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 protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Rv3195 | Rv3716c | Rv3195 | Rv3716c | Rv3195, (MTV014.39), len: 472 aa. Hypothetical protein, equivalent to Q49746|ML0642|B1937_C3_231 hypothetical 50.3 KDA protein from Mycobacterium leprae (479 aa), FASTA scores: opt: 2503, E(): 1e-138, (79.35% identity in 475 aa overlap). Similar in part to Q9FCI9|2SC3B6.23c conserved hypothetical protein from Streptomyces coelicolor (487 aa), FASTA scores: opt: 1382,E(): 2.7e-73, (46.4% identity in 489 aa overlap); Q9X8I7|SCE9.14 hypothetical 41.2 KDA protein from Streptomyces coelicolor (375 aa), FASTA scores: opt: 319,E(): 2.4e-11, (25.6% identity in 383 aa overlap); etc. | Conserved protein; Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | 0.781 |
| Rv3195 | clpP1 | Rv3195 | Rv2461c | Rv3195, (MTV014.39), len: 472 aa. Hypothetical protein, equivalent to Q49746|ML0642|B1937_C3_231 hypothetical 50.3 KDA protein from Mycobacterium leprae (479 aa), FASTA scores: opt: 2503, E(): 1e-138, (79.35% identity in 475 aa overlap). Similar in part to Q9FCI9|2SC3B6.23c conserved hypothetical protein from Streptomyces coelicolor (487 aa), FASTA scores: opt: 1382,E(): 2.7e-73, (46.4% identity in 489 aa overlap); Q9X8I7|SCE9.14 hypothetical 41.2 KDA protein from Streptomyces coelicolor (375 aa), FASTA scores: opt: 319,E(): 2.4e-11, (25.6% identity in 383 aa overlap); etc. | Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family. | 0.444 |
| Rv3195 | clpP2 | Rv3195 | Rv2460c | Rv3195, (MTV014.39), len: 472 aa. Hypothetical protein, equivalent to Q49746|ML0642|B1937_C3_231 hypothetical 50.3 KDA protein from Mycobacterium leprae (479 aa), FASTA scores: opt: 2503, E(): 1e-138, (79.35% identity in 475 aa overlap). Similar in part to Q9FCI9|2SC3B6.23c conserved hypothetical protein from Streptomyces coelicolor (487 aa), FASTA scores: opt: 1382,E(): 2.7e-73, (46.4% identity in 489 aa overlap); Q9X8I7|SCE9.14 hypothetical 41.2 KDA protein from Streptomyces coelicolor (375 aa), FASTA scores: opt: 319,E(): 2.4e-11, (25.6% identity in 383 aa overlap); etc. | Probable ATP-dependent CLP protease proteolytic subunit 2 ClpP2 (endopeptidase CLP 2); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA. Belongs to the peptidase S14 family. | 0.807 |
| Rv3716c | Rv3195 | Rv3716c | Rv3195 | Conserved protein; Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | Rv3195, (MTV014.39), len: 472 aa. Hypothetical protein, equivalent to Q49746|ML0642|B1937_C3_231 hypothetical 50.3 KDA protein from Mycobacterium leprae (479 aa), FASTA scores: opt: 2503, E(): 1e-138, (79.35% identity in 475 aa overlap). Similar in part to Q9FCI9|2SC3B6.23c conserved hypothetical protein from Streptomyces coelicolor (487 aa), FASTA scores: opt: 1382,E(): 2.7e-73, (46.4% identity in 489 aa overlap); Q9X8I7|SCE9.14 hypothetical 41.2 KDA protein from Streptomyces coelicolor (375 aa), FASTA scores: opt: 319,E(): 2.4e-11, (25.6% identity in 383 aa overlap); etc. | 0.781 |
| Rv3716c | clpP1 | Rv3716c | Rv2461c | Conserved protein; Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family. | 0.465 |
| Rv3716c | clpP2 | Rv3716c | Rv2460c | Conserved protein; Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | Probable ATP-dependent CLP protease proteolytic subunit 2 ClpP2 (endopeptidase CLP 2); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA. Belongs to the peptidase S14 family. | 0.809 |
| Rv3716c | clpX | Rv3716c | Rv2457c | Conserved protein; Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | Probable ATP-dependent CLP protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpP2. Does not seem to act on anti-sigma-L factor RslA. | 0.420 |
| clpB | clpP1 | Rv0384c | Rv2461c | Probable endopeptidase ATP binding protein (chain B) ClpB (ClpB protein) (heat shock protein F84.1); 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 [...] | Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family. | 0.940 |
| clpB | clpP2 | Rv0384c | Rv2460c | Probable endopeptidase ATP binding protein (chain B) ClpB (ClpB protein) (heat shock protein F84.1); 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 [...] | Probable ATP-dependent CLP protease proteolytic subunit 2 ClpP2 (endopeptidase CLP 2); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA. Belongs to the peptidase S14 family. | 0.916 |
| clpB | clpX | Rv0384c | Rv2457c | Probable endopeptidase ATP binding protein (chain B) ClpB (ClpB protein) (heat shock protein F84.1); 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 [...] | Probable ATP-dependent CLP protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpP2. Does not seem to act on anti-sigma-L factor RslA. | 0.649 |
