Export your current network:
... as a bitmap image:
file format is 'PNG': portable network graphic
... as a high-resolution bitmap:
same PNG format, but at higher resolution
... 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 |
AEA66220.1 | PSEBR_a87 | PSEBR_c2g7 | PSEBR_a87 | Conserved hypothetical protein. | Putative copper-binding protein. | 0.623 |
AEA66220.1 | PSEBR_a89 | PSEBR_c2g7 | PSEBR_a89 | Conserved hypothetical protein. | Conserved hypothetical protein. | 0.727 |
AEA66220.1 | PSEBR_a90 | PSEBR_c2g7 | PSEBR_a90 | Conserved hypothetical protein. | Conserved hypothetical protein. | 0.777 |
AEA66220.1 | PSEBR_a91 | PSEBR_c2g7 | PSEBR_a91 | Conserved hypothetical protein. | Conserved hypothetical protein. | 0.716 |
AEA66220.1 | cyoE-2 | PSEBR_c2g7 | PSEBR_a88 | Conserved hypothetical protein. | Putative 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. | 0.675 |
AEA68168.1 | PSEBR_a89 | PSEBR_a1945 | PSEBR_a89 | Conserved hypothetical protein. | Conserved hypothetical protein. | 0.639 |
AEA68168.1 | PSEBR_a90 | PSEBR_a1945 | PSEBR_a90 | Conserved hypothetical protein. | Conserved hypothetical protein. | 0.736 |
AEA68168.1 | PSEBR_a91 | PSEBR_a1945 | PSEBR_a91 | Conserved hypothetical protein. | Conserved hypothetical protein. | 0.677 |
AEA68168.1 | PSEBR_a92 | PSEBR_a1945 | PSEBR_a92 | Conserved hypothetical protein. | Putative cytochrome-c oxidase, subunit III. | 0.515 |
AEA68168.1 | PSEBR_a93 | PSEBR_a1945 | PSEBR_a93 | Conserved hypothetical protein. | Putative cytochrome-c oxidase assembly protein. | 0.457 |
AEA68168.1 | PSEBR_a95 | PSEBR_a1945 | PSEBR_a95 | Conserved hypothetical protein. | Putative 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). | 0.583 |
PSEBR_a87 | AEA66220.1 | PSEBR_a87 | PSEBR_c2g7 | Putative copper-binding protein. | Conserved hypothetical protein. | 0.623 |
PSEBR_a87 | PSEBR_a89 | PSEBR_a87 | PSEBR_a89 | Putative copper-binding protein. | Conserved hypothetical protein. | 0.932 |
PSEBR_a87 | PSEBR_a90 | PSEBR_a87 | PSEBR_a90 | Putative copper-binding protein. | Conserved hypothetical protein. | 0.849 |
PSEBR_a87 | PSEBR_a91 | PSEBR_a87 | PSEBR_a91 | Putative copper-binding protein. | Conserved hypothetical protein. | 0.924 |
PSEBR_a87 | PSEBR_a92 | PSEBR_a87 | PSEBR_a92 | Putative copper-binding protein. | Putative cytochrome-c oxidase, subunit III. | 0.513 |
PSEBR_a87 | PSEBR_a93 | PSEBR_a87 | PSEBR_a93 | Putative copper-binding protein. | Putative cytochrome-c oxidase assembly protein. | 0.770 |
PSEBR_a87 | PSEBR_a94 | PSEBR_a87 | PSEBR_a94 | Putative copper-binding protein. | Putative 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. | 0.523 |
PSEBR_a87 | PSEBR_a95 | PSEBR_a87 | PSEBR_a95 | Putative copper-binding protein. | Putative 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). | 0.859 |
PSEBR_a87 | cyoE-2 | PSEBR_a87 | PSEBR_a88 | Putative copper-binding protein. | Putative 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. | 0.904 |
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