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 |
| AGA24686.1 | AGA27986.1 | Sinac_0235 | Sinac_3748 | Beta-ketoacyl-acyl-carrier-protein synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.808 |
| AGA24686.1 | AGA29468.1 | Sinac_0235 | Sinac_5318 | Beta-ketoacyl-acyl-carrier-protein synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | PFAM: Biotin/lipoate A/B protein ligase family. | 0.807 |
| AGA25747.1 | AGA27986.1 | Sinac_1363 | Sinac_3748 | Beta-ketoacyl-acyl-carrier-protein synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.808 |
| AGA25747.1 | AGA29468.1 | Sinac_1363 | Sinac_5318 | Beta-ketoacyl-acyl-carrier-protein synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | PFAM: Biotin/lipoate A/B protein ligase family. | 0.807 |
| AGA25770.1 | AGA27986.1 | Sinac_1387 | Sinac_3748 | 3-oxoacyl-(acyl-carrier-protein) synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.808 |
| AGA25770.1 | AGA29468.1 | Sinac_1387 | Sinac_5318 | 3-oxoacyl-(acyl-carrier-protein) synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | PFAM: Biotin/lipoate A/B protein ligase family. | 0.807 |
| AGA26058.1 | AGA27986.1 | Sinac_1682 | Sinac_3748 | 3-oxoacyl-(acyl-carrier-protein) synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.808 |
| AGA26058.1 | AGA29468.1 | Sinac_1682 | Sinac_5318 | 3-oxoacyl-(acyl-carrier-protein) synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | PFAM: Biotin/lipoate A/B protein ligase family. | 0.807 |
| AGA26564.1 | AGA27986.1 | Sinac_2246 | Sinac_3748 | PFAM: Beta-ketoacyl synthase, N-terminal domain; Beta-ketoacyl synthase, C-terminal domain; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.808 |
| AGA26564.1 | AGA29468.1 | Sinac_2246 | Sinac_5318 | PFAM: Beta-ketoacyl synthase, N-terminal domain; Beta-ketoacyl synthase, C-terminal domain; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | PFAM: Biotin/lipoate A/B protein ligase family. | 0.807 |
| AGA27986.1 | AGA24686.1 | Sinac_3748 | Sinac_0235 | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | Beta-ketoacyl-acyl-carrier-protein synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | 0.808 |
| AGA27986.1 | AGA25747.1 | Sinac_3748 | Sinac_1363 | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | Beta-ketoacyl-acyl-carrier-protein synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | 0.808 |
| AGA27986.1 | AGA25770.1 | Sinac_3748 | Sinac_1387 | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 3-oxoacyl-(acyl-carrier-protein) synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | 0.808 |
| AGA27986.1 | AGA26058.1 | Sinac_3748 | Sinac_1682 | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 3-oxoacyl-(acyl-carrier-protein) synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | 0.808 |
| AGA27986.1 | AGA26564.1 | Sinac_3748 | Sinac_2246 | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | PFAM: Beta-ketoacyl synthase, N-terminal domain; Beta-ketoacyl synthase, C-terminal domain; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.808 |
| AGA27986.1 | AGA29468.1 | Sinac_3748 | Sinac_5318 | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | PFAM: Biotin/lipoate A/B protein ligase family. | 0.923 |
| AGA27986.1 | AGA30310.1 | Sinac_3748 | Sinac_6212 | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | PFAM: Beta-ketoacyl synthase, N-terminal domain; Beta-ketoacyl synthase, C-terminal domain; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.808 |
| AGA27986.1 | AGA30609.1 | Sinac_3748 | Sinac_6534 | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | PFAM: Biotin/lipoate A/B protein ligase family. | 0.923 |
| AGA27986.1 | gcvH | Sinac_3748 | Sinac_5322 | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | Glycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | 0.839 |
| AGA27986.1 | lipA | Sinac_3748 | Sinac_3747 | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | Lipoate synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.999 |
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