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 |
| XM1_0855 | dnaJ | XM1_0855 | XM1_0732 | Putative Thioredoxin domain-containing protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | 0.627 |
| XM1_0855 | dnaK | XM1_0855 | XM1_0731 | Putative Thioredoxin domain-containing protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Chaperone Hsp70, co-chaperone with DnaJ; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.602 |
| XM1_0855 | groES | XM1_0855 | XM1_1162 | Putative Thioredoxin domain-containing protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Cpn10 chaperonin GroES, small subunit of GroESL(Chaperonin Cpn10,1-95); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.590 |
| XM1_0855 | groL | XM1_0855 | XM1_1163 | Putative Thioredoxin domain-containing protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Cpn60 chaperonin GroEL, large subunit of GroESL(Chaperonin Cpn60/TCP-1,23-525); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.731 |
| XM1_0855 | grpE | XM1_0855 | XM1_0797 | Putative Thioredoxin domain-containing protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Protein GrpE, Heat Shock Chaperone (HSP-70 cofactor); 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 [...] | 0.900 |
| XM1_0855 | hscA | XM1_0855 | XM1_2213 | Putative Thioredoxin domain-containing protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | DnaK-like molecular chaperone specific for IscU; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.541 |
| XM1_0855 | hslU | XM1_0855 | XM1_0819 | Putative Thioredoxin domain-containing protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Molecular chaperone and ATPase component of HslUV protease; 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. | 0.890 |
| XM1_0855 | hslV | XM1_0855 | XM1_0818 | Putative Thioredoxin domain-containing protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.881 |
| XM1_2231 | dnaJ | XM1_2231 | XM1_0732 | Putative Molecular chaperone; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor. | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | 0.853 |
| XM1_2231 | groES | XM1_2231 | XM1_1162 | Putative Molecular chaperone; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor. | Cpn10 chaperonin GroES, small subunit of GroESL(Chaperonin Cpn10,1-95); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.869 |
| XM1_2231 | groL | XM1_2231 | XM1_1163 | Putative Molecular chaperone; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor. | Cpn60 chaperonin GroEL, large subunit of GroESL(Chaperonin Cpn60/TCP-1,23-525); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.908 |
| XM1_2231 | grpE | XM1_2231 | XM1_0797 | Putative Molecular chaperone; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor. | Protein GrpE, Heat Shock Chaperone (HSP-70 cofactor); 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 [...] | 0.933 |
| XM1_2231 | hrcA | XM1_2231 | XM1_0798 | Putative Molecular chaperone; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.842 |
| XM1_2231 | hslU | XM1_2231 | XM1_0819 | Putative Molecular chaperone; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor. | Molecular chaperone and ATPase component of HslUV protease; 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. | 0.536 |
| XM1_2231 | hslV | XM1_2231 | XM1_0818 | Putative Molecular chaperone; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor. | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.500 |
| dnaJ | XM1_0855 | XM1_0732 | XM1_0855 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | Putative Thioredoxin domain-containing protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.627 |
| dnaJ | XM1_2231 | XM1_0732 | XM1_2231 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | Putative Molecular chaperone; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor. | 0.853 |
| dnaJ | dnaK | XM1_0732 | XM1_0731 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | Chaperone Hsp70, co-chaperone with DnaJ; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.993 |
| dnaJ | groES | XM1_0732 | XM1_1162 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | Cpn10 chaperonin GroES, small subunit of GroESL(Chaperonin Cpn10,1-95); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.675 |
| dnaJ | groL | XM1_0732 | XM1_1163 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | Cpn60 chaperonin GroEL, large subunit of GroESL(Chaperonin Cpn60/TCP-1,23-525); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.821 |
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