosynthesis anti-sigma factor FlgM; Regulates the flagellar specific sigma28 transcription factor; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar hook 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. | 0.912 |
| ALX95640.1 | flgB | AV650_19730 | AV650_19720 | Flagellar biosynthesis anti-sigma factor FlgM; Regulates the flagellar specific sigma28 transcription factor; 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. | 0.918 |
| ALX95640.1 | flgC | AV650_19730 | AV650_19715 | Flagellar biosynthesis anti-sigma factor FlgM; Regulates the flagellar specific sigma28 transcription factor; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar basal-body rod protein FlgC; 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. | 0.896 |
| ALX95640.1 | flgD | AV650_19730 | AV650_19710 | Flagellar biosynthesis anti-sigma factor FlgM; Regulates the flagellar specific sigma28 transcription factor; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar basal body rod modification protein; Required for flagellar hook formation. May act as a scaffolding protein. | 0.920 |
| ALX95640.1 | flgE | AV650_19730 | AV650_19705 | Flagellar biosynthesis anti-sigma factor FlgM; Regulates the flagellar specific sigma28 transcription factor; Derived by automated computational analysis using gene prediction method: Protein Homology. | FlgF, with FlgB and C, makes up the proximal portion of the flagellar basal body rod; frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.881 |
| ALX95640.1 | flgK | AV650_19730 | AV650_19675 | Flagellar biosynthesis anti-sigma factor FlgM; Regulates the flagellar specific sigma28 transcription factor; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar biosynthesis protein FlgK; With FlgL acts as a hook filament junction protein to join the flagellar filament to the hook; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.918 |
| ALX95640.1 | fliA | AV650_19730 | AV650_19570 | Flagellar biosynthesis anti-sigma factor FlgM; Regulates the flagellar specific sigma28 transcription factor; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar biosynthesis sigma factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes; Belongs to the sigma-70 factor family. FliA subfamily. | 0.997 |
| ALX95640.1 | fliG | AV650_19730 | AV650_19610 | Flagellar biosynthesis anti-sigma factor FlgM; Regulates the flagellar specific sigma28 transcription factor; 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. | 0.574 |
| ALX95640.1 | fliM | AV650_19730 | AV650_19640 | Flagellar biosynthesis anti-sigma factor FlgM; Regulates the flagellar specific sigma28 transcription factor; 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. | 0.842 |
| ALX95640.1 | fliN | AV650_19730 | AV650_19645 | Flagellar biosynthesis anti-sigma factor FlgM; Regulates the flagellar specific sigma28 transcription factor; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.727 |
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