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 |
| SHE90945.1 | SHE91043.1 | SAMN04487965_0925 | SAMN04487965_0927 | Bacterioferritin-associated ferredoxin. | 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; Belongs to the bacterioferritin family. | 0.972 |
| SHE91043.1 | SHE90945.1 | SAMN04487965_0927 | SAMN04487965_0925 | 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; Belongs to the bacterioferritin family. | Bacterioferritin-associated ferredoxin. | 0.972 |
| SHE91043.1 | SHF03413.1 | SAMN04487965_0927 | SAMN04487965_1213 | 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; Belongs to the bacterioferritin family. | rubredoxin-NAD+ reductase; Belongs to the FAD-dependent oxidoreductase family. | 0.459 |
| SHE91043.1 | SHF11128.1 | SAMN04487965_0927 | SAMN04487965_1394 | 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; Belongs to the bacterioferritin family. | Assimilatory nitrate reductase catalytic subunit; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. | 0.877 |
| SHE91043.1 | SHF18228.1 | SAMN04487965_0927 | SAMN04487965_1566 | 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; Belongs to the bacterioferritin family. | Copper-resistance protein, CopA family. | 0.513 |
| SHE91043.1 | SHF56034.1 | SAMN04487965_0927 | SAMN04487965_2248 | 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; Belongs to the bacterioferritin family. | Anti-anti-sigma factor. | 0.724 |
| SHE91043.1 | SHG10988.1 | SAMN04487965_0927 | SAMN04487965_3302 | 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; Belongs to the bacterioferritin family. | Starvation-inducible DNA-binding protein; Belongs to the Dps family. | 0.432 |
| SHE91043.1 | SHG14856.1 | SAMN04487965_0927 | SAMN04487965_3415 | 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; Belongs to the bacterioferritin family. | Anti-anti-sigma factor. | 0.724 |
| SHE91043.1 | cyaY | SAMN04487965_0927 | SAMN04487965_2764 | 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; Belongs to the bacterioferritin family. | CyaY protein; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. | 0.530 |
| SHE91043.1 | hemH | SAMN04487965_0927 | SAMN04487965_0716 | 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; Belongs to the bacterioferritin family. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.956 |
| SHE91043.1 | nuoC | SAMN04487965_0927 | SAMN04487965_2113 | 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; Belongs to the bacterioferritin family. | NADH dehydrogenase subunit C; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family. | 0.473 |
| SHF03413.1 | SHE91043.1 | SAMN04487965_1213 | SAMN04487965_0927 | rubredoxin-NAD+ reductase; Belongs to the FAD-dependent oxidoreductase family. | 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; Belongs to the bacterioferritin family. | 0.459 |
| SHF03413.1 | SHF11128.1 | SAMN04487965_1213 | SAMN04487965_1394 | rubredoxin-NAD+ reductase; Belongs to the FAD-dependent oxidoreductase family. | Assimilatory nitrate reductase catalytic subunit; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. | 0.888 |
| SHF03413.1 | SHF18228.1 | SAMN04487965_1213 | SAMN04487965_1566 | rubredoxin-NAD+ reductase; Belongs to the FAD-dependent oxidoreductase family. | Copper-resistance protein, CopA family. | 0.467 |
| SHF11128.1 | SHE91043.1 | SAMN04487965_1394 | SAMN04487965_0927 | Assimilatory nitrate reductase catalytic subunit; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. | 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; Belongs to the bacterioferritin family. | 0.877 |
| SHF11128.1 | SHF03413.1 | SAMN04487965_1394 | SAMN04487965_1213 | Assimilatory nitrate reductase catalytic subunit; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. | rubredoxin-NAD+ reductase; Belongs to the FAD-dependent oxidoreductase family. | 0.888 |
| SHF11128.1 | SHF18228.1 | SAMN04487965_1394 | SAMN04487965_1566 | Assimilatory nitrate reductase catalytic subunit; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. | Copper-resistance protein, CopA family. | 0.765 |
| SHF11128.1 | nuoC | SAMN04487965_1394 | SAMN04487965_2113 | Assimilatory nitrate reductase catalytic subunit; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. | NADH dehydrogenase subunit C; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family. | 0.439 |
| SHF18228.1 | SHE91043.1 | SAMN04487965_1566 | SAMN04487965_0927 | Copper-resistance protein, CopA family. | 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; Belongs to the bacterioferritin family. | 0.513 |
| SHF18228.1 | SHF03413.1 | SAMN04487965_1566 | SAMN04487965_1213 | Copper-resistance protein, CopA family. | rubredoxin-NAD+ reductase; Belongs to the FAD-dependent oxidoreductase family. | 0.467 |
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