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
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DR97_1965 | hemH | DR97_1965 | DR97_1964 | annotation not available | Protoporphyrin/coproporphyrin ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX | 0.920 |
| DR97_2231 | bfr | DR97_2231 | DR97_3676 | annotation not available | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex | 0.876 |
| DR97_2231 | bfrB | DR97_2231 | DR97_4411 | annotation not available | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex | 0.834 |
| DR97_2231 | hemH | DR97_2231 | DR97_1964 | annotation not available | Protoporphyrin/coproporphyrin ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX | 0.927 |
| DR97_2231 | pigA | DR97_2231 | DR97_1447 | annotation not available | Heme oxygenase (biliverdin-ix-beta and delta-forming); Involved in heme degradation. Catalyzes the degradation of heme to biliverdin, with the release of iron. Forms biliverdin delta (70%) and beta (30%) | 0.901 |
| DR97_3614 | DR97_4998 | DR97_3614 | DR97_4998 | Protoporphyrinogen ix oxidase; Uncharacterized protein | annotation not available | 0.901 |
| DR97_3614 | hemH | DR97_3614 | DR97_1964 | Protoporphyrinogen ix oxidase; Uncharacterized protein | Protoporphyrin/coproporphyrin ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX | 0.950 |
| DR97_4998 | DR97_3614 | DR97_4998 | DR97_3614 | annotation not available | Protoporphyrinogen ix oxidase; Uncharacterized protein | 0.901 |
| DR97_4998 | hemH | DR97_4998 | DR97_1964 | annotation not available | Protoporphyrin/coproporphyrin ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX | 0.935 |
| bfr | DR97_2231 | DR97_3676 | DR97_2231 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex | annotation not available | 0.876 |
| bfr | bfrB | DR97_3676 | DR97_4411 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex | 0.902 |
| bfr | hemH | DR97_3676 | DR97_1964 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex | Protoporphyrin/coproporphyrin ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX | 0.924 |
| bfr | pigA | DR97_3676 | DR97_1447 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex | Heme oxygenase (biliverdin-ix-beta and delta-forming); Involved in heme degradation. Catalyzes the degradation of heme to biliverdin, with the release of iron. Forms biliverdin delta (70%) and beta (30%) | 0.927 |
| bfrB | DR97_2231 | DR97_4411 | DR97_2231 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex | annotation not available | 0.834 |
| bfrB | bfr | DR97_4411 | DR97_3676 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex | 0.902 |
| bfrB | hemH | DR97_4411 | DR97_1964 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex | Protoporphyrin/coproporphyrin ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX | 0.941 |
| bfrB | pigA | DR97_4411 | DR97_1447 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex | Heme oxygenase (biliverdin-ix-beta and delta-forming); Involved in heme degradation. Catalyzes the degradation of heme to biliverdin, with the release of iron. Forms biliverdin delta (70%) and beta (30%) | 0.915 |
| cyoE1 | cyoE2 | DR97_3070 | DR97_473 | 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 | 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 | 0.834 |
| cyoE1 | hemH | DR97_3070 | DR97_1964 | 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 | Protoporphyrin/coproporphyrin ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX | 0.928 |
| cyoE1 | pigA | DR97_3070 | DR97_1447 | 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 | Heme oxygenase (biliverdin-ix-beta and delta-forming); Involved in heme degradation. Catalyzes the degradation of heme to biliverdin, with the release of iron. Forms biliverdin delta (70%) and beta (30%) | 0.900 |
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