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 |
| clpB | dnaJ1 | DIP2104 | DIP2118 | Putative ATP-dependent protease regulatory subunit, ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belong [...] | Chaperone protein cofactor 1; 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 D [...] | 0.790 |
| clpB | dnaJ2 | DIP2104 | DIP1720 | Putative ATP-dependent protease regulatory subunit, ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belong [...] | Chaperone protein 2; 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, DnaK [...] | 0.730 |
| clpB | dnaK | DIP2104 | DIP2120 | Putative ATP-dependent protease regulatory subunit, ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belong [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.992 |
| clpB | groEL1 | DIP2104 | DIP0576 | Putative ATP-dependent protease regulatory subunit, ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belong [...] | 60 kDa chaperonin 1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.629 |
| clpB | groEL2 | DIP2104 | DIP2020 | Putative ATP-dependent protease regulatory subunit, ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belong [...] | Chaperonin GroEL2; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.571 |
| clpB | groES | DIP2104 | DIP0575 | Putative ATP-dependent protease regulatory subunit, ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belong [...] | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.777 |
| clpB | grpE | DIP2104 | DIP2119 | Putative ATP-dependent protease regulatory subunit, ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belong [...] | Chaperone protein cofactor GrpE; 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. Several rounds [...] | 0.922 |
| clpB | hspR | DIP2104 | DIP2117 | Putative ATP-dependent protease regulatory subunit, ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belong [...] | Putative chaperone locus transcriptional regulator, HspR; Similar to Streptomyces coelicolor putative heat shock protein HspR or SCH44.08c SW:HSPR_STRCO (P40183) (151 aa) fasta scores: E(): 5.4e-16, 52.59% id in 135 aa, and to Mycobacterium tuberculosis HspR or Rv0353 or MTCY13E10.13 TR:O06302 (EMBL:Z95324) (126 aa) fasta scores: E(): 6.6e-23, 66.66% id in 117 aa. | 0.600 |
| clpB2 | dnaJ1 | DIP2101 | DIP2118 | Putative heat shock protein (partial); Similar to Corynebacterium glutamicum ClpB protein SWALL:CLPB_CORGL (SWALL:P53532) (852 aa) fasta scores: E(): 0.027, 44.44% id in 99 aa, and to Mycobacterium leprae heat shock protein ClpB or ML2490 SWALL:Q9CB26 (EMBL:AL583925) (848 aa) fasta scores: E(): 0.66, 35.41% id in 96 aa. Note: Similar also to the C-terminal part of DIP2104 (849 aa) E(): 7.2e-08; 53.465% identity in 101 aa overlap. | Chaperone protein cofactor 1; 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 D [...] | 0.790 |
| clpB2 | dnaJ2 | DIP2101 | DIP1720 | Putative heat shock protein (partial); Similar to Corynebacterium glutamicum ClpB protein SWALL:CLPB_CORGL (SWALL:P53532) (852 aa) fasta scores: E(): 0.027, 44.44% id in 99 aa, and to Mycobacterium leprae heat shock protein ClpB or ML2490 SWALL:Q9CB26 (EMBL:AL583925) (848 aa) fasta scores: E(): 0.66, 35.41% id in 96 aa. Note: Similar also to the C-terminal part of DIP2104 (849 aa) E(): 7.2e-08; 53.465% identity in 101 aa overlap. | Chaperone protein 2; 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, DnaK [...] | 0.730 |
| clpB2 | dnaK | DIP2101 | DIP2120 | Putative heat shock protein (partial); Similar to Corynebacterium glutamicum ClpB protein SWALL:CLPB_CORGL (SWALL:P53532) (852 aa) fasta scores: E(): 0.027, 44.44% id in 99 aa, and to Mycobacterium leprae heat shock protein ClpB or ML2490 SWALL:Q9CB26 (EMBL:AL583925) (848 aa) fasta scores: E(): 0.66, 35.41% id in 96 aa. Note: Similar also to the C-terminal part of DIP2104 (849 aa) E(): 7.2e-08; 53.465% identity in 101 aa overlap. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.982 |
| clpB2 | groEL1 | DIP2101 | DIP0576 | Putative heat shock protein (partial); Similar to Corynebacterium glutamicum ClpB protein SWALL:CLPB_CORGL (SWALL:P53532) (852 aa) fasta scores: E(): 0.027, 44.44% id in 99 aa, and to Mycobacterium leprae heat shock protein ClpB or ML2490 SWALL:Q9CB26 (EMBL:AL583925) (848 aa) fasta scores: E(): 0.66, 35.41% id in 96 aa. Note: Similar also to the C-terminal part of DIP2104 (849 aa) E(): 7.2e-08; 53.465% identity in 101 aa overlap. | 60 kDa chaperonin 1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.551 |
