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 |
| OIJ24237.1 | OIJ25257.1 | UG56_023850 | UG56_018670 | Peptidylprolyl isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cell division protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family. | 0.712 |
| OIJ24237.1 | OIJ26164.1 | UG56_023850 | UG56_014190 | Peptidylprolyl isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Rod shape-determining protein RodA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family. | 0.712 |
| OIJ24237.1 | OIJ28744.1 | UG56_023850 | UG56_000485 | Peptidylprolyl isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.409 |
| OIJ24237.1 | UG56_015255 | UG56_023850 | UG56_015255 | Peptidylprolyl isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family. | 0.712 |
| OIJ24237.1 | dinB-2 | UG56_023850 | UG56_022855 | Peptidylprolyl isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | DNA polymerase IV; 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. | 0.720 |
| OIJ25216.1 | OIJ25257.1 | UG56_018435 | UG56_018670 | DNA polymerase III subunit beta; 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 [...] | Cell division protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family. | 0.407 |
| OIJ25216.1 | OIJ27154.1 | UG56_018435 | UG56_008830 | DNA polymerase III subunit beta; 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 [...] | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.875 |
| OIJ25216.1 | UG56_015255 | UG56_018435 | UG56_015255 | DNA polymerase III subunit beta; 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 [...] | Undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family. | 0.484 |
| OIJ25216.1 | dinB-2 | UG56_018435 | UG56_022855 | DNA polymerase III subunit beta; 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 [...] | DNA polymerase IV; 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. | 0.910 |
| OIJ25216.1 | recA | UG56_018435 | UG56_026430 | DNA polymerase III subunit beta; 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 [...] | Recombinase RecA; 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. | 0.955 |
| OIJ25257.1 | OIJ24237.1 | UG56_018670 | UG56_023850 | Cell division protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family. | Peptidylprolyl isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.712 |
| OIJ25257.1 | OIJ25216.1 | UG56_018670 | UG56_018435 | Cell division protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family. | DNA polymerase III subunit beta; 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 [...] | 0.407 |
| OIJ25257.1 | OIJ28744.1 | UG56_018670 | UG56_000485 | Cell division protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.712 |
| OIJ25257.1 | UG56_015255 | UG56_018670 | UG56_015255 | Cell division protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family. | Undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family. | 0.484 |
| OIJ25257.1 | dinB-2 | UG56_018670 | UG56_022855 | Cell division protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family. | DNA polymerase IV; 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. | 0.734 |
| OIJ25471.1 | dinB-2 | UG56_017900 | UG56_022855 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | DNA polymerase IV; 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. | 0.754 |
| OIJ25471.1 | recA | UG56_017900 | UG56_026430 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Recombinase RecA; 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. | 0.552 |
| OIJ26164.1 | OIJ24237.1 | UG56_014190 | UG56_023850 | Rod shape-determining protein RodA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family. | Peptidylprolyl isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.712 |
| OIJ26164.1 | OIJ28744.1 | UG56_014190 | UG56_000485 | Rod shape-determining protein RodA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.712 |
| OIJ26164.1 | dinB-2 | UG56_014190 | UG56_022855 | Rod shape-determining protein RodA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family. | DNA polymerase IV; 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. | 0.734 |
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