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 |
| AIQ56007.1 | AIQ56008.1 | PBOR_02790 | PBOR_02795 | Cytochrome B; 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). | Quinol oxidase subunit 1; 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 |
| AIQ56007.1 | AIQ56009.1 | PBOR_02790 | PBOR_02800 | Cytochrome B; 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 oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| AIQ56007.1 | AIQ56010.1 | PBOR_02790 | PBOR_02805 | Cytochrome B; 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 IV; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.998 |
| AIQ56007.1 | AIQ56410.1 | PBOR_02790 | PBOR_05285 | Cytochrome B; 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 aa3 quinol oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.991 |
| AIQ56007.1 | AIQ56411.1 | PBOR_02790 | PBOR_05290 | Cytochrome B; 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 o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| AIQ56007.1 | AIQ56412.1 | PBOR_02790 | PBOR_05295 | Cytochrome B; 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). | Quinol oxidase subunit 1; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | 0.999 |
| AIQ56007.1 | AIQ56413.1 | PBOR_02790 | PBOR_05300 | Cytochrome B; 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). | Quinol oxidase subunit 2; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.979 |
| AIQ56007.1 | AIQ57280.1 | PBOR_02790 | PBOR_10310 | Cytochrome B; 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 II; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.975 |
| AIQ56007.1 | AIQ60725.1 | PBOR_02790 | PBOR_30170 | Cytochrome B; 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 Caa3 oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.843 |
| AIQ56007.1 | ctaB | PBOR_02790 | PBOR_30230 | Cytochrome B; 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; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. | 0.996 |
| AIQ56008.1 | AIQ56007.1 | PBOR_02795 | PBOR_02790 | Quinol oxidase subunit 1; 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. | Cytochrome B; 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 |
| AIQ56008.1 | AIQ56009.1 | PBOR_02795 | PBOR_02800 | Quinol oxidase subunit 1; 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. | Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| AIQ56008.1 | AIQ56010.1 | PBOR_02795 | PBOR_02805 | Quinol oxidase subunit 1; 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. | Cytochrome C oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.998 |
| AIQ56008.1 | AIQ56410.1 | PBOR_02795 | PBOR_05285 | Quinol oxidase subunit 1; 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. | Cytochrome aa3 quinol oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.992 |
| AIQ56008.1 | AIQ56411.1 | PBOR_02795 | PBOR_05290 | Quinol oxidase subunit 1; 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. | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| AIQ56008.1 | AIQ56412.1 | PBOR_02795 | PBOR_05295 | Quinol oxidase subunit 1; 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. | Quinol oxidase subunit 1; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | 0.904 |
| AIQ56008.1 | AIQ56413.1 | PBOR_02795 | PBOR_05300 | Quinol oxidase subunit 1; 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. | Quinol oxidase subunit 2; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.998 |
| AIQ56008.1 | AIQ57280.1 | PBOR_02795 | PBOR_10310 | Quinol oxidase subunit 1; 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. | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.992 |
| AIQ56008.1 | AIQ60725.1 | PBOR_02795 | PBOR_30170 | Quinol oxidase subunit 1; 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. | Cytochrome Caa3 oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.670 |
| AIQ56008.1 | ctaB | PBOR_02795 | PBOR_30230 | Quinol oxidase subunit 1; 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. | 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; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. | 0.995 |
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