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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| defA | mhqR | BSU15720 | BSU13670 | 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 (By similarity). | Transcriptional regulator (MarR family); Negatively regulates mhqA, mhqED, mhqNOP, and azoR2 which may contribute to the degradation of aromatic compounds. | 0.493 |
| defA | yfiV | BSU15720 | BSU08410 | 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 (By similarity). | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.639 |
| defA | ypoP | BSU15720 | BSU21700 | 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 (By similarity). | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.638 |
| defA | ysmB | BSU15720 | BSU28400 | 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 (By similarity). | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.568 |
| defB | mhqR | BSU14560 | BSU13670 | Formylmethionine deformylase A; 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. | Transcriptional regulator (MarR family); Negatively regulates mhqA, mhqED, mhqNOP, and azoR2 which may contribute to the degradation of aromatic compounds. | 0.495 |
| defB | yfiV | BSU14560 | BSU08410 | Formylmethionine deformylase A; 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. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.582 |
| defB | ypoP | BSU14560 | BSU21700 | Formylmethionine deformylase A; 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. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.588 |
| defB | ysmB | BSU14560 | BSU28400 | Formylmethionine deformylase A; 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. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.501 |
| mhqR | defA | BSU13670 | BSU15720 | Transcriptional regulator (MarR family); Negatively regulates mhqA, mhqED, mhqNOP, and azoR2 which may contribute to the degradation of aromatic compounds. | 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 (By similarity). | 0.493 |
| mhqR | defB | BSU13670 | BSU14560 | Transcriptional regulator (MarR family); Negatively regulates mhqA, mhqED, mhqNOP, and azoR2 which may contribute to the degradation of aromatic compounds. | Formylmethionine deformylase A; 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. | 0.495 |
| mhqR | yfiV | BSU13670 | BSU08410 | Transcriptional regulator (MarR family); Negatively regulates mhqA, mhqED, mhqNOP, and azoR2 which may contribute to the degradation of aromatic compounds. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.632 |
| mhqR | yfmP | BSU13670 | BSU07390 | Transcriptional regulator (MarR family); Negatively regulates mhqA, mhqED, mhqNOP, and azoR2 which may contribute to the degradation of aromatic compounds. | Transcriptional regulator (MerR family) of metal efflux transporter expression; Repressor of the yfmOP operon. A mutation in yfmP leads to overexpression of yfmO, probably causing a decrease in cellular copper that is eventually responsible for a reduced copper induction of copZA. | 0.450 |
| mhqR | ypoP | BSU13670 | BSU21700 | Transcriptional regulator (MarR family); Negatively regulates mhqA, mhqED, mhqNOP, and azoR2 which may contribute to the degradation of aromatic compounds. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.466 |
| mhqR | ywaE | BSU13670 | BSU38450 | Transcriptional regulator (MarR family); Negatively regulates mhqA, mhqED, mhqNOP, and azoR2 which may contribute to the degradation of aromatic compounds. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.913 |
| mprF | yfiU | BSU08425 | BSU08400 | Phosphatidylglycerol lysyltransferase involved in lysinylation of phospholipids; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects B.subtilis against its own CAMPs and against those produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with po [...] | Putative efflux transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. | 0.404 |
| mprF | yfiV | BSU08425 | BSU08410 | Phosphatidylglycerol lysyltransferase involved in lysinylation of phospholipids; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects B.subtilis against its own CAMPs and against those produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with po [...] | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.562 |
| yfiU | mprF | BSU08400 | BSU08425 | Putative efflux transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. | Phosphatidylglycerol lysyltransferase involved in lysinylation of phospholipids; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects B.subtilis against its own CAMPs and against those produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with po [...] | 0.404 |
| yfiU | yfiV | BSU08400 | BSU08410 | Putative efflux transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.515 |
| yfiV | defA | BSU08410 | BSU15720 | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 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 (By similarity). | 0.639 |
| yfiV | defB | BSU08410 | BSU14560 | Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | Formylmethionine deformylase A; 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. | 0.582 |
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