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 |
| dinB | dnaE2 | CC_2466 | CC_3211 | DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | DNA polymerase III, alpha subunit, putative; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). Along with ImuA and ImuB is required for the error-prone processing of DNA lesions (By similarity). | 0.883 |
| dinB | imuB | CC_2466 | CC_3212 | DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | Hypothetical protein; Along with DnaE2 and ImuA is required for the error-prone processing of DNA lesions. | 0.798 |
| dinB | lexA | CC_2466 | CC_1902 | DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | Repressor LexA; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. | 0.953 |
| dinB | recA | CC_2466 | CC_1087 | DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | recA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family. | 0.934 |
| dinB | recR | CC_2466 | CC_0269 | DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | Recombination protein RecR; May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. | 0.426 |
| dinB | ruvB | CC_2466 | CC_3236 | DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | Holliday junction DNA helicase RuvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. | 0.583 |
| dinB | uvrA | CC_2466 | CC_2590 | DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | Excinuclease ABC, subunit A; 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. | 0.865 |
| dinB | uvrB | CC_2466 | CC_2981 | DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | Excinuclease ABC, subunit B; 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 dissociate [...] | 0.786 |
| dinB | uvrC | CC_2466 | CC_2881 | DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | Excinuclease ABC, subunit C; 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. | 0.673 |
| dnaE2 | dinB | CC_3211 | CC_2466 | DNA polymerase III, alpha subunit, putative; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). Along with ImuA and ImuB is required for the error-prone processing of DNA lesions (By similarity). | DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | 0.883 |
| dnaE2 | imuB | CC_3211 | CC_3212 | DNA polymerase III, alpha subunit, putative; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). Along with ImuA and ImuB is required for the error-prone processing of DNA lesions (By similarity). | Hypothetical protein; Along with DnaE2 and ImuA is required for the error-prone processing of DNA lesions. | 0.986 |
| dnaE2 | lexA | CC_3211 | CC_1902 | DNA polymerase III, alpha subunit, putative; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). Along with ImuA and ImuB is required for the error-prone processing of DNA lesions (By similarity). | Repressor LexA; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. | 0.785 |
| dnaE2 | recA | CC_3211 | CC_1087 | DNA polymerase III, alpha subunit, putative; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). Along with ImuA and ImuB is required for the error-prone processing of DNA lesions (By similarity). | recA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family. | 0.800 |
| dnaE2 | ruvB | CC_3211 | CC_3236 | DNA polymerase III, alpha subunit, putative; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). Along with ImuA and ImuB is required for the error-prone processing of DNA lesions (By similarity). | Holliday junction DNA helicase RuvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. | 0.497 |
| dnaE2 | uvrA | CC_3211 | CC_2590 | DNA polymerase III, alpha subunit, putative; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). Along with ImuA and ImuB is required for the error-prone processing of DNA lesions (By similarity). | Excinuclease ABC, subunit A; 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. | 0.782 |
| dnaE2 | uvrB | CC_3211 | CC_2981 | DNA polymerase III, alpha subunit, putative; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). Along with ImuA and ImuB is required for the error-prone processing of DNA lesions (By similarity). | Excinuclease ABC, subunit B; 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 dissociate [...] | 0.520 |
| dnaE2 | uvrC | CC_3211 | CC_2881 | DNA polymerase III, alpha subunit, putative; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). Along with ImuA and ImuB is required for the error-prone processing of DNA lesions (By similarity). | Excinuclease ABC, subunit C; 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. | 0.578 |
| imuB | dinB | CC_3212 | CC_2466 | Hypothetical protein; Along with DnaE2 and ImuA is required for the error-prone processing of DNA lesions. | DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | 0.798 |
| imuB | dnaE2 | CC_3212 | CC_3211 | Hypothetical protein; Along with DnaE2 and ImuA is required for the error-prone processing of DNA lesions. | DNA polymerase III, alpha subunit, putative; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). Along with ImuA and ImuB is required for the error-prone processing of DNA lesions (By similarity). | 0.986 |
| imuB | lexA | CC_3212 | CC_1902 | Hypothetical protein; Along with DnaE2 and ImuA is required for the error-prone processing of DNA lesions. | Repressor LexA; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. | 0.935 |
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