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 |
| CspC | GroL | TTE1738 | TTE0580 | Cold shock proteins; Best Blastp hit = gi|10176234|dbj|BAB07329.1| (AP001519) cold-shock protein [Bacillus halodurans], score 106, E-value 3.00E-23. | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.451 |
| CspC | GrpE | TTE1738 | TTE0954 | Cold shock proteins; Best Blastp hit = gi|10176234|dbj|BAB07329.1| (AP001519) cold-shock protein [Bacillus halodurans], score 106, E-value 3.00E-23. | Molecular chaperone GrpE (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. [...] | 0.409 |
| CspC | hslO | TTE1738 | TTE1737 | Cold shock proteins; Best Blastp hit = gi|10176234|dbj|BAB07329.1| (AP001519) cold-shock protein [Bacillus halodurans], score 106, E-value 3.00E-23. | Disulfide bond chaperones of the HSP33 family; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.752 |
| DnaJ | GroL | TTE0956 | TTE0580 | Molecular chaperones (contain C-terminal Zn finger domain); 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-de [...] | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.968 |
| DnaJ | GrpE | TTE0956 | TTE0954 | Molecular chaperones (contain C-terminal Zn finger domain); 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-de [...] | Molecular chaperone GrpE (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. [...] | 0.998 |
| DnaJ | HslU | TTE0956 | TTE1447 | Molecular chaperones (contain C-terminal Zn finger domain); 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-de [...] | ATP-dependent protease, ATPase subunit; 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. | 0.748 |
| DnaJ | HslV | TTE0956 | TTE1448 | Molecular chaperones (contain C-terminal Zn finger domain); 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-de [...] | Proteasome protease subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.632 |
| DnaJ | IbpA | TTE0956 | TTE2578 | Molecular chaperones (contain C-terminal Zn finger domain); 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-de [...] | Molecular chaperone (small heat shock protein); Best Blastp hit = gi|7441335|pir||D72385 'heat shock protein, class I - Thermotoga maritima (strain MSB8)' gi|4980878|gb|AAD35461.1|AE001717_7 '(AE001717) heat shock protein, class I [Thermotoga maritima]', score 97.8, E-value 6.00E-20. | 0.700 |
| DnaJ | Lon | TTE0956 | TTE0627 | Molecular chaperones (contain C-terminal Zn finger domain); 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-de [...] | ATP-dependent Lon protease, bacterial type; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.655 |
| DnaJ | hslO | TTE0956 | TTE1737 | Molecular chaperones (contain C-terminal Zn finger domain); 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-de [...] | Disulfide bond chaperones of the HSP33 family; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.652 |
| GroL | CspC | TTE0580 | TTE1738 | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Cold shock proteins; Best Blastp hit = gi|10176234|dbj|BAB07329.1| (AP001519) cold-shock protein [Bacillus halodurans], score 106, E-value 3.00E-23. | 0.451 |
| GroL | DnaJ | TTE0580 | TTE0956 | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Molecular chaperones (contain C-terminal Zn finger domain); 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-de [...] | 0.968 |
| GroL | GrpE | TTE0580 | TTE0954 | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Molecular chaperone GrpE (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. [...] | 0.994 |
| GroL | HslU | TTE0580 | TTE1447 | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | ATP-dependent protease, ATPase subunit; 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. | 0.857 |
| GroL | HslV | TTE0580 | TTE1448 | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Proteasome protease subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.772 |
| GroL | IbpA | TTE0580 | TTE2578 | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Molecular chaperone (small heat shock protein); Best Blastp hit = gi|7441335|pir||D72385 'heat shock protein, class I - Thermotoga maritima (strain MSB8)' gi|4980878|gb|AAD35461.1|AE001717_7 '(AE001717) heat shock protein, class I [Thermotoga maritima]', score 97.8, E-value 6.00E-20. | 0.428 |
| GroL | Lon | TTE0580 | TTE0627 | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | ATP-dependent Lon protease, bacterial type; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.780 |
| GroL | TTE1517 | TTE0580 | TTE1517 | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Predicted RNA-binding protein homologous to eukaryotic snRNP; Best Blastp hit = gi|10175136|dbj|BAB06235.1| (AP001515) fibronectin/fibrinogen-binding protein [Bacillus halodurans], score 413, E-value 1.00E-114. | 0.425 |
| GroL | hslO | TTE0580 | TTE1737 | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Disulfide bond chaperones of the HSP33 family; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.726 |
| GrpE | CspC | TTE0954 | TTE1738 | Molecular chaperone GrpE (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. [...] | Cold shock proteins; Best Blastp hit = gi|10176234|dbj|BAB07329.1| (AP001519) cold-shock protein [Bacillus halodurans], score 106, E-value 3.00E-23. | 0.409 |
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