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 |
| AMIS_11020 | AMIS_14150 | Hypothetical protein. | Putative cytochrome c oxidase subunit II; 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). | 0.928 |
| AMIS_11020 | AMIS_14160 | Hypothetical protein. | Hypothetical protein. | 0.928 |
| AMIS_11020 | AMIS_14210 | Hypothetical protein. | Putative cytochrome c oxidase subunit III. | 0.928 |
| AMIS_11020 | AMIS_14220 | Hypothetical protein. | Putative cytochrome c heme-binding subunit. | 0.928 |
| AMIS_11020 | AMIS_14230 | Hypothetical protein. | Putative ubiquinol-cytochrome c reductase iron-sulphur subunit. | 0.928 |
| AMIS_11020 | AMIS_14240 | Hypothetical protein. | Putative cytochrome b subunit. | 0.928 |
| AMIS_11020 | AMIS_16050 | Hypothetical protein. | Hypothetical protein; Rieske [2Fe-2S] domain. | 0.457 |
| AMIS_11020 | AMIS_47180 | Hypothetical protein. | Hypothetical protein. | 0.694 |
| AMIS_14150 | AMIS_11020 | Putative cytochrome c oxidase subunit II; 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). | Hypothetical protein. | 0.928 |
| AMIS_14150 | AMIS_14160 | Putative cytochrome c oxidase subunit II; 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). | Hypothetical protein. | 0.998 |
| AMIS_14150 | AMIS_14210 | Putative cytochrome c oxidase subunit II; 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). | Putative cytochrome c oxidase subunit III. | 0.999 |
| AMIS_14150 | AMIS_14220 | Putative cytochrome c oxidase subunit II; 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). | Putative cytochrome c heme-binding subunit. | 0.994 |
| AMIS_14150 | AMIS_14230 | Putative cytochrome c oxidase subunit II; 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). | Putative ubiquinol-cytochrome c reductase iron-sulphur subunit. | 0.994 |
| AMIS_14150 | AMIS_14240 | Putative cytochrome c oxidase subunit II; 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). | Putative cytochrome b subunit. | 0.999 |
| AMIS_14150 | AMIS_16050 | Putative cytochrome c oxidase subunit II; 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). | Hypothetical protein; Rieske [2Fe-2S] domain. | 0.962 |
| AMIS_14150 | AMIS_47180 | Putative cytochrome c oxidase subunit II; 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). | Hypothetical protein. | 0.928 |
| AMIS_14150 | AMIS_70010 | Putative cytochrome c oxidase subunit II; 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). | Hypothetical protein. | 0.940 |
| AMIS_14160 | AMIS_11020 | Hypothetical protein. | Hypothetical protein. | 0.928 |
| AMIS_14160 | AMIS_14150 | Hypothetical protein. | Putative cytochrome c oxidase subunit II; 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). | 0.998 |
| AMIS_14160 | AMIS_14210 | Hypothetical protein. | Putative cytochrome c oxidase subunit III. | 0.994 |
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