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 |
| dinG | dnaN | L248_0348 | L248_1977 | ATP-dependent DNA helicase DinG; 3'-5' exonuclease. | DnaN; 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 replication as well as for [...] | 0.972 |
| dinG | pcrA | L248_0348 | L248_1483 | ATP-dependent DNA helicase DinG; 3'-5' exonuclease. | PcrA. | 0.911 |
| dinG | polA | L248_0348 | L248_0037 | ATP-dependent DNA helicase DinG; 3'-5' exonuclease. | PolA; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.994 |
| dinG | recJ | L248_0348 | L248_0439 | ATP-dependent DNA helicase DinG; 3'-5' exonuclease. | single-stranded-DNA-specific exonuclease. | 0.817 |
| dinG | uvrB | L248_0348 | L248_1307 | ATP-dependent DNA helicase DinG; 3'-5' exonuclease. | UvrB; 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 and the UvrB-DNA prein [...] | 0.489 |
| dinG | uvrC | L248_0348 | L248_0212 | ATP-dependent DNA helicase DinG; 3'-5' exonuclease. | UvrC; 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. | 0.757 |
| dnaN | dinG | L248_1977 | L248_0348 | DnaN; 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 replication as well as for [...] | ATP-dependent DNA helicase DinG; 3'-5' exonuclease. | 0.972 |
| dnaN | pcrA | L248_1977 | L248_1483 | DnaN; 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 replication as well as for [...] | PcrA. | 0.981 |
| dnaN | polA | L248_1977 | L248_0037 | DnaN; 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 replication as well as for [...] | PolA; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.999 |
| dnaN | recJ | L248_1977 | L248_0439 | DnaN; 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 replication as well as for [...] | single-stranded-DNA-specific exonuclease. | 0.655 |
| dnaN | uvrC | L248_1977 | L248_0212 | DnaN; 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 replication as well as for [...] | UvrC; 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. | 0.731 |
| murC | polA | L248_0036 | L248_0037 | MurC; Cell wall formation; Belongs to the MurCDEF family. | PolA; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.777 |
| murC | recJ | L248_0036 | L248_0439 | MurC; Cell wall formation; Belongs to the MurCDEF family. | single-stranded-DNA-specific exonuclease. | 0.408 |
| murC | uvrC | L248_0036 | L248_0212 | MurC; Cell wall formation; Belongs to the MurCDEF family. | UvrC; 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. | 0.757 |
| pcrA | dinG | L248_1483 | L248_0348 | PcrA. | ATP-dependent DNA helicase DinG; 3'-5' exonuclease. | 0.911 |
| pcrA | dnaN | L248_1483 | L248_1977 | PcrA. | DnaN; 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 replication as well as for [...] | 0.981 |
| pcrA | polA | L248_1483 | L248_0037 | PcrA. | PolA; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.960 |
| pcrA | recJ | L248_1483 | L248_0439 | PcrA. | single-stranded-DNA-specific exonuclease. | 0.638 |
| pcrA | uvrA | L248_1483 | L248_1308 | PcrA. | UvrA; 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. | 0.733 |
| pcrA | uvrA-2 | L248_1483 | L248_1426 | PcrA. | UvrA. | 0.691 |
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