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 |
| bamA | bamB | b0177 | b2512 | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam [...] | Outer membrane protein assembly factor bamb; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...] | 0.999 |
| bamA | ppiD | b0177 | b0441 | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam [...] | Periplasmic folding chaperone, has an inactive ppiase domain; PPIases accelerate the folding of proteins. Seems to be involved in the folding of outer membrane proteins. Its preference at the P1 position of the peptide substrate is Glu > Leu > Ala > His > Val > Phe > Ile > Gly > Lys > Thr | 0.646 |
| bamA | yfgM | b0177 | b2513 | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam [...] | annotation not available | 0.681 |
| bamB | bamA | b2512 | b0177 | Outer membrane protein assembly factor bamb; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...] | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam [...] | 0.999 |
| bamB | der | b2512 | b2511 | Outer membrane protein assembly factor bamb; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...] | 50S ribosomal subunit stability factor; GTPase that plays an essential role in the late steps of ribosome biogenesis. GTPase point mutations (but not a deletion mutant) are suppressed by mild overexpression of RelA, probably due to increased levels of the stringent response mediator (p)ppGpp. 50S subunits assembled in the absence of Der are defective and unable to assemble into 70S ribosomes. GTPase activity is stimulated by YihI. Overexpression rescues an rrmJ deletion, stabilizing the 70S ribosome. Der and RrmJ are likely to share a mechanism to stabilize 50S ribosomal subunits at a [...] | 0.950 |
| bamB | hisS | b2512 | b2514 | Outer membrane protein assembly factor bamb; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...] | Histidine--tRNA ligase; Histidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | 0.976 |
| bamB | ispG | b2512 | b2515 | Outer membrane protein assembly factor bamb; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...] | (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin); Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate, using flavodoxin as the reducing agent | 0.777 |
| bamB | rodZ | b2512 | b2516 | Outer membrane protein assembly factor bamb; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...] | Transmembrane component of cytoskeleton; Cytoskeletal protein that is involved in cell-shape control through regulation of the length of the long axis | 0.771 |
| bamB | secE | b2512 | b3981 | Outer membrane protein assembly factor bamb; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...] | Preprotein translocase membrane subunit; Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true it also results in FtsH-mediated degradation of SecY | 0.439 |
| bamB | yfgM | b2512 | b2513 | Outer membrane protein assembly factor bamb; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...] | annotation not available | 0.994 |
| der | bamB | b2511 | b2512 | 50S ribosomal subunit stability factor; GTPase that plays an essential role in the late steps of ribosome biogenesis. GTPase point mutations (but not a deletion mutant) are suppressed by mild overexpression of RelA, probably due to increased levels of the stringent response mediator (p)ppGpp. 50S subunits assembled in the absence of Der are defective and unable to assemble into 70S ribosomes. GTPase activity is stimulated by YihI. Overexpression rescues an rrmJ deletion, stabilizing the 70S ribosome. Der and RrmJ are likely to share a mechanism to stabilize 50S ribosomal subunits at a [...] | Outer membrane protein assembly factor bamb; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...] | 0.950 |
| der | hisS | b2511 | b2514 | 50S ribosomal subunit stability factor; GTPase that plays an essential role in the late steps of ribosome biogenesis. GTPase point mutations (but not a deletion mutant) are suppressed by mild overexpression of RelA, probably due to increased levels of the stringent response mediator (p)ppGpp. 50S subunits assembled in the absence of Der are defective and unable to assemble into 70S ribosomes. GTPase activity is stimulated by YihI. Overexpression rescues an rrmJ deletion, stabilizing the 70S ribosome. Der and RrmJ are likely to share a mechanism to stabilize 50S ribosomal subunits at a [...] | Histidine--tRNA ligase; Histidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | 0.945 |
| der | ispG | b2511 | b2515 | 50S ribosomal subunit stability factor; GTPase that plays an essential role in the late steps of ribosome biogenesis. GTPase point mutations (but not a deletion mutant) are suppressed by mild overexpression of RelA, probably due to increased levels of the stringent response mediator (p)ppGpp. 50S subunits assembled in the absence of Der are defective and unable to assemble into 70S ribosomes. GTPase activity is stimulated by YihI. Overexpression rescues an rrmJ deletion, stabilizing the 70S ribosome. Der and RrmJ are likely to share a mechanism to stabilize 50S ribosomal subunits at a [...] | (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin); Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate, using flavodoxin as the reducing agent | 0.668 |
| der | rodZ | b2511 | b2516 | 50S ribosomal subunit stability factor; GTPase that plays an essential role in the late steps of ribosome biogenesis. GTPase point mutations (but not a deletion mutant) are suppressed by mild overexpression of RelA, probably due to increased levels of the stringent response mediator (p)ppGpp. 50S subunits assembled in the absence of Der are defective and unable to assemble into 70S ribosomes. GTPase activity is stimulated by YihI. Overexpression rescues an rrmJ deletion, stabilizing the 70S ribosome. Der and RrmJ are likely to share a mechanism to stabilize 50S ribosomal subunits at a [...] | Transmembrane component of cytoskeleton; Cytoskeletal protein that is involved in cell-shape control through regulation of the length of the long axis | 0.544 |
| der | yfgM | b2511 | b2513 | 50S ribosomal subunit stability factor; GTPase that plays an essential role in the late steps of ribosome biogenesis. GTPase point mutations (but not a deletion mutant) are suppressed by mild overexpression of RelA, probably due to increased levels of the stringent response mediator (p)ppGpp. 50S subunits assembled in the absence of Der are defective and unable to assemble into 70S ribosomes. GTPase activity is stimulated by YihI. Overexpression rescues an rrmJ deletion, stabilizing the 70S ribosome. Der and RrmJ are likely to share a mechanism to stabilize 50S ribosomal subunits at a [...] | annotation not available | 0.930 |
| hisS | bamB | b2514 | b2512 | Histidine--tRNA ligase; Histidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | Outer membrane protein assembly factor bamb; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...] | 0.976 |
| hisS | der | b2514 | b2511 | Histidine--tRNA ligase; Histidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | 50S ribosomal subunit stability factor; GTPase that plays an essential role in the late steps of ribosome biogenesis. GTPase point mutations (but not a deletion mutant) are suppressed by mild overexpression of RelA, probably due to increased levels of the stringent response mediator (p)ppGpp. 50S subunits assembled in the absence of Der are defective and unable to assemble into 70S ribosomes. GTPase activity is stimulated by YihI. Overexpression rescues an rrmJ deletion, stabilizing the 70S ribosome. Der and RrmJ are likely to share a mechanism to stabilize 50S ribosomal subunits at a [...] | 0.945 |
| hisS | ispG | b2514 | b2515 | Histidine--tRNA ligase; Histidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin); Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate, using flavodoxin as the reducing agent | 0.950 |
| hisS | rodZ | b2514 | b2516 | Histidine--tRNA ligase; Histidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | Transmembrane component of cytoskeleton; Cytoskeletal protein that is involved in cell-shape control through regulation of the length of the long axis | 0.701 |
| hisS | yfgM | b2514 | b2513 | Histidine--tRNA ligase; Histidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | annotation not available | 0.987 |
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