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 |
| AIJ22189.1 | AIJ26636.1 | AMETH_2097 | AMETH_6544 | Parallel beta-helix repeat-containing protein. | ATPase. | 0.538 |
| AIJ22189.1 | arc | AMETH_2097 | AMETH_3546 | Parallel beta-helix repeat-containing protein. | Vesicle-fusing ATPase; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. | 0.538 |
| AIJ26527.1 | AIJ26636.1 | AMETH_6435 | AMETH_6544 | ATPase; Belongs to the AAA ATPase family. | ATPase. | 0.560 |
| AIJ26527.1 | arc | AMETH_6435 | AMETH_3546 | ATPase; Belongs to the AAA ATPase family. | Vesicle-fusing ATPase; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. | 0.564 |
| AIJ26636.1 | AIJ22189.1 | AMETH_6544 | AMETH_2097 | ATPase. | Parallel beta-helix repeat-containing protein. | 0.538 |
| AIJ26636.1 | AIJ26527.1 | AMETH_6544 | AMETH_6435 | ATPase. | ATPase; Belongs to the AAA ATPase family. | 0.560 |
| arc | AIJ22189.1 | AMETH_3546 | AMETH_2097 | Vesicle-fusing ATPase; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. | Parallel beta-helix repeat-containing protein. | 0.538 |
| arc | AIJ26527.1 | AMETH_3546 | AMETH_6435 | Vesicle-fusing ATPase; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. | ATPase; Belongs to the AAA ATPase family. | 0.564 |
| clpA | clpX | AMETH_2565 | AMETH_1735 | ATPase AAA-2 domain protein; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease ATP-binding subunit clpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.523 |
| clpA | ftsH | AMETH_2565 | AMETH_6573 | ATPase AAA-2 domain protein; Belongs to the ClpA/ClpB family. | Cell division protease FtsH; 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. | 0.610 |
| clpA | lon | AMETH_2565 | AMETH_0614 | ATPase AAA-2 domain protein; Belongs to the ClpA/ClpB family. | Lon protease; 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. | 0.650 |
| clpB | clpX | AMETH_6796 | AMETH_1735 | ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease ATP-binding subunit clpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.523 |
| clpB | ftsH | AMETH_6796 | AMETH_6573 | ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Cell division protease FtsH; 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. | 0.569 |
| clpB | lon | AMETH_6796 | AMETH_0614 | ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Lon protease; 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. | 0.650 |
| clpC | clpX | AMETH_6555 | AMETH_1735 | ATP-dependent chaperone ClpB; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease ATP-binding subunit clpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.523 |
| clpC | ftsH | AMETH_6555 | AMETH_6573 | ATP-dependent chaperone ClpB; Belongs to the ClpA/ClpB family. | Cell division protease FtsH; 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. | 0.602 |
| clpC | lon | AMETH_6555 | AMETH_0614 | ATP-dependent chaperone ClpB; Belongs to the ClpA/ClpB family. | Lon protease; 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. | 0.650 |
| clpX | clpA | AMETH_1735 | AMETH_2565 | ATP-dependent Clp protease ATP-binding subunit clpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | ATPase AAA-2 domain protein; Belongs to the ClpA/ClpB family. | 0.523 |
| clpX | clpB | AMETH_1735 | AMETH_6796 | ATP-dependent Clp protease ATP-binding subunit clpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 0.523 |
| clpX | clpC | AMETH_1735 | AMETH_6555 | ATP-dependent Clp protease ATP-binding subunit clpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | ATP-dependent chaperone ClpB; Belongs to the ClpA/ClpB family. | 0.523 |
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