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 |
| SEP59025.1 | topA | SAMN05216362_101192 | SAMN05216362_101122 | DNA translocase FtsK; Belongs to the FtsK/SpoIIIE/SftA family. | DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.645 |
| SEP59025.1 | xerD | SAMN05216362_101192 | SAMN05216362_102137 | DNA translocase FtsK; Belongs to the FtsK/SpoIIIE/SftA family. | Tyrosine recombinase XerD subunit; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.668 |
| SEP70541.1 | SEP70584.1 | SAMN05216362_102134 | SAMN05216362_102135 | Pyrimidine-nucleoside phosphorylase. | Purine-nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | 0.939 |
| SEP70541.1 | deoB | SAMN05216362_102134 | SAMN05216362_102136 | Pyrimidine-nucleoside phosphorylase. | Phosphopentomutase; Phosphotransfer between the C1 and C5 carbon atoms of pentose; Belongs to the phosphopentomutase family. | 0.996 |
| SEP70541.1 | xerD | SAMN05216362_102134 | SAMN05216362_102137 | Pyrimidine-nucleoside phosphorylase. | Tyrosine recombinase XerD subunit; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.558 |
| SEP70584.1 | SEP70541.1 | SAMN05216362_102135 | SAMN05216362_102134 | Purine-nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | Pyrimidine-nucleoside phosphorylase. | 0.939 |
| SEP70584.1 | deoB | SAMN05216362_102135 | SAMN05216362_102136 | Purine-nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | Phosphopentomutase; Phosphotransfer between the C1 and C5 carbon atoms of pentose; Belongs to the phosphopentomutase family. | 0.981 |
| SEP70584.1 | xerD | SAMN05216362_102135 | SAMN05216362_102137 | Purine-nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | Tyrosine recombinase XerD subunit; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.591 |
| SEQ25527.1 | xerD | SAMN05216362_10976 | SAMN05216362_102137 | Competence protein ComFC. | Tyrosine recombinase XerD subunit; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.611 |
| SEQ49931.1 | xerD | SAMN05216362_11554 | SAMN05216362_102137 | Putative SOS response-associated peptidase YedK; Belongs to the SOS response-associated peptidase family. | Tyrosine recombinase XerD subunit; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.483 |
| deoB | SEP70541.1 | SAMN05216362_102136 | SAMN05216362_102134 | Phosphopentomutase; Phosphotransfer between the C1 and C5 carbon atoms of pentose; Belongs to the phosphopentomutase family. | Pyrimidine-nucleoside phosphorylase. | 0.996 |
| deoB | SEP70584.1 | SAMN05216362_102136 | SAMN05216362_102135 | Phosphopentomutase; Phosphotransfer between the C1 and C5 carbon atoms of pentose; Belongs to the phosphopentomutase family. | Purine-nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | 0.981 |
| deoB | xerD | SAMN05216362_102136 | SAMN05216362_102137 | Phosphopentomutase; Phosphotransfer between the C1 and C5 carbon atoms of pentose; Belongs to the phosphopentomutase family. | Tyrosine recombinase XerD subunit; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.657 |
| hslU | hslV | SAMN05216362_101125 | SAMN05216362_101124 | ATP-dependent HslUV protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | ATP dependent peptidase CodWX, CodW component. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.999 |
| hslU | topA | SAMN05216362_101125 | SAMN05216362_101122 | ATP-dependent HslUV protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.615 |
| hslU | xerD | SAMN05216362_101125 | SAMN05216362_102137 | ATP-dependent HslUV protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | Tyrosine recombinase XerD subunit; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.535 |
| hslV | hslU | SAMN05216362_101124 | SAMN05216362_101125 | ATP dependent peptidase CodWX, CodW component. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | ATP-dependent HslUV protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.999 |
| hslV | topA | SAMN05216362_101124 | SAMN05216362_101122 | ATP dependent peptidase CodWX, CodW component. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.579 |
| hslV | xerD | SAMN05216362_101124 | SAMN05216362_102137 | ATP dependent peptidase CodWX, CodW component. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Tyrosine recombinase XerD subunit; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.739 |
| topA | SEP59025.1 | SAMN05216362_101122 | SAMN05216362_101192 | DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | DNA translocase FtsK; Belongs to the FtsK/SpoIIIE/SftA family. | 0.645 |
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