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 |
| AFY91748.1 | AFY92257.1 | Cha6605_0457 | Cha6605_1020 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | Hypothetical protein. | 0.491 |
| AFY91748.1 | ndhH | Cha6605_0457 | Cha6605_2806 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.942 |
| AFY91748.1 | ndhH-2 | Cha6605_0457 | Cha6605_3745 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.942 |
| AFY92257.1 | AFY91748.1 | Cha6605_1020 | Cha6605_0457 | Hypothetical protein. | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | 0.491 |
| AFY92257.1 | AFY95282.1 | Cha6605_1020 | Cha6605_4346 | Hypothetical protein. | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | 0.491 |
| AFY92257.1 | ndhH | Cha6605_1020 | Cha6605_2806 | Hypothetical protein. | NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.496 |
| AFY92257.1 | ndhH-2 | Cha6605_1020 | Cha6605_3745 | Hypothetical protein. | NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.496 |
| AFY95282.1 | AFY92257.1 | Cha6605_4346 | Cha6605_1020 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | Hypothetical protein. | 0.491 |
| AFY95282.1 | ndhH | Cha6605_4346 | Cha6605_2806 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.783 |
| AFY95282.1 | ndhH-2 | Cha6605_4346 | Cha6605_3745 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.783 |
| ndhH | AFY91748.1 | Cha6605_2806 | Cha6605_0457 | NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | 0.942 |
| ndhH | AFY92257.1 | Cha6605_2806 | Cha6605_1020 | NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | Hypothetical protein. | 0.496 |
| ndhH | AFY95282.1 | Cha6605_2806 | Cha6605_4346 | NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | 0.783 |
| ndhH | ndhH-2 | Cha6605_2806 | Cha6605_3745 | NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.900 |
| ndhH-2 | AFY91748.1 | Cha6605_3745 | Cha6605_0457 | NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | 0.942 |
| ndhH-2 | AFY92257.1 | Cha6605_3745 | Cha6605_1020 | NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | Hypothetical protein. | 0.496 |
| ndhH-2 | AFY95282.1 | Cha6605_3745 | Cha6605_4346 | NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | 0.783 |
| ndhH-2 | ndhH | Cha6605_3745 | Cha6605_2806 | NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.900 |