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 |
| ALP40208.1 | htpG | WL1483_4463 | WL1483_3770 | Histone deacetylase/AcuC/AphA family protein. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.925 |
| ALP40208.1 | ppiA | WL1483_4463 | WL1483_2003 | Histone deacetylase/AcuC/AphA family protein. | Peptidylprolyl isomerase; 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. | 0.512 |
| ALP40208.1 | ppiB | WL1483_4463 | WL1483_4229 | Histone deacetylase/AcuC/AphA family 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. | 0.512 |
| ALP41276.1 | ALP43533.1 | WL1483_1857 | WL1483_4114 | DnaJ family molecular chaperone. | Hypothetical protein. | 0.940 |
| ALP41276.1 | dnaK | WL1483_1857 | WL1483_830 | DnaJ family molecular chaperone. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.948 |
| ALP41276.1 | groL | WL1483_1857 | WL1483_4310 | DnaJ family molecular chaperone. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.838 |
| ALP41276.1 | hscA | WL1483_1857 | WL1483_1117 | DnaJ family molecular chaperone. | Chaperone protein HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.940 |
| ALP41276.1 | htpG | WL1483_1857 | WL1483_3770 | DnaJ family molecular chaperone. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.981 |
| ALP41276.1 | ppiA | WL1483_1857 | WL1483_2003 | DnaJ family molecular chaperone. | Peptidylprolyl isomerase; 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. | 0.800 |
| ALP41276.1 | ppiB | WL1483_1857 | WL1483_4229 | DnaJ family molecular chaperone. | 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. | 0.800 |
| ALP41276.1 | yegD | WL1483_1857 | WL1483_3458 | DnaJ family molecular chaperone. | Chaperone. | 0.940 |
| ALP43533.1 | ALP41276.1 | WL1483_4114 | WL1483_1857 | Hypothetical protein. | DnaJ family molecular chaperone. | 0.940 |
| ALP43533.1 | dnaJ | WL1483_4114 | WL1483_3642 | 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 [...] | 0.940 |
| ALP43533.1 | groL | WL1483_4114 | WL1483_4310 | Hypothetical protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.911 |
| ALP43533.1 | htpG | WL1483_4114 | WL1483_3770 | Hypothetical protein. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.972 |
| ALP43533.1 | ppiA | WL1483_4114 | WL1483_2003 | Hypothetical protein. | Peptidylprolyl isomerase; 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. | 0.434 |
| ALP43533.1 | ppiB | WL1483_4114 | WL1483_4229 | Hypothetical 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. | 0.434 |
| dnaJ | ALP43533.1 | WL1483_3642 | WL1483_4114 | 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. | 0.940 |
| dnaJ | dnaK | WL1483_3642 | WL1483_830 | 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 [...] | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | groL | WL1483_3642 | WL1483_4310 | 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 [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.961 |
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