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 |
| KMJ52243.1 | KMJ53339.1 | ACG97_14520 | ACG97_08535 | 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). | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.956 |
| KMJ52243.1 | KMJ53341.1 | ACG97_14520 | ACG97_08545 | 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). | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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. Belongs to the complex I 75 kDa subunit family. | 0.944 |
| KMJ52243.1 | KMJ53593.1 | ACG97_14520 | ACG97_07670 | 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). | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KMJ52243.1 | KMJ53594.1 | ACG97_14520 | ACG97_07675 | 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). | Cytochrome B; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.999 |
| KMJ52243.1 | KMJ53595.1 | ACG97_14520 | ACG97_07680 | 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). | Ubiquinol-cytochrome C reductase; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.999 |
| KMJ52243.1 | KMJ54729.1 | ACG97_14520 | ACG97_00095 | 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). | NAD-dependent dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.901 |
| KMJ52243.1 | acpP | ACG97_14520 | ACG97_01570 | 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). | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 0.931 |
| KMJ52243.1 | nuoB | ACG97_14520 | ACG97_08520 | 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). | NADH dehydrogenase; 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. | 0.976 |
| KMJ52243.1 | nuoC | ACG97_14520 | ACG97_08525 | 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). | NADH dehydrogenase; 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; Belongs to the complex I 30 kDa subunit family. | 0.988 |
| KMJ52243.1 | nuoD | ACG97_14520 | ACG97_08530 | 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). | NADH dehydrogenase; 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; Belongs to the complex I 49 kDa subunit family. | 0.979 |
| KMJ53339.1 | KMJ52243.1 | ACG97_08535 | ACG97_14520 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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). | 0.956 |
| KMJ53339.1 | KMJ53341.1 | ACG97_08535 | ACG97_08545 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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. Belongs to the complex I 75 kDa subunit family. | 0.999 |
| KMJ53339.1 | KMJ53593.1 | ACG97_08535 | ACG97_07670 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KMJ53339.1 | KMJ53594.1 | ACG97_08535 | ACG97_07675 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.989 |
| KMJ53339.1 | KMJ53595.1 | ACG97_08535 | ACG97_07680 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Ubiquinol-cytochrome C reductase; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.999 |
| KMJ53339.1 | KMJ54729.1 | ACG97_08535 | ACG97_00095 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NAD-dependent dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KMJ53339.1 | acpP | ACG97_08535 | ACG97_01570 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 0.999 |
| KMJ53339.1 | nuoB | ACG97_08535 | ACG97_08520 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; 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. | 0.999 |
| KMJ53339.1 | nuoC | ACG97_08535 | ACG97_08525 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; 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; Belongs to the complex I 30 kDa subunit family. | 0.999 |
| KMJ53339.1 | nuoD | ACG97_08535 | ACG97_08530 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; 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; Belongs to the complex I 49 kDa subunit family. | 0.999 |
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