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 |
| Noc_0603 | Noc_2342 | Noc_0603 | Noc_2342 | Thioredoxin domain-containing protein. | Protein of unknown function DUF971. | 0.423 |
| Noc_0603 | dnaJ | Noc_0603 | Noc_2810 | Thioredoxin domain-containing protein. | Heat shock 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, [...] | 0.866 |
| Noc_0603 | groL | Noc_0603 | Noc_2921 | Thioredoxin domain-containing protein. | Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.809 |
| Noc_0603 | groS | Noc_0603 | Noc_2922 | Thioredoxin domain-containing protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.590 |
| Noc_0603 | grpE | Noc_0603 | Noc_2812 | Thioredoxin domain-containing protein. | GrpE 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 ATP-dependent i [...] | 0.868 |
| Noc_0603 | hslU | Noc_0603 | Noc_2341 | Thioredoxin domain-containing protein. | Heat shock protein 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. | 0.881 |
| Noc_0603 | hslV | Noc_0603 | Noc_2340 | Thioredoxin domain-containing protein. | HslV component of HslUV peptidase, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.869 |
| Noc_0603 | htpG | Noc_0603 | Noc_1718 | Thioredoxin domain-containing protein. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.871 |
| Noc_0603 | lon | Noc_0603 | Noc_1387 | Thioredoxin domain-containing protein. | Peptidase S16, ATP-dependent protease La; 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 |
| Noc_0870 | dnaJ | Noc_0870 | Noc_2810 | Heat shock protein Hsp15; Belongs to the HSP15 family. | Heat shock 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, [...] | 0.714 |
| Noc_0870 | grpE | Noc_0870 | Noc_2812 | Heat shock protein Hsp15; Belongs to the HSP15 family. | GrpE 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 ATP-dependent i [...] | 0.709 |
| Noc_0870 | hslU | Noc_0870 | Noc_2341 | Heat shock protein Hsp15; Belongs to the HSP15 family. | Heat shock protein 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. | 0.766 |
| Noc_0870 | hslV | Noc_0870 | Noc_2340 | Heat shock protein Hsp15; Belongs to the HSP15 family. | HslV component of HslUV peptidase, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.823 |
| Noc_0870 | htpG | Noc_0870 | Noc_1718 | Heat shock protein Hsp15; Belongs to the HSP15 family. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.501 |
| Noc_2342 | Noc_0603 | Noc_2342 | Noc_0603 | Protein of unknown function DUF971. | Thioredoxin domain-containing protein. | 0.423 |
| Noc_2342 | hslU | Noc_2342 | Noc_2341 | Protein of unknown function DUF971. | Heat shock protein 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. | 0.863 |
| Noc_2342 | hslV | Noc_2342 | Noc_2340 | Protein of unknown function DUF971. | HslV component of HslUV peptidase, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.831 |
| dnaJ | Noc_0603 | Noc_2810 | Noc_0603 | Heat shock 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, [...] | Thioredoxin domain-containing protein. | 0.866 |
| dnaJ | Noc_0870 | Noc_2810 | Noc_0870 | Heat shock 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, [...] | Heat shock protein Hsp15; Belongs to the HSP15 family. | 0.714 |
| dnaJ | groL | Noc_2810 | Noc_2921 | Heat shock 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, [...] | Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.951 |
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