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 | clpB1 | ZOBELLIA_3574 | ZOBELLIA_4745 | CbpA is a 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; Contains an N-terminal J domain; Localized in the cytoplasm; High confidence in function and specificity. | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 0.591 |
| cbpA | clpB2 | ZOBELLIA_3574 | ZOBELLIA_405 | CbpA is a 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; Contains an N-terminal J domain; Localized in the cytoplasm; High confidence in function and specificity. | ClpB is a homohexamer that is a part of a stress-induced multi-chaperone system involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates contributing to the solubilization and refolding of denatured protein aggregates by dnaK; Contains 2 AAA ATPase domains; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | 0.591 |
| cbpA | clpC | ZOBELLIA_3574 | ZOBELLIA_469 | CbpA is a 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; Contains an N-terminal J domain; Localized in the cytoplasm; High confidence in function and specificity. | ClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | 0.598 |
| cbpA | dnaK | ZOBELLIA_3574 | ZOBELLIA_4708 | CbpA is a 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; Contains an N-terminal J domain; Localized in the cytoplasm; High confidence in function and specificity. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.977 |
| cbpA | groL | ZOBELLIA_3574 | ZOBELLIA_1162 | CbpA is a 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; Contains an N-terminal J domain; Localized in the cytoplasm; High confidence in function and specificity. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.677 |
| cbpA | groS | ZOBELLIA_3574 | ZOBELLIA_1161 | CbpA is a 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; Contains an N-terminal J domain; Localized in the cytoplasm; High confidence in function and specificity. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.494 |
| cbpA | grpE | ZOBELLIA_3574 | ZOBELLIA_2823 | CbpA is a 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; Contains an N-terminal J domain; Localized in the cytoplasm; High confidence in function and specificity. | Co-chaperone HSP-70 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 [...] | 0.790 |
| cbpA | htpG | ZOBELLIA_3574 | ZOBELLIA_607 | CbpA is a 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; Contains an N-terminal J domain; Localized in the cytoplasm; High confidence in function and specificity. | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.847 |
| clpB1 | cbpA | ZOBELLIA_4745 | ZOBELLIA_3574 | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | CbpA is a 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; Contains an N-terminal J domain; Localized in the cytoplasm; High confidence in function and specificity. | 0.591 |
| clpB1 | djlA | ZOBELLIA_4745 | ZOBELLIA_1886 | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | The protein DjlA is a Regulatory dnaK co-chaperone. Contains a N-terminal transmembrane helix and a C-terminal DnaJ domain; Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.602 |
| clpB1 | dnaJ | ZOBELLIA_4745 | ZOBELLIA_2824 | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Co-chaperone protein 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 [...] | 0.591 |
| clpB1 | dnaK | ZOBELLIA_4745 | ZOBELLIA_4708 | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.958 |
| clpB1 | groL | ZOBELLIA_4745 | ZOBELLIA_1162 | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.602 |
| clpB1 | groS | ZOBELLIA_4745 | ZOBELLIA_1161 | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.632 |
| clpB1 | grpE | ZOBELLIA_4745 | ZOBELLIA_2823 | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Co-chaperone HSP-70 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 [...] | 0.765 |
| clpB1 | htpG | ZOBELLIA_4745 | ZOBELLIA_607 | Chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.680 |
| clpB2 | cbpA | ZOBELLIA_405 | ZOBELLIA_3574 | ClpB is a homohexamer that is a part of a stress-induced multi-chaperone system involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates contributing to the solubilization and refolding of denatured protein aggregates by dnaK; Contains 2 AAA ATPase domains; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | CbpA is a 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; Contains an N-terminal J domain; Localized in the cytoplasm; High confidence in function and specificity. | 0.591 |
| clpB2 | djlA | ZOBELLIA_405 | ZOBELLIA_1886 | ClpB is a homohexamer that is a part of a stress-induced multi-chaperone system involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates contributing to the solubilization and refolding of denatured protein aggregates by dnaK; Contains 2 AAA ATPase domains; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | The protein DjlA is a Regulatory dnaK co-chaperone. Contains a N-terminal transmembrane helix and a C-terminal DnaJ domain; Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.602 |
| clpB2 | dnaJ | ZOBELLIA_405 | ZOBELLIA_2824 | ClpB is a homohexamer that is a part of a stress-induced multi-chaperone system involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates contributing to the solubilization and refolding of denatured protein aggregates by dnaK; Contains 2 AAA ATPase domains; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Co-chaperone protein 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 [...] | 0.591 |
| clpB2 | dnaK | ZOBELLIA_405 | ZOBELLIA_4708 | ClpB is a homohexamer that is a part of a stress-induced multi-chaperone system involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates contributing to the solubilization and refolding of denatured protein aggregates by dnaK; Contains 2 AAA ATPase domains; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.958 |
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