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 |
| AEA68866.1 | AEA68867.1 | PSEBR_a2581 | PSEBR_a2582 | Formate dehydrogenase, gamma subunit. | Formate dehydrogenase beta subunit. | 0.999 |
| AEA68866.1 | AEA69925.1 | PSEBR_a2581 | PSEBR_a3585 | Formate dehydrogenase, gamma subunit. | NADH-quinone oxidoreductase subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | 0.989 |
| AEA68866.1 | AEA71438.1 | PSEBR_a2581 | PSEBR_a5008 | Formate dehydrogenase, gamma subunit. | Conserved hypothetical protein. | 0.638 |
| AEA68866.1 | nuoC | PSEBR_a2581 | PSEBR_a3583 | Formate dehydrogenase, gamma subunit. | NADH-quinone oxidoreductase subunit C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family. | 0.999 |
| AEA68867.1 | AEA68866.1 | PSEBR_a2582 | PSEBR_a2581 | Formate dehydrogenase beta subunit. | Formate dehydrogenase, gamma subunit. | 0.999 |
| AEA68867.1 | AEA69924.1 | PSEBR_a2582 | PSEBR_a3584 | Formate dehydrogenase beta subunit. | NADH-quinone oxidoreductase subunit E. | 0.992 |
| AEA68867.1 | AEA71438.1 | PSEBR_a2582 | PSEBR_a5008 | Formate dehydrogenase beta subunit. | Conserved hypothetical protein. | 0.661 |
| AEA68867.1 | nuoC | PSEBR_a2582 | PSEBR_a3583 | Formate dehydrogenase beta subunit. | NADH-quinone oxidoreductase subunit C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family. | 0.999 |
| AEA69924.1 | AEA68867.1 | PSEBR_a3584 | PSEBR_a2582 | NADH-quinone oxidoreductase subunit E. | Formate dehydrogenase beta subunit. | 0.992 |
| AEA69924.1 | AEA69925.1 | PSEBR_a3584 | PSEBR_a3585 | NADH-quinone oxidoreductase subunit E. | NADH-quinone oxidoreductase subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | 0.998 |
| AEA69924.1 | AEA71438.1 | PSEBR_a3584 | PSEBR_a5008 | NADH-quinone oxidoreductase subunit E. | Conserved hypothetical protein. | 0.638 |
| AEA69924.1 | nuoC | PSEBR_a3584 | PSEBR_a3583 | NADH-quinone oxidoreductase subunit E. | NADH-quinone oxidoreductase subunit C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family. | 0.999 |
| AEA69925.1 | AEA68866.1 | PSEBR_a3585 | PSEBR_a2581 | NADH-quinone oxidoreductase subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | Formate dehydrogenase, gamma subunit. | 0.989 |
| AEA69925.1 | AEA69924.1 | PSEBR_a3585 | PSEBR_a3584 | NADH-quinone oxidoreductase subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | NADH-quinone oxidoreductase subunit E. | 0.998 |
| AEA69925.1 | AEA71438.1 | PSEBR_a3585 | PSEBR_a5008 | NADH-quinone oxidoreductase subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | Conserved hypothetical protein. | 0.661 |
| AEA69925.1 | nuoC | PSEBR_a3585 | PSEBR_a3583 | NADH-quinone oxidoreductase subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | NADH-quinone oxidoreductase subunit C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family. | 0.999 |
| AEA71437.1 | AEA71438.1 | PSEBR_a5007 | PSEBR_a5008 | Putative phospholipid biosynthesis-related protein; putative membrane protein. | Conserved hypothetical protein. | 0.955 |
| AEA71437.1 | AEA71439.1 | PSEBR_a5007 | PSEBR_a5009 | Putative phospholipid biosynthesis-related protein; putative membrane protein. | Conserved hypothetical protein. | 0.968 |
| AEA71437.1 | AEA71440.1 | PSEBR_a5007 | PSEBR_a5010 | Putative phospholipid biosynthesis-related protein; putative membrane protein. | Conserved hypothetical protein. | 0.824 |
| AEA71437.1 | AEA71441.1 | PSEBR_a5007 | PSEBR_a5011 | Putative phospholipid biosynthesis-related protein; putative membrane protein. | Putative phospholipd biosynthesis-related protein. | 0.958 |
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