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 |
| ABP70061.1 | ABP71940.1 | Rsph17025_1160 | Rsph17025_3056 | PFAM: helicase domain protein; nucleic acid binding, OB-fold, tRNA/helicase-type; DEAD/DEAH box helicase domain protein; SMART: DEAD-like helicases-like. | TIGRFAM: Mg chelatase, subunit ChlI; PFAM: magnesium chelatase, ChlI subunit; ATPase associated with various cellular activities, AAA_5; SMART: AAA ATPase. | 0.410 |
| ABP70061.1 | lexA | Rsph17025_1160 | Rsph17025_3094 | PFAM: helicase domain protein; nucleic acid binding, OB-fold, tRNA/helicase-type; DEAD/DEAH box helicase domain protein; SMART: DEAD-like helicases-like. | SOS-response transcriptional repressor, LexA; 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. | 0.527 |
| ABP70061.1 | polA | Rsph17025_1160 | Rsph17025_0200 | PFAM: helicase domain protein; nucleic acid binding, OB-fold, tRNA/helicase-type; DEAD/DEAH box helicase domain protein; SMART: DEAD-like helicases-like. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.744 |
| ABP70061.1 | ruvA | Rsph17025_1160 | Rsph17025_1231 | PFAM: helicase domain protein; nucleic acid binding, OB-fold, tRNA/helicase-type; DEAD/DEAH box helicase domain protein; SMART: DEAD-like helicases-like. | Holliday junction DNA helicase RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. | 0.690 |
| ABP70061.1 | ruvB | Rsph17025_1160 | Rsph17025_1233 | PFAM: helicase domain protein; nucleic acid binding, OB-fold, tRNA/helicase-type; DEAD/DEAH box helicase domain protein; SMART: DEAD-like helicases-like. | Holliday junction DNA helicase RuvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. | 0.630 |
| ABP70061.1 | ruvC | Rsph17025_1160 | Rsph17025_1230 | PFAM: helicase domain protein; nucleic acid binding, OB-fold, tRNA/helicase-type; DEAD/DEAH box helicase domain protein; SMART: DEAD-like helicases-like. | Crossover junction endodeoxyribonuclease RuvC; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. | 0.615 |
| ABP71940.1 | ABP70061.1 | Rsph17025_3056 | Rsph17025_1160 | TIGRFAM: Mg chelatase, subunit ChlI; PFAM: magnesium chelatase, ChlI subunit; ATPase associated with various cellular activities, AAA_5; SMART: AAA ATPase. | PFAM: helicase domain protein; nucleic acid binding, OB-fold, tRNA/helicase-type; DEAD/DEAH box helicase domain protein; SMART: DEAD-like helicases-like. | 0.410 |
| ABP71940.1 | def-3 | Rsph17025_3056 | Rsph17025_0150 | TIGRFAM: Mg chelatase, subunit ChlI; PFAM: magnesium chelatase, ChlI subunit; ATPase associated with various cellular activities, AAA_5; SMART: AAA ATPase. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Belongs to the polypeptide deformylase family. | 0.502 |
| ABP71940.1 | ruvC | Rsph17025_3056 | Rsph17025_1230 | TIGRFAM: Mg chelatase, subunit ChlI; PFAM: magnesium chelatase, ChlI subunit; ATPase associated with various cellular activities, AAA_5; SMART: AAA ATPase. | Crossover junction endodeoxyribonuclease RuvC; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. | 0.687 |
| def | def-2 | Rsph17025_0148 | Rsph17025_0149 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.812 |
| def | def-3 | Rsph17025_0148 | Rsph17025_0150 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Belongs to the polypeptide deformylase family. | 0.809 |
| def | polA | Rsph17025_0148 | Rsph17025_0200 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.490 |
| def | ruvC | Rsph17025_0148 | Rsph17025_1230 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Crossover junction endodeoxyribonuclease RuvC; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. | 0.628 |
| def-2 | def | Rsph17025_0149 | Rsph17025_0148 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.812 |
| def-2 | def-3 | Rsph17025_0149 | Rsph17025_0150 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Belongs to the polypeptide deformylase family. | 0.838 |
| def-2 | polA | Rsph17025_0149 | Rsph17025_0200 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.459 |
| def-2 | ruvC | Rsph17025_0149 | Rsph17025_1230 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Crossover junction endodeoxyribonuclease RuvC; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. | 0.594 |
| def-3 | ABP71940.1 | Rsph17025_0150 | Rsph17025_3056 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Belongs to the polypeptide deformylase family. | TIGRFAM: Mg chelatase, subunit ChlI; PFAM: magnesium chelatase, ChlI subunit; ATPase associated with various cellular activities, AAA_5; SMART: AAA ATPase. | 0.502 |
| def-3 | def | Rsph17025_0150 | Rsph17025_0148 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Belongs to the polypeptide deformylase family. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.809 |
| def-3 | def-2 | Rsph17025_0150 | Rsph17025_0149 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Belongs to the polypeptide deformylase family. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.838 |
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