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 |
| dinB | dnaN | b0231 | b3701 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and 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 Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | DNA polymerase III, beta subunit; 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. DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA. In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent. Coordinates protein traffic at the replicati [...] | 0.999 |
| dinB | lexA | b0231 | b4043 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and 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 Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | Transcriptional repressor of SOS regulon; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. 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. Implicated in hydroxy radical-mediated cell death induced by hydroxyurea treatment .The SOS response controls an apoptotic-like death (ALD) induced (in the absence [...] | 0.959 |
| dinB | polA | b0231 | b3863 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and 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 Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | 5' to 3' DNA polymerase and 3' to 5'/5' to 3' exonuclease; In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. It is able to utilize nicked circular duplex DNA as a template and can unwind the parental DNA strand from its template. | 0.952 |
| dinB | polB | b0231 | b0060 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and 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 Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | DNA polymerase II; Thought to be involved in DNA repair and/or mutagenesis. Its processivity is enhanced by the beta sliding clamp (dnaN) and clamp loader. | 0.994 |
| dinB | recA | b0231 | b2699 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and 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 Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | DNA recombination and repair protein; Required for homologous recombination and the bypass of mutagenic DNA lesions by the SOS response. Catalyzes ATP-driven homologous pairing and strand exchange of DNA molecules necessary for DNA recombinational repair. Catalyzes 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. The SOS response controls an apoptotic-like death (ALD) induced (in the absence of the mazE-mazF toxin-antitoxin module) in resp [...] | 0.953 |
| dinB | umuC | b0231 | b1184 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and 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 Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | Translesion error-prone DNA polymerase V subunit; Involved in UV protection and mutation. Poorly processive, error-prone DNA polymerase involved in translesion repair. Essential for induced (or SOS) mutagenesis. Able to replicate DNA across DNA lesions (thymine photodimers and abasic sites, translesion synthesis) in the presence of activated RecA; efficiency is maximal in the presence of the beta sliding-clamp and clamp-loading complex of DNA polymerase III plus single-stranded binding protein (SSB). RecA and to a lesser extent the beta clamp- complex may target Pol V to replication co [...] | 0.721 |
| dinB | umuD | b0231 | b1183 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and 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 Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | Translesion error-prone DNA polymerase V subunit; Involved in UV protection and mutation. Poorly processive, error-prone DNA polymerase involved in translesion repair. Essential for induced (or SOS) mutagenesis. Able to replicate DNA across DNA lesions (thymine photodimers and abasic sites, called translesion synthesis) in the presence of activated RecA; efficiency is maximal in the presence of the beta sliding-clamp and clamp-loading complex of DNA polymerase III plus single-stranded binding protein (SSB). RecA and to a lesser extent the beta clamp-complex may target Pol V to replicat [...] | 0.991 |
| dinB | uvrA | b0231 | b4058 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and 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 Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | ATPase and DNA damage recognition protein of nucleotide excision repair excinuclease UvrABC; 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. | 0.882 |
| dinB | xthA | b0231 | b1749 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and 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 Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | Exonuclease III; Major apurinic-apyrimidinic endonuclease of E.coli. It removes the damaged DNA at cytosines and guanines by cleaving on the 3'-side of the AP site by a beta-elimination reaction. It exhibits 3'- 5'-exonuclease, 3'-phosphomonoesterase, 3'-repair diesterase and ribonuclease H activities. | 0.571 |
| dinB | ygdG | b0231 | b2798 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and 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 Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | Ssb-binding protein, misidentified as ExoIX; Has flap endonuclease activity , but does not seem to have exonuclease activity (and. During DNA replication, flap endonucleases cleave the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. | 0.466 |
| dnaN | dinB | b3701 | b0231 | DNA polymerase III, beta subunit; 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. DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA. In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent. Coordinates protein traffic at the replicati [...] | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and 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 Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | 0.999 |
