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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AML34982.1 | cbpA | EAG7_01236 | EAG7_03734 | Chaperone protein ClpB. | Curved DNA-binding protein; 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. | 0.640 |
| AML34982.1 | clpB_3 | EAG7_01236 | EAG7_05362 | Chaperone protein ClpB. | Chaperone protein 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. | 0.903 |
| AML34982.1 | dnaJ | EAG7_01236 | EAG7_03351 | Chaperone protein ClpB. | 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, D [...] | 0.666 |
| AML34982.1 | dnaK_3 | EAG7_01236 | EAG7_03352 | Chaperone protein ClpB. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.879 |
| AML34982.1 | groL | EAG7_01236 | EAG7_03715 | Chaperone protein ClpB. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.611 |
| AML34982.1 | groS | EAG7_01236 | EAG7_03716 | Chaperone protein ClpB. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.574 |
| AML34982.1 | grpE | EAG7_01236 | EAG7_05297 | Chaperone protein ClpB. | 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-dependent i [...] | 0.707 |
| AML34982.1 | htpG | EAG7_01236 | EAG7_02893 | Chaperone protein ClpB. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.669 |
| AML35290.1 | cbpA | EAG7_01544 | EAG7_03734 | Protein ClpV1. | Curved DNA-binding protein; 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. | 0.640 |
| AML35290.1 | dnaJ | EAG7_01544 | EAG7_03351 | Protein ClpV1. | 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, D [...] | 0.666 |
| AML35290.1 | dnaK_3 | EAG7_01544 | EAG7_03352 | Protein ClpV1. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.879 |
| AML35290.1 | groL | EAG7_01544 | EAG7_03715 | Protein ClpV1. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.611 |
| AML35290.1 | groS | EAG7_01544 | EAG7_03716 | Protein ClpV1. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.574 |
| AML35290.1 | grpE | EAG7_01544 | EAG7_05297 | Protein ClpV1. | 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-dependent i [...] | 0.707 |
| AML35290.1 | htpG | EAG7_01544 | EAG7_02893 | Protein ClpV1. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.669 |
| cbpA | AML34982.1 | EAG7_03734 | EAG7_01236 | Curved DNA-binding protein; 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. | Chaperone protein ClpB. | 0.640 |
| cbpA | AML35290.1 | EAG7_03734 | EAG7_01544 | Curved DNA-binding protein; 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 ClpV1. | 0.640 |
| cbpA | clpB_3 | EAG7_03734 | EAG7_05362 | Curved DNA-binding protein; 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. | Chaperone protein 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. | 0.640 |
| cbpA | dnaK_3 | EAG7_03734 | EAG7_03352 | Curved DNA-binding protein; 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. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.964 |
| cbpA | groL | EAG7_03734 | EAG7_03715 | Curved DNA-binding protein; 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. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.785 |
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