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 |
| gcvH | lipA | sce2013 | sce1573 | Glycine cleavage system protein H homologue; 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. | Lipoyl 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. | 0.929 |
| gcvH | lipB | sce2013 | sce2545 | Glycine cleavage system protein H homologue; 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. | Putative 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. | 0.876 |
| lipA | gcvH | sce1573 | sce2013 | Lipoyl 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. | Glycine cleavage system protein H homologue; 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. | 0.929 |
| lipA | lipB | sce1573 | sce2545 | Lipoyl 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. | Putative 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. | 0.998 |
| lipB | gcvH | sce2545 | sce2013 | Putative 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 protein H homologue; 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. | 0.876 |
| lipB | lipA | sce2545 | sce1573 | Putative 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. | Lipoyl 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. | 0.998 |
| lipB | sce1201 | sce2545 | sce1201 | Putative 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; Specificity unclear. | 0.808 |
| lipB | sce2526 | sce2545 | sce2526 | Putative 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; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.808 |
| lipB | sce3106 | sce2545 | sce3106 | Putative 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. | Hypothetical protein predicted by Glimmer/Critica. | 0.808 |
| lipB | sce3351 | sce2545 | sce3351 | Putative 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. | Putative beta-ketoacyl synthase; Family membership; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.808 |
| lipB | sce3813 | sce2545 | sce3813 | Putative 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-ACP synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | 0.808 |
| lipB | sce5922 | sce2545 | sce5922 | Putative 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. | Oxoacyl-(acyl-carrier-protein) synthase II; Family membership; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.808 |
| lipB | sce8358 | sce2545 | sce8358 | Putative 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. | Putative 3-oxoacyl-[acyl-carrier-protein] synthase domain protein; Family membership. | 0.808 |
| lipB | sce9335 | sce2545 | sce9335 | Putative 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. | Hypothetical protein predicted by Glimmer/Critica. | 0.808 |
| sce1201 | lipB | sce1201 | sce2545 | 3-oxoacyl-[acyl-carrier-protein] synthase; Specificity unclear. | Putative 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 |
| sce1201 | sce2526 | sce1201 | sce2526 | 3-oxoacyl-[acyl-carrier-protein] synthase; Specificity unclear. | 3-oxoacyl-[acyl-carrier-protein] synthase; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.900 |
| sce1201 | sce3106 | sce1201 | sce3106 | 3-oxoacyl-[acyl-carrier-protein] synthase; Specificity unclear. | Hypothetical protein predicted by Glimmer/Critica. | 0.900 |
| sce1201 | sce3351 | sce1201 | sce3351 | 3-oxoacyl-[acyl-carrier-protein] synthase; Specificity unclear. | Putative beta-ketoacyl synthase; Family membership; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.900 |
| sce1201 | sce3813 | sce1201 | sce3813 | 3-oxoacyl-[acyl-carrier-protein] synthase; Specificity unclear. | Beta-ketoacyl-ACP synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | 0.900 |
| sce1201 | sce5922 | sce1201 | sce5922 | 3-oxoacyl-[acyl-carrier-protein] synthase; Specificity unclear. | Oxoacyl-(acyl-carrier-protein) synthase II; Family membership; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.900 |
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