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 |
| AKG03576.1 | AKG04674.1 | AAV35_001435 | AAV35_007590 | Cytochrome B5. | Cytochrome c oxidase subunit IVB. | 0.989 |
| AKG03576.1 | AKG04675.1 | AAV35_001435 | AAV35_007595 | Cytochrome B5. | Cytochrome (ubi)quinol oxidase subunit III. | 0.992 |
| AKG03576.1 | AKG04676.1 | AAV35_001435 | AAV35_007600 | Cytochrome B5. | 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. | 0.991 |
| AKG03576.1 | AKG04677.1 | AAV35_001435 | AAV35_007605 | Cytochrome B5. | 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). | 0.990 |
| AKG03576.1 | AKG04940.1 | AAV35_001435 | AAV35_009095 | Cytochrome B5. | Cytochrome aa3 quinol oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. | 0.884 |
| AKG03576.1 | AKG04941.1 | AAV35_001435 | AAV35_009100 | Cytochrome B5. | Cytochrome aa3 quinol oxidase subunit III. | 0.894 |
| AKG03576.1 | AKG05232.1 | AAV35_001435 | AAV35_010850 | Cytochrome B5. | Cytochrome aa3 quinol oxidase subunit III. | 0.906 |
| AKG03576.1 | AKG05654.1 | AAV35_001435 | AAV35_001440 | Cytochrome B5. | Cytochrome C; Belongs to the heme-copper respiratory oxidase family. | 0.999 |
| AKG03576.1 | AKG05792.1 | AAV35_001435 | AAV35_010845 | Cytochrome B5. | Cytochrome ubiquinol oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. | 0.990 |
| AKG03576.1 | APC65599.1 | AAV35_001435 | AAV35_010840 | Cytochrome B5. | 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). | 0.953 |
| AKG03576.1 | atpB | AAV35_001435 | AAV35_002270 | Cytochrome B5. | F0F1 ATP synthase subunit A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family. | 0.758 |
| AKG03952.1 | AKG04890.1 | AAV35_003545 | AAV35_008790 | PTS fructose transporter subunit IIA. | PTS mannose transporter subunit IIABC; Phosphoenolpyruvate-dependent sugar phosphotransferase system; catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane; IIB is phosphorylated by IIA and then transfers the phosphoryl group to the sugar; IIC forms the translocation channel. | 0.991 |
| AKG03952.1 | atpA | AAV35_003545 | AAV35_002290 | PTS fructose transporter subunit IIA. | F0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | 0.416 |
| AKG03952.1 | atpB | AAV35_003545 | AAV35_002270 | PTS fructose transporter subunit IIA. | F0F1 ATP synthase subunit A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family. | 0.420 |
| AKG03952.1 | atpC | AAV35_003545 | AAV35_002305 | PTS fructose transporter subunit IIA. | F0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. | 0.418 |
| AKG03952.1 | atpD | AAV35_003545 | AAV35_002300 | PTS fructose transporter subunit IIA. | F0F1 ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | 0.417 |
| AKG03952.1 | atpE | AAV35_003545 | AAV35_002275 | PTS fructose transporter subunit IIA. | F0F1 ATP synthase subunit C; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.432 |
| AKG04251.1 | AKG04256.1 | AAV35_005260 | AAV35_005285 | Na+/H+ antiporter subunit G. | Na+/H+ antiporter subunit A. | 0.999 |
| AKG04256.1 | AKG04251.1 | AAV35_005285 | AAV35_005260 | Na+/H+ antiporter subunit A. | Na+/H+ antiporter subunit G. | 0.999 |
| AKG04256.1 | atpA | AAV35_005285 | AAV35_002290 | Na+/H+ antiporter subunit A. | F0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | 0.465 |
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