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 |
| ACPL_4490 | ACPL_7900 | ACPL_4490 | ACPL_7900 | Flagellar FliL protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | Flagellar hook-associated protein 2; 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. | 0.951 |
| ACPL_4490 | ACPL_7903 | ACPL_4490 | ACPL_7903 | Flagellar FliL protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | Flagellar basal-body rod protein flgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | 0.948 |
| ACPL_4490 | ACPL_7919 | ACPL_4490 | ACPL_7919 | Flagellar FliL protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | Flagellar protein FliO/FliZ. | 0.974 |
| ACPL_4490 | flgC | ACPL_4490 | ACPL_7904 | Flagellar FliL protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | Flagellar basal body rod protein. | 0.897 |
| ACPL_4490 | flgD | ACPL_4490 | ACPL_7927 | Flagellar FliL protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | Basal-body rod modification protein flgD; Flagellar hook capping protein. | 0.893 |
| ACPL_4490 | fliE | ACPL_4490 | ACPL_7905 | Flagellar FliL protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | Flagellar hook-basal body complex protein FliE. | 0.944 |
| ACPL_4490 | fliF | ACPL_4490 | ACPL_7906 | Flagellar FliL protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | Flagellar M-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.895 |
| ACPL_4490 | fliH | ACPL_4490 | ACPL_7908 | Flagellar FliL protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | Flagellar biosynthesis/type III secretory pathway protein. | 0.967 |
| ACPL_4490 | fliM | ACPL_4490 | ACPL_7921 | Flagellar FliL protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | Flagellar motor switch protein. | 0.925 |
| ACPL_4490 | pclO-2 | ACPL_4490 | ACPL_7914 | Flagellar FliL protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | Protein piccolo; Type V secretory pathway, adhesin AidA. | 0.918 |
| ACPL_7900 | ACPL_4490 | ACPL_7900 | ACPL_4490 | Flagellar hook-associated protein 2; 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 FliL protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | 0.951 |
| ACPL_7900 | ACPL_7903 | ACPL_7900 | ACPL_7903 | Flagellar hook-associated protein 2; 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. | 0.986 |
| ACPL_7900 | ACPL_7919 | ACPL_7900 | ACPL_7919 | Flagellar hook-associated protein 2; 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 FliO/FliZ. | 0.915 |
| ACPL_7900 | flgC | ACPL_7900 | ACPL_7904 | Flagellar hook-associated protein 2; 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. | 0.985 |
| ACPL_7900 | flgD | ACPL_7900 | ACPL_7927 | Flagellar hook-associated protein 2; 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. | Basal-body rod modification protein flgD; Flagellar hook capping protein. | 0.963 |
| ACPL_7900 | fliE | ACPL_7900 | ACPL_7905 | Flagellar hook-associated protein 2; 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-basal body complex protein FliE. | 0.984 |
| ACPL_7900 | fliF | ACPL_7900 | ACPL_7906 | Flagellar hook-associated protein 2; 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; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.984 |
| ACPL_7900 | fliH | ACPL_7900 | ACPL_7908 | Flagellar hook-associated protein 2; 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/type III secretory pathway protein. | 0.985 |
| ACPL_7900 | fliM | ACPL_7900 | ACPL_7921 | Flagellar hook-associated protein 2; 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. | 0.970 |
| ACPL_7900 | pclO-2 | ACPL_7900 | ACPL_7914 | Flagellar hook-associated protein 2; 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. | Protein piccolo; Type V secretory pathway, adhesin AidA. | 0.901 |
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