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 |
| AHM59250.1 | AHM61081.1 | D770_04915 | D770_14135 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | 0.715 |
| AHM59250.1 | AHM63100.1 | D770_04915 | D770_24275 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Hypothetical protein. | 0.795 |
| AHM59250.1 | dnaK | D770_04915 | D770_12340 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Chaperone protein dnak; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.935 |
| AHM59250.1 | groL | D770_04915 | D770_03500 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Chaperonin groel; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.665 |
| AHM59250.1 | groS | D770_04915 | D770_03495 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.458 |
| AHM59250.1 | grpE | D770_04915 | D770_10825 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Molecular chaperone 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 [...] | 0.821 |
| AHM59250.1 | hslU | D770_04915 | D770_19490 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | ATP-dependent protease ATP-binding 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. | 0.573 |
| AHM59250.1 | hslV | D770_04915 | D770_09270 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.443 |
| AHM59250.1 | htpG | D770_04915 | D770_12640 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.836 |
| AHM59250.1 | lon | D770_04915 | D770_19480 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | 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. | 0.579 |
| AHM61081.1 | AHM59250.1 | D770_14135 | D770_04915 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | 0.715 |
| AHM61081.1 | AHM63100.1 | D770_14135 | D770_24275 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Hypothetical protein. | 0.795 |
| AHM61081.1 | dnaK | D770_14135 | D770_12340 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Chaperone protein dnak; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.958 |
| AHM61081.1 | groL | D770_14135 | D770_03500 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Chaperonin groel; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.706 |
| AHM61081.1 | groS | D770_14135 | D770_03495 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.458 |
| AHM61081.1 | grpE | D770_14135 | D770_10825 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Molecular chaperone 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 [...] | 0.831 |
| AHM61081.1 | hslU | D770_14135 | D770_19490 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | ATP-dependent protease ATP-binding 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. | 0.573 |
| AHM61081.1 | hslV | D770_14135 | D770_09270 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.443 |
| AHM61081.1 | htpG | D770_14135 | D770_12640 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.836 |
| AHM61081.1 | lon | D770_14135 | D770_19480 | COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. | 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. | 0.466 |
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