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 |
| AKO96995.1 | AKO98410.1 | MALG_01823 | MALG_03266 | DNA or RNA helicase of superfamily II. | Thioredoxin domain protein-containing protein. | 0.429 |
| AKO96995.1 | AKO98656.1 | MALG_01823 | MALG_03513 | DNA or RNA helicase of superfamily II. | Thioredoxin; Belongs to the thioredoxin family. | 0.429 |
| AKO96995.1 | clpX | MALG_01823 | MALG_02427 | DNA or RNA helicase of superfamily II. | Endopeptidase Clp ATP-binding protein regulatory subunit (clpX); ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.452 |
| AKO96995.1 | dnaJ | MALG_01823 | MALG_03177 | DNA or RNA helicase of superfamily II. | 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 [...] | 0.986 |
| AKO96995.1 | groS | MALG_01823 | MALG_00646 | DNA or RNA helicase of superfamily II. | Co-chaperonin GroES (HSP10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.878 |
| AKO96995.1 | grpE | MALG_01823 | MALG_03574 | DNA or RNA helicase of superfamily II. | 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. [...] | 0.863 |
| AKO96995.1 | hslU | MALG_01823 | MALG_03516 | DNA or RNA helicase of superfamily II. | ATP-dependent protease HslVU, 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. | 0.863 |
| AKO96995.1 | hslV | MALG_01823 | MALG_03514 | DNA or RNA helicase of superfamily II. | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.870 |
| AKO96995.1 | lon | MALG_01823 | MALG_02002 | DNA or RNA helicase of superfamily II. | 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. | 0.848 |
| AKO98410.1 | AKO96995.1 | MALG_03266 | MALG_01823 | Thioredoxin domain protein-containing protein. | DNA or RNA helicase of superfamily II. | 0.429 |
| AKO98410.1 | dnaJ | MALG_03266 | MALG_03177 | Thioredoxin domain protein-containing 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 [...] | 0.679 |
| AKO98410.1 | groS | MALG_03266 | MALG_00646 | Thioredoxin domain protein-containing protein. | Co-chaperonin GroES (HSP10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.539 |
| AKO98410.1 | grpE | MALG_03266 | MALG_03574 | Thioredoxin domain protein-containing protein. | 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. [...] | 0.841 |
| AKO98410.1 | hslU | MALG_03266 | MALG_03516 | Thioredoxin domain protein-containing protein. | ATP-dependent protease HslVU, 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. | 0.839 |
| AKO98410.1 | hslV | MALG_03266 | MALG_03514 | Thioredoxin domain protein-containing protein. | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.830 |
| AKO98410.1 | lon | MALG_03266 | MALG_02002 | Thioredoxin domain protein-containing protein. | 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. | 0.556 |
| AKO98656.1 | AKO96995.1 | MALG_03513 | MALG_01823 | Thioredoxin; Belongs to the thioredoxin family. | DNA or RNA helicase of superfamily II. | 0.429 |
| AKO98656.1 | AKO98658.1 | MALG_03513 | MALG_03515 | Thioredoxin; Belongs to the thioredoxin family. | Hypothetical protein. | 0.482 |
| AKO98656.1 | dnaJ | MALG_03513 | MALG_03177 | Thioredoxin; Belongs to the thioredoxin family. | 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 [...] | 0.510 |
| AKO98656.1 | groS | MALG_03513 | MALG_00646 | Thioredoxin; Belongs to the thioredoxin family. | Co-chaperonin GroES (HSP10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.542 |
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