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 |
| AKO95333.1 | AKO95748.1 | MALG_00117 | MALG_00553 | NADH dehydrogenase, FAD-containing subunit. | 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). | 0.455 |
| AKO95333.1 | AKO95752.1 | MALG_00117 | MALG_00557 | NADH dehydrogenase, FAD-containing subunit. | Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.452 |
| AKO95333.1 | AKO96168.1 | MALG_00117 | MALG_00974 | NADH dehydrogenase, FAD-containing subunit. | Cytochrome d oxidase, subunit II (cydB). | 0.651 |
| AKO95333.1 | AKO96169.1 | MALG_00117 | MALG_00975 | NADH dehydrogenase, FAD-containing subunit. | Cytochrome bd-type quinol oxidase, subunit 1. | 0.658 |
| AKO95333.1 | AKO96753.1 | MALG_00117 | MALG_01575 | NADH dehydrogenase, FAD-containing subunit. | Heme/copper-type cytochrome/quinol oxidase, subunit 2. | 0.455 |
| AKO95333.1 | AKO96754.1 | MALG_00117 | MALG_01576 | NADH dehydrogenase, FAD-containing subunit. | Cytochrome c oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family. | 0.442 |
| AKO95333.1 | AKO97328.1 | MALG_00117 | MALG_02161 | NADH dehydrogenase, FAD-containing subunit. | Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | 0.442 |
| AKO95333.1 | AKO98204.1 | MALG_00117 | MALG_03057 | NADH dehydrogenase, FAD-containing subunit. | Cytochrome b subunit of the bc complex; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.567 |
| AKO95748.1 | AKO95333.1 | MALG_00553 | MALG_00117 | 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). | NADH dehydrogenase, FAD-containing subunit. | 0.455 |
| AKO95748.1 | AKO95752.1 | MALG_00553 | MALG_00557 | 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). | Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.999 |
| AKO95748.1 | AKO95893.1 | MALG_00553 | MALG_00698 | 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-type, subunit I; Belongs to the heme-copper respiratory oxidase family. | 0.927 |
| AKO95748.1 | AKO96168.1 | MALG_00553 | MALG_00974 | 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 d oxidase, subunit II (cydB). | 0.677 |
| AKO95748.1 | AKO96169.1 | MALG_00553 | MALG_00975 | 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 bd-type quinol oxidase, subunit 1. | 0.641 |
| AKO95748.1 | AKO96753.1 | MALG_00553 | MALG_01575 | 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). | Heme/copper-type cytochrome/quinol oxidase, subunit 2. | 0.924 |
| AKO95748.1 | AKO96754.1 | MALG_00553 | MALG_01576 | 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 I; Belongs to the heme-copper respiratory oxidase family. | 0.999 |
| AKO95748.1 | AKO97328.1 | MALG_00553 | MALG_02161 | 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 I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | 0.999 |
| AKO95748.1 | AKO98204.1 | MALG_00553 | MALG_03057 | 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 b subunit of the bc complex; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.994 |
| AKO95752.1 | AKO95333.1 | MALG_00557 | MALG_00117 | Heme/copper-type cytochrome/quinol oxidase, subunit 3. | NADH dehydrogenase, FAD-containing subunit. | 0.452 |
| AKO95752.1 | AKO95748.1 | MALG_00557 | MALG_00553 | Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 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 |
| AKO95752.1 | AKO95893.1 | MALG_00557 | MALG_00698 | Heme/copper-type cytochrome/quinol oxidase, subunit 3. | Cytochrome c oxidase, cbb3-type, subunit I; Belongs to the heme-copper respiratory oxidase family. | 0.940 |
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