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 |
| ABS22566.1 | ABS22568.1 | Bcer98_2320 | Bcer98_2322 | Transcriptional regulator, LysR family; PFAM: regulatory protein LysR; LysR substrate-binding; KEGG: btl:BALH_3308 transcriptional regulator, LysR family. | PFAM: LrgB family protein; KEGG: btl:BALH_3309 murein hydrolase export regulator. | 0.529 |
| ABS22566.1 | cidA | Bcer98_2320 | Bcer98_2321 | Transcriptional regulator, LysR family; PFAM: regulatory protein LysR; LysR substrate-binding; KEGG: btl:BALH_3308 transcriptional regulator, LysR family. | LrgA family protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypothesized to regulate the sub [...] | 0.530 |
| ABS22568.1 | ABS22566.1 | Bcer98_2322 | Bcer98_2320 | PFAM: LrgB family protein; KEGG: btl:BALH_3309 murein hydrolase export regulator. | Transcriptional regulator, LysR family; PFAM: regulatory protein LysR; LysR substrate-binding; KEGG: btl:BALH_3308 transcriptional regulator, LysR family. | 0.529 |
| ABS22568.1 | cidA | Bcer98_2322 | Bcer98_2321 | PFAM: LrgB family protein; KEGG: btl:BALH_3309 murein hydrolase export regulator. | LrgA family protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypothesized to regulate the sub [...] | 0.986 |
| ABS23873.1 | cidA | Bcer98_3676 | Bcer98_2321 | PFAM: LrgB family protein; KEGG: baa:BA_0197 hypothetical protein. | LrgA family protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypothesized to regulate the sub [...] | 0.894 |
| cidA | ABS22566.1 | Bcer98_2321 | Bcer98_2320 | LrgA family protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypothesized to regulate the sub [...] | Transcriptional regulator, LysR family; PFAM: regulatory protein LysR; LysR substrate-binding; KEGG: btl:BALH_3308 transcriptional regulator, LysR family. | 0.530 |
| cidA | ABS22568.1 | Bcer98_2321 | Bcer98_2322 | LrgA family protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypothesized to regulate the sub [...] | PFAM: LrgB family protein; KEGG: btl:BALH_3309 murein hydrolase export regulator. | 0.986 |
| cidA | ABS23873.1 | Bcer98_2321 | Bcer98_3676 | LrgA family protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypothesized to regulate the sub [...] | PFAM: LrgB family protein; KEGG: baa:BA_0197 hypothetical protein. | 0.894 |
| cidA | lrgB | Bcer98_2321 | Bcer98_3956 | LrgA family protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypothesized to regulate the sub [...] | LrgB family protein; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like protein CidA. The LrgAB and CidA proteins may affect the proton motive force of the membrane. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses; Belongs to the CidB/LrgB family. LrgB subfamily. | 0.893 |
| lrgB | cidA | Bcer98_3956 | Bcer98_2321 | LrgB family protein; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like protein CidA. The LrgAB and CidA proteins may affect the proton motive force of the membrane. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses; Belongs to the CidB/LrgB family. LrgB subfamily. | LrgA family protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypothesized to regulate the sub [...] | 0.893 |