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 |
| SDQ34289.1 | SDQ61323.1 | SAMN04489742_0731 | SAMN04489742_1829 | Exodeoxyribonuclease-3. | Exodeoxyribonuclease-3. | 0.928 |
| SDQ34289.1 | SDQ65563.1 | SAMN04489742_0731 | SAMN04489742_2005 | Exodeoxyribonuclease-3. | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | 0.713 |
| SDQ34289.1 | nth | SAMN04489742_0731 | SAMN04489742_2960 | Exodeoxyribonuclease-3. | DNA-(apurinic or apyrimidinic site) lyase; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. | 0.957 |
| SDQ34289.1 | ung | SAMN04489742_0731 | SAMN04489742_1331 | Exodeoxyribonuclease-3. | Uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.582 |
| SDQ49255.1 | SDQ49285.1 | SAMN04489742_1329 | SAMN04489742_1330 | LytR cell envelope-related transcriptional attenuator. | Protein of unknown function. | 0.705 |
| SDQ49255.1 | ung | SAMN04489742_1329 | SAMN04489742_1331 | LytR cell envelope-related transcriptional attenuator. | Uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.529 |
| SDQ49285.1 | SDQ49255.1 | SAMN04489742_1330 | SAMN04489742_1329 | Protein of unknown function. | LytR cell envelope-related transcriptional attenuator. | 0.705 |
| SDQ49285.1 | ung | SAMN04489742_1330 | SAMN04489742_1331 | Protein of unknown function. | Uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.651 |
| SDQ49335.1 | ung | SAMN04489742_1332 | SAMN04489742_1331 | NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains. | Uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.553 |
| SDQ61323.1 | SDQ34289.1 | SAMN04489742_1829 | SAMN04489742_0731 | Exodeoxyribonuclease-3. | Exodeoxyribonuclease-3. | 0.928 |
| SDQ61323.1 | SDQ65563.1 | SAMN04489742_1829 | SAMN04489742_2005 | Exodeoxyribonuclease-3. | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | 0.713 |
| SDQ61323.1 | nth | SAMN04489742_1829 | SAMN04489742_2960 | Exodeoxyribonuclease-3. | DNA-(apurinic or apyrimidinic site) lyase; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. | 0.605 |
| SDQ61323.1 | ung | SAMN04489742_1829 | SAMN04489742_1331 | Exodeoxyribonuclease-3. | Uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.582 |
| SDQ65563.1 | SDQ34289.1 | SAMN04489742_2005 | SAMN04489742_0731 | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | Exodeoxyribonuclease-3. | 0.713 |
| SDQ65563.1 | SDQ61323.1 | SAMN04489742_2005 | SAMN04489742_1829 | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | Exodeoxyribonuclease-3. | 0.713 |
| SDQ65563.1 | SDQ71754.1 | SAMN04489742_2005 | SAMN04489742_2271 | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family. | 0.713 |
| SDQ65563.1 | ung | SAMN04489742_2005 | SAMN04489742_1331 | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | Uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.671 |
| SDQ71754.1 | SDQ65563.1 | SAMN04489742_2271 | SAMN04489742_2005 | Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family. | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] | 0.713 |
| SDQ71754.1 | nth | SAMN04489742_2271 | SAMN04489742_2960 | Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family. | DNA-(apurinic or apyrimidinic site) lyase; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. | 0.605 |
| SDQ71754.1 | ung | SAMN04489742_2271 | SAMN04489742_1331 | Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family. | Uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.582 |
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