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 |
| AMA52180.1 | AMA52181.1 | AN935_07780 | AN935_07785 | 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 ubiquinol 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 |
| AMA52180.1 | AMA54323.1 | AN935_07780 | AN935_19305 | 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 ubiquinol oxidase subunit II; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. | 0.996 |
| AMA52180.1 | qoxB | AN935_07780 | AN935_19300 | 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 ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | 0.999 |
| AMA52181.1 | AMA52180.1 | AN935_07785 | AN935_07780 | Cytochrome ubiquinol 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. | 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 |
| AMA52181.1 | AMA54323.1 | AN935_07785 | AN935_19305 | Cytochrome ubiquinol 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. | Cytochrome ubiquinol oxidase subunit II; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. | 0.999 |
| AMA52181.1 | qoxB | AN935_07785 | AN935_19300 | Cytochrome ubiquinol 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. | Cytochrome ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | 0.971 |
| AMA54323.1 | AMA52180.1 | AN935_19305 | AN935_07780 | Cytochrome ubiquinol oxidase subunit II; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. | 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). | 0.996 |
| AMA54323.1 | AMA52181.1 | AN935_19305 | AN935_07785 | Cytochrome ubiquinol oxidase subunit II; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. | Cytochrome ubiquinol 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 |
| AMA54323.1 | qoxB | AN935_19305 | AN935_19300 | Cytochrome ubiquinol oxidase subunit II; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. | Cytochrome ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | 0.999 |
| qoxB | AMA52180.1 | AN935_19300 | AN935_07780 | Cytochrome ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | 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 |
| qoxB | AMA52181.1 | AN935_19300 | AN935_07785 | Cytochrome ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | Cytochrome ubiquinol 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. | 0.971 |
| qoxB | AMA54323.1 | AN935_19300 | AN935_19305 | Cytochrome ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | Cytochrome ubiquinol oxidase subunit II; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. | 0.999 |