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 |
| ETA79385.1 | ETA82253.1 | T472_0217035 | T472_0202050 | Thioredoxin; Belongs to the thioredoxin family. | FAD-dependent pyridine nucleotide-disulfide oxidoreductase. | 0.869 |
| ETA79385.1 | dnaJ | T472_0217035 | T472_0213095 | Thioredoxin; Belongs to the thioredoxin family. | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | 0.559 |
| ETA79385.1 | dnaK | T472_0217035 | T472_0213090 | Thioredoxin; Belongs to the thioredoxin family. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.495 |
| ETA79385.1 | groEL-2 | T472_0217035 | T472_0219360 | Thioredoxin; Belongs to the thioredoxin family. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.792 |
| ETA79385.1 | groES | T472_0217035 | T472_0219365 | Thioredoxin; Belongs to the thioredoxin family. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.418 |
| ETA79385.1 | grpE | T472_0217035 | T472_0213085 | Thioredoxin; Belongs to the thioredoxin family. | Heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP- [...] | 0.584 |
| ETA79385.1 | htpG | T472_0217035 | T472_0206130 | Thioredoxin; Belongs to the thioredoxin family. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.524 |
| ETA82039.1 | groEL-2 | T472_0203500 | T472_0219360 | Protein kinase. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.767 |
| ETA82253.1 | ETA79385.1 | T472_0202050 | T472_0217035 | FAD-dependent pyridine nucleotide-disulfide oxidoreductase. | Thioredoxin; Belongs to the thioredoxin family. | 0.869 |
| ETA82253.1 | dnaJ | T472_0202050 | T472_0213095 | FAD-dependent pyridine nucleotide-disulfide oxidoreductase. | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | 0.656 |
| ETA82253.1 | dnaK | T472_0202050 | T472_0213090 | FAD-dependent pyridine nucleotide-disulfide oxidoreductase. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.523 |
| ETA82253.1 | groEL-2 | T472_0202050 | T472_0219360 | FAD-dependent pyridine nucleotide-disulfide oxidoreductase. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.800 |
| ETA82253.1 | groES | T472_0202050 | T472_0219365 | FAD-dependent pyridine nucleotide-disulfide oxidoreductase. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.549 |
| ETA82253.1 | grpE | T472_0202050 | T472_0213085 | FAD-dependent pyridine nucleotide-disulfide oxidoreductase. | Heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP- [...] | 0.637 |
| ETA82253.1 | guaB | T472_0202050 | T472_0219335 | FAD-dependent pyridine nucleotide-disulfide oxidoreductase. | Inosine 5'-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family. | 0.601 |
| ETA82253.1 | htpG | T472_0202050 | T472_0206130 | FAD-dependent pyridine nucleotide-disulfide oxidoreductase. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.630 |
| dnaJ | ETA79385.1 | T472_0213095 | T472_0217035 | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | Thioredoxin; Belongs to the thioredoxin family. | 0.559 |
| dnaJ | ETA82253.1 | T472_0213095 | T472_0202050 | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | FAD-dependent pyridine nucleotide-disulfide oxidoreductase. | 0.656 |
| dnaJ | dnaK | T472_0213095 | T472_0213090 | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | groEL-2 | T472_0213095 | T472_0219360 | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.893 |
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