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 |
| LBAT_0915 | LBAT_0917 | LBAT_0915 | LBAT_0917 | Aldose epimerase. | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.831 |
| LBAT_0915 | hslU | LBAT_0915 | LBAT_0916 | Aldose epimerase. | ATP-dependent protease ATP-binding subunit; 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. | 0.831 |
| LBAT_0915 | topA | LBAT_0915 | LBAT_0920 | Aldose epimerase. | 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 [...] | 0.686 |
| LBAT_0915 | trmFO | LBAT_0915 | LBAT_0919 | Aldose epimerase. | tRNA (uracil-5-)-methyltransferase Gid; Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs; Belongs to the MnmG family. TrmFO subfamily. | 0.787 |
| LBAT_0915 | xerC | LBAT_0915 | LBAT_0918 | Aldose epimerase. | Recombinase; 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. | 0.837 |
| LBAT_0917 | LBAT_0915 | LBAT_0917 | LBAT_0915 | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Aldose epimerase. | 0.831 |
| LBAT_0917 | clpP | LBAT_0917 | LBAT_1144 | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.767 |
| LBAT_0917 | groL | LBAT_0917 | LBAT_0456 | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.749 |
| LBAT_0917 | groS | LBAT_0917 | LBAT_0455 | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.667 |
| LBAT_0917 | grpE | LBAT_0917 | LBAT_0712 | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP- [...] | 0.805 |
| LBAT_0917 | hslO | LBAT_0917 | LBAT_0343 | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Heat shock protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.750 |
| LBAT_0917 | hslU | LBAT_0917 | LBAT_0916 | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | ATP-dependent protease ATP-binding subunit; 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 |
| LBAT_0917 | topA | LBAT_0917 | LBAT_0920 | ATP-dependent protease peptidase subunit; 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 [...] | 0.738 |
| LBAT_0917 | trmFO | LBAT_0917 | LBAT_0919 | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | tRNA (uracil-5-)-methyltransferase Gid; Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs; Belongs to the MnmG family. TrmFO subfamily. | 0.859 |
| LBAT_0917 | xerC | LBAT_0917 | LBAT_0918 | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Recombinase; 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. | 0.927 |
| clpP | LBAT_0917 | LBAT_1144 | LBAT_0917 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.767 |
| clpP | groL | LBAT_1144 | LBAT_0456 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.816 |
| clpP | groS | LBAT_1144 | LBAT_0455 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.846 |
| clpP | grpE | LBAT_1144 | LBAT_0712 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP- [...] | 0.831 |
| groL | LBAT_0917 | LBAT_0456 | LBAT_0917 | Chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.749 |
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