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 |
| btuE | gor | b1710 | b3500 | Glutathione peroxidase; Non-specific peroxidase that can use thioredoxin or glutathione as a reducing agent. In vitro, utilizes preferentially thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert- butyl-, and linoleic acid hydroperoxides, suggesting that it may have one or more organic hydroperoxide as its physiological substrate. Belongs to the glutathione peroxidase family. BtuE subfamily. | Glutathione oxidoreductase; Maintains high levels of reduced glutathione in the cytosol; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. | 0.986 |
| btuE | gstA | b1710 | b1635 | Glutathione peroxidase; Non-specific peroxidase that can use thioredoxin or glutathione as a reducing agent. In vitro, utilizes preferentially thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert- butyl-, and linoleic acid hydroperoxides, suggesting that it may have one or more organic hydroperoxide as its physiological substrate. Belongs to the glutathione peroxidase family. BtuE subfamily. | Glutathionine S-transferase; Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity. Belongs to the GST superfamily. Beta family. | 0.944 |
| gor | btuE | b3500 | b1710 | Glutathione oxidoreductase; Maintains high levels of reduced glutathione in the cytosol; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. | Glutathione peroxidase; Non-specific peroxidase that can use thioredoxin or glutathione as a reducing agent. In vitro, utilizes preferentially thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert- butyl-, and linoleic acid hydroperoxides, suggesting that it may have one or more organic hydroperoxide as its physiological substrate. Belongs to the glutathione peroxidase family. BtuE subfamily. | 0.986 |
| gor | gstA | b3500 | b1635 | Glutathione oxidoreductase; Maintains high levels of reduced glutathione in the cytosol; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. | Glutathionine S-transferase; Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity. Belongs to the GST superfamily. Beta family. | 0.955 |
| gstA | btuE | b1635 | b1710 | Glutathionine S-transferase; Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity. Belongs to the GST superfamily. Beta family. | Glutathione peroxidase; Non-specific peroxidase that can use thioredoxin or glutathione as a reducing agent. In vitro, utilizes preferentially thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert- butyl-, and linoleic acid hydroperoxides, suggesting that it may have one or more organic hydroperoxide as its physiological substrate. Belongs to the glutathione peroxidase family. BtuE subfamily. | 0.944 |
| gstA | gor | b1635 | b3500 | Glutathionine S-transferase; Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity. Belongs to the GST superfamily. Beta family. | Glutathione oxidoreductase; Maintains high levels of reduced glutathione in the cytosol; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. | 0.955 |