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 |
| lexA | polYA | BSU17850 | BSU23870 | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | DNA-damage lesion bypass DNA polymerase; 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 (By similarity). | 0.888 |
| lexA | polYB | BSU17850 | BSU23710 | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | Y family DNA polymerase V bypassing lesions during replication; 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 (By similarity). | 0.887 |
| lexA | uvrX | BSU17850 | BSU21500 | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | Lesion bypass phage DNA polymerase; Evidence 2b: Function of strongly homologous gene; enzyme. | 0.732 |
| lexA | yobH | BSU17850 | BSU18930 | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | Putative DNA repair protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the DNA polymerase type-Y family. | 0.620 |
| lexA | yozK | BSU17850 | BSU18940 | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | Putative DNA repair protein fragment; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; extrachromosomal origin. | 0.674 |
| lexA | yozL | BSU17850 | BSU18950 | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12137951. | 0.487 |
| lexA | yqjX | BSU17850 | BSU23700 | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12137951, 16267290. | 0.490 |
| polYA | lexA | BSU23870 | BSU17850 | DNA-damage lesion bypass DNA polymerase; 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 (By similarity). | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | 0.888 |
| polYA | uvrX | BSU23870 | BSU21500 | DNA-damage lesion bypass DNA polymerase; 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 (By similarity). | Lesion bypass phage DNA polymerase; Evidence 2b: Function of strongly homologous gene; enzyme. | 0.481 |
| polYA | yozK | BSU23870 | BSU18940 | DNA-damage lesion bypass DNA polymerase; 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 (By similarity). | Putative DNA repair protein fragment; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; extrachromosomal origin. | 0.759 |
| polYA | yozL | BSU23870 | BSU18950 | DNA-damage lesion bypass DNA polymerase; 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 (By similarity). | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12137951. | 0.689 |
| polYA | yqjX | BSU23870 | BSU23700 | DNA-damage lesion bypass DNA polymerase; 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 (By similarity). | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12137951, 16267290. | 0.693 |
| polYB | lexA | BSU23710 | BSU17850 | Y family DNA polymerase V bypassing lesions during replication; 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 (By similarity). | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | 0.887 |
| polYB | yozL | BSU23710 | BSU18950 | Y family DNA polymerase V bypassing lesions during replication; 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 (By similarity). | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12137951. | 0.689 |
| polYB | yqjX | BSU23710 | BSU23700 | Y family DNA polymerase V bypassing lesions during replication; 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 (By similarity). | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12137951, 16267290. | 0.935 |
| uvrX | lexA | BSU21500 | BSU17850 | Lesion bypass phage DNA polymerase; Evidence 2b: Function of strongly homologous gene; enzyme. | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | 0.732 |
| uvrX | polYA | BSU21500 | BSU23870 | Lesion bypass phage DNA polymerase; Evidence 2b: Function of strongly homologous gene; enzyme. | DNA-damage lesion bypass DNA polymerase; 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 (By similarity). | 0.481 |
| uvrX | yozL | BSU21500 | BSU18950 | Lesion bypass phage DNA polymerase; Evidence 2b: Function of strongly homologous gene; enzyme. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12137951. | 0.851 |
| uvrX | yqjX | BSU21500 | BSU23700 | Lesion bypass phage DNA polymerase; Evidence 2b: Function of strongly homologous gene; enzyme. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12137951, 16267290. | 0.866 |
| yobH | lexA | BSU18930 | BSU17850 | Putative DNA repair protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the DNA polymerase type-Y family. | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | 0.620 |
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