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 |
| AGX02034.1 | AGX03712.1 | N288_19980 | N288_08955 | Thioredoxin; Phage-associated protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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). | 0.914 |
| AGX02034.1 | AGX05148.1 | N288_19980 | N288_16295 | Thioredoxin; Phage-associated protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Photosynthetic protein synthase I; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.725 |
| AGX02034.1 | AGX05226.1 | N288_19980 | N288_16695 | Thioredoxin; Phage-associated protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B5; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.491 |
| AGX02034.1 | AGX05921.1 | N288_19980 | N288_20240 | Thioredoxin; Phage-associated protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Quinol oxidase subunit 2; 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. | 0.491 |
| AGX02334.1 | AGX03712.1 | N288_01835 | N288_08955 | Thioredoxin; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 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). | 0.914 |
| AGX02334.1 | AGX05148.1 | N288_01835 | N288_16295 | Thioredoxin; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Photosynthetic protein synthase I; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.725 |
| AGX02334.1 | AGX05226.1 | N288_01835 | N288_16695 | Thioredoxin; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Cytochrome B5; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.491 |
| AGX02334.1 | AGX05921.1 | N288_01835 | N288_20240 | Thioredoxin; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Quinol oxidase subunit 2; 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. | 0.491 |
| AGX03683.1 | AGX03712.1 | N288_08805 | N288_08955 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 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). | 0.914 |
| AGX03683.1 | AGX05148.1 | N288_08805 | N288_16295 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Photosynthetic protein synthase I; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.698 |
| AGX03683.1 | AGX05226.1 | N288_08805 | N288_16695 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Cytochrome B5; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.453 |
| AGX03683.1 | AGX05921.1 | N288_08805 | N288_20240 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Quinol oxidase subunit 2; 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. | 0.453 |
| AGX03712.1 | AGX02034.1 | N288_08955 | N288_19980 | 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). | Thioredoxin; Phage-associated protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.914 |
| AGX03712.1 | AGX02334.1 | N288_08955 | N288_01835 | 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). | Thioredoxin; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.914 |
| AGX03712.1 | AGX03683.1 | N288_08955 | N288_08805 | 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). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.914 |
| AGX03712.1 | AGX03716.1 | N288_08955 | N288_08975 | 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 assembly protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.960 |
| AGX03712.1 | AGX03717.1 | N288_08955 | N288_08980 | 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). | Membrane protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.639 |
| AGX03712.1 | AGX05148.1 | N288_08955 | N288_16295 | 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). | Photosynthetic protein synthase I; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.911 |
| AGX03712.1 | AGX05226.1 | N288_08955 | N288_16695 | 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 B5; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.993 |
| AGX03712.1 | AGX05279.1 | N288_08955 | N288_16960 | 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 CBB3; Component of the menaquinol-cytochrome c reductase complex. | 0.999 |
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