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 |
| OAH53657.1 | OAH53659.1 | AWH48_10255 | AWH48_10265 | 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 B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| OAH53657.1 | OAH54849.1 | AWH48_10255 | AWH48_08615 | 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. | 0.998 |
| OAH53657.1 | OAH55884.1 | AWH48_10255 | AWH48_04200 | 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 C oxidase Cbb3; Component of the menaquinol-cytochrome c reductase complex. | 0.999 |
| OAH53657.1 | OAH55885.1 | AWH48_10255 | AWH48_04205 | 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 |
| OAH53657.1 | OAH56039.1 | AWH48_10255 | AWH48_05040 | 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 |
| OAH53657.1 | OAH56128.1 | AWH48_10255 | AWH48_05505 | 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). | L-aspartate oxidase; Catalyzes the oxidation of L-aspartate to iminoaspartate. | 0.877 |
| OAH53657.1 | OAH57101.1 | AWH48_10255 | AWH48_19435 | 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). | Pyridine nucleotide-disulfide oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.877 |
| OAH53657.1 | OAH57602.1 | AWH48_10255 | AWH48_18845 | 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). | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| OAH53657.1 | OAH58319.1 | AWH48_10255 | AWH48_18255 | 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). | NAD-dependent dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| OAH53657.1 | sdhA | AWH48_10255 | AWH48_05765 | 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). | Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.877 |
| OAH53659.1 | OAH53657.1 | AWH48_10265 | AWH48_10255 | Cytochrome B oxidoreductase; 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 |
| OAH53659.1 | OAH54849.1 | AWH48_10265 | AWH48_08615 | Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C551; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.986 |
| OAH53659.1 | OAH55884.1 | AWH48_10265 | AWH48_04200 | Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C oxidase Cbb3; Component of the menaquinol-cytochrome c reductase complex. | 0.990 |
| OAH53659.1 | OAH55885.1 | AWH48_10265 | AWH48_04205 | Cytochrome B oxidoreductase; 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. | 0.991 |
| OAH53659.1 | OAH56039.1 | AWH48_10265 | AWH48_05040 | Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.985 |
| OAH53659.1 | OAH56128.1 | AWH48_10265 | AWH48_05505 | Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | L-aspartate oxidase; Catalyzes the oxidation of L-aspartate to iminoaspartate. | 0.510 |
| OAH53659.1 | OAH57101.1 | AWH48_10265 | AWH48_19435 | Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Pyridine nucleotide-disulfide oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.510 |
| OAH53659.1 | OAH57602.1 | AWH48_10265 | AWH48_18845 | Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.965 |
| OAH53659.1 | OAH58319.1 | AWH48_10265 | AWH48_18255 | Cytochrome B oxidoreductase; 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. | 0.815 |
| OAH53659.1 | sdhA | AWH48_10265 | AWH48_05765 | Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.510 |
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