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 |
| flgA | flgJ | azo2741 | azo2732 | Flagella basal body P-ring formation protein flgA precursor. Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a chaperon protein for the P-ring assembly (by similarity). signal peptide no TMHs; High confidence in function and specificity. | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | 0.992 |
| flgA | fliJ | azo2741 | azo2720 | Flagella basal body P-ring formation protein flgA precursor. Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a chaperon protein for the P-ring assembly (by similarity). signal peptide no TMHs; High confidence in function and specificity. | Flagellar fliJ protein. FLAGELLAR PROTEIN THAT AFFECTS CHEMOTACTIC EVENTS. Might have a chaperon-like activity InterPro: Flagellar FliJ protein no signal peptide no TMHs; Family membership. | 0.914 |
| flgA | fliK | azo2741 | azo2721 | Flagella basal body P-ring formation protein flgA precursor. Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a chaperon protein for the P-ring assembly (by similarity). signal peptide no TMHs; High confidence in function and specificity. | Flagellar hook-length control protein. Controls the length of the flagellar hook. no TMHs no signal peptide; Family membership. | 0.936 |
| flgA | fliL | azo2741 | azo2722 | Flagella basal body P-ring formation protein flgA precursor. Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a chaperon protein for the P-ring assembly (by similarity). signal peptide no TMHs; High confidence in function and specificity. | Putative flagellar basal body-associated protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | 0.973 |
| flgA | fliM | azo2741 | azo2723 | Flagella basal body P-ring formation protein flgA precursor. Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a chaperon protein for the P-ring assembly (by similarity). signal peptide no TMHs; High confidence in function and specificity. | Flagellar motor switch protein fliM. FLIM IS ONE OF THREE PROTEINS (FLIG FLIN FLIM) THAT FORM A SWITCH COMPLEX THAT IS PROPOSED TO BE LOCATED AT THE BASE OF THE BASAL BODY. THIS COMPLEX INTERACTS WITH THE CHEY AND CHEZ CHEMOTAXIS PROTEINS IN ADDITION TO CONTACTING COMPONENTS OF THE MOTOR THAT DETERMINE THE DIRECTION OF FLAGELLAR ROTATION. InterPro: Flagellar motor switch protein FliM Pfam:Flagellar motor switch protein FliM no TMHs signale peptide: no analysis; High confidence in function and specificity. | 0.972 |
| flgA | fliN | azo2741 | azo2724 | Flagella basal body P-ring formation protein flgA precursor. Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a chaperon protein for the P-ring assembly (by similarity). signal peptide no TMHs; High confidence in function and specificity. | Flagellar motor switch protein fliN (Flagellar motor switch protein mopA) (Fragment). FliN is one of three proteins (FliG FliN FliM) that form a switch complex that is proposed to be located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins in addition to contacting components of the motor that determine the dirction of flagellar rotation (by similarity). InterPro: Surface presentation of antigens (SPOA) protein, Flagellar motor switch FliN protein Pfam: Surface presentation of antigens (SPOA) protein no signal peptide no TMHs; High confid [...] | 0.930 |
| flgA | fliO | azo2741 | azo2725 | Flagella basal body P-ring formation protein flgA precursor. Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a chaperon protein for the P-ring assembly (by similarity). signal peptide no TMHs; High confidence in function and specificity. | Flagellar biosynthesis protein,FliO, 26% identity to TrEMBL;Q8XBA2, Q83ML3. SProt;P22586 Has Signal peptide. Has PF04347, Flagellar biosynthesis protein,FliO;IPR007442; FliO is an essential component of the flagellum-specific protein export apparatus. It is an integral membrane protein. Its precise molecular function is unknown. | 0.968 |
| flgA | fliP | azo2741 | azo2726 | Flagella basal body P-ring formation protein flgA precursor. Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a chaperon protein for the P-ring assembly (by similarity). signal peptide no TMHs; High confidence in function and specificity. | Flagellar biosynthetic protein FliP; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. | 0.926 |
| flgA | fliQ | azo2741 | azo2727 | Flagella basal body P-ring formation protein flgA precursor. Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a chaperon protein for the P-ring assembly (by similarity). signal peptide no TMHs; High confidence in function and specificity. | Flagellar biosynthesis protein FliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. | 0.913 |
| flgA | fliR | azo2741 | azo2728 | Flagella basal body P-ring formation protein flgA precursor. Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a chaperon protein for the P-ring assembly (by similarity). signal peptide no TMHs; High confidence in function and specificity. | Flagellar biosynthesis protein FliR; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. | 0.743 |
| flgJ | flgA | azo2732 | azo2741 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Flagella basal body P-ring formation protein flgA precursor. Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a chaperon protein for the P-ring assembly (by similarity). signal peptide no TMHs; High confidence in function and specificity. | 0.992 |
| flgJ | fliJ | azo2732 | azo2720 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Flagellar fliJ protein. FLAGELLAR PROTEIN THAT AFFECTS CHEMOTACTIC EVENTS. Might have a chaperon-like activity InterPro: Flagellar FliJ protein no signal peptide no TMHs; Family membership. | 0.946 |
| flgJ | fliK | azo2732 | azo2721 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Flagellar hook-length control protein. Controls the length of the flagellar hook. no TMHs no signal peptide; Family membership. | 0.990 |
| flgJ | fliL | azo2732 | azo2722 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Putative flagellar basal body-associated protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | 0.978 |
| flgJ | fliM | azo2732 | azo2723 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Flagellar motor switch protein fliM. FLIM IS ONE OF THREE PROTEINS (FLIG FLIN FLIM) THAT FORM A SWITCH COMPLEX THAT IS PROPOSED TO BE LOCATED AT THE BASE OF THE BASAL BODY. THIS COMPLEX INTERACTS WITH THE CHEY AND CHEZ CHEMOTAXIS PROTEINS IN ADDITION TO CONTACTING COMPONENTS OF THE MOTOR THAT DETERMINE THE DIRECTION OF FLAGELLAR ROTATION. InterPro: Flagellar motor switch protein FliM Pfam:Flagellar motor switch protein FliM no TMHs signale peptide: no analysis; High confidence in function and specificity. | 0.986 |
| flgJ | fliN | azo2732 | azo2724 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Flagellar motor switch protein fliN (Flagellar motor switch protein mopA) (Fragment). FliN is one of three proteins (FliG FliN FliM) that form a switch complex that is proposed to be located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins in addition to contacting components of the motor that determine the dirction of flagellar rotation (by similarity). InterPro: Surface presentation of antigens (SPOA) protein, Flagellar motor switch FliN protein Pfam: Surface presentation of antigens (SPOA) protein no signal peptide no TMHs; High confid [...] | 0.963 |
| flgJ | fliO | azo2732 | azo2725 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Flagellar biosynthesis protein,FliO, 26% identity to TrEMBL;Q8XBA2, Q83ML3. SProt;P22586 Has Signal peptide. Has PF04347, Flagellar biosynthesis protein,FliO;IPR007442; FliO is an essential component of the flagellum-specific protein export apparatus. It is an integral membrane protein. Its precise molecular function is unknown. | 0.974 |
| flgJ | fliP | azo2732 | azo2726 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Flagellar biosynthetic protein FliP; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. | 0.956 |
| flgJ | fliQ | azo2732 | azo2727 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Flagellar biosynthesis protein FliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. | 0.952 |
| flgJ | fliR | azo2732 | azo2728 | Peptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. | Flagellar biosynthesis protein FliR; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. | 0.763 |
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