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 |
| BH0609 | htpG | gene:10726478 | gene:10726901 | Sulfite reductase (NADPH); Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. | Class III heat-shock protein (chaperonin); Molecular chaperone. Has ATPase activity. | 0.837 |
| BH1545 | acuC | gene:10727443 | gene:10729149 | Peptidyl-prolyl cis-trans isomerase B; 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. | Acetoin dehydrogenase; BH3237. | 0.555 |
| BH1545 | dnaJ | gene:10727443 | gene:10727242 | Peptidyl-prolyl cis-trans isomerase B; 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. | Heat-shock protein (activation of DnaK); 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 interaction [...] | 0.916 |
| BH1545 | dnaK | gene:10727443 | gene:10727240 | Peptidyl-prolyl cis-trans isomerase B; 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. | Class I heat-shock protein (chaperonin); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.767 |
| BH1545 | groES | gene:10727443 | gene:10726430 | Peptidyl-prolyl cis-trans isomerase B; 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. | Class I heat-shock protein (chaperonin); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.480 |
| BH1545 | htpG | gene:10727443 | gene:10726901 | Peptidyl-prolyl cis-trans isomerase B; 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. | Class III heat-shock protein (chaperonin); Molecular chaperone. Has ATPase activity. | 0.962 |
| acuC | BH1545 | gene:10729149 | gene:10727443 | Acetoin dehydrogenase; BH3237. | Peptidyl-prolyl cis-trans isomerase B; 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. | 0.555 |
| acuC | htpG | gene:10729149 | gene:10726901 | Acetoin dehydrogenase; BH3237. | Class III heat-shock protein (chaperonin); Molecular chaperone. Has ATPase activity. | 0.846 |
| clpQ | clpY | gene:10728362 | gene:10728361 | Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | ATP-dependent Clp protease (heat-shock protein); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.999 |
| clpQ | dnaJ | gene:10728362 | gene:10727242 | Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Heat-shock protein (activation of DnaK); 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 interaction [...] | 0.695 |
| clpQ | dnaK | gene:10728362 | gene:10727240 | Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Class I heat-shock protein (chaperonin); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.665 |
| clpQ | groEL | gene:10728362 | gene:10726431 | Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Class I heat-shock protein (chaperonin); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.777 |
| clpQ | groES | gene:10728362 | gene:10726430 | Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Class I heat-shock protein (chaperonin); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.766 |
| clpQ | htpG | gene:10728362 | gene:10726901 | Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Class III heat-shock protein (chaperonin); Molecular chaperone. Has ATPase activity. | 0.845 |
| clpY | clpQ | gene:10728361 | gene:10728362 | ATP-dependent Clp protease (heat-shock protein); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.999 |
| clpY | dnaJ | gene:10728361 | gene:10727242 | ATP-dependent Clp protease (heat-shock protein); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | Heat-shock protein (activation of DnaK); 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 interaction [...] | 0.773 |
| clpY | dnaK | gene:10728361 | gene:10727240 | ATP-dependent Clp protease (heat-shock protein); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | Class I heat-shock protein (chaperonin); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.721 |
| clpY | groEL | gene:10728361 | gene:10726431 | ATP-dependent Clp protease (heat-shock protein); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | Class I heat-shock protein (chaperonin); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.855 |
| clpY | groES | gene:10728361 | gene:10726430 | ATP-dependent Clp protease (heat-shock protein); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | Class I heat-shock protein (chaperonin); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.835 |
| clpY | htpG | gene:10728361 | gene:10726901 | ATP-dependent Clp protease (heat-shock protein); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | Class III heat-shock protein (chaperonin); Molecular chaperone. Has ATPase activity. | 0.832 |
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