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 |
| cbpA | djlA | b1000 | b0055 | DnaK co-chaperone; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | Membrane-anchored DnaK co-chaperone, DNA-binding protein; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host. | 0.904 |
| cbpA | djlB | b1000 | b0646 | DnaK co-chaperone; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | Putative HscC co-chaperone, uncharacterized J domain-containing protein; Putative enzyme of polynucleotide modification; Protein involved in protein folding. | 0.605 |
| cbpA | djlC | b1000 | b0649 | DnaK co-chaperone; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | J domain-containing HscC co-chaperone; Hsc56. | 0.514 |
| cbpA | groL | b1000 | b4143 | DnaK co-chaperone; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.815 |
| cbpA | grpE | b1000 | b2614 | DnaK co-chaperone; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | Heat shock protein; 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-depen [...] | 0.985 |
| cbpA | hscC | b1000 | b0650 | DnaK co-chaperone; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | Hsp70 family chaperone Hsc62; Probable chaperone. Has ATPase activity. Not stimulated by DnaJ. | 0.937 |
| cbpA | htpG | b1000 | b0473 | DnaK co-chaperone; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | Protein refolding molecular co-chaperone Hsp90, Hsp70-dependent; Molecular chaperone. Has ATPase activity. | 0.876 |
| djlA | cbpA | b0055 | b1000 | Membrane-anchored DnaK co-chaperone, DNA-binding protein; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host. | DnaK co-chaperone; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | 0.904 |
| djlA | djlB | b0055 | b0646 | Membrane-anchored DnaK co-chaperone, DNA-binding protein; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host. | Putative HscC co-chaperone, uncharacterized J domain-containing protein; Putative enzyme of polynucleotide modification; Protein involved in protein folding. | 0.639 |
| djlA | djlC | b0055 | b0649 | Membrane-anchored DnaK co-chaperone, DNA-binding protein; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host. | J domain-containing HscC co-chaperone; Hsc56. | 0.482 |
| djlA | dnaJ | b0055 | b0015 | Membrane-anchored DnaK co-chaperone, DNA-binding protein; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host. | Chaperone Hsp40, DnaK co-chaperone; Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. 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 t [...] | 0.860 |
| djlA | grpE | b0055 | b2614 | Membrane-anchored DnaK co-chaperone, DNA-binding protein; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host. | Heat shock protein; 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-depen [...] | 0.662 |
| djlA | hscC | b0055 | b0650 | Membrane-anchored DnaK co-chaperone, DNA-binding protein; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host. | Hsp70 family chaperone Hsc62; Probable chaperone. Has ATPase activity. Not stimulated by DnaJ. | 0.779 |
| djlA | htpG | b0055 | b0473 | Membrane-anchored DnaK co-chaperone, DNA-binding protein; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host. | Protein refolding molecular co-chaperone Hsp90, Hsp70-dependent; Molecular chaperone. Has ATPase activity. | 0.602 |
| djlB | cbpA | b0646 | b1000 | Putative HscC co-chaperone, uncharacterized J domain-containing protein; Putative enzyme of polynucleotide modification; Protein involved in protein folding. | DnaK co-chaperone; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | 0.605 |
| djlB | djlA | b0646 | b0055 | Putative HscC co-chaperone, uncharacterized J domain-containing protein; Putative enzyme of polynucleotide modification; Protein involved in protein folding. | Membrane-anchored DnaK co-chaperone, DNA-binding protein; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host. | 0.639 |
| djlB | dnaJ | b0646 | b0015 | Putative HscC co-chaperone, uncharacterized J domain-containing protein; Putative enzyme of polynucleotide modification; Protein involved in protein folding. | Chaperone Hsp40, DnaK co-chaperone; Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. 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 t [...] | 0.511 |
| djlB | hscC | b0646 | b0650 | Putative HscC co-chaperone, uncharacterized J domain-containing protein; Putative enzyme of polynucleotide modification; Protein involved in protein folding. | Hsp70 family chaperone Hsc62; Probable chaperone. Has ATPase activity. Not stimulated by DnaJ. | 0.960 |
| djlB | htpG | b0646 | b0473 | Putative HscC co-chaperone, uncharacterized J domain-containing protein; Putative enzyme of polynucleotide modification; Protein involved in protein folding. | Protein refolding molecular co-chaperone Hsp90, Hsp70-dependent; Molecular chaperone. Has ATPase activity. | 0.670 |
| djlC | cbpA | b0649 | b1000 | J domain-containing HscC co-chaperone; Hsc56. | DnaK co-chaperone; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | 0.514 |
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