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 |
| bepA | loiP | b2494 | b2936 | OM protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions; Belongs to the peptidase M48 family. BepA subfamily. | Phe-Phe periplasmic metalloprotease, OM lipoprotein; Metalloprotease that cleaves substrates preferentially between Phe-Phe residues. Plays a role in response to some stress conditions. Seems to regulate the expression of speB. | 0.468 |
| crfC | htpX | b4109 | b1829 | Clamp-binding sister replication fork colocalization protein, dynamin-related; Important for the colocalization of sister nascent DNA strands after replication fork passage during DNA replication, and for positioning and subsequent partitioning of sister chromosomes. Does not have GTPase activity on its own; Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. | Putative endopeptidase; Membrane-localized protease able to endoproteolytically degrade overproduced SecY but not YccA, another membrane protein. It seems to cleave SecY at specific cytoplasmic sites. Does not require ATP. Its natural substrate has not been identified. Probably plays a role in the quality control of integral membrane proteins. Belongs to the peptidase M48B family. | 0.412 |
| crfC | loiP | b4109 | b2936 | Clamp-binding sister replication fork colocalization protein, dynamin-related; Important for the colocalization of sister nascent DNA strands after replication fork passage during DNA replication, and for positioning and subsequent partitioning of sister chromosomes. Does not have GTPase activity on its own; Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. | Phe-Phe periplasmic metalloprotease, OM lipoprotein; Metalloprotease that cleaves substrates preferentially between Phe-Phe residues. Plays a role in response to some stress conditions. Seems to regulate the expression of speB. | 0.412 |
| dcp | loiP | b1538 | b2936 | Dipeptidyl carboxypeptidase II; Removes dipeptides from the C-termini of N-blocked tripeptides, tetrapeptides and larger peptides. Belongs to the peptidase M3 family. | Phe-Phe periplasmic metalloprotease, OM lipoprotein; Metalloprotease that cleaves substrates preferentially between Phe-Phe residues. Plays a role in response to some stress conditions. Seems to regulate the expression of speB. | 0.460 |
| ftsH | htpX | b3178 | b1829 | Protease, ATP-dependent zinc-metallo; 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. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent [...] | Putative endopeptidase; Membrane-localized protease able to endoproteolytically degrade overproduced SecY but not YccA, another membrane protein. It seems to cleave SecY at specific cytoplasmic sites. Does not require ATP. Its natural substrate has not been identified. Probably plays a role in the quality control of integral membrane proteins. Belongs to the peptidase M48B family. | 0.905 |
| ftsH | loiP | b3178 | b2936 | Protease, ATP-dependent zinc-metallo; 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. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent [...] | Phe-Phe periplasmic metalloprotease, OM lipoprotein; Metalloprotease that cleaves substrates preferentially between Phe-Phe residues. Plays a role in response to some stress conditions. Seems to regulate the expression of speB. | 0.420 |
| htpX | crfC | b1829 | b4109 | Putative endopeptidase; Membrane-localized protease able to endoproteolytically degrade overproduced SecY but not YccA, another membrane protein. It seems to cleave SecY at specific cytoplasmic sites. Does not require ATP. Its natural substrate has not been identified. Probably plays a role in the quality control of integral membrane proteins. Belongs to the peptidase M48B family. | Clamp-binding sister replication fork colocalization protein, dynamin-related; Important for the colocalization of sister nascent DNA strands after replication fork passage during DNA replication, and for positioning and subsequent partitioning of sister chromosomes. Does not have GTPase activity on its own; Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. | 0.412 |
