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 |
| CCH85518.1 | dnaJ-2 | MODMU_0046 | MODMU_5177 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | Chaperone protein dnaJ, heat shock protein (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 [...] | 0.986 |
| CCH85518.1 | groL | MODMU_0046 | MODMU_4858 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 60 kDa chaperonin (Protein Cpn60) (groEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.887 |
| CCH85518.1 | grpE | MODMU_0046 | MODMU_5178 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 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. [...] | 0.990 |
| CCH85518.1 | hrcA | MODMU_0046 | MODMU_1759 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 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. | 0.889 |
| CCH85518.1 | hspR | MODMU_0046 | MODMU_5176 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | Heat shock regulator; Function of strongly homologous gene; regulator. | 0.667 |
| CCH85518.1 | rplK | MODMU_0046 | MODMU_4935 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 50S ribosomal subunit protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | 0.592 |
| CCH85518.1 | rplM | MODMU_0046 | MODMU_4877 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 50S ribosomal subunit protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. | 0.683 |
| CCH85518.1 | rplN | MODMU_0046 | MODMU_4909 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 50S ribosomal subunit protein L14; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family. | 0.654 |
| dnaJ-2 | CCH85518.1 | MODMU_5177 | MODMU_0046 | Chaperone protein dnaJ, heat shock protein (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 [...] | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 0.986 |
| dnaJ-2 | dnaK | MODMU_5177 | MODMU_5179 | Chaperone protein dnaJ, heat shock protein (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 [...] | Chaperone protein dnaK (Heat shock protein 70) (Heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.998 |
| dnaJ-2 | groL | MODMU_5177 | MODMU_4858 | Chaperone protein dnaJ, heat shock protein (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 [...] | 60 kDa chaperonin (Protein Cpn60) (groEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.828 |
| dnaJ-2 | grpE | MODMU_5177 | MODMU_5178 | Chaperone protein dnaJ, heat shock protein (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 [...] | 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. [...] | 0.990 |
| dnaJ-2 | hrcA | MODMU_5177 | MODMU_1759 | Chaperone protein dnaJ, heat shock protein (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 [...] | 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. | 0.865 |
| dnaJ-2 | hspR | MODMU_5177 | MODMU_5176 | Chaperone protein dnaJ, heat shock protein (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 [...] | Heat shock regulator; Function of strongly homologous gene; regulator. | 0.947 |
| dnaJ-2 | rplK | MODMU_5177 | MODMU_4935 | Chaperone protein dnaJ, heat shock protein (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 [...] | 50S ribosomal subunit protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | 0.832 |
| dnaJ-2 | rplM | MODMU_5177 | MODMU_4877 | Chaperone protein dnaJ, heat shock protein (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 [...] | 50S ribosomal subunit protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. | 0.859 |
| dnaJ-2 | rplN | MODMU_5177 | MODMU_4909 | Chaperone protein dnaJ, heat shock protein (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 [...] | 50S ribosomal subunit protein L14; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family. | 0.863 |
| dnaJ-2 | rplO | MODMU_5177 | MODMU_4900 | Chaperone protein dnaJ, heat shock protein (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 [...] | 50S ribosomal subunit protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family. | 0.833 |
| dnaK | dnaJ-2 | MODMU_5179 | MODMU_5177 | Chaperone protein dnaK (Heat shock protein 70) (Heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperone protein dnaJ, heat shock protein (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 [...] | 0.998 |
| dnaK | groL | MODMU_5179 | MODMU_4858 | Chaperone protein dnaK (Heat shock protein 70) (Heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 60 kDa chaperonin (Protein Cpn60) (groEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.959 |
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