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 |
| KPH73961.1 | KPH74468.1 | AFL42_11125 | AFL42_10100 | Cytochrome B; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KPH73961.1 | KPH74469.1 | AFL42_11125 | AFL42_10105 | Cytochrome B; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.955 |
| KPH73961.1 | KPH76020.1 | AFL42_11125 | AFL42_07525 | Cytochrome B; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KPH73961.1 | KPH76021.1 | AFL42_11125 | AFL42_07530 | Cytochrome B; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome b6; Electron transport protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KPH73961.1 | KPH76022.1 | AFL42_11125 | AFL42_07535 | Cytochrome B; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KPH73961.1 | KPH76717.1 | AFL42_11125 | AFL42_05435 | Cytochrome B; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome C551; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KPH74468.1 | KPH73961.1 | AFL42_10100 | AFL42_11125 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.999 |
| KPH74468.1 | KPH74469.1 | AFL42_10100 | AFL42_10105 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.992 |
| KPH74468.1 | KPH76020.1 | AFL42_10100 | AFL42_07525 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.954 |
| KPH74468.1 | KPH76021.1 | AFL42_10100 | AFL42_07530 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome b6; Electron transport protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.951 |
| KPH74468.1 | KPH76022.1 | AFL42_10100 | AFL42_07535 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.863 |
| KPH74468.1 | KPH76717.1 | AFL42_10100 | AFL42_05435 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C551; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.882 |
| KPH74469.1 | KPH73961.1 | AFL42_10105 | AFL42_11125 | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.955 |
| KPH74469.1 | KPH74468.1 | AFL42_10105 | AFL42_10100 | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.992 |
| KPH74469.1 | KPH76020.1 | AFL42_10105 | AFL42_07525 | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.955 |
| KPH74469.1 | KPH76021.1 | AFL42_10105 | AFL42_07530 | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome b6; Electron transport protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.952 |
| KPH74469.1 | KPH76022.1 | AFL42_10105 | AFL42_07535 | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.917 |
| KPH74469.1 | KPH76717.1 | AFL42_10105 | AFL42_05435 | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C551; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.871 |
| KPH76020.1 | KPH73961.1 | AFL42_07525 | AFL42_11125 | Cytochrome Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.999 |
| KPH76020.1 | KPH74468.1 | AFL42_07525 | AFL42_10100 | Cytochrome Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.954 |
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