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 |
| AKO51009.1 | AKO51047.1 | ABA45_00050 | ABA45_00290 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B559 subunit alpha; 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). | 0.816 |
| AKO51047.1 | AKO51009.1 | ABA45_00290 | ABA45_00050 | Cytochrome B559 subunit alpha; 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. | 0.816 |
| AKO51047.1 | AKO51800.1 | ABA45_00290 | ABA45_04680 | Cytochrome B559 subunit alpha; 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 C554; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.493 |
| AKO51047.1 | AKO52068.1 | ABA45_00290 | ABA45_06190 | Cytochrome B559 subunit alpha; 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. | 0.796 |
| AKO51047.1 | AKO52912.1 | ABA45_00290 | ABA45_11275 | Cytochrome B559 subunit alpha; 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; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.979 |
| AKO51047.1 | AKO53411.1 | ABA45_00290 | ABA45_14110 | Cytochrome B559 subunit alpha; 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. | 0.493 |
| AKO51047.1 | AKO53551.1 | ABA45_00290 | ABA45_14935 | Cytochrome B559 subunit alpha; 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. | 0.796 |
| AKO51047.1 | AKO53878.1 | ABA45_00290 | ABA45_16755 | Cytochrome B559 subunit alpha; 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. | 0.674 |
| AKO51800.1 | AKO51047.1 | ABA45_04680 | ABA45_00290 | Cytochrome C554; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B559 subunit alpha; 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). | 0.493 |
| AKO51800.1 | AKO53411.1 | ABA45_04680 | ABA45_14110 | Cytochrome C554; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.639 |
| AKO51800.1 | AKO53878.1 | ABA45_04680 | ABA45_16755 | Cytochrome C554; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.775 |
| AKO52068.1 | AKO51047.1 | ABA45_06190 | ABA45_00290 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B559 subunit alpha; 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). | 0.796 |
| AKO52912.1 | AKO51047.1 | ABA45_11275 | ABA45_00290 | Cytochrome Cbb3; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | Cytochrome B559 subunit alpha; 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). | 0.979 |
| AKO53411.1 | AKO51047.1 | ABA45_14110 | ABA45_00290 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B559 subunit alpha; 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). | 0.493 |
| AKO53411.1 | AKO51800.1 | ABA45_14110 | ABA45_04680 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C554; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.639 |
| AKO53551.1 | AKO51047.1 | ABA45_14935 | ABA45_00290 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B559 subunit alpha; 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). | 0.796 |
| AKO53878.1 | AKO51047.1 | ABA45_16755 | ABA45_00290 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B559 subunit alpha; 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). | 0.674 |
| AKO53878.1 | AKO51800.1 | ABA45_16755 | ABA45_04680 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C554; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.775 |