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 |
| Rv2264c | dnaJ1 | Rv2264c | Rv0352 | Rv2264c, (MTV022.14c), len: 592 aa. Conserved hypothetical Pro-rich protein, similar to hypothetical proteins Rv0312 (MTCY63.17, 620 aa and Rv0350) that has highly Pro-, Thr-rich C-terminus. Contains PS00343 Gram-positive cocci surface proteins 'anchoring' hexapeptide. FASTA scores: Z96800|MTCY63_17 Mycobacterium tuberculosis cosmid (620 aa) opt: 1075, E(): 8.8e-24; (38.9% identity in 627 aa overlap). Predicted to be an outer membrane protein (See Song et al., 2008). | Probable chaperone protein DnaJ1; 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 betwe [...] | 0.939 |
| Rv2264c | dnaJ2 | Rv2264c | Rv2373c | Rv2264c, (MTV022.14c), len: 592 aa. Conserved hypothetical Pro-rich protein, similar to hypothetical proteins Rv0312 (MTCY63.17, 620 aa and Rv0350) that has highly Pro-, Thr-rich C-terminus. Contains PS00343 Gram-positive cocci surface proteins 'anchoring' hexapeptide. FASTA scores: Z96800|MTCY63_17 Mycobacterium tuberculosis cosmid (620 aa) opt: 1075, E(): 8.8e-24; (38.9% identity in 627 aa overlap). Predicted to be an outer membrane protein (See Song et al., 2008). | Probable chaperone protein DnaJ2; 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 betwe [...] | 0.942 |
| Rv2264c | groEL1 | Rv2264c | Rv3417c | Rv2264c, (MTV022.14c), len: 592 aa. Conserved hypothetical Pro-rich protein, similar to hypothetical proteins Rv0312 (MTCY63.17, 620 aa and Rv0350) that has highly Pro-, Thr-rich C-terminus. Contains PS00343 Gram-positive cocci surface proteins 'anchoring' hexapeptide. FASTA scores: Z96800|MTCY63_17 Mycobacterium tuberculosis cosmid (620 aa) opt: 1075, E(): 8.8e-24; (38.9% identity in 627 aa overlap). Predicted to be an outer membrane protein (See Song et al., 2008). | 60 kDa chaperonin 1 GroEL1 (protein CPN60-1) (GroEL protein 1); Prevents aggregation of substrate proteins and promotes their refolding. Functions in the absence of co-chaperone CH10 and ATP. | 0.853 |
| Rv2264c | groEL2 | Rv2264c | Rv0440 | Rv2264c, (MTV022.14c), len: 592 aa. Conserved hypothetical Pro-rich protein, similar to hypothetical proteins Rv0312 (MTCY63.17, 620 aa and Rv0350) that has highly Pro-, Thr-rich C-terminus. Contains PS00343 Gram-positive cocci surface proteins 'anchoring' hexapeptide. FASTA scores: Z96800|MTCY63_17 Mycobacterium tuberculosis cosmid (620 aa) opt: 1075, E(): 8.8e-24; (38.9% identity in 627 aa overlap). Predicted to be an outer membrane protein (See Song et al., 2008). | 60 kDa chaperonin 2; Prevents aggregation of substrate proteins and promotes their refolding. | 0.850 |
| Rv2264c | groES | Rv2264c | Rv3418c | Rv2264c, (MTV022.14c), len: 592 aa. Conserved hypothetical Pro-rich protein, similar to hypothetical proteins Rv0312 (MTCY63.17, 620 aa and Rv0350) that has highly Pro-, Thr-rich C-terminus. Contains PS00343 Gram-positive cocci surface proteins 'anchoring' hexapeptide. FASTA scores: Z96800|MTCY63_17 Mycobacterium tuberculosis cosmid (620 aa) opt: 1075, E(): 8.8e-24; (38.9% identity in 627 aa overlap). Predicted to be an outer membrane protein (See Song et al., 2008). | 10 kDa chaperonin GroES (protein CPN10) (protein GroES) (BCG-a heat shock protein) (10 kDa antigen); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.824 |
| Rv2264c | grpE | Rv2264c | Rv0351 | Rv2264c, (MTV022.14c), len: 592 aa. Conserved hypothetical Pro-rich protein, similar to hypothetical proteins Rv0312 (MTCY63.17, 620 aa and Rv0350) that has highly Pro-, Thr-rich C-terminus. Contains PS00343 Gram-positive cocci surface proteins 'anchoring' hexapeptide. FASTA scores: Z96800|MTCY63_17 Mycobacterium tuberculosis cosmid (620 aa) opt: 1075, E(): 8.8e-24; (38.9% identity in 627 aa overlap). Predicted to be an outer membrane protein (See Song et al., 2008). | Probable GrpE protein (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 cycle. Severa [...] | 0.961 |
| Rv2264c | hrcA | Rv2264c | Rv2374c | Rv2264c, (MTV022.14c), len: 592 aa. Conserved hypothetical Pro-rich protein, similar to hypothetical proteins Rv0312 (MTCY63.17, 620 aa and Rv0350) that has highly Pro-, Thr-rich C-terminus. Contains PS00343 Gram-positive cocci surface proteins 'anchoring' hexapeptide. FASTA scores: Z96800|MTCY63_17 Mycobacterium tuberculosis cosmid (620 aa) opt: 1075, E(): 8.8e-24; (38.9% identity in 627 aa overlap). Predicted to be an outer membrane protein (See Song et al., 2008). | Probable heat shock protein transcriptional repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons; Belongs to the HrcA family. | 0.770 |
