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 |
| HELO_2223 | dnaJ | HELO_2223 | HELO_4158 | Hypothetical protein; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit - Homo sapiens (Human),InterPro: TPR repeat, Specificity unclear. | K03686 molecular chaperone 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 betwee [...] | 0.764 |
| HELO_2223 | dnaK | HELO_2223 | HELO_4159 | Hypothetical protein; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit - Homo sapiens (Human),InterPro: TPR repeat, Specificity unclear. | K04043 molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.911 |
| HELO_2223 | htpG | HELO_2223 | HELO_3424 | Hypothetical protein; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit - Homo sapiens (Human),InterPro: TPR repeat, Specificity unclear. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.921 |
| HELO_3036 | dnaJ | HELO_3036 | HELO_4158 | Cellulose synthase 2 operon protein C precursor -Acetobacter xylinus (Gluconacetobacter xylinus),Hypothetical protein. | K03686 molecular chaperone 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 betwee [...] | 0.764 |
| HELO_3036 | dnaK | HELO_3036 | HELO_4159 | Cellulose synthase 2 operon protein C precursor -Acetobacter xylinus (Gluconacetobacter xylinus),Hypothetical protein. | K04043 molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.911 |
| HELO_3036 | htpG | HELO_3036 | HELO_3424 | Cellulose synthase 2 operon protein C precursor -Acetobacter xylinus (Gluconacetobacter xylinus),Hypothetical protein. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.921 |
| dnaJ | HELO_2223 | HELO_4158 | HELO_2223 | K03686 molecular chaperone 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 betwee [...] | Hypothetical protein; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit - Homo sapiens (Human),InterPro: TPR repeat, Specificity unclear. | 0.764 |
| dnaJ | HELO_3036 | HELO_4158 | HELO_3036 | K03686 molecular chaperone 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 betwee [...] | Cellulose synthase 2 operon protein C precursor -Acetobacter xylinus (Gluconacetobacter xylinus),Hypothetical protein. | 0.764 |
| dnaJ | dnaK | HELO_4158 | HELO_4159 | K03686 molecular chaperone 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 betwee [...] | K04043 molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | groL | HELO_4158 | HELO_2875 | K03686 molecular chaperone 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 betwee [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.924 |
| dnaJ | groS | HELO_4158 | HELO_2874 | K03686 molecular chaperone 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 betwee [...] | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.808 |
| dnaJ | hslU | HELO_4158 | HELO_3769 | K03686 molecular chaperone 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 betwee [...] | ATP-dependent protease ATP-binding 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. | 0.897 |
| dnaJ | hslV | HELO_4158 | HELO_3768 | K03686 molecular chaperone 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 betwee [...] | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.870 |
| dnaJ | htpG | HELO_4158 | HELO_3424 | K03686 molecular chaperone 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 betwee [...] | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.988 |
| dnaJ | ppiB | HELO_4158 | HELO_2355 | K03686 molecular chaperone 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 betwee [...] | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.912 |
| dnaK | HELO_2223 | HELO_4159 | HELO_2223 | K04043 molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Hypothetical protein; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit - Homo sapiens (Human),InterPro: TPR repeat, Specificity unclear. | 0.911 |
| dnaK | HELO_3036 | HELO_4159 | HELO_3036 | K04043 molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Cellulose synthase 2 operon protein C precursor -Acetobacter xylinus (Gluconacetobacter xylinus),Hypothetical protein. | 0.911 |
| dnaK | dnaJ | HELO_4159 | HELO_4158 | K04043 molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | K03686 molecular chaperone 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 betwee [...] | 0.999 |
| dnaK | groL | HELO_4159 | HELO_2875 | K04043 molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.993 |
| dnaK | groS | HELO_4159 | HELO_2874 | K04043 molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.981 |
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