| dnaN | lexA | b3701 | b4043 | DNA polymerase III, beta subunit; 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. DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA. In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent. Coordinates protein traffic at the replicati [...] | Transcriptional repressor of SOS regulon; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. 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. Implicated in hydroxy radical-mediated cell death induced by hydroxyurea treatment .The SOS response controls an apoptotic-like death (ALD) induced (in the absence [...] | 0.762 |
| dnaN | polA | b3701 | b3863 | DNA polymerase III, beta subunit; 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. DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA. In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent. Coordinates protein traffic at the replicati [...] | 5' to 3' DNA polymerase and 3' to 5'/5' to 3' exonuclease; In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. It is able to utilize nicked circular duplex DNA as a template and can unwind the parental DNA strand from its template. | 0.998 |
| dnaN | polB | b3701 | b0060 | DNA polymerase III, beta subunit; 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. DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA. In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent. Coordinates protein traffic at the replicati [...] | DNA polymerase II; Thought to be involved in DNA repair and/or mutagenesis. Its processivity is enhanced by the beta sliding clamp (dnaN) and clamp loader. | 0.998 |
| dnaN | recA | b3701 | b2699 | DNA polymerase III, beta subunit; 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. DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA. In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent. Coordinates protein traffic at the replicati [...] | DNA recombination and repair protein; Required for homologous recombination and the bypass of mutagenic DNA lesions by the SOS response. Catalyzes ATP-driven homologous pairing and strand exchange of DNA molecules necessary for DNA recombinational repair. Catalyzes 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. The SOS response controls an apoptotic-like death (ALD) induced (in the absence of the mazE-mazF toxin-antitoxin module) in resp [...] | 0.989 |
| dnaN | umuC | b3701 | b1184 | DNA polymerase III, beta subunit; 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. DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA. In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent. Coordinates protein traffic at the replicati [...] | Translesion error-prone DNA polymerase V subunit; Involved in UV protection and mutation. Poorly processive, error-prone DNA polymerase involved in translesion repair. Essential for induced (or SOS) mutagenesis. Able to replicate DNA across DNA lesions (thymine photodimers and abasic sites, translesion synthesis) in the presence of activated RecA; efficiency is maximal in the presence of the beta sliding-clamp and clamp-loading complex of DNA polymerase III plus single-stranded binding protein (SSB). RecA and to a lesser extent the beta clamp- complex may target Pol V to replication co [...] | 0.998 |
| dnaN | umuD | b3701 | b1183 | DNA polymerase III, beta subunit; 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. DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA. In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent. Coordinates protein traffic at the replicati [...] | Translesion error-prone DNA polymerase V subunit; Involved in UV protection and mutation. Poorly processive, error-prone DNA polymerase involved in translesion repair. Essential for induced (or SOS) mutagenesis. Able to replicate DNA across DNA lesions (thymine photodimers and abasic sites, called translesion synthesis) in the presence of activated RecA; efficiency is maximal in the presence of the beta sliding-clamp and clamp-loading complex of DNA polymerase III plus single-stranded binding protein (SSB). RecA and to a lesser extent the beta clamp-complex may target Pol V to replicat [...] | 0.984 |
| dnaN | uvrA | b3701 | b4058 | DNA polymerase III, beta subunit; 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. DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA. In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent. Coordinates protein traffic at the replicati [...] | ATPase and DNA damage recognition protein of nucleotide excision repair excinuclease UvrABC; 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. | 0.666 |
| dnaN | xthA | b3701 | b1749 | DNA polymerase III, beta subunit; 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. DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA. In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent. Coordinates protein traffic at the replicati [...] | Exonuclease III; Major apurinic-apyrimidinic endonuclease of E.coli. It removes the damaged DNA at cytosines and guanines by cleaving on the 3'-side of the AP site by a beta-elimination reaction. It exhibits 3'- 5'-exonuclease, 3'-phosphomonoesterase, 3'-repair diesterase and ribonuclease H activities. | 0.896 |
| dnaN | ygdG | b3701 | b2798 | DNA polymerase III, beta subunit; 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. DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA. In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent. Coordinates protein traffic at the replicati [...] | Ssb-binding protein, misidentified as ExoIX; Has flap endonuclease activity , but does not seem to have exonuclease activity (and. During DNA replication, flap endonucleases cleave the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. | 0.937 |
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