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 |
AKP45859.1 | AKP46727.1 | BSM4216_0515 | BSM4216_1446 | Cytochrome c551. | Cytochrome c oxidase polypeptide 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). | 0.969 |
AKP45859.1 | AKP46728.1 | BSM4216_0515 | BSM4216_1447 | Cytochrome c551. | Cytochrome c oxidase polypeptide 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. | 0.782 |
AKP45859.1 | AKP46729.1 | BSM4216_0515 | BSM4216_1448 | Cytochrome c551. | Cytochrome c oxidase polypeptide III. | 0.890 |
AKP45859.1 | AKP46964.1 | BSM4216_0515 | BSM4216_1688 | Cytochrome c551. | Putative oxidoreductasewith Rieske iron-sulfur protein 2Fe-2S subunit. | 0.901 |
AKP45859.1 | AKP47433.1 | BSM4216_0515 | BSM4216_2188 | Cytochrome c551. | Cytochrome O ubiquinol oxidase subunit III. | 0.872 |
AKP45859.1 | AKP47434.1 | BSM4216_0515 | BSM4216_2189 | Cytochrome c551. | Quinol oxidase subunit I. | 0.782 |
AKP45859.1 | AKP47566.1 | BSM4216_0515 | BSM4216_2326 | Cytochrome c551. | Menaquinone-cytochrome C oxidoreductasecytochrome C subunit; Component of the menaquinol-cytochrome c reductase complex. | 0.887 |
AKP45859.1 | AKP47567.1 | BSM4216_0515 | BSM4216_2327 | Cytochrome c551. | Menaquinone-cytochrome c reductasecytochrome B subunit. | 0.920 |
AKP45859.1 | AKP47568.1 | BSM4216_0515 | BSM4216_2328 | Cytochrome c551. | Menaquinone-cytochrome C reductase iron-sulfur subunit. | 0.966 |
AKP46727.1 | AKP45859.1 | BSM4216_1446 | BSM4216_0515 | Cytochrome c oxidase polypeptide 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). | Cytochrome c551. | 0.969 |
AKP46727.1 | AKP46728.1 | BSM4216_1446 | BSM4216_1447 | Cytochrome c oxidase polypeptide 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). | Cytochrome c oxidase polypeptide 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 |
AKP46727.1 | AKP46729.1 | BSM4216_1446 | BSM4216_1448 | Cytochrome c oxidase polypeptide 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). | Cytochrome c oxidase polypeptide III. | 0.999 |
AKP46727.1 | AKP46964.1 | BSM4216_1446 | BSM4216_1688 | Cytochrome c oxidase polypeptide 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). | Putative oxidoreductasewith Rieske iron-sulfur protein 2Fe-2S subunit. | 0.998 |
AKP46727.1 | AKP47433.1 | BSM4216_1446 | BSM4216_2188 | Cytochrome c oxidase polypeptide 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). | Cytochrome O ubiquinol oxidase subunit III. | 0.999 |
AKP46727.1 | AKP47434.1 | BSM4216_1446 | BSM4216_2189 | Cytochrome c oxidase polypeptide 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). | Quinol oxidase subunit I. | 0.999 |
AKP46727.1 | AKP47566.1 | BSM4216_1446 | BSM4216_2326 | Cytochrome c oxidase polypeptide 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). | Menaquinone-cytochrome C oxidoreductasecytochrome C subunit; Component of the menaquinol-cytochrome c reductase complex. | 0.999 |
AKP46727.1 | AKP47567.1 | BSM4216_1446 | BSM4216_2327 | Cytochrome c oxidase polypeptide 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). | Menaquinone-cytochrome c reductasecytochrome B subunit. | 0.999 |
AKP46727.1 | AKP47568.1 | BSM4216_1446 | BSM4216_2328 | Cytochrome c oxidase polypeptide 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). | Menaquinone-cytochrome C reductase iron-sulfur subunit. | 0.998 |
AKP46727.1 | AKP47834.1 | BSM4216_1446 | BSM4216_2599 | Cytochrome c oxidase polypeptide 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). | Membrane-attached cytochrome c550. | 0.979 |
AKP46728.1 | AKP45859.1 | BSM4216_1447 | BSM4216_0515 | Cytochrome c oxidase polypeptide 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 c551. | 0.782 |
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