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 |
| atpB | coxB | sync_2318 | sync_2127 | ATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | 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). | 0.766 |
| atpB | ndhA | sync_2318 | sync_2625 | ATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | NADH dehydrogenase I chain 1 (or H); NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. | 0.938 |
| atpB | petB | sync_2318 | sync_0549 | ATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Cytochrome b6; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. | 0.927 |
| atpB | petC | sync_2318 | sync_2149 | ATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Cytochrome b6-f complex, iron-sulfur subunit; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. Belongs to the Rieske iron-sulfur protein family. | 0.499 |
| atpB | sync_1927 | sync_2318 | sync_1927 | ATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Possible 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). | 0.766 |
| atpB | sync_1928 | sync_2318 | sync_1928 | ATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Cytochrome c oxidase subunit I; Identified by match to protein family HMM PF00115; Belongs to the heme-copper respiratory oxidase family. | 0.761 |
| atpB | sync_1929 | sync_2318 | sync_1929 | ATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Cytochrome c oxidase subunit III. | 0.932 |
| atpB | sync_2125 | sync_2318 | sync_2125 | ATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Cytochrome c oxidase, subunit III. | 0.932 |
| atpB | sync_2126 | sync_2318 | sync_2126 | ATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | 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. | 0.761 |
| coxB | atpB | sync_2127 | sync_2318 | 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). | ATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | 0.766 |
| coxB | cyoE | sync_2127 | sync_2129 | 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). | 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. | 0.996 |
| coxB | ndhA | sync_2127 | sync_2625 | 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 I chain 1 (or H); NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. | 0.903 |
| coxB | petB | sync_2127 | sync_0549 | 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 b6; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. | 0.973 |
| coxB | petC | sync_2127 | sync_2149 | 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 b6-f complex, iron-sulfur subunit; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. Belongs to the Rieske iron-sulfur protein family. | 0.908 |
| coxB | sync_1927 | sync_2127 | sync_1927 | 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). | Possible 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). | 0.918 |
| coxB | sync_1928 | sync_2127 | sync_1928 | 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; Identified by match to protein family HMM PF00115; Belongs to the heme-copper respiratory oxidase family. | 0.998 |
| coxB | sync_1929 | sync_2127 | sync_1929 | 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 III. | 0.998 |
| coxB | sync_2125 | sync_2127 | sync_2125 | 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 III. | 0.999 |
| coxB | sync_2126 | sync_2127 | sync_2126 | 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 |
| cyoE | coxB | sync_2129 | sync_2127 | 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. | 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). | 0.996 |
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