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 |
| csaA | dnaJ | BSU19040 | BSU25460 | Molecular chaperone; Can suppress growth and secretion defects in E.coli secA and secB mutants. Probably a molecular chaperone for exported proteins or may act by stabilizing the SecA protein. | Co-factor of molecular chaperone; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwe [...] | 0.701 |
| csaA | ffh | BSU19040 | BSU15980 | Molecular chaperone; Can suppress growth and secretion defects in E.coli secA and secB mutants. Probably a molecular chaperone for exported proteins or may act by stabilizing the SecA protein. | Signal recognition particle-like (SRP) GTPase; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individua [...] | 0.566 |
| csaA | nnrA | BSU19040 | BSU38720 | Molecular chaperone; Can suppress growth and secretion defects in E.coli secA and secB mutants. Probably a molecular chaperone for exported proteins or may act by stabilizing the SecA protein. | NAD(P)H dehydratase; Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. | 0.614 |
| csaA | oxaAB | BSU19040 | BSU23890 | Molecular chaperone; Can suppress growth and secretion defects in E.coli secA and secB mutants. Probably a molecular chaperone for exported proteins or may act by stabilizing the SecA protein. | Sec-independent factor for membrane protein insertion (YidC/SpoIIIJ family); Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins (By similarity). Also involved in protein secretion processes. It has an overlapping, although partly distinct, function compared to SpoIIIJ(MisCB). | 0.622 |
| csaA | pheS | BSU19040 | BSU28640 | Molecular chaperone; Can suppress growth and secretion defects in E.coli secA and secB mutants. Probably a molecular chaperone for exported proteins or may act by stabilizing the SecA protein. | phenylalanyl-tRNA synthetase (alpha subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. | 0.897 |
| csaA | secA | BSU19040 | BSU35300 | Molecular chaperone; Can suppress growth and secretion defects in E.coli secA and secB mutants. Probably a molecular chaperone for exported proteins or may act by stabilizing the SecA protein. | Translocase binding subunit (ATPase); Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family. | 0.930 |
| csaA | secDF | BSU19040 | BSU27650 | Molecular chaperone; Can suppress growth and secretion defects in E.coli secA and secB mutants. Probably a molecular chaperone for exported proteins or may act by stabilizing the SecA protein. | Protein-export membrane protein; Required for efficient translocation of secretory pre- proteins under conditions of hypersecretion but is not required for the release of mature proteins from the membrane. In the N-terminal section; belongs to the SecD/SecF family. SecD subfamily. | 0.798 |
| csaA | tig | BSU19040 | BSU28230 | Molecular chaperone; Can suppress growth and secretion defects in E.coli secA and secB mutants. Probably a molecular chaperone for exported proteins or may act by stabilizing the SecA protein. | Prolyl isomerase (trigger factor); Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity). Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.643 |
| csaA | yobQ | BSU19040 | BSU19050 | Molecular chaperone; Can suppress growth and secretion defects in E.coli secA and secB mutants. Probably a molecular chaperone for exported proteins or may act by stabilizing the SecA protein. | Putative transcriptional regulator (AraC/XylS family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 0.800 |
| csaA | yobR | BSU19040 | BSU19060 | Molecular chaperone; Can suppress growth and secretion defects in E.coli secA and secB mutants. Probably a molecular chaperone for exported proteins or may act by stabilizing the SecA protein. | Putative acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the acetyltransferase family. | 0.681 |
| dnaJ | csaA | BSU25460 | BSU19040 | Co-factor of molecular chaperone; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwe [...] | Molecular chaperone; Can suppress growth and secretion defects in E.coli secA and secB mutants. Probably a molecular chaperone for exported proteins or may act by stabilizing the SecA protein. | 0.701 |
| dnaJ | ffh | BSU25460 | BSU15980 | Co-factor of molecular chaperone; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwe [...] | Signal recognition particle-like (SRP) GTPase; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individua [...] | 0.623 |
| dnaJ | oxaAB | BSU25460 | BSU23890 | Co-factor of molecular chaperone; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwe [...] | Sec-independent factor for membrane protein insertion (YidC/SpoIIIJ family); Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins (By similarity). Also involved in protein secretion processes. It has an overlapping, although partly distinct, function compared to SpoIIIJ(MisCB). | 0.473 |
| dnaJ | secA | BSU25460 | BSU35300 | Co-factor of molecular chaperone; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwe [...] | Translocase binding subunit (ATPase); Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family. | 0.675 |
| dnaJ | secDF | BSU25460 | BSU27650 | Co-factor of molecular chaperone; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwe [...] | Protein-export membrane protein; Required for efficient translocation of secretory pre- proteins under conditions of hypersecretion but is not required for the release of mature proteins from the membrane. In the N-terminal section; belongs to the SecD/SecF family. SecD subfamily. | 0.635 |
| dnaJ | tig | BSU25460 | BSU28230 | Co-factor of molecular chaperone; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwe [...] | Prolyl isomerase (trigger factor); Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity). Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.819 |
| ffh | csaA | BSU15980 | BSU19040 | Signal recognition particle-like (SRP) GTPase; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individua [...] | Molecular chaperone; Can suppress growth and secretion defects in E.coli secA and secB mutants. Probably a molecular chaperone for exported proteins or may act by stabilizing the SecA protein. | 0.566 |
| ffh | dnaJ | BSU15980 | BSU25460 | Signal recognition particle-like (SRP) GTPase; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individua [...] | Co-factor of molecular chaperone; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwe [...] | 0.623 |
| ffh | oxaAB | BSU15980 | BSU23890 | Signal recognition particle-like (SRP) GTPase; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individua [...] | Sec-independent factor for membrane protein insertion (YidC/SpoIIIJ family); Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins (By similarity). Also involved in protein secretion processes. It has an overlapping, although partly distinct, function compared to SpoIIIJ(MisCB). | 0.949 |
| ffh | secA | BSU15980 | BSU35300 | Signal recognition particle-like (SRP) GTPase; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individua [...] | Translocase binding subunit (ATPase); Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family. | 0.995 |
page 1 of 3