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 |
| ARI75943.1 | ARI76008.1 | HM131_03465 | HM131_03795 | (2Fe-2S)-binding protein; 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). | 0.997 |
| ARI75943.1 | ARI76153.1 | HM131_03465 | HM131_04575 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome-c oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.585 |
| ARI75943.1 | ARI76529.1 | HM131_03465 | HM131_06650 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.915 |
| ARI75943.1 | ARI77263.1 | HM131_03465 | HM131_10605 | (2Fe-2S)-binding protein; 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. | 0.922 |
| ARI75943.1 | ARI77264.1 | HM131_03465 | HM131_10610 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C oxidase Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.922 |
| ARI75943.1 | ARI77606.1 | HM131_03465 | HM131_12460 | (2Fe-2S)-binding protein; 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). | 0.999 |
| ARI75943.1 | ARI77662.1 | HM131_03465 | HM131_12750 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.922 |
| ARI75943.1 | tuf | HM131_03465 | HM131_00440 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Elongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. | 0.544 |
| ARI76008.1 | ARI75943.1 | HM131_03795 | HM131_03465 | 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). | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.997 |
| ARI76008.1 | ARI76153.1 | HM131_03795 | HM131_04575 | 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-c oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.807 |
| ARI76008.1 | ARI76529.1 | HM131_03795 | HM131_06650 | 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). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.977 |
| ARI76008.1 | ARI77262.1 | HM131_03795 | HM131_10600 | 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). | Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.997 |
| ARI76008.1 | ARI77263.1 | HM131_03795 | HM131_10605 | 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 b6; Electron transport protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.994 |
| ARI76008.1 | ARI77264.1 | HM131_03795 | HM131_10610 | 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 C oxidase Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.991 |
| ARI76008.1 | ARI77606.1 | HM131_03795 | HM131_12460 | 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 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). | 0.999 |
| ARI76008.1 | ARI77662.1 | HM131_03795 | HM131_12750 | 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). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.991 |
| ARI76008.1 | tuf | HM131_03795 | HM131_00440 | 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). | Elongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. | 0.944 |
| ARI76153.1 | ARI75943.1 | HM131_04575 | HM131_03465 | Cytochrome-c oxidase; 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. | 0.585 |
| ARI76153.1 | ARI76008.1 | HM131_04575 | HM131_03795 | Cytochrome-c oxidase; 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). | 0.807 |
| ARI76153.1 | ARI76529.1 | HM131_04575 | HM131_06650 | Cytochrome-c oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.949 |
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