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 |
| KJB90401.1 | KJB96736.1 | N826_36875 | N826_33280 | Cytochrome C biogenesis protein CcsA; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Selenium-binding protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.715 |
| KJB90401.1 | KJB96737.1 | N826_36875 | N826_33285 | Cytochrome C biogenesis protein CcsA; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.914 |
| KJB92735.1 | KJB93865.1 | N826_21310 | N826_13290 | 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). | Redox-active disulfide protein 2; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.754 |
| KJB92735.1 | KJB94436.1 | N826_21310 | N826_11730 | 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). | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.985 |
| KJB92735.1 | KJB95595.1 | N826_21310 | N826_04105 | 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). | Thiol oxidoreductase DsbE; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.775 |
| KJB92735.1 | KJB96249.1 | N826_21310 | N826_35125 | 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). | Alkyl hydroperoxide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.783 |
| KJB92735.1 | KJB96737.1 | N826_21310 | N826_33285 | 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). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.769 |
| KJB93865.1 | KJB92735.1 | N826_13290 | N826_21310 | Redox-active disulfide protein 2; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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). | 0.754 |
| KJB93865.1 | KJB94436.1 | N826_13290 | N826_11730 | Redox-active disulfide protein 2; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.943 |
| KJB93865.1 | KJB94718.1 | N826_13290 | N826_09380 | Redox-active disulfide protein 2; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C oxidase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.754 |
| KJB93865.1 | KJB95013.1 | N826_13290 | N826_06540 | Redox-active disulfide protein 2; Derived by automated computational analysis using gene prediction method: Protein Homology. | Ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.754 |
| KJB93865.1 | KJB96737.1 | N826_13290 | N826_33285 | Redox-active disulfide protein 2; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.734 |
| KJB94018.1 | KJB96736.1 | N826_19885 | N826_33280 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Selenium-binding protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.715 |
| KJB94018.1 | KJB96737.1 | N826_19885 | N826_33285 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.918 |
| KJB94436.1 | KJB92735.1 | N826_11730 | N826_21310 | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 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). | 0.985 |
| KJB94436.1 | KJB93865.1 | N826_11730 | N826_13290 | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Redox-active disulfide protein 2; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.943 |
| KJB94436.1 | KJB94718.1 | N826_11730 | N826_09380 | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Cytochrome C oxidase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.984 |
| KJB94436.1 | KJB95013.1 | N826_11730 | N826_06540 | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.982 |
| KJB94436.1 | KJB95595.1 | N826_11730 | N826_04105 | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Thiol oxidoreductase DsbE; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.943 |
| KJB94436.1 | KJB96249.1 | N826_11730 | N826_35125 | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Alkyl hydroperoxide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.949 |
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