| clpB | groES | Rv0384c | Rv3418c | Probable endopeptidase ATP binding protein (chain B) ClpB (ClpB protein) (heat shock protein F84.1); 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 [...] | 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. | 0.891 |
| clpC1 | clpP1 | Rv3596c | Rv2461c | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family. | 0.997 |
| clpC1 | clpP2 | Rv3596c | Rv2460c | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | Probable ATP-dependent CLP protease proteolytic subunit 2 ClpP2 (endopeptidase CLP 2); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA. Belongs to the peptidase S14 family. | 0.996 |
| clpC1 | clpX | Rv3596c | Rv2457c | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | Probable ATP-dependent CLP protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpP2. Does not seem to act on anti-sigma-L factor RslA. | 0.822 |
| clpC1 | groES | Rv3596c | Rv3418c | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | 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. | 0.721 |
| clpC2 | clpP1 | Rv2667 | Rv2461c | Rv2667, (MTCY441.36), len: 252 aa. Possible clpC2,ATP-dependent protease atp-binding subunit, highly similar to Q9X8L2|SCE9.40 hypothetical 27.3 KDA protein from Streptomyces coelicolor (258 aa), FASTA scores: opt: 877,E(): 2.2e-46, (57.25% identity in 255 aa overlap). The second half of the protein is highly similar to N-terminal of several CLP-family proteins e.g. P24428|CLPC_MYCLE|ML0235 probable ATP-dependent CLP protease ATP-binding subunit from Mycobacterium leprae (848 aa), FASTA scores: opt: 307, E(): 3.2e-11, (38.6% identity in 158 aa overlap); O06286|CLPC_MYCTU|Rv3596c|MT3703 [...] | Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family. | 0.875 |
| clpC2 | clpP2 | Rv2667 | Rv2460c | Rv2667, (MTCY441.36), len: 252 aa. Possible clpC2,ATP-dependent protease atp-binding subunit, highly similar to Q9X8L2|SCE9.40 hypothetical 27.3 KDA protein from Streptomyces coelicolor (258 aa), FASTA scores: opt: 877,E(): 2.2e-46, (57.25% identity in 255 aa overlap). The second half of the protein is highly similar to N-terminal of several CLP-family proteins e.g. P24428|CLPC_MYCLE|ML0235 probable ATP-dependent CLP protease ATP-binding subunit from Mycobacterium leprae (848 aa), FASTA scores: opt: 307, E(): 3.2e-11, (38.6% identity in 158 aa overlap); O06286|CLPC_MYCTU|Rv3596c|MT3703 [...] | Probable ATP-dependent CLP protease proteolytic subunit 2 ClpP2 (endopeptidase CLP 2); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA. Belongs to the peptidase S14 family. | 0.816 |
| clpC2 | clpX | Rv2667 | Rv2457c | Rv2667, (MTCY441.36), len: 252 aa. Possible clpC2,ATP-dependent protease atp-binding subunit, highly similar to Q9X8L2|SCE9.40 hypothetical 27.3 KDA protein from Streptomyces coelicolor (258 aa), FASTA scores: opt: 877,E(): 2.2e-46, (57.25% identity in 255 aa overlap). The second half of the protein is highly similar to N-terminal of several CLP-family proteins e.g. P24428|CLPC_MYCLE|ML0235 probable ATP-dependent CLP protease ATP-binding subunit from Mycobacterium leprae (848 aa), FASTA scores: opt: 307, E(): 3.2e-11, (38.6% identity in 158 aa overlap); O06286|CLPC_MYCTU|Rv3596c|MT3703 [...] | Probable ATP-dependent CLP protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpP2. Does not seem to act on anti-sigma-L factor RslA. | 0.593 |
| clpC2 | groES | Rv2667 | Rv3418c | Rv2667, (MTCY441.36), len: 252 aa. Possible clpC2,ATP-dependent protease atp-binding subunit, highly similar to Q9X8L2|SCE9.40 hypothetical 27.3 KDA protein from Streptomyces coelicolor (258 aa), FASTA scores: opt: 877,E(): 2.2e-46, (57.25% identity in 255 aa overlap). The second half of the protein is highly similar to N-terminal of several CLP-family proteins e.g. P24428|CLPC_MYCLE|ML0235 probable ATP-dependent CLP protease ATP-binding subunit from Mycobacterium leprae (848 aa), FASTA scores: opt: 307, E(): 3.2e-11, (38.6% identity in 158 aa overlap); O06286|CLPC_MYCTU|Rv3596c|MT3703 [...] | 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. | 0.699 |
| clpP1 | Rv3195 | Rv2461c | Rv3195 | Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family. | Rv3195, (MTV014.39), len: 472 aa. Hypothetical protein, equivalent to Q49746|ML0642|B1937_C3_231 hypothetical 50.3 KDA protein from Mycobacterium leprae (479 aa), FASTA scores: opt: 2503, E(): 1e-138, (79.35% identity in 475 aa overlap). Similar in part to Q9FCI9|2SC3B6.23c conserved hypothetical protein from Streptomyces coelicolor (487 aa), FASTA scores: opt: 1382,E(): 2.7e-73, (46.4% identity in 489 aa overlap); Q9X8I7|SCE9.14 hypothetical 41.2 KDA protein from Streptomyces coelicolor (375 aa), FASTA scores: opt: 319,E(): 2.4e-11, (25.6% identity in 383 aa overlap); etc. | 0.444 |
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