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 |
| KRL24611.1 | ftsH | FC37_GL000215 | FC37_GL000217 | tRNA-dihydrouridine synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | Cell division protein; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.575 |
| KRL24611.1 | hslO | FC37_GL000215 | FC37_GL000216 | tRNA-dihydrouridine synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | 33 kda chaperonin; 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. | 0.664 |
| KRL24611.1 | lysS | FC37_GL000215 | FC37_GL000214 | tRNA-dihydrouridine synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.816 |
| KRL24617.1 | KRL25161.1 | FC37_GL000221 | FC37_GL001811 | Hypothetical protein. | Atp-dependent protease hs ivu peptidase subunit-like protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.518 |
| KRL24617.1 | ftsH | FC37_GL000221 | FC37_GL000217 | Hypothetical protein. | Cell division protein; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.423 |
| KRL24617.1 | grpE | FC37_GL000221 | FC37_GL001663 | Hypothetical protein. | Nucleotide exchange factor, co-chaperone for dnak; 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 cyc [...] | 0.519 |
| KRL24617.1 | hslO | FC37_GL000221 | FC37_GL000216 | Hypothetical protein. | 33 kda chaperonin; 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. | 0.703 |
| KRL24617.1 | hslU | FC37_GL000221 | FC37_GL001810 | Hypothetical protein. | 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. | 0.519 |
| KRL25161.1 | KRL24617.1 | FC37_GL001811 | FC37_GL000221 | Atp-dependent protease hs ivu peptidase subunit-like protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Hypothetical protein. | 0.518 |
| KRL25161.1 | dnaJ | FC37_GL001811 | FC37_GL001661 | Atp-dependent protease hs ivu peptidase subunit-like protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 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, [...] | 0.589 |
| KRL25161.1 | dnaK | FC37_GL001811 | FC37_GL001662 | Atp-dependent protease hs ivu peptidase subunit-like protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.518 |
| KRL25161.1 | ftsH | FC37_GL001811 | FC37_GL000217 | Atp-dependent protease hs ivu peptidase subunit-like protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Cell division protein; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.456 |
| KRL25161.1 | groL | FC37_GL001811 | FC37_GL000592 | Atp-dependent protease hs ivu peptidase subunit-like protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 60 kda chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.719 |
| KRL25161.1 | grpE | FC37_GL001811 | FC37_GL001663 | Atp-dependent protease hs ivu peptidase subunit-like protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Nucleotide exchange factor, co-chaperone for dnak; 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 cyc [...] | 0.704 |
| KRL25161.1 | hslO | FC37_GL001811 | FC37_GL000216 | Atp-dependent protease hs ivu peptidase subunit-like protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 33 kda chaperonin; 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. | 0.715 |
| KRL25161.1 | hslU | FC37_GL001811 | FC37_GL001810 | Atp-dependent protease hs ivu peptidase subunit-like protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 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. | 0.999 |
| dnaJ | KRL25161.1 | FC37_GL001661 | FC37_GL001811 | 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, [...] | Atp-dependent protease hs ivu peptidase subunit-like protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.589 |
| dnaJ | dnaK | FC37_GL001661 | FC37_GL001662 | 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, [...] | Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | ftsH | FC37_GL001661 | FC37_GL000217 | 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, [...] | Cell division protein; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.652 |
| dnaJ | groL | FC37_GL001661 | FC37_GL000592 | 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, [...] | 60 kda chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.918 |
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