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 |
| AFK61201.1 | AFK61204.1 | TKWG_02975 | TKWG_02990 | Putative bifunctional protein; 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). | COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.999 |
| AFK61201.1 | AFK61242.1 | TKWG_02975 | TKWG_03230 | Putative bifunctional protein; 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). | Ubiquinol-cytochrome C reductase iron-sulfur subunit; COG0723 Rieske Fe-S protein. | 0.981 |
| AFK61201.1 | AFK61243.1 | TKWG_02975 | TKWG_03245 | Putative bifunctional protein; 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). | COG2857 Cytochrome c1. | 0.970 |
| AFK61201.1 | AFK63468.1 | TKWG_02975 | TKWG_17930 | Putative bifunctional protein; 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). | COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | 0.913 |
| AFK61201.1 | AFK63469.1 | TKWG_02975 | TKWG_17935 | Putative bifunctional protein; 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). | COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1; Belongs to the heme-copper respiratory oxidase family. | 0.991 |
| AFK61201.1 | AFK63470.1 | TKWG_02975 | TKWG_17940 | Putative bifunctional protein; 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). | COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | 0.944 |
| AFK61201.1 | AFK63471.1 | TKWG_02975 | TKWG_17945 | Putative bifunctional protein; 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). | COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.985 |
| AFK61201.1 | ctaB | TKWG_02975 | TKWG_03020 | Putative bifunctional protein; 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). | Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.959 |
| AFK61201.1 | nuoN | TKWG_02975 | TKWG_09455 | Putative bifunctional protein; 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:ubiquinone oxidoreductase subunit N; 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 ubiquinone. 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 subunit 2 family. | 0.939 |
| AFK61204.1 | AFK61201.1 | TKWG_02990 | TKWG_02975 | COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | Putative bifunctional protein; 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 |
| AFK61204.1 | AFK61242.1 | TKWG_02990 | TKWG_03230 | COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | Ubiquinol-cytochrome C reductase iron-sulfur subunit; COG0723 Rieske Fe-S protein. | 0.955 |
| AFK61204.1 | AFK61243.1 | TKWG_02990 | TKWG_03245 | COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | COG2857 Cytochrome c1. | 0.931 |
| AFK61204.1 | AFK63468.1 | TKWG_02990 | TKWG_17930 | COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | 0.838 |
| AFK61204.1 | AFK63469.1 | TKWG_02990 | TKWG_17935 | COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1; Belongs to the heme-copper respiratory oxidase family. | 0.960 |
| AFK61204.1 | AFK63470.1 | TKWG_02990 | TKWG_17940 | COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | 0.892 |
| AFK61204.1 | ctaB | TKWG_02990 | TKWG_03020 | COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.945 |
| AFK61204.1 | nuoN | TKWG_02990 | TKWG_09455 | COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | NADH:ubiquinone oxidoreductase subunit N; 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 ubiquinone. 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 subunit 2 family. | 0.835 |
| AFK61242.1 | AFK61201.1 | TKWG_03230 | TKWG_02975 | Ubiquinol-cytochrome C reductase iron-sulfur subunit; COG0723 Rieske Fe-S protein. | Putative bifunctional protein; 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). | 0.981 |
| AFK61242.1 | AFK61204.1 | TKWG_03230 | TKWG_02990 | Ubiquinol-cytochrome C reductase iron-sulfur subunit; COG0723 Rieske Fe-S protein. | COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.955 |
| AFK61242.1 | AFK61243.1 | TKWG_03230 | TKWG_03245 | Ubiquinol-cytochrome C reductase iron-sulfur subunit; COG0723 Rieske Fe-S protein. | COG2857 Cytochrome c1. | 0.999 |
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