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 |
| ALU98854.1 | cbpA | ATE51_00628 | ATE51_01128 | Hypothetical protein. | Curved DNA-binding protein. | 0.485 |
| ALU98854.1 | dnaJ | ATE51_00628 | ATE51_02390 | Hypothetical protein. | 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 [...] | 0.485 |
| ALU98854.1 | dnaK | ATE51_00628 | ATE51_02132 | Hypothetical protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.895 |
| ALU98854.1 | guaB | ATE51_00628 | ATE51_01492 | Hypothetical protein. | Inosine-5'-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family. | 0.442 |
| ALU98854.1 | htpG | ATE51_00628 | ATE51_03166 | Hypothetical protein. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.933 |
| ALV00226.1 | cbpA | ATE51_03434 | ATE51_01128 | Tetratricopeptide repeat protein. | Curved DNA-binding protein. | 0.485 |
| ALV00226.1 | dnaJ | ATE51_03434 | ATE51_02390 | Tetratricopeptide repeat protein. | 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 [...] | 0.485 |
| ALV00226.1 | dnaK | ATE51_03434 | ATE51_02132 | Tetratricopeptide repeat protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.897 |
| ALV00226.1 | guaB | ATE51_03434 | ATE51_01492 | Tetratricopeptide repeat protein. | Inosine-5'-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family. | 0.505 |
| ALV00226.1 | htpG | ATE51_03434 | ATE51_03166 | Tetratricopeptide repeat protein. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.933 |
| cbpA | ALU98854.1 | ATE51_01128 | ATE51_00628 | Curved DNA-binding protein. | Hypothetical protein. | 0.485 |
| cbpA | ALV00226.1 | ATE51_01128 | ATE51_03434 | Curved DNA-binding protein. | Tetratricopeptide repeat protein. | 0.485 |
| cbpA | dnaK | ATE51_01128 | ATE51_02132 | Curved DNA-binding protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.994 |
| cbpA | groL | ATE51_01128 | ATE51_01160 | Curved DNA-binding protein. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.819 |
| cbpA | groS | ATE51_01128 | ATE51_01162 | Curved DNA-binding protein. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.664 |
| cbpA | hslU | ATE51_01128 | ATE51_02278 | Curved DNA-binding protein. | ATP-dependent protease ATPase subunit HslU; 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. | 0.580 |
| cbpA | htpG | ATE51_01128 | ATE51_03166 | Curved DNA-binding protein. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.858 |
| cbpA | ppiB | ATE51_01128 | ATE51_01264 | Curved DNA-binding protein. | 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. | 0.674 |
| dnaJ | ALU98854.1 | ATE51_02390 | ATE51_00628 | 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 [...] | Hypothetical protein. | 0.485 |
| dnaJ | ALV00226.1 | ATE51_02390 | ATE51_03434 | 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 [...] | Tetratricopeptide repeat protein. | 0.485 |
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