| htpX | ftsH | b1829 | b3178 | Putative endopeptidase; Membrane-localized protease able to endoproteolytically degrade overproduced SecY but not YccA, another membrane protein. It seems to cleave SecY at specific cytoplasmic sites. Does not require ATP. Its natural substrate has not been identified. Probably plays a role in the quality control of integral membrane proteins. Belongs to the peptidase M48B family. | Protease, ATP-dependent zinc-metallo; 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. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent [...] | 0.905 |
| htpX | loiP | b1829 | b2936 | Putative endopeptidase; Membrane-localized protease able to endoproteolytically degrade overproduced SecY but not YccA, another membrane protein. It seems to cleave SecY at specific cytoplasmic sites. Does not require ATP. Its natural substrate has not been identified. Probably plays a role in the quality control of integral membrane proteins. Belongs to the peptidase M48B family. | Phe-Phe periplasmic metalloprotease, OM lipoprotein; Metalloprotease that cleaves substrates preferentially between Phe-Phe residues. Plays a role in response to some stress conditions. Seems to regulate the expression of speB. | 0.532 |
| loiP | bepA | b2936 | b2494 | Phe-Phe periplasmic metalloprotease, OM lipoprotein; Metalloprotease that cleaves substrates preferentially between Phe-Phe residues. Plays a role in response to some stress conditions. Seems to regulate the expression of speB. | OM protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions; Belongs to the peptidase M48 family. BepA subfamily. | 0.468 |
| loiP | crfC | b2936 | b4109 | Phe-Phe periplasmic metalloprotease, OM lipoprotein; Metalloprotease that cleaves substrates preferentially between Phe-Phe residues. Plays a role in response to some stress conditions. Seems to regulate the expression of speB. | Clamp-binding sister replication fork colocalization protein, dynamin-related; Important for the colocalization of sister nascent DNA strands after replication fork passage during DNA replication, and for positioning and subsequent partitioning of sister chromosomes. Does not have GTPase activity on its own; Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. | 0.412 |
| loiP | dcp | b2936 | b1538 | Phe-Phe periplasmic metalloprotease, OM lipoprotein; Metalloprotease that cleaves substrates preferentially between Phe-Phe residues. Plays a role in response to some stress conditions. Seems to regulate the expression of speB. | Dipeptidyl carboxypeptidase II; Removes dipeptides from the C-termini of N-blocked tripeptides, tetrapeptides and larger peptides. Belongs to the peptidase M3 family. | 0.460 |
| loiP | ftsH | b2936 | b3178 | Phe-Phe periplasmic metalloprotease, OM lipoprotein; Metalloprotease that cleaves substrates preferentially between Phe-Phe residues. Plays a role in response to some stress conditions. Seems to regulate the expression of speB. | Protease, ATP-dependent zinc-metallo; 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. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent [...] | 0.420 |
| loiP | htpX | b2936 | b1829 | Phe-Phe periplasmic metalloprotease, OM lipoprotein; Metalloprotease that cleaves substrates preferentially between Phe-Phe residues. Plays a role in response to some stress conditions. Seems to regulate the expression of speB. | Putative endopeptidase; Membrane-localized protease able to endoproteolytically degrade overproduced SecY but not YccA, another membrane protein. It seems to cleave SecY at specific cytoplasmic sites. Does not require ATP. Its natural substrate has not been identified. Probably plays a role in the quality control of integral membrane proteins. Belongs to the peptidase M48B family. | 0.532 |
| loiP | tktA | b2936 | b2935 | Phe-Phe periplasmic metalloprotease, OM lipoprotein; Metalloprotease that cleaves substrates preferentially between Phe-Phe residues. Plays a role in response to some stress conditions. Seems to regulate the expression of speB. | Transketolase 1, thiamine triphosphate-binding; Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. Thus, catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose- 5-phosphate. | 0.438 |
| tktA | loiP | b2935 | b2936 | Transketolase 1, thiamine triphosphate-binding; Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. Thus, catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose- 5-phosphate. | Phe-Phe periplasmic metalloprotease, OM lipoprotein; Metalloprotease that cleaves substrates preferentially between Phe-Phe residues. Plays a role in response to some stress conditions. Seems to regulate the expression of speB. | 0.438 |