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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KNB69853.1 | KNB70045.1 | ADS79_28870 | ADS79_29970 | Cytochrome B; 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 |
| KNB69853.1 | KNB71056.1 | ADS79_28870 | ADS79_19725 | Cytochrome B; 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 Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KNB69853.1 | KNB71057.1 | ADS79_28870 | ADS79_19730 | Cytochrome B; 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 b6; Electron transport protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KNB69853.1 | KNB71058.1 | ADS79_28870 | ADS79_19735 | Cytochrome B; 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). | Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KNB69853.1 | KNB71842.1 | ADS79_28870 | ADS79_24150 | Cytochrome B; 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. | 0.999 |
| KNB69853.1 | KNB71920.1 | ADS79_28870 | ADS79_24570 | Cytochrome B; 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 |
| KNB69853.1 | KNB73021.1 | ADS79_28870 | ADS79_12205 | Cytochrome B; 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 C551; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KNB69853.1 | nuoB | ADS79_28870 | ADS79_24130 | Cytochrome B; 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 a menaquinone. 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 |
| KNB69853.1 | nuoC | ADS79_28870 | ADS79_24135 | Cytochrome B; 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-quinone oxidoreductase subunit C; 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 a menaquinone. 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 |
| KNB69853.1 | nuoD | ADS79_28870 | ADS79_24140 | Cytochrome B; 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 a menaquinone. 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 |
| KNB70045.1 | KNB69853.1 | ADS79_29970 | ADS79_28870 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B; 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 |
| KNB70045.1 | KNB71056.1 | ADS79_29970 | ADS79_19725 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.975 |
| KNB70045.1 | KNB71057.1 | ADS79_29970 | ADS79_19730 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome b6; Electron transport protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.986 |
| KNB70045.1 | KNB71058.1 | ADS79_29970 | ADS79_19735 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.997 |
| KNB70045.1 | KNB71842.1 | ADS79_29970 | ADS79_24150 | Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.606 |
| KNB70045.1 | nuoB | ADS79_29970 | ADS79_24130 | 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 a menaquinone. 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. | 0.717 |
| KNB70045.1 | nuoC | ADS79_29970 | ADS79_24135 | Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH-quinone oxidoreductase subunit C; 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 a menaquinone. 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. | 0.591 |
| KNB70045.1 | nuoD | ADS79_29970 | ADS79_24140 | 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 a menaquinone. 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. | 0.605 |
| KNB71056.1 | KNB69853.1 | ADS79_19725 | ADS79_28870 | Cytochrome Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B; 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 |
| KNB71056.1 | KNB70045.1 | ADS79_19725 | ADS79_29970 | Cytochrome Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.975 |
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