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 |
| ABZ98262.1 | dinP | LEPBI_I2161 | LEPBI_II0150 | Putative DNA polymerase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | DNA polymerase IV, devoid of proofreading, 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. | 0.974 |
| ABZ98262.1 | dnaN | LEPBI_I2161 | LEPBI_I0002 | Putative DNA polymerase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | DNA polymerase III, beta chain; 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 initiation of r [...] | 0.990 |
| ABZ98262.1 | polA | LEPBI_I2161 | LEPBI_I0674 | Putative DNA polymerase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | DNA polymerase I (POL I); In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.981 |
| ABZ98262.1 | recA | LEPBI_I2161 | LEPBI_I2446 | Putative DNA polymerase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Protein RecA (Recombinase A); 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. | 0.820 |
| ABZ98262.1 | uvrA | LEPBI_I2161 | LEPBI_I1837 | Putative DNA polymerase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | UvrABC system protein A (UvrA protein; 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. | 0.467 |
| ABZ99683.1 | ABZ99684.1 | LEPBI_II0148 | LEPBI_II0149 | Conserved hypothetical protein; Homologs of previously reported genes of unknown function. | Conserved hypothetical protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.786 |
| ABZ99683.1 | dinP | LEPBI_II0148 | LEPBI_II0150 | Conserved hypothetical protein; Homologs of previously reported genes of unknown function. | DNA polymerase IV, devoid of proofreading, 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. | 0.819 |
| ABZ99684.1 | ABZ99683.1 | LEPBI_II0149 | LEPBI_II0148 | Conserved hypothetical protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Conserved hypothetical protein; Homologs of previously reported genes of unknown function. | 0.786 |
| ABZ99684.1 | dinP | LEPBI_II0149 | LEPBI_II0150 | Conserved hypothetical protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | DNA polymerase IV, devoid of proofreading, 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. | 0.862 |
| dinP | ABZ98262.1 | LEPBI_II0150 | LEPBI_I2161 | DNA polymerase IV, devoid of proofreading, 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. | Putative DNA polymerase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.974 |
| dinP | ABZ99683.1 | LEPBI_II0150 | LEPBI_II0148 | DNA polymerase IV, devoid of proofreading, 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. | Conserved hypothetical protein; Homologs of previously reported genes of unknown function. | 0.819 |
| dinP | ABZ99684.1 | LEPBI_II0150 | LEPBI_II0149 | DNA polymerase IV, devoid of proofreading, 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. | Conserved hypothetical protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.862 |
| dinP | dnaE | LEPBI_II0150 | LEPBI_I2936 | DNA polymerase IV, devoid of proofreading, 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; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.766 |
| dinP | dnaN | LEPBI_II0150 | LEPBI_I0002 | DNA polymerase IV, devoid of proofreading, 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, beta chain; 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 initiation of r [...] | 0.986 |
| dinP | flgL | LEPBI_II0150 | LEPBI_I3212 | DNA polymerase IV, devoid of proofreading, 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. | Flagellar hook-associated protein 3 (HAP3); Function of homologous gene experimentally demonstrated in an other organism; structure. | 0.751 |
| dinP | lexA | LEPBI_II0150 | LEPBI_I1316 | DNA polymerase IV, devoid of proofreading, 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. | LexA repressor; 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. | 0.923 |
| dinP | polA | LEPBI_II0150 | LEPBI_I0674 | DNA polymerase IV, devoid of proofreading, 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 I (POL I); In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.825 |
| dinP | recA | LEPBI_II0150 | LEPBI_I2446 | DNA polymerase IV, devoid of proofreading, 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. | Protein RecA (Recombinase A); 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. | 0.932 |
| dinP | uvrA | LEPBI_II0150 | LEPBI_I1837 | DNA polymerase IV, devoid of proofreading, 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. | UvrABC system protein A (UvrA protein; 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. | 0.765 |
| dnaE | dinP | LEPBI_I2936 | LEPBI_II0150 | DNA polymerase III alpha subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | DNA polymerase IV, devoid of proofreading, 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. | 0.766 |
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