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 |
| atpF | atpH | STM3869 | STM3868 | Membrane-bound ATP synthase, F0 sector, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Membrane-bound ATP synthase, F1 sector, delta-subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | 0.999 |
| atpF | dsbA | STM3869 | STM3997 | Membrane-bound ATP synthase, F0 sector, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. It is required for pilus biogenesis (By similarity). Belongs to the thioredoxin family. DsbA subfamily. | 0.491 |
| atpF | grxC | STM3869 | STM3702 | Membrane-bound ATP synthase, F0 sector, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Glutaredoxin 3; Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. | 0.870 |
| atpF | rpoA | STM3869 | STM3415 | Membrane-bound ATP synthase, F0 sector, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | RNA polymerase, alpha subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.965 |
| atpF | rpoZ | STM3869 | STM3741 | Membrane-bound ATP synthase, F0 sector, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | RNA polymerase, omega subunit; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity). | 0.473 |
| atpF | rpsL | STM3869 | STM3448 | Membrane-bound ATP synthase, F0 sector, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 30S ribosomal subunit protein S12; With S4 and S5 plays an important role in translational accuracy. | 0.976 |
| atpF | secB | STM3869 | STM3701 | Membrane-bound ATP synthase, F0 sector, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Molecular chaperone in protein export; One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA; Belongs to the SecB family. | 0.439 |
| atpF | yibN | STM3869 | STM3703 | Membrane-bound ATP synthase, F0 sector, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Putative rhodanese-related sulfurtransferases; Similar to E. coli orf, hypothetical protein (AAC76635.1); Blastp hit to AAC76635.1 (143 aa), 93% identity in aa 1 - 143. | 0.784 |
| atpH | atpF | STM3868 | STM3869 | Membrane-bound ATP synthase, F1 sector, delta-subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | Membrane-bound ATP synthase, F0 sector, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |
| atpH | rpoA | STM3868 | STM3415 | Membrane-bound ATP synthase, F1 sector, delta-subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | RNA polymerase, alpha subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.978 |
| atpH | rpoZ | STM3868 | STM3741 | Membrane-bound ATP synthase, F1 sector, delta-subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | RNA polymerase, omega subunit; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity). | 0.581 |
| atpH | rpsL | STM3868 | STM3448 | Membrane-bound ATP synthase, F1 sector, delta-subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | 30S ribosomal subunit protein S12; With S4 and S5 plays an important role in translational accuracy. | 0.978 |
| atpH | yibN | STM3868 | STM3703 | Membrane-bound ATP synthase, F1 sector, delta-subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | Putative rhodanese-related sulfurtransferases; Similar to E. coli orf, hypothetical protein (AAC76635.1); Blastp hit to AAC76635.1 (143 aa), 93% identity in aa 1 - 143. | 0.676 |
| dsbA | atpF | STM3997 | STM3869 | Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. It is required for pilus biogenesis (By similarity). Belongs to the thioredoxin family. DsbA subfamily. | Membrane-bound ATP synthase, F0 sector, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.491 |
| dsbA | grxC | STM3997 | STM3702 | Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. It is required for pilus biogenesis (By similarity). Belongs to the thioredoxin family. DsbA subfamily. | Glutaredoxin 3; Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. | 0.512 |
| dsbA | yibN | STM3997 | STM3703 | Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. It is required for pilus biogenesis (By similarity). Belongs to the thioredoxin family. DsbA subfamily. | Putative rhodanese-related sulfurtransferases; Similar to E. coli orf, hypothetical protein (AAC76635.1); Blastp hit to AAC76635.1 (143 aa), 93% identity in aa 1 - 143. | 0.739 |
| gpsA | grxC | STM3700 | STM3702 | Glycerol-3-phosphate dehydrogenase [NAD+]. (SW:GPDA_SALTY); Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family. | Glutaredoxin 3; Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. | 0.777 |
| gpsA | secB | STM3700 | STM3701 | Glycerol-3-phosphate dehydrogenase [NAD+]. (SW:GPDA_SALTY); Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family. | Molecular chaperone in protein export; One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA; Belongs to the SecB family. | 0.907 |
| gpsA | yibN | STM3700 | STM3703 | Glycerol-3-phosphate dehydrogenase [NAD+]. (SW:GPDA_SALTY); Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family. | Putative rhodanese-related sulfurtransferases; Similar to E. coli orf, hypothetical protein (AAC76635.1); Blastp hit to AAC76635.1 (143 aa), 93% identity in aa 1 - 143. | 0.704 |
| grxC | atpF | STM3702 | STM3869 | Glutaredoxin 3; Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. | Membrane-bound ATP synthase, F0 sector, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.870 |
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