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 |
| EDS73814.1 | hslO | CLOSPI_02239 | CLOSPI_02240 | TIM-barrel protein, nifR3 family; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | Chaperonin HslO; 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. | 0.607 |
| EDS73814.1 | tilS | CLOSPI_02239 | CLOSPI_02243 | TIM-barrel protein, nifR3 family; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | tRNA(Ile)-lysidine synthetase; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. Belongs to the tRNA(Ile)-lysidine synthase family. | 0.479 |
| EDS74589.1 | FbpA | CLOSPI_01644 | CLOSPI_00548 | S4 domain protein; KEGG: tma:TM0462 1.2e-06 conserved hypothetical protein K06180; COG: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog). | Fibronectin-binding protein A domain protein; KEGG: fnu:FN0522 1.5e-05 exonuclease SBCC K03546; COG: COG1293 Predicted RNA-binding protein homologous to eukaryotic snRNP; Psort location: Cytoplasmic, score: 8.87. | 0.916 |
| EDS74589.1 | grpE | CLOSPI_01644 | CLOSPI_00866 | S4 domain protein; KEGG: tma:TM0462 1.2e-06 conserved hypothetical protein K06180; COG: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog). | Co-chaperone 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-depend [...] | 0.552 |
| EDS74589.1 | hslO | CLOSPI_01644 | CLOSPI_02240 | S4 domain protein; KEGG: tma:TM0462 1.2e-06 conserved hypothetical protein K06180; COG: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog). | Chaperonin HslO; 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. | 0.775 |
| EDS74589.1 | htpG | CLOSPI_01644 | CLOSPI_00715 | S4 domain protein; KEGG: tma:TM0462 1.2e-06 conserved hypothetical protein K06180; COG: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog). | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.402 |
| FbpA | EDS74589.1 | CLOSPI_00548 | CLOSPI_01644 | Fibronectin-binding protein A domain protein; KEGG: fnu:FN0522 1.5e-05 exonuclease SBCC K03546; COG: COG1293 Predicted RNA-binding protein homologous to eukaryotic snRNP; Psort location: Cytoplasmic, score: 8.87. | S4 domain protein; KEGG: tma:TM0462 1.2e-06 conserved hypothetical protein K06180; COG: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog). | 0.916 |
| FbpA | hslO | CLOSPI_00548 | CLOSPI_02240 | Fibronectin-binding protein A domain protein; KEGG: fnu:FN0522 1.5e-05 exonuclease SBCC K03546; COG: COG1293 Predicted RNA-binding protein homologous to eukaryotic snRNP; Psort location: Cytoplasmic, score: 8.87. | Chaperonin HslO; 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. | 0.527 |
| coaX | hslO | CLOSPI_01335 | CLOSPI_02240 | Pantothenate kinase, type III; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. | Chaperonin HslO; 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. | 0.452 |
| grpE | EDS74589.1 | CLOSPI_00866 | CLOSPI_01644 | Co-chaperone 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-depend [...] | S4 domain protein; KEGG: tma:TM0462 1.2e-06 conserved hypothetical protein K06180; COG: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog). | 0.552 |
| grpE | hflB | CLOSPI_00866 | CLOSPI_02241 | Co-chaperone 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-depend [...] | ATP-dependent metallopeptidase HflB; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.480 |
| grpE | hslO | CLOSPI_00866 | CLOSPI_02240 | Co-chaperone 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-depend [...] | Chaperonin HslO; 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. | 0.517 |
| grpE | htpG | CLOSPI_00866 | CLOSPI_00715 | Co-chaperone 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-depend [...] | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.746 |
| grpE | lon | CLOSPI_00866 | CLOSPI_00899 | Co-chaperone 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-depend [...] | Endopeptidase La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.781 |
| hflB | grpE | CLOSPI_02241 | CLOSPI_00866 | ATP-dependent metallopeptidase HflB; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | Co-chaperone 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-depend [...] | 0.480 |
| hflB | hpt | CLOSPI_02241 | CLOSPI_02242 | ATP-dependent metallopeptidase HflB; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | KEGG: spn:SP_0012 2.4e-50 hypoxanthine-guanine phosphoribosyltransferase K00760; COG: COG0634 Hypoxanthine-guanine phosphoribosyltransferase; Psort location: Cytoplasmic, score: 9.98; Belongs to the purine/pyrimidine phosphoribosyltransferase family. | 0.951 |
| hflB | hslO | CLOSPI_02241 | CLOSPI_02240 | ATP-dependent metallopeptidase HflB; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | Chaperonin HslO; 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. | 0.697 |
| hflB | lon | CLOSPI_02241 | CLOSPI_00899 | ATP-dependent metallopeptidase HflB; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | Endopeptidase La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.713 |
| hflB | tilS | CLOSPI_02241 | CLOSPI_02243 | ATP-dependent metallopeptidase HflB; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | tRNA(Ile)-lysidine synthetase; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. Belongs to the tRNA(Ile)-lysidine synthase family. | 0.797 |
| hpt | hflB | CLOSPI_02242 | CLOSPI_02241 | KEGG: spn:SP_0012 2.4e-50 hypoxanthine-guanine phosphoribosyltransferase K00760; COG: COG0634 Hypoxanthine-guanine phosphoribosyltransferase; Psort location: Cytoplasmic, score: 9.98; Belongs to the purine/pyrimidine phosphoribosyltransferase family. | ATP-dependent metallopeptidase HflB; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.951 |
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