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 |
| MG_055 | MG_277 | MG_055 | MG_277 | Preprotein translocase, SecE subunit; MG055 has 1 transmembrane region. The expression of this M. genitalium protein was reported in a proteome analysis (Eur. J. Biochem. 267, 1571-1582 (2000)); identified by similarity to EGAD:56896; match to protein family HMM TIGR00964. | Membrane protein, putative; The orthologous gene in Mycoplasma pneumoniae was annotated as secretory protein gene secD. This was was based on psi-BLAST analysis and the authors commented the secD-like domain of the M. pneumoniae gene and MG277 should further complete the secretory repertoire in these mollicutes (Dandekar et al. 2000. NAR. 28:3278-88); identified by similarity to EGAD:57056. | 0.989 |
| MG_055 | ffh | MG_055 | MG_048 | Preprotein translocase, SecE subunit; MG055 has 1 transmembrane region. The expression of this M. genitalium protein was reported in a proteome analysis (Eur. J. Biochem. 267, 1571-1582 (2000)); identified by similarity to EGAD:56896; match to protein family HMM TIGR00964. | Signal recognition particle protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Belongs to the GTP-binding SRP family. SRP54 subfamily. | 0.978 |
| MG_055 | ftsY | MG_055 | MG_297 | Preprotein translocase, SecE subunit; MG055 has 1 transmembrane region. The expression of this M. genitalium protein was reported in a proteome analysis (Eur. J. Biochem. 267, 1571-1582 (2000)); identified by similarity to EGAD:56896; match to protein family HMM TIGR00964. | Signal recognition particle-docking protein FtsY; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). | 0.975 |
| MG_055 | secA | MG_055 | MG_072 | Preprotein translocase, SecE subunit; MG055 has 1 transmembrane region. The expression of this M. genitalium protein was reported in a proteome analysis (Eur. J. Biochem. 267, 1571-1582 (2000)); identified by similarity to EGAD:56896; match to protein family HMM TIGR00964. | Preprotein translocase, SecA subunit; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. | 0.997 |
| MG_055 | secG | MG_055 | MG_476 | Preprotein translocase, SecE subunit; MG055 has 1 transmembrane region. The expression of this M. genitalium protein was reported in a proteome analysis (Eur. J. Biochem. 267, 1571-1582 (2000)); identified by similarity to EGAD:56896; match to protein family HMM TIGR00964. | Hypothetical protein; Involved in protein export. Participates in an early event of protein translocation (By similarity); Belongs to the SecG family. | 0.999 |
| MG_055 | secY | MG_055 | MG_170 | Preprotein translocase, SecE subunit; MG055 has 1 transmembrane region. The expression of this M. genitalium protein was reported in a proteome analysis (Eur. J. Biochem. 267, 1571-1582 (2000)); identified by similarity to EGAD:56896; match to protein family HMM TIGR00964. | Preprotein translocase, SecY subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.999 |
| MG_055 | yidC | MG_055 | MG_464 | Preprotein translocase, SecE subunit; MG055 has 1 transmembrane region. The expression of this M. genitalium protein was reported in a proteome analysis (Eur. J. Biochem. 267, 1571-1582 (2000)); identified by similarity to EGAD:56896; match to protein family HMM TIGR00964. | Membrane protein, putative; Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins (By similarity). | 0.980 |
| MG_277 | MG_055 | MG_277 | MG_055 | Membrane protein, putative; The orthologous gene in Mycoplasma pneumoniae was annotated as secretory protein gene secD. This was was based on psi-BLAST analysis and the authors commented the secD-like domain of the M. pneumoniae gene and MG277 should further complete the secretory repertoire in these mollicutes (Dandekar et al. 2000. NAR. 28:3278-88); identified by similarity to EGAD:57056. | Preprotein translocase, SecE subunit; MG055 has 1 transmembrane region. The expression of this M. genitalium protein was reported in a proteome analysis (Eur. J. Biochem. 267, 1571-1582 (2000)); identified by similarity to EGAD:56896; match to protein family HMM TIGR00964. | 0.989 |
| MG_277 | ffh | MG_277 | MG_048 | Membrane protein, putative; The orthologous gene in Mycoplasma pneumoniae was annotated as secretory protein gene secD. This was was based on psi-BLAST analysis and the authors commented the secD-like domain of the M. pneumoniae gene and MG277 should further complete the secretory repertoire in these mollicutes (Dandekar et al. 2000. NAR. 28:3278-88); identified by similarity to EGAD:57056. | Signal recognition particle protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Belongs to the GTP-binding SRP family. SRP54 subfamily. | 0.937 |
