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 |
| TP_0102 | dnaN | TP_0102 | TP_0002 | Rep helicase, single-stranded DNA-dependent ATPase (rep); Similar to GB:AE000783 percent identity: 45.60; identified by sequence similarity; putative. | DNA polymerase III, subunit beta (dnaN); Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initia [...] | 0.944 |
| TP_0102 | ligA | TP_0102 | TP_0634 | Rep helicase, single-stranded DNA-dependent ATPase (rep); Similar to GB:AE000783 percent identity: 45.60; identified by sequence similarity; putative. | DNA ligase (lig); DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | 0.808 |
| TP_0102 | mutL | TP_0102 | TP_0303 | Rep helicase, single-stranded DNA-dependent ATPase (rep); Similar to GB:AE000783 percent identity: 45.60; identified by sequence similarity; putative. | DNA mismatch repair protein (mutL); This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex (By similarity). | 0.948 |
| TP_0102 | radA | TP_0102 | TP_1022 | Rep helicase, single-stranded DNA-dependent ATPase (rep); Similar to GB:AE000783 percent identity: 45.60; identified by sequence similarity; putative. | DNA repair protein (sms); DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function. Belongs to the RecA family. RadA subfamily. | 0.747 |
| TP_0102 | uvrA | TP_0102 | TP_0514 | Rep helicase, single-stranded DNA-dependent ATPase (rep); Similar to GB:AE000783 percent identity: 45.60; identified by sequence similarity; putative. | Excinuclease ABC, subunit A (uvrA); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. | 0.637 |
| TP_0102 | uvrB | TP_0102 | TP_0116 | Rep helicase, single-stranded DNA-dependent ATPase (rep); Similar to GB:AE000783 percent identity: 45.60; identified by sequence similarity; putative. | Excinuclease ABC, subunit B (uvrB); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dis [...] | 0.944 |
| TP_0102 | uvrC | TP_0102 | TP_0472 | Rep helicase, single-stranded DNA-dependent ATPase (rep); Similar to GB:AE000783 percent identity: 45.60; identified by sequence similarity; putative. | Excinuclease ABC, subunit C (uvrC); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | 0.739 |
| TP_0102 | uvrD | TP_0102 | TP_1028 | Rep helicase, single-stranded DNA-dependent ATPase (rep); Similar to GB:AE000783 percent identity: 45.60; identified by sequence similarity; putative. | DNA helicase II (uvrD); Similar to GP:2618592 percent identity: 40.96; identified by sequence similarity; putative. | 0.937 |
| TP_0565 | uvrC | TP_0565 | TP_0472 | Predicted coding region TP0565; Hypothetical protein; identified by Glimmer; putative. | Excinuclease ABC, subunit C (uvrC); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | 0.707 |
| dnaN | TP_0102 | TP_0002 | TP_0102 | DNA polymerase III, subunit beta (dnaN); Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initia [...] | Rep helicase, single-stranded DNA-dependent ATPase (rep); Similar to GB:AE000783 percent identity: 45.60; identified by sequence similarity; putative. | 0.944 |
| dnaN | ligA | TP_0002 | TP_0634 | DNA polymerase III, subunit beta (dnaN); Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initia [...] | DNA ligase (lig); DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | 0.732 |
| dnaN | mutL | TP_0002 | TP_0303 | DNA polymerase III, subunit beta (dnaN); Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initia [...] | DNA mismatch repair protein (mutL); This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex (By similarity). | 0.999 |
| dnaN | mutY | TP_0002 | TP_0343 | DNA polymerase III, subunit beta (dnaN); Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initia [...] | A/G-specific adenine glycosylase, putative; Similar to GB:AE000511 PID:2313226 percent identity: 38.92; identified by sequence similarity; putative. | 0.692 |
| dnaN | radA | TP_0002 | TP_1022 | DNA polymerase III, subunit beta (dnaN); Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initia [...] | DNA repair protein (sms); DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function. Belongs to the RecA family. RadA subfamily. | 0.407 |
| dnaN | uvrA | TP_0002 | TP_0514 | DNA polymerase III, subunit beta (dnaN); Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initia [...] | Excinuclease ABC, subunit A (uvrA); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. | 0.483 |
| dnaN | uvrB | TP_0002 | TP_0116 | DNA polymerase III, subunit beta (dnaN); Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initia [...] | Excinuclease ABC, subunit B (uvrB); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dis [...] | 0.407 |
| dnaN | uvrC | TP_0002 | TP_0472 | DNA polymerase III, subunit beta (dnaN); Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initia [...] | Excinuclease ABC, subunit C (uvrC); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | 0.744 |
| dnaN | uvrD | TP_0002 | TP_1028 | DNA polymerase III, subunit beta (dnaN); Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initia [...] | DNA helicase II (uvrD); Similar to GP:2618592 percent identity: 40.96; identified by sequence similarity; putative. | 0.944 |
| ligA | TP_0102 | TP_0634 | TP_0102 | DNA ligase (lig); DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | Rep helicase, single-stranded DNA-dependent ATPase (rep); Similar to GB:AE000783 percent identity: 45.60; identified by sequence similarity; putative. | 0.808 |
| ligA | dnaN | TP_0634 | TP_0002 | DNA ligase (lig); DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | DNA polymerase III, subunit beta (dnaN); Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initia [...] | 0.732 |
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