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 |
| ABF39460.1 | ABF41997.1 | Acid345_0455 | Acid345_2996 | 4Fe-4S ferredoxin, iron-sulfur binding protein. | 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). | 0.939 |
| ABF39460.1 | ABF42000.1 | Acid345_0455 | Acid345_2999 | 4Fe-4S ferredoxin, iron-sulfur binding protein. | Quinol:cytochrome c oxidoreductase quinone-binding subunit 2. | 0.927 |
| ABF39460.1 | ABF42001.1 | Acid345_0455 | Acid345_3000 | 4Fe-4S ferredoxin, iron-sulfur binding protein. | Quinol:cytochrome c oxidoreductase monoheme cytochrome subunit. | 0.919 |
| ABF39460.1 | ABF42002.1 | Acid345_0455 | Acid345_3001 | 4Fe-4S ferredoxin, iron-sulfur binding protein. | Quinol:cytochrome c oxidoreductase membrane protein. | 0.917 |
| ABF39460.1 | ABF42003.1 | Acid345_0455 | Acid345_3002 | 4Fe-4S ferredoxin, iron-sulfur binding protein. | Quinol:cytochrome c oxidoreductase quinone-binding subunit 1. | 0.604 |
| ABF39460.1 | ABF42004.1 | Acid345_0455 | Acid345_3003 | 4Fe-4S ferredoxin, iron-sulfur binding protein. | Quinol:cytochrome c oxidoreductase iron-sulfur protein precursor. | 0.996 |
| ABF39460.1 | ABF42005.1 | Acid345_0455 | Acid345_3004 | 4Fe-4S ferredoxin, iron-sulfur binding protein. | Quinol:cytochrome c oxidoreductase pentaheme cytochrome subunit. | 0.932 |
| ABF41994.1 | ABF41995.1 | Acid345_2993 | Acid345_2994 | Caa(3)-type oxidase, subunit IV. | Cytochrome c oxidase, subunit III. | 0.949 |
| ABF41994.1 | ABF41997.1 | Acid345_2993 | Acid345_2996 | Caa(3)-type oxidase, subunit IV. | 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). | 0.962 |
| ABF41994.1 | ABF41998.1 | Acid345_2993 | Acid345_2997 | Caa(3)-type oxidase, subunit IV. | Electron transport protein SCO1/SenC. | 0.948 |
| ABF41994.1 | ABF42000.1 | Acid345_2993 | Acid345_2999 | Caa(3)-type oxidase, subunit IV. | Quinol:cytochrome c oxidoreductase quinone-binding subunit 2. | 0.892 |
| ABF41994.1 | ABF42001.1 | Acid345_2993 | Acid345_3000 | Caa(3)-type oxidase, subunit IV. | Quinol:cytochrome c oxidoreductase monoheme cytochrome subunit. | 0.909 |
| ABF41994.1 | ABF42002.1 | Acid345_2993 | Acid345_3001 | Caa(3)-type oxidase, subunit IV. | Quinol:cytochrome c oxidoreductase membrane protein. | 0.898 |
| ABF41994.1 | ABF42003.1 | Acid345_2993 | Acid345_3002 | Caa(3)-type oxidase, subunit IV. | Quinol:cytochrome c oxidoreductase quinone-binding subunit 1. | 0.838 |
| ABF41994.1 | ABF42004.1 | Acid345_2993 | Acid345_3003 | Caa(3)-type oxidase, subunit IV. | Quinol:cytochrome c oxidoreductase iron-sulfur protein precursor. | 0.860 |
| ABF41994.1 | ABF42005.1 | Acid345_2993 | Acid345_3004 | Caa(3)-type oxidase, subunit IV. | Quinol:cytochrome c oxidoreductase pentaheme cytochrome subunit. | 0.873 |
| ABF41995.1 | ABF41994.1 | Acid345_2994 | Acid345_2993 | Cytochrome c oxidase, subunit III. | Caa(3)-type oxidase, subunit IV. | 0.949 |
| ABF41995.1 | ABF41997.1 | Acid345_2994 | Acid345_2996 | Cytochrome c oxidase, subunit III. | 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). | 0.999 |
| ABF41995.1 | ABF41998.1 | Acid345_2994 | Acid345_2997 | Cytochrome c oxidase, subunit III. | Electron transport protein SCO1/SenC. | 0.950 |
| ABF41995.1 | ABF42000.1 | Acid345_2994 | Acid345_2999 | Cytochrome c oxidase, subunit III. | Quinol:cytochrome c oxidoreductase quinone-binding subunit 2. | 0.873 |
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