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 annotation | node2 annotation | score |
| OXB_1748 | OXB_1921 | Cytochrome C-553. | Heme/copper-type cytochrome/quinol oxidase; 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 |
| OXB_1748 | OXB_1922 | Cytochrome C-553. | Cytochrome C oxidase subunit i. | 0.829 |
| OXB_1748 | OXB_1923 | Cytochrome C-553. | Heme/copper-type cytochrome/quinol oxidase. | 0.935 |
| OXB_1748 | OXB_1924 | Cytochrome C-553. | Cytochrome C oxidase subunit 4b. | 0.765 |
| OXB_1748 | OXB_1925 | Cytochrome C-553. | Cytochrome C oxidase subunit ctag. | 0.805 |
| OXB_1748 | OXB_1926 | Cytochrome C-553. | Membrane protein. | 0.456 |
| OXB_1748 | OXB_1928 | Cytochrome C-553. | Ylba like protein. | 0.753 |
| OXB_1748 | OXB_2334 | Cytochrome C-553. | Yphf protein. | 0.770 |
| OXB_1748 | OXB_2355 | Cytochrome C-553. | Menaquinol-cytochrome c reductase cytochrome b/c. | 0.974 |
| OXB_1748 | OXB_2928 | Cytochrome C-553. | Cytochrome C-551. | 0.462 |
| OXB_1921 | OXB_1748 | Heme/copper-type cytochrome/quinol oxidase; 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-553. | 0.999 |
| OXB_1921 | OXB_1922 | Heme/copper-type cytochrome/quinol oxidase; 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 i. | 0.999 |
| OXB_1921 | OXB_1923 | Heme/copper-type cytochrome/quinol oxidase; 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). | Heme/copper-type cytochrome/quinol oxidase. | 0.999 |
| OXB_1921 | OXB_1924 | Heme/copper-type cytochrome/quinol oxidase; 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 4b. | 0.999 |
| OXB_1921 | OXB_1925 | Heme/copper-type cytochrome/quinol oxidase; 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 ctag. | 0.952 |
| OXB_1921 | OXB_1926 | Heme/copper-type cytochrome/quinol oxidase; 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). | Membrane protein. | 0.634 |
| OXB_1921 | OXB_1928 | Heme/copper-type cytochrome/quinol oxidase; 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). | Ylba like protein. | 0.486 |
| OXB_1921 | OXB_2334 | Heme/copper-type cytochrome/quinol oxidase; 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). | Yphf protein. | 0.500 |
| OXB_1921 | OXB_2355 | Heme/copper-type cytochrome/quinol oxidase; 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 cytochrome b/c. | 0.999 |
| OXB_1921 | OXB_2928 | Heme/copper-type cytochrome/quinol oxidase; 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-551. | 0.732 |
page 1 of 5