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 |
| bisC | msrA | b3551 | b4219 | Biotin sulfoxide reductase; This enzyme may serve as a scavenger, allowing the cell to utilize biotin sulfoxide as a biotin source. It reduces a spontaneous oxidation product of biotin, D-biotin D-sulfoxide (BSO or BDS), back to biotin. Also exhibits methionine-(S)-sulfoxide (Met-S-SO) reductase activity, acting specifically on the (S) enantiomer in the free, but not the protein-bound form. It thus plays a role in assimilation of oxidized methionines. | Methionine sulfoxide reductase A; Could have an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.521 |
| bisC | msrB | b3551 | b1778 | Biotin sulfoxide reductase; This enzyme may serve as a scavenger, allowing the cell to utilize biotin sulfoxide as a biotin source. It reduces a spontaneous oxidation product of biotin, D-biotin D-sulfoxide (BSO or BDS), back to biotin. Also exhibits methionine-(S)-sulfoxide (Met-S-SO) reductase activity, acting specifically on the (S) enantiomer in the free, but not the protein-bound form. It thus plays a role in assimilation of oxidized methionines. | Methionine sulfoxide reductase B. | 0.645 |
| bisC | yedY | b3551 | b1971 | Biotin sulfoxide reductase; This enzyme may serve as a scavenger, allowing the cell to utilize biotin sulfoxide as a biotin source. It reduces a spontaneous oxidation product of biotin, D-biotin D-sulfoxide (BSO or BDS), back to biotin. Also exhibits methionine-(S)-sulfoxide (Met-S-SO) reductase activity, acting specifically on the (S) enantiomer in the free, but not the protein-bound form. It thus plays a role in assimilation of oxidized methionines. | Membrane-anchored, periplasmic TMAO, DMSO reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The catalytic subunit Ms [...] | 0.815 |
| bisC | yedZ | b3551 | b1972 | Biotin sulfoxide reductase; This enzyme may serve as a scavenger, allowing the cell to utilize biotin sulfoxide as a biotin source. It reduces a spontaneous oxidation product of biotin, D-biotin D-sulfoxide (BSO or BDS), back to biotin. Also exhibits methionine-(S)-sulfoxide (Met-S-SO) reductase activity, acting specifically on the (S) enantiomer in the free, but not the protein-bound form. It thus plays a role in assimilation of oxidized methionines. | Inner membrane heme subunit for periplasmic YedYZ reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides el [...] | 0.453 |
| ddpC | yedZ | b1485 | b1972 | D,D-dipeptide ABC transporter permease; Part of the ABC transporter complex DdpABCDF, which is probably involved in D,D-dipeptide transport. Probably responsible for the translocation of the substrate across the membrane; Belongs to the binding-protein-dependent transport system permease family. OppBC subfamily. | Inner membrane heme subunit for periplasmic YedYZ reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides el [...] | 0.529 |
| ddpC | yiaB | b1485 | b3563 | D,D-dipeptide ABC transporter permease; Part of the ABC transporter complex DdpABCDF, which is probably involved in D,D-dipeptide transport. Probably responsible for the translocation of the substrate across the membrane; Belongs to the binding-protein-dependent transport system permease family. OppBC subfamily. | YiaAB family inner membrane protein. | 0.893 |
| hiuH | yedV | b1970 | b1968 | Hydroxyisourate hydrolase; Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo- 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). | Putative sensory kinase in two-component regulatory system with YedW; Member of a two-component regulatory system HprR/HprS involved in response to hydrogen peroxide. Senses H(2)O(2), maybe via the redox state of the membrane. Activates HprR by phosphorylation. Can also phosphorylate CusR. | 0.609 |
| hiuH | yedW | b1970 | b1969 | Hydroxyisourate hydrolase; Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo- 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). | Response regulator family protein; Member of a two-component regulatory system HprR/HprS involved in response to hydrogen peroxide. Regulates the expression of at least 5 operons, cyoABCDE, hprRS, hiuH, cusRS and cusCFBA. Bifunctional regulator that acts as an activator and a repressor. | 0.776 |
| hiuH | yedY | b1970 | b1971 | Hydroxyisourate hydrolase; Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo- 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). | Membrane-anchored, periplasmic TMAO, DMSO reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The catalytic subunit Ms [...] | 0.895 |
| hiuH | yedZ | b1970 | b1972 | Hydroxyisourate hydrolase; Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo- 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). | Inner membrane heme subunit for periplasmic YedYZ reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides el [...] | 0.931 |
| msrA | bisC | b4219 | b3551 | Methionine sulfoxide reductase A; Could have an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | Biotin sulfoxide reductase; This enzyme may serve as a scavenger, allowing the cell to utilize biotin sulfoxide as a biotin source. It reduces a spontaneous oxidation product of biotin, D-biotin D-sulfoxide (BSO or BDS), back to biotin. Also exhibits methionine-(S)-sulfoxide (Met-S-SO) reductase activity, acting specifically on the (S) enantiomer in the free, but not the protein-bound form. It thus plays a role in assimilation of oxidized methionines. | 0.521 |
| msrA | msrB | b4219 | b1778 | Methionine sulfoxide reductase A; Could have an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | Methionine sulfoxide reductase B. | 0.999 |
| msrA | yedY | b4219 | b1971 | Methionine sulfoxide reductase A; Could have an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | Membrane-anchored, periplasmic TMAO, DMSO reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The catalytic subunit Ms [...] | 0.785 |
| msrA | yedZ | b4219 | b1972 | Methionine sulfoxide reductase A; Could have an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | Inner membrane heme subunit for periplasmic YedYZ reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides el [...] | 0.597 |
| msrB | bisC | b1778 | b3551 | Methionine sulfoxide reductase B. | Biotin sulfoxide reductase; This enzyme may serve as a scavenger, allowing the cell to utilize biotin sulfoxide as a biotin source. It reduces a spontaneous oxidation product of biotin, D-biotin D-sulfoxide (BSO or BDS), back to biotin. Also exhibits methionine-(S)-sulfoxide (Met-S-SO) reductase activity, acting specifically on the (S) enantiomer in the free, but not the protein-bound form. It thus plays a role in assimilation of oxidized methionines. | 0.645 |
| msrB | msrA | b1778 | b4219 | Methionine sulfoxide reductase B. | Methionine sulfoxide reductase A; Could have an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.999 |
| msrB | yedY | b1778 | b1971 | Methionine sulfoxide reductase B. | Membrane-anchored, periplasmic TMAO, DMSO reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The catalytic subunit Ms [...] | 0.810 |
| msrB | yedZ | b1778 | b1972 | Methionine sulfoxide reductase B. | Inner membrane heme subunit for periplasmic YedYZ reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides el [...] | 0.452 |
| surA | yedY | b0053 | b1971 | Peptidyl-prolyl cis-trans isomerase (PPIase); Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane- associated steps of protein maturation. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis. | Membrane-anchored, periplasmic TMAO, DMSO reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The catalytic subunit Ms [...] | 0.427 |
| surA | yedZ | b0053 | b1972 | Peptidyl-prolyl cis-trans isomerase (PPIase); Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane- associated steps of protein maturation. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis. | Inner membrane heme subunit for periplasmic YedYZ reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides el [...] | 0.455 |
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