| clpB2 | groEL2 | DIP2101 | DIP2020 | Putative heat shock protein (partial); Similar to Corynebacterium glutamicum ClpB protein SWALL:CLPB_CORGL (SWALL:P53532) (852 aa) fasta scores: E(): 0.027, 44.44% id in 99 aa, and to Mycobacterium leprae heat shock protein ClpB or ML2490 SWALL:Q9CB26 (EMBL:AL583925) (848 aa) fasta scores: E(): 0.66, 35.41% id in 96 aa. Note: Similar also to the C-terminal part of DIP2104 (849 aa) E(): 7.2e-08; 53.465% identity in 101 aa overlap. | Chaperonin GroEL2; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.571 |
| clpB2 | groES | DIP2101 | DIP0575 | Putative heat shock protein (partial); Similar to Corynebacterium glutamicum ClpB protein SWALL:CLPB_CORGL (SWALL:P53532) (852 aa) fasta scores: E(): 0.027, 44.44% id in 99 aa, and to Mycobacterium leprae heat shock protein ClpB or ML2490 SWALL:Q9CB26 (EMBL:AL583925) (848 aa) fasta scores: E(): 0.66, 35.41% id in 96 aa. Note: Similar also to the C-terminal part of DIP2104 (849 aa) E(): 7.2e-08; 53.465% identity in 101 aa overlap. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.643 |
| clpB2 | grpE | DIP2101 | DIP2119 | Putative heat shock protein (partial); Similar to Corynebacterium glutamicum ClpB protein SWALL:CLPB_CORGL (SWALL:P53532) (852 aa) fasta scores: E(): 0.027, 44.44% id in 99 aa, and to Mycobacterium leprae heat shock protein ClpB or ML2490 SWALL:Q9CB26 (EMBL:AL583925) (848 aa) fasta scores: E(): 0.66, 35.41% id in 96 aa. Note: Similar also to the C-terminal part of DIP2104 (849 aa) E(): 7.2e-08; 53.465% identity in 101 aa overlap. | Chaperone protein cofactor GrpE; 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. Several rounds [...] | 0.882 |
| clpC | dnaJ1 | DIP1983 | DIP2118 | ATP-dependent Clp protease ATP-binding subunit; Similar to Bacillus subtilis negative regulator of genetic competence ClpC SW:CLPC_BACSU (P37571) (810 aa) fasta scores: E(): 2.6e-134, 58.11% id in 826 aa, and to Mycobacterium tuberculosis probable ATP-dependent Clp protease ATP-binding subunit Rv3596c SW:CLPC_MYCTU (O06286) (848 aa) fasta scores: E(): 1.7e-186, 81.81% id in 847 aa; Belongs to the ClpA/ClpB family. | Chaperone protein cofactor 1; 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 D [...] | 0.693 |
| clpC | dnaJ2 | DIP1983 | DIP1720 | ATP-dependent Clp protease ATP-binding subunit; Similar to Bacillus subtilis negative regulator of genetic competence ClpC SW:CLPC_BACSU (P37571) (810 aa) fasta scores: E(): 2.6e-134, 58.11% id in 826 aa, and to Mycobacterium tuberculosis probable ATP-dependent Clp protease ATP-binding subunit Rv3596c SW:CLPC_MYCTU (O06286) (848 aa) fasta scores: E(): 1.7e-186, 81.81% id in 847 aa; Belongs to the ClpA/ClpB family. | Chaperone protein 2; 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, DnaK [...] | 0.693 |
| clpC | dnaK | DIP1983 | DIP2120 | ATP-dependent Clp protease ATP-binding subunit; Similar to Bacillus subtilis negative regulator of genetic competence ClpC SW:CLPC_BACSU (P37571) (810 aa) fasta scores: E(): 2.6e-134, 58.11% id in 826 aa, and to Mycobacterium tuberculosis probable ATP-dependent Clp protease ATP-binding subunit Rv3596c SW:CLPC_MYCTU (O06286) (848 aa) fasta scores: E(): 1.7e-186, 81.81% id in 847 aa; Belongs to the ClpA/ClpB family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.959 |
| clpC | groEL1 | DIP1983 | DIP0576 | ATP-dependent Clp protease ATP-binding subunit; Similar to Bacillus subtilis negative regulator of genetic competence ClpC SW:CLPC_BACSU (P37571) (810 aa) fasta scores: E(): 2.6e-134, 58.11% id in 826 aa, and to Mycobacterium tuberculosis probable ATP-dependent Clp protease ATP-binding subunit Rv3596c SW:CLPC_MYCTU (O06286) (848 aa) fasta scores: E(): 1.7e-186, 81.81% id in 847 aa; Belongs to the ClpA/ClpB family. | 60 kDa chaperonin 1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.503 |
| clpC | groEL2 | DIP1983 | DIP2020 | ATP-dependent Clp protease ATP-binding subunit; Similar to Bacillus subtilis negative regulator of genetic competence ClpC SW:CLPC_BACSU (P37571) (810 aa) fasta scores: E(): 2.6e-134, 58.11% id in 826 aa, and to Mycobacterium tuberculosis probable ATP-dependent Clp protease ATP-binding subunit Rv3596c SW:CLPC_MYCTU (O06286) (848 aa) fasta scores: E(): 1.7e-186, 81.81% id in 847 aa; Belongs to the ClpA/ClpB family. | Chaperonin GroEL2; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.503 |
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