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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CoxB | OME87041.1 | BK123_29995 | BK123_32135 | 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). | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.997 |
| CoxB | OME91514.1 | BK123_29995 | BK123_18845 | 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). | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.996 |
| CoxB | OME92127.1 | BK123_29995 | BK123_15990 | 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). | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.978 |
| CoxB | OME93593.1 | BK123_29995 | BK123_10065 | 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.854 |
| CoxB | OME94870.1 | BK123_29995 | BK123_07170 | 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: Protein Homology. | 0.987 |
| CoxB | OME95348.1 | BK123_29995 | BK123_06405 | 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: Protein Homology. | 0.719 |
| CoxB | OME96393.1 | BK123_29995 | BK123_02045 | 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 C551; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.978 |
| CoxB | OME96636.1 | BK123_29995 | BK123_03340 | 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 b6; Electron transport protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.995 |
| CoxB | OME96637.1 | BK123_29995 | BK123_03345 | 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). | Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.997 |
| OME87041.1 | CoxB | BK123_32135 | BK123_29995 | 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). | 0.997 |
| OME87041.1 | OME91514.1 | BK123_32135 | BK123_18845 | Derived by automated computational analysis using gene prediction method: Protein Homology. | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.998 |
| OME87041.1 | OME92127.1 | BK123_32135 | BK123_15990 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.783 |
| OME87041.1 | OME93593.1 | BK123_32135 | BK123_10065 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome-c oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.992 |
| OME87041.1 | OME94870.1 | BK123_32135 | BK123_07170 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.730 |
| OME87041.1 | OME95348.1 | BK123_32135 | BK123_06405 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.956 |
| OME87041.1 | OME96393.1 | BK123_32135 | BK123_02045 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C551; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.780 |
| OME87041.1 | OME96636.1 | BK123_32135 | BK123_03340 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome b6; Electron transport protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.843 |
| OME87041.1 | OME96637.1 | BK123_32135 | BK123_03345 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.951 |
| OME91514.1 | CoxB | BK123_18845 | BK123_29995 | (2Fe-2S)-binding protein; 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). | 0.996 |
| OME91514.1 | OME87041.1 | BK123_18845 | BK123_32135 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.998 |
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