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 annotation | node2 annotation | score |
| Daro_1471 | Daro_3015 | Cytochrome c oxidase subunit 2; 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, class II. | 0.405 |
| Daro_1471 | Daro_3283 | Cytochrome c oxidase subunit 2; 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, class II. | 0.405 |
| Daro_2814 | Daro_3283 | Cytochrome B561, bacterial. | Cytochrome c, class II. | 0.495 |
| Daro_3015 | Daro_1471 | Cytochrome c, class II. | Cytochrome c oxidase subunit 2; 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). | 0.405 |
| Daro_3015 | Daro_3282 | Cytochrome c, class II. | Cytochrome B561, bacterial. | 0.551 |
| Daro_3015 | Daro_3283 | Cytochrome c, class II. | Cytochrome c, class II. | 0.420 |
| Daro_3282 | Daro_3015 | Cytochrome B561, bacterial. | Cytochrome c, class II. | 0.551 |
| Daro_3282 | Daro_3283 | Cytochrome B561, bacterial. | Cytochrome c, class II. | 0.904 |
| Daro_3283 | Daro_1471 | Cytochrome c, class II. | Cytochrome c oxidase subunit 2; 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). | 0.405 |
| Daro_3283 | Daro_2814 | Cytochrome c, class II. | Cytochrome B561, bacterial. | 0.495 |
| Daro_3283 | Daro_3015 | Cytochrome c, class II. | Cytochrome c, class II. | 0.420 |
| Daro_3283 | Daro_3282 | Cytochrome c, class II. | Cytochrome B561, bacterial. | 0.904 |
| Daro_3283 | Daro_3284 | Cytochrome c, class II. | PAS/PAC sensor signal transduction histidine kinase. | 0.440 |
| Daro_3283 | Daro_3285 | Cytochrome c, class II. | Response regulator receiver modulated metal dependent phosphohydrolase. | 0.440 |
| Daro_3284 | Daro_3283 | PAS/PAC sensor signal transduction histidine kinase. | Cytochrome c, class II. | 0.440 |
| Daro_3284 | Daro_3285 | PAS/PAC sensor signal transduction histidine kinase. | Response regulator receiver modulated metal dependent phosphohydrolase. | 0.834 |
| Daro_3285 | Daro_3283 | Response regulator receiver modulated metal dependent phosphohydrolase. | Cytochrome c, class II. | 0.440 |
| Daro_3285 | Daro_3284 | Response regulator receiver modulated metal dependent phosphohydrolase. | PAS/PAC sensor signal transduction histidine kinase. | 0.834 |