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 |
| blt | bmrA | BSU26590 | BSU34820 | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | Efflux transporter (ATP-binding and permease protein); An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). | 0.917 |
| blt | mdr | BSU26590 | BSU03070 | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | 0.938 |
| bmrA | blt | BSU34820 | BSU26590 | Efflux transporter (ATP-binding and permease protein); An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | 0.917 |
| bmrA | ebrA | BSU34820 | BSU17300 | Efflux transporter (ATP-binding and permease protein); An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). | Small multidrug resistance efflux transporter; Part of a multidrug efflux pump. Confers resistance to cationic lipophilic dyes such as ethidium bromide, acriflavine, pyronine Y and safranin O. The efflux is probably coupled to an influx of protons (By similarity). | 0.564 |
| bmrA | mdr | BSU34820 | BSU03070 | Efflux transporter (ATP-binding and permease protein); An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | 0.850 |
| ebrA | bmrA | BSU17300 | BSU34820 | Small multidrug resistance efflux transporter; Part of a multidrug efflux pump. Confers resistance to cationic lipophilic dyes such as ethidium bromide, acriflavine, pyronine Y and safranin O. The efflux is probably coupled to an influx of protons (By similarity). | Efflux transporter (ATP-binding and permease protein); An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). | 0.564 |
| ebrA | mdr | BSU17300 | BSU03070 | Small multidrug resistance efflux transporter; Part of a multidrug efflux pump. Confers resistance to cationic lipophilic dyes such as ethidium bromide, acriflavine, pyronine Y and safranin O. The efflux is probably coupled to an influx of protons (By similarity). | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | 0.600 |
| mdr | blt | BSU03070 | BSU26590 | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | 0.938 |
| mdr | bmrA | BSU03070 | BSU34820 | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | Efflux transporter (ATP-binding and permease protein); An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). | 0.850 |
| mdr | ebrA | BSU03070 | BSU17300 | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | Small multidrug resistance efflux transporter; Part of a multidrug efflux pump. Confers resistance to cationic lipophilic dyes such as ethidium bromide, acriflavine, pyronine Y and safranin O. The efflux is probably coupled to an influx of protons (By similarity). | 0.600 |
| mdr | tcyN | BSU03070 | BSU29340 | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | Sulfur-containing amino-acid ABC transporter (ATP-binding protein); Part of the ABC transporter complex TcyJKLMN involved in L- cystine import. Responsible for energy coupling to the transport system (Probable). Is also involved in cystathionine, djenkolate, and S- methylcysteine transport; Belongs to the ABC transporter superfamily. L-cystine importer (TC 3.A.1.3.13) family. | 0.745 |
| mdr | ureA | BSU03070 | BSU36660 | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | Urease (gamma subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the urease gamma subunit family. | 0.680 |
| mdr | ybdK | BSU03070 | BSU02010 | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | Two-component sensor histidine kinase [YbdJ]; Member of the two-component regulatory system YbdK/YbdJ. Probably activates YbdJ by phosphorylation. | 0.754 |
| mdr | ycgE | BSU03070 | BSU03080 | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. | 0.590 |
| mdr | ydfH | BSU03070 | BSU05410 | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | Two-component sensor histidine kinase [YdfI]; Member of the two-component regulatory system YdfH/YdfI. May activate YdfI by phosphorylation. | 0.689 |
| mdr | ytzD | BSU03070 | BSU29430 | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | Hypothetical protein; Evidence 5: No homology to any previously reported sequences; PubMedId: 11423008. | 0.607 |
| mdr | yvmA | BSU03070 | BSU35090 | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | 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. | 0.669 |
| tcyN | mdr | BSU29340 | BSU03070 | Sulfur-containing amino-acid ABC transporter (ATP-binding protein); Part of the ABC transporter complex TcyJKLMN involved in L- cystine import. Responsible for energy coupling to the transport system (Probable). Is also involved in cystathionine, djenkolate, and S- methylcysteine transport; Belongs to the ABC transporter superfamily. L-cystine importer (TC 3.A.1.3.13) family. | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | 0.745 |
| tcyN | ureA | BSU29340 | BSU36660 | Sulfur-containing amino-acid ABC transporter (ATP-binding protein); Part of the ABC transporter complex TcyJKLMN involved in L- cystine import. Responsible for energy coupling to the transport system (Probable). Is also involved in cystathionine, djenkolate, and S- methylcysteine transport; Belongs to the ABC transporter superfamily. L-cystine importer (TC 3.A.1.3.13) family. | Urease (gamma subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the urease gamma subunit family. | 0.630 |
| tcyN | ybdK | BSU29340 | BSU02010 | Sulfur-containing amino-acid ABC transporter (ATP-binding protein); Part of the ABC transporter complex TcyJKLMN involved in L- cystine import. Responsible for energy coupling to the transport system (Probable). Is also involved in cystathionine, djenkolate, and S- methylcysteine transport; Belongs to the ABC transporter superfamily. L-cystine importer (TC 3.A.1.3.13) family. | Two-component sensor histidine kinase [YbdJ]; Member of the two-component regulatory system YbdK/YbdJ. Probably activates YbdJ by phosphorylation. | 0.757 |
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