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 |
| A7J50_0059 | A7J50_0060 | A7J50_0059 | A7J50_0060 | 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 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 |
| A7J50_0059 | A7J50_0061 | A7J50_0059 | A7J50_0061 | 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). | Pfam:pfam04442 Cytochrome c oxidase assembly protein CtaG/Cox11. | 0.969 |
| A7J50_0059 | A7J50_0062 | A7J50_0059 | A7J50_0062 | 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). | MFS transporter; Pfam:pfam00510 Cytochrome c oxidase subunit III. | 0.999 |
| A7J50_0059 | A7J50_0064 | A7J50_0059 | A7J50_0064 | 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). | Hypothetical protein; Pfam:pfam02104 SURF1 family. | 0.944 |
| A7J50_0059 | A7J50_0065 | A7J50_0059 | A7J50_0065 | 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). | Hypothetical protein. | 0.924 |
| A7J50_0059 | A7J50_0066 | A7J50_0059 | A7J50_0066 | 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). | Pfam:pfam02628 Cytochrome oxidase assembly protein. | 0.910 |
| A7J50_0059 | A7J50_0068 | A7J50_0059 | A7J50_0068 | 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). | Copper-binding protein; Pfam:pfam02630 SCO1/SenC. | 0.842 |
| A7J50_0059 | A7J50_0849 | A7J50_0059 | A7J50_0849 | 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). | Ubiquinol-cytochrome c reductase iron-sulfur subunit; 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. | 0.988 |
| A7J50_0059 | A7J50_0850 | A7J50_0059 | A7J50_0850 | 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 B; 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. | 0.998 |
| A7J50_0059 | A7J50_0851 | A7J50_0059 | A7J50_0851 | 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). | Ubiquinol-cytochrome c reductase; Pfam:pfam02167 Cytochrome C1 family. | 0.971 |
| A7J50_0059 | A7J50_1116 | A7J50_0059 | A7J50_1116 | 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 B6; Pfam:pfam03150 Di-heme cytochrome c peroxidase. | 0.503 |
| A7J50_0059 | A7J50_1527 | A7J50_0059 | A7J50_1527 | 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). | YceI-like family protein; Pfam:pfam04264 YceI-like domain; Belongs to the UPF0312 family. | 0.952 |
| A7J50_0059 | A7J50_1611 | A7J50_0059 | A7J50_1611 | 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). | Hypothetical protein. | 0.588 |
| A7J50_0059 | A7J50_2635 | A7J50_0059 | A7J50_2635 | 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). | (Fe-S)-binding protein; Pfam:pfam11614 IG-like fold at C-terminal of FixG, putative oxidoreductase. | 0.578 |
| A7J50_0059 | A7J50_3378 | A7J50_0059 | A7J50_3378 | 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). | Hypothetical protein. | 0.983 |
| A7J50_0059 | A7J50_3456 | A7J50_0059 | A7J50_3456 | 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). | NADH dehydrogenase subunit E; Pfam:pfam01257 Thioredoxin-like [2Fe-2S] ferredoxin. | 0.781 |
| A7J50_0059 | A7J50_3457 | A7J50_0059 | A7J50_3457 | 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). | NADH dehydrogenase subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | 0.730 |
| A7J50_0059 | A7J50_3458 | A7J50_0059 | A7J50_3458 | 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). | NADH-quinone oxidoreductase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 75 kDa subunit family. | 0.670 |
| A7J50_0059 | A7J50_3464 | A7J50_0059 | A7J50_3464 | 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). | NADH:ubiquinone oxidoreductase subunit M; Pfam:pfam00361 NADH-Ubiquinone/plastoquinone (complex I), various chains. | 0.935 |
| A7J50_0059 | A7J50_4251 | A7J50_0059 | A7J50_4251 | 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). | Pfam:pfam00115 Cytochrome C and Quinol oxidase polypeptide I; Belongs to the heme-copper respiratory oxidase family. | 0.775 |
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