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 |
| dnaK | groEL | BSU25470 | BSU06030 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.999 |
| dnaK | grpE | BSU25470 | BSU25480 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Nucleotide exchange factor for DnaK activity; 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. S [...] | 0.999 |
| dnaK | htpG | BSU25470 | BSU39820 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.999 |
| dnaK | pksJ | BSU25470 | BSU17180 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.486 |
| dnaK | pksN | BSU25470 | BSU17210 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.479 |
| dnaK | ppiB | BSU25470 | BSU23360 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Peptidyl-prolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.785 |
| dnaK | rtpA | BSU25470 | BSU02530 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | anti-TRAP regulator; By forming a complex with tryptophan-activated TRAP, and masking its RNA binding site, it inhibits TRAP's RNA binding ability, thereby abolishing TRAP regulation of gene expression, leading to antitermination and increased trp operon expression. AT acts by competing with messenger RNA for the RNA binding domain of TRAP. | 0.976 |
| groEL | dnaK | BSU06030 | BSU25470 | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| groEL | grpE | BSU06030 | BSU25480 | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Nucleotide exchange factor for DnaK activity; 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. S [...] | 0.999 |
| groEL | htpG | BSU06030 | BSU39820 | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.991 |
| groEL | pksJ | BSU06030 | BSU17180 | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.476 |
| groEL | pksN | BSU06030 | BSU17210 | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.516 |
| groEL | ppiB | BSU06030 | BSU23360 | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Peptidyl-prolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.563 |
| groEL | rtpA | BSU06030 | BSU02530 | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | anti-TRAP regulator; By forming a complex with tryptophan-activated TRAP, and masking its RNA binding site, it inhibits TRAP's RNA binding ability, thereby abolishing TRAP regulation of gene expression, leading to antitermination and increased trp operon expression. AT acts by competing with messenger RNA for the RNA binding domain of TRAP. | 0.807 |
| grpE | dnaK | BSU25480 | BSU25470 | Nucleotide exchange factor for DnaK activity; 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. S [...] | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| grpE | groEL | BSU25480 | BSU06030 | Nucleotide exchange factor for DnaK activity; 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. S [...] | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.999 |
| grpE | htpG | BSU25480 | BSU39820 | Nucleotide exchange factor for DnaK activity; 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. S [...] | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.971 |
| grpE | rtpA | BSU25480 | BSU02530 | Nucleotide exchange factor for DnaK activity; 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. S [...] | anti-TRAP regulator; By forming a complex with tryptophan-activated TRAP, and masking its RNA binding site, it inhibits TRAP's RNA binding ability, thereby abolishing TRAP regulation of gene expression, leading to antitermination and increased trp operon expression. AT acts by competing with messenger RNA for the RNA binding domain of TRAP. | 0.868 |
| htpG | dnaK | BSU39820 | BSU25470 | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| htpG | groEL | BSU39820 | BSU06030 | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.991 |
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