| MG_277 | ftsY | MG_277 | MG_297 | Membrane protein, putative; The orthologous gene in Mycoplasma pneumoniae was annotated as secretory protein gene secD. This was was based on psi-BLAST analysis and the authors commented the secD-like domain of the M. pneumoniae gene and MG277 should further complete the secretory repertoire in these mollicutes (Dandekar et al. 2000. NAR. 28:3278-88); identified by similarity to EGAD:57056. | Signal recognition particle-docking protein FtsY; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). | 0.934 |
| MG_277 | secA | MG_277 | MG_072 | Membrane protein, putative; The orthologous gene in Mycoplasma pneumoniae was annotated as secretory protein gene secD. This was was based on psi-BLAST analysis and the authors commented the secD-like domain of the M. pneumoniae gene and MG277 should further complete the secretory repertoire in these mollicutes (Dandekar et al. 2000. NAR. 28:3278-88); identified by similarity to EGAD:57056. | Preprotein translocase, SecA subunit; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. | 0.945 |
| MG_277 | secG | MG_277 | MG_476 | Membrane protein, putative; The orthologous gene in Mycoplasma pneumoniae was annotated as secretory protein gene secD. This was was based on psi-BLAST analysis and the authors commented the secD-like domain of the M. pneumoniae gene and MG277 should further complete the secretory repertoire in these mollicutes (Dandekar et al. 2000. NAR. 28:3278-88); identified by similarity to EGAD:57056. | Hypothetical protein; Involved in protein export. Participates in an early event of protein translocation (By similarity); Belongs to the SecG family. | 0.993 |
| MG_277 | secY | MG_277 | MG_170 | Membrane protein, putative; The orthologous gene in Mycoplasma pneumoniae was annotated as secretory protein gene secD. This was was based on psi-BLAST analysis and the authors commented the secD-like domain of the M. pneumoniae gene and MG277 should further complete the secretory repertoire in these mollicutes (Dandekar et al. 2000. NAR. 28:3278-88); identified by similarity to EGAD:57056. | Preprotein translocase, SecY subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.989 |
| MG_277 | yidC | MG_277 | MG_464 | Membrane protein, putative; The orthologous gene in Mycoplasma pneumoniae was annotated as secretory protein gene secD. This was was based on psi-BLAST analysis and the authors commented the secD-like domain of the M. pneumoniae gene and MG277 should further complete the secretory repertoire in these mollicutes (Dandekar et al. 2000. NAR. 28:3278-88); identified by similarity to EGAD:57056. | Membrane protein, putative; Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins (By similarity). | 0.990 |
| atpE | secY | MG_404 | MG_170 | ATP synthase F0, C subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Preprotein translocase, SecY subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.486 |
| atpE | yidC | MG_404 | MG_464 | ATP synthase F0, C subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Membrane protein, putative; Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins (By similarity). | 0.939 |
| ffh | MG_055 | MG_048 | MG_055 | Signal recognition particle protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Belongs to the GTP-binding SRP family. SRP54 subfamily. | Preprotein translocase, SecE subunit; MG055 has 1 transmembrane region. The expression of this M. genitalium protein was reported in a proteome analysis (Eur. J. Biochem. 267, 1571-1582 (2000)); identified by similarity to EGAD:56896; match to protein family HMM TIGR00964. | 0.978 |
| ffh | MG_277 | MG_048 | MG_277 | Signal recognition particle protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Belongs to the GTP-binding SRP family. SRP54 subfamily. | Membrane protein, putative; The orthologous gene in Mycoplasma pneumoniae was annotated as secretory protein gene secD. This was was based on psi-BLAST analysis and the authors commented the secD-like domain of the M. pneumoniae gene and MG277 should further complete the secretory repertoire in these mollicutes (Dandekar et al. 2000. NAR. 28:3278-88); identified by similarity to EGAD:57056. | 0.937 |
| ffh | ftsY | MG_048 | MG_297 | Signal recognition particle protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Belongs to the GTP-binding SRP family. SRP54 subfamily. | Signal recognition particle-docking protein FtsY; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). | 0.999 |
| ffh | gltX | MG_048 | MG_462 | Signal recognition particle protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Belongs to the GTP-binding SRP family. SRP54 subfamily. | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.877 |
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