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 |
| prkC | prpC | BSU15770 | BSU15760 | Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...] | Phosphorylated protein phosphatase; Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB. | 0.999 |
| prkC | ptkA | BSU15770 | BSU36250 | Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...] | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family. | 0.732 |
| prkC | rsbT | BSU15770 | BSU04690 | Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...] | Switch protein/serine-threonine kinase; Provides the crucial link between the upstream module (communication of environmental stress) and the downstream module (integration of the environmental signals with signals of energy stress) that compose the signal transduction pathway controlling the sigma-B factor. Phosphorylates and inactivates its specific antagonist protein RsbS thanks to its serine kinase activity. Upon phosphorylation of RsbS, RsbT is released to stimulate RsbU, a PP2C phosphatase, thereby initiating the signaling cascade that ultimately activates sigma-B. The activity o [...] | 0.604 |
| prkC | rsbW | BSU15770 | BSU04720 | Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...] | Switch protein/serine kinase and anti-sigma factor (inhibitory sigma-B binding protein); Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, RsbV. Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B). | 0.686 |
| prkC | spoIIAB | BSU15770 | BSU23460 | Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...] | Anti-sigma factor (antagonist of sigma(F)) and serine kinase; Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti- anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition. | 0.741 |
| prkC | yabT | BSU15770 | BSU00660 | Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...] | Putative serine/threonine-protein kinase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.966 |
| prkC | ybdM | BSU15770 | BSU02030 | Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...] | Putative protein kinase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.790 |
| prkC | yfkJ | BSU15770 | BSU07880 | Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...] | Protein-tyrosine-phosphatase; Dephosphorylates the phosphotyrosine-containing proteins. Involved in ethanol stress resistance. | 0.472 |
| prkC | ymfM | BSU15770 | BSU16910 | Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...] | Conserved hypothetical protein with ACT domain; Evidence 7: Gene remnant. | 0.573 |
| prpC | prkC | BSU15760 | BSU15770 | Phosphorylated protein phosphatase; Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB. | Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...] | 0.999 |
| prpC | yabT | BSU15760 | BSU00660 | Phosphorylated protein phosphatase; Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB. | Putative serine/threonine-protein kinase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.816 |
| prpC | ybdM | BSU15760 | BSU02030 | Phosphorylated protein phosphatase; Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB. | Putative protein kinase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.910 |
| prpC | yfkJ | BSU15760 | BSU07880 | Phosphorylated protein phosphatase; Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB. | Protein-tyrosine-phosphatase; Dephosphorylates the phosphotyrosine-containing proteins. Involved in ethanol stress resistance. | 0.682 |
| prpC | ymfM | BSU15760 | BSU16910 | Phosphorylated protein phosphatase; Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB. | Conserved hypothetical protein with ACT domain; Evidence 7: Gene remnant. | 0.504 |
| ptkA | prkC | BSU36250 | BSU15770 | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family. | Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...] | 0.732 |
| ptkA | rsbT | BSU36250 | BSU04690 | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family. | Switch protein/serine-threonine kinase; Provides the crucial link between the upstream module (communication of environmental stress) and the downstream module (integration of the environmental signals with signals of energy stress) that compose the signal transduction pathway controlling the sigma-B factor. Phosphorylates and inactivates its specific antagonist protein RsbS thanks to its serine kinase activity. Upon phosphorylation of RsbS, RsbT is released to stimulate RsbU, a PP2C phosphatase, thereby initiating the signaling cascade that ultimately activates sigma-B. The activity o [...] | 0.809 |
| ptkA | rsbW | BSU36250 | BSU04720 | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family. | Switch protein/serine kinase and anti-sigma factor (inhibitory sigma-B binding protein); Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, RsbV. Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B). | 0.667 |
| ptkA | spoIIAB | BSU36250 | BSU23460 | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family. | Anti-sigma factor (antagonist of sigma(F)) and serine kinase; Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti- anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition. | 0.671 |
| ptkA | yabT | BSU36250 | BSU00660 | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family. | Putative serine/threonine-protein kinase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.872 |
| ptkA | ybdM | BSU36250 | BSU02030 | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family. | Putative protein kinase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.837 |
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