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 |
| AGA24592.1 | AGA24593.1 | Sinac_0134 | Sinac_0135 | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | 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. [...] | 0.919 |
| AGA24592.1 | AGA24594.1 | Sinac_0134 | Sinac_0136 | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | 0.920 |
| AGA24592.1 | AGA29491.1 | Sinac_0134 | Sinac_5341 | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.410 |
| AGA24592.1 | hslU | Sinac_0134 | Sinac_5342 | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | 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. | 0.497 |
| AGA24593.1 | AGA24592.1 | Sinac_0135 | Sinac_0134 | 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. [...] | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | 0.919 |
| AGA24593.1 | AGA24594.1 | Sinac_0135 | Sinac_0136 | 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. [...] | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | 0.931 |
| AGA24593.1 | AGA26182.1 | Sinac_0135 | Sinac_1817 | 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. [...] | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | 0.797 |
| AGA24593.1 | AGA26183.1 | Sinac_0135 | Sinac_1818 | 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. [...] | Molecular chaperone; PFAM: von Willebrand factor type A domain; Hsp70 protein; Belongs to the heat shock protein 70 family. | 0.797 |
| AGA24593.1 | AGA27268.1 | Sinac_0135 | Sinac_2984 | 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. [...] | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | 0.797 |
| AGA24593.1 | AGA27332.1 | Sinac_0135 | Sinac_3051 | 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. [...] | Molecular chaperone; PFAM: DNA-K related protein; Hsp70 protein. | 0.797 |
| AGA24593.1 | AGA29491.1 | Sinac_0135 | Sinac_5341 | 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. [...] | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.799 |
| AGA24593.1 | dnaK | Sinac_0135 | Sinac_1485 | 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. [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.797 |
| AGA24593.1 | dnaK-2 | Sinac_0135 | Sinac_3501 | 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. [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.797 |
| AGA24593.1 | hslU | Sinac_0135 | Sinac_5342 | 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. [...] | 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. | 0.802 |
| AGA24594.1 | AGA24592.1 | Sinac_0136 | Sinac_0134 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | 0.920 |
| AGA24594.1 | AGA24593.1 | Sinac_0136 | Sinac_0135 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | 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. [...] | 0.931 |
| AGA24594.1 | AGA26182.1 | Sinac_0136 | Sinac_1817 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | 0.799 |
| AGA24594.1 | AGA26183.1 | Sinac_0136 | Sinac_1818 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Molecular chaperone; PFAM: von Willebrand factor type A domain; Hsp70 protein; Belongs to the heat shock protein 70 family. | 0.799 |
| AGA24594.1 | AGA27268.1 | Sinac_0136 | Sinac_2984 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | 0.825 |
| AGA24594.1 | AGA27332.1 | Sinac_0136 | Sinac_3051 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Molecular chaperone; PFAM: DNA-K related protein; Hsp70 protein. | 0.823 |
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