Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... 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 annotated functions of the network proteins
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ABF63307.1 | ABF65621.1 | TM1040_0574 | TM1040_2889 | annotation not available | 33 kDa chaperonin; 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 | 0.696 |
| ABF63307.1 | dnaJ | TM1040_0574 | TM1040_0009 | annotation not available | Chaperone protein DnaJ; 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, D [...] | 0.542 |
| ABF63307.1 | hslU | TM1040_0574 | TM1040_2851 | annotation not available | ATP-dependent protease ATPase 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 | 0.436 |
| ABF65620.1 | ABF65621.1 | TM1040_2888 | TM1040_2889 | annotation not available | 33 kDa chaperonin; 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 | 0.770 |
| ABF65620.1 | ABF65622.1 | TM1040_2888 | TM1040_2890 | annotation not available | annotation not available | 0.710 |
| ABF65620.1 | ABF65623.1 | TM1040_2888 | TM1040_2891 | annotation not available | annotation not available | 0.764 |
| ABF65620.1 | ABF65626.1 | TM1040_2888 | TM1040_2894 | annotation not available | annotation not available | 0.490 |
| ABF65621.1 | ABF63307.1 | TM1040_2889 | TM1040_0574 | 33 kDa chaperonin; 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 | 0.696 |
| ABF65621.1 | ABF65620.1 | TM1040_2889 | TM1040_2888 | 33 kDa chaperonin; 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 | 0.770 |
| ABF65621.1 | ABF65622.1 | TM1040_2889 | TM1040_2890 | 33 kDa chaperonin; 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 | 0.885 |
| ABF65621.1 | ABF65623.1 | TM1040_2889 | TM1040_2891 | 33 kDa chaperonin; 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 | 0.888 |
| ABF65621.1 | ABF65626.1 | TM1040_2889 | TM1040_2894 | 33 kDa chaperonin; 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 | 0.687 |
| ABF65621.1 | dnaJ | TM1040_2889 | TM1040_0009 | 33 kDa chaperonin; 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 | Chaperone protein DnaJ; 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, D [...] | 0.588 |
| ABF65621.1 | hslU | TM1040_2889 | TM1040_2851 | 33 kDa chaperonin; 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 protease ATPase 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 | 0.513 |
| ABF65621.1 | prmA | TM1040_2889 | TM1040_2376 | 33 kDa chaperonin; 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 protein L11 methyltransferase; Methylates ribosomal protein L11 | 0.476 |
| ABF65621.1 | rnr | TM1040_2889 | TM1040_2994 | 33 kDa chaperonin; 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 | Ribonuclease R; 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs | 0.486 |
| ABF65621.1 | tig | TM1040_2889 | TM1040_1033 | 33 kDa chaperonin; 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; Belongs to the FKBP-type PPIase family. Tig subfamily | 0.489 |
| ABF65622.1 | ABF65620.1 | TM1040_2890 | TM1040_2888 | annotation not available | annotation not available | 0.710 |
| ABF65622.1 | ABF65621.1 | TM1040_2890 | TM1040_2889 | annotation not available | 33 kDa chaperonin; 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 | 0.885 |
| ABF65622.1 | ABF65623.1 | TM1040_2890 | TM1040_2891 | annotation not available | annotation not available | 0.893 |
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