| Rv2264c | htpG | Rv2264c | Rv2299c | Rv2264c, (MTV022.14c), len: 592 aa. Conserved hypothetical Pro-rich protein, similar to hypothetical proteins Rv0312 (MTCY63.17, 620 aa and Rv0350) that has highly Pro-, Thr-rich C-terminus. Contains PS00343 Gram-positive cocci surface proteins 'anchoring' hexapeptide. FASTA scores: Z96800|MTCY63_17 Mycobacterium tuberculosis cosmid (620 aa) opt: 1075, E(): 8.8e-24; (38.9% identity in 627 aa overlap). Predicted to be an outer membrane protein (See Song et al., 2008). | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.977 |
| Rv2264c | hycE | Rv2264c | Rv0087 | Rv2264c, (MTV022.14c), len: 592 aa. Conserved hypothetical Pro-rich protein, similar to hypothetical proteins Rv0312 (MTCY63.17, 620 aa and Rv0350) that has highly Pro-, Thr-rich C-terminus. Contains PS00343 Gram-positive cocci surface proteins 'anchoring' hexapeptide. FASTA scores: Z96800|MTCY63_17 Mycobacterium tuberculosis cosmid (620 aa) opt: 1075, E(): 8.8e-24; (38.9% identity in 627 aa overlap). Predicted to be an outer membrane protein (See Song et al., 2008). | Possible formate hydrogenase HycE (FHL); Rv0087, (MTCY251.05), len: 492 aa. Possible hycE (alternate gene name: hevE), formate hydrogenlyase, similar to others. Belongs to the complex I 49 kDa subunit family. | 0.432 |
| dnaJ1 | Rv2264c | Rv0352 | Rv2264c | Probable chaperone protein DnaJ1; 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 betwe [...] | Rv2264c, (MTV022.14c), len: 592 aa. Conserved hypothetical Pro-rich protein, similar to hypothetical proteins Rv0312 (MTCY63.17, 620 aa and Rv0350) that has highly Pro-, Thr-rich C-terminus. Contains PS00343 Gram-positive cocci surface proteins 'anchoring' hexapeptide. FASTA scores: Z96800|MTCY63_17 Mycobacterium tuberculosis cosmid (620 aa) opt: 1075, E(): 8.8e-24; (38.9% identity in 627 aa overlap). Predicted to be an outer membrane protein (See Song et al., 2008). | 0.939 |
| dnaJ1 | dnaK | Rv0352 | Rv0350 | Probable chaperone protein DnaJ1; 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 betwe [...] | Probable 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. | 0.999 |
| dnaJ1 | groEL1 | Rv0352 | Rv3417c | Probable chaperone protein DnaJ1; 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 betwe [...] | 60 kDa chaperonin 1 GroEL1 (protein CPN60-1) (GroEL protein 1); Prevents aggregation of substrate proteins and promotes their refolding. Functions in the absence of co-chaperone CH10 and ATP. | 0.973 |
| dnaJ1 | groEL2 | Rv0352 | Rv0440 | Probable chaperone protein DnaJ1; 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 betwe [...] | 60 kDa chaperonin 2; Prevents aggregation of substrate proteins and promotes their refolding. | 0.987 |
| dnaJ1 | groES | Rv0352 | Rv3418c | Probable chaperone protein DnaJ1; 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 betwe [...] | 10 kDa chaperonin GroES (protein CPN10) (protein GroES) (BCG-a heat shock protein) (10 kDa antigen); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.872 |
| dnaJ1 | grpE | Rv0352 | Rv0351 | Probable chaperone protein DnaJ1; 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 betwe [...] | Probable GrpE protein (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 cycle. Severa [...] | 0.999 |
| dnaJ1 | hrcA | Rv0352 | Rv2374c | Probable chaperone protein DnaJ1; 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 betwe [...] | Probable heat shock protein transcriptional repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons; Belongs to the HrcA family. | 0.842 |
| dnaJ1 | htpG | Rv0352 | Rv2299c | Probable chaperone protein DnaJ1; 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 betwe [...] | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.965 |
| dnaJ2 | Rv2264c | Rv2373c | Rv2264c | Probable chaperone protein DnaJ2; 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 betwe [...] | Rv2264c, (MTV022.14c), len: 592 aa. Conserved hypothetical Pro-rich protein, similar to hypothetical proteins Rv0312 (MTCY63.17, 620 aa and Rv0350) that has highly Pro-, Thr-rich C-terminus. Contains PS00343 Gram-positive cocci surface proteins 'anchoring' hexapeptide. FASTA scores: Z96800|MTCY63_17 Mycobacterium tuberculosis cosmid (620 aa) opt: 1075, E(): 8.8e-24; (38.9% identity in 627 aa overlap). Predicted to be an outer membrane protein (See Song et al., 2008). | 0.942 |
| dnaJ2 | dnaK | Rv2373c | Rv0350 | Probable chaperone protein DnaJ2; 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 betwe [...] | Probable 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. | 0.996 |
| dnaJ2 | groEL1 | Rv2373c | Rv3417c | Probable chaperone protein DnaJ2; 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 betwe [...] | 60 kDa chaperonin 1 GroEL1 (protein CPN60-1) (GroEL protein 1); Prevents aggregation of substrate proteins and promotes their refolding. Functions in the absence of co-chaperone CH10 and ATP. | 0.940 |
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