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 |
| Ahcy | AhcyL1 | FBpp0312000 | FBpp0072886 | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | 0.936 |
| Ahcy | AhcyL2 | FBpp0312000 | FBpp0089085 | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | Adenosylhomocysteinase like 2 (AhcyL2) encodes a protein that, together with the product of AhcyL1, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | 0.913 |
| Ahcy | CG10623 | FBpp0312000 | FBpp0311160 | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | CG10623 protein; Zinc ion binding; betaine-homocysteine S-methyltransferase activity; S-adenosylmethionine-homocysteine S-methyltransferase activity. It is involved in the biological process described with: S-methylmethionine cycle; methionine biosynthetic process. | 0.959 |
| Ahcy | Cbs | FBpp0312000 | FBpp0076938 | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | Cystathionine beta-synthase (Cbs) encodes an enzyme involved in endoplasmic reticulum stress response; Belongs to the cysteine synthase/cystathionine beta- synthase family. | 0.979 |
| Ahcy | Eip55E | FBpp0312000 | FBpp0311547 | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | Ecdysone-induced protein 55E (Eip55E) encodes a protein involved in glutathione biosynthesis. | 0.955 |
| AhcyL1 | Ahcy | FBpp0072886 | FBpp0312000 | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | 0.936 |
| AhcyL1 | AhcyL2 | FBpp0072886 | FBpp0089085 | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | Adenosylhomocysteinase like 2 (AhcyL2) encodes a protein that, together with the product of AhcyL1, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | 0.940 |
| AhcyL1 | CG10623 | FBpp0072886 | FBpp0311160 | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | CG10623 protein; Zinc ion binding; betaine-homocysteine S-methyltransferase activity; S-adenosylmethionine-homocysteine S-methyltransferase activity. It is involved in the biological process described with: S-methylmethionine cycle; methionine biosynthetic process. | 0.931 |
| AhcyL1 | Cbs | FBpp0072886 | FBpp0076938 | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | Cystathionine beta-synthase (Cbs) encodes an enzyme involved in endoplasmic reticulum stress response; Belongs to the cysteine synthase/cystathionine beta- synthase family. | 0.973 |
| AhcyL1 | Eip55E | FBpp0072886 | FBpp0311547 | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | Ecdysone-induced protein 55E (Eip55E) encodes a protein involved in glutathione biosynthesis. | 0.904 |
| AhcyL2 | Ahcy | FBpp0089085 | FBpp0312000 | Adenosylhomocysteinase like 2 (AhcyL2) encodes a protein that, together with the product of AhcyL1, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | 0.913 |
| AhcyL2 | AhcyL1 | FBpp0089085 | FBpp0072886 | Adenosylhomocysteinase like 2 (AhcyL2) encodes a protein that, together with the product of AhcyL1, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | 0.940 |
| AhcyL2 | CG10623 | FBpp0089085 | FBpp0311160 | Adenosylhomocysteinase like 2 (AhcyL2) encodes a protein that, together with the product of AhcyL1, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | CG10623 protein; Zinc ion binding; betaine-homocysteine S-methyltransferase activity; S-adenosylmethionine-homocysteine S-methyltransferase activity. It is involved in the biological process described with: S-methylmethionine cycle; methionine biosynthetic process. | 0.935 |
| AhcyL2 | Cbs | FBpp0089085 | FBpp0076938 | Adenosylhomocysteinase like 2 (AhcyL2) encodes a protein that, together with the product of AhcyL1, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | Cystathionine beta-synthase (Cbs) encodes an enzyme involved in endoplasmic reticulum stress response; Belongs to the cysteine synthase/cystathionine beta- synthase family