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 |
| KLU01856.1 | KLU03578.1 | RISK_006040 | RISK_004369 | Flagellar hook-associated 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; Belongs to the flagella basal body rod proteins family. | 0.972 |
| KLU01856.1 | KLU05172.1 | RISK_006040 | RISK_002934 | Flagellar hook-associated 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. | Light-harvesting LHII, alpha subunit B / Histone protein. | 0.903 |
| KLU01856.1 | KLU06037.1 | RISK_006040 | RISK_001888 | Flagellar hook-associated 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. | Chemotaxis protein methyltransferase CheR; Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. Belongs to the CheB family. | 0.992 |
| KLU01856.1 | KLU06140.1 | RISK_006040 | RISK_001991 | Flagellar hook-associated 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 hook protein FlgE. | 0.998 |
| KLU01856.1 | KLU07342.1 | RISK_006040 | RISK_000420 | Flagellar hook-associated 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. | Chemotaxis protein methyltransferase CheR; Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. Belongs to the CheB family. | 0.992 |
| KLU01856.1 | KLU07937.1 | RISK_006040 | RISK_000116 | Flagellar hook-associated 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. | 0.948 |
| KLU01856.1 | KLU07939.1 | RISK_006040 | RISK_000118 | Flagellar hook-associated 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 rotation protein MotB. | 0.888 |
| KLU01856.1 | KLU07940.1 | RISK_006040 | RISK_000119 | Flagellar hook-associated 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 rotation protein MotA. | 0.941 |
| KLU01856.1 | KLU07941.1 | RISK_006040 | RISK_000120 | Flagellar hook-associated 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 protein FlbD. | 0.474 |
| KLU01856.1 | flgK | RISK_006040 | RISK_005725 | Flagellar hook-associated 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 hook-associated protein FlgK. | 0.983 |
| KLU03578.1 | KLU01856.1 | RISK_004369 | RISK_006040 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Flagellar hook-associated 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. | 0.972 |
| KLU03578.1 | KLU05172.1 | RISK_004369 | RISK_002934 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Light-harvesting LHII, alpha subunit B / Histone protein. | 0.707 |
| KLU03578.1 | KLU06037.1 | RISK_004369 | RISK_001888 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Chemotaxis protein methyltransferase CheR; Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. Belongs to the CheB family. | 0.983 |
| KLU03578.1 | KLU06140.1 | RISK_004369 | RISK_001991 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Flagellar hook protein FlgE. | 0.999 |
| KLU03578.1 | KLU07342.1 | RISK_004369 | RISK_000420 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Chemotaxis protein methyltransferase CheR; Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. Belongs to the CheB family. | 0.983 |
| KLU03578.1 | KLU07937.1 | RISK_004369 | RISK_000116 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Flagellar motor switch protein FliN. | 0.980 |
| KLU03578.1 | KLU07939.1 | RISK_004369 | RISK_000118 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Flagellar motor rotation protein MotB. | 0.866 |
| KLU03578.1 | KLU07940.1 | RISK_004369 | RISK_000119 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Flagellar motor rotation protein MotA. | 0.983 |
| KLU03578.1 | flgK | RISK_004369 | RISK_005725 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Flagellar hook-associated protein FlgK. | 0.984 |
| KLU05172.1 | KLU01856.1 | RISK_002934 | RISK_006040 | Light-harvesting LHII, alpha subunit B / Histone protein. | Flagellar hook-associated 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. | 0.903 |
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