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 | KIR60669.1 | TK50_23400 | TK50_22535 | 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). | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.793 |
| CoxB | KIR60810.1 | TK50_23400 | TK50_23440 | 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. | 0.998 |
| CoxB | KIR60811.1 | TK50_23400 | TK50_23445 | 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. | 0.999 |
| CoxB | KIR63147.1 | TK50_23400 | TK50_19890 | 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). | Peptidase M16; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.784 |
| CoxB | KIR63148.1 | TK50_23400 | TK50_19895 | 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). | Peptidase M16; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.784 |
| CoxB | KIR63332.1 | TK50_23400 | TK50_21070 | 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). | Peptidase M16; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.784 |
| CoxB | KIR64696.1 | TK50_23400 | TK50_03455 | 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). | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.908 |
| CoxB | KIR64698.1 | TK50_23400 | TK50_03465 | 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). | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. | 0.902 |
| CoxB | NuoF | TK50_23400 | TK50_03460 | 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). | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | 0.793 |
| KIR60669.1 | CoxB | TK50_22535 | TK50_23400 | NADH dehydrogenase; 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). | 0.793 |
| KIR60669.1 | KIR60810.1 | TK50_22535 | TK50_23440 | NADH dehydrogenase; 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. | 0.980 |
| KIR60669.1 | KIR60811.1 | TK50_22535 | TK50_23445 | NADH dehydrogenase; 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. | 0.965 |
| KIR60669.1 | KIR63147.1 | TK50_22535 | TK50_19890 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase M16; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.803 |
| KIR60669.1 | KIR63148.1 | TK50_22535 | TK50_19895 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase M16; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.803 |
| KIR60669.1 | KIR63332.1 | TK50_22535 | TK50_21070 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase M16; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.803 |
| KIR60669.1 | KIR64696.1 | TK50_22535 | TK50_03455 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KIR60669.1 | KIR64698.1 | TK50_22535 | TK50_03465 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. | 0.997 |
| KIR60810.1 | CoxB | TK50_23440 | TK50_23400 | (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). | 0.998 |
| KIR60810.1 | KIR60669.1 | TK50_23440 | TK50_22535 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.980 |
| KIR60810.1 | KIR60811.1 | TK50_23440 | TK50_23445 | (2Fe-2S)-binding protein; 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. | 0.999 |
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