Export your current network:
... as a bitmap image:
file format is 'PNG': portable network graphic
... as a high-resolution bitmap:
same PNG format, but resolution at 400 dpi
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as simple tabular text output:
TSV: tab separated values - can be opened in Excel
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... 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 annotated functions of the network proteins
Browse interactions in tabular form:
| node1 | node2 | node1 annotation | node2 annotation | score |
| PP1S2633_1V6.1 | PP1S3133_1V6.1 | Cytochrome c 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 | Predicted protein | 0.574 |
| PP1S2633_1V6.1 | PP1S31_108V6.2 | Cytochrome c 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 | Predicted protein | 0.708 |
| PP1S2633_1V6.1 | PP1S35_384V6.1 | Cytochrome c 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 | Predicted protein | 0.953 |
| PP1S2633_1V6.1 | PP1S3_324V6.1 | Cytochrome c 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 | Predicted protein | 0.708 |
| PP1S2633_1V6.1 | PP1S46_63V6.1 | Cytochrome c 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 | Predicted protein | 0.953 |
| PP1S2633_1V6.1 | PP1S5_30V6.1 | Cytochrome c 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 | Predicted protein | 0.708 |
| PP1S2633_1V6.1 | PP1S66_138V6.1 | Cytochrome c 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 | Predicted protein | 0.708 |
| PP1S2633_1V6.1 | PP1S77_205V6.1 | Cytochrome c 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 | Annotation not available | 0.708 |
| PP1S2633_1V6.1 | PP1S7_210V6.1 | Cytochrome c 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 | Predicted protein | 0.835 |
| PP1S2633_1V6.1 | PP1S98_5V6.1 | Cytochrome c 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 | Predicted protein | 0.708 |
| PP1S3133_1V6.1 | PP1S2633_1V6.1 | Predicted protein | Cytochrome c 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 | 0.574 |
| PP1S3133_1V6.1 | PP1S31_108V6.2 | Predicted protein | Predicted protein | 0.455 |
| PP1S3133_1V6.1 | PP1S35_384V6.1 | Predicted protein | Predicted protein | 0.741 |
| PP1S3133_1V6.1 | PP1S3_324V6.1 | Predicted protein | Predicted protein | 0.455 |
| PP1S3133_1V6.1 | PP1S46_63V6.1 | Predicted protein | Predicted protein | 0.741 |
| PP1S3133_1V6.1 | PP1S5_30V6.1 | Predicted protein | Predicted protein | 0.455 |
| PP1S3133_1V6.1 | PP1S66_138V6.1 | Predicted protein | Predicted protein | 0.455 |
| PP1S3133_1V6.1 | PP1S77_205V6.1 | Predicted protein | Annotation not available | 0.455 |
| PP1S3133_1V6.1 | PP1S7_210V6.1 | Predicted protein | Predicted protein | 0.622 |
| PP1S3133_1V6.1 | PP1S98_5V6.1 | Predicted protein | Predicted protein | 0.455 |
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