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 |
| DM42_1089 | DM42_2984 | DM42_1089 | DM42_2984 | annotation not available | Molecular chaperone hsp33; 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 | 0.779 |
| DM42_1089 | dnaJ | DM42_1089 | DM42_1085 | annotation not available | Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, DnaK and GrpE are require [...] | 0.647 |
| DM42_1089 | hslU | DM42_1089 | DM42_1920 | annotation not available | 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 | 0.583 |
| DM42_1089 | hslV | DM42_1089 | DM42_1921 | annotation not available | Atp-dependent hsluv protease, peptidase subunit hslv; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery | 0.630 |
| DM42_1089 | htpG | DM42_1089 | DM42_2714 | annotation not available | Histidine kinase-, dna gyrase b-, and hsp90-like atpase family protein; Molecular chaperone. Has ATPase activity | 0.621 |
| DM42_2984 | DM42_1089 | DM42_2984 | DM42_1089 | Molecular chaperone hsp33; 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 | annotation not available | 0.779 |
| DM42_2984 | DM42_2985 | DM42_2984 | DM42_2985 | Molecular chaperone hsp33; 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 | annotation not available | 0.801 |
| DM42_2984 | DM42_2986 | DM42_2984 | DM42_2986 | Molecular chaperone hsp33; 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 | Hypothetical protein; Uncharacterized protein | 0.656 |
| DM42_2984 | dnaJ | DM42_2984 | DM42_1085 | Molecular chaperone hsp33; 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 | Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, DnaK and GrpE are require [...] | 0.668 |
| DM42_2984 | hslU | DM42_2984 | DM42_1920 | Molecular chaperone hsp33; 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 | 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 | 0.662 |
| DM42_2984 | hslV | DM42_2984 | DM42_1921 | Molecular chaperone hsp33; 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 | Atp-dependent hsluv protease, peptidase subunit hslv; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery | 0.632 |
| DM42_2984 | htpG | DM42_2984 | DM42_2714 | Molecular chaperone hsp33; 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 | Histidine kinase-, dna gyrase b-, and hsp90-like atpase family protein; Molecular chaperone. Has ATPase activity | 0.678 |
| DM42_2984 | mutM | DM42_2984 | DM42_2272 | Molecular chaperone hsp33; 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 | Formamidopyrimidine-dna glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates | 0.619 |
| DM42_2984 | sun | DM42_2984 | DM42_1887 | Molecular chaperone hsp33; 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 | Ribosomal rna small subunit methyltransferase b; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA | 0.611 |
| DM42_2984 | tig | DM42_2984 | DM42_3174 | Molecular chaperone hsp33; 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 | Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase | 0.632 |
| DM42_2985 | DM42_2984 | DM42_2985 | DM42_2984 | annotation not available | Molecular chaperone hsp33; 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 | 0.801 |
| DM42_2985 | DM42_2986 | DM42_2985 | DM42_2986 | annotation not available | Hypothetical protein; Uncharacterized protein | 0.601 |
| DM42_2986 | DM42_2984 | DM42_2986 | DM42_2984 | Hypothetical protein; Uncharacterized protein | Molecular chaperone hsp33; 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 | 0.656 |
| DM42_2986 | DM42_2985 | DM42_2986 | DM42_2985 | Hypothetical protein; Uncharacterized protein | annotation not available | 0.601 |
| dnaJ | DM42_1089 | DM42_1085 | DM42_1089 | Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, DnaK and GrpE are require [...] | annotation not available | 0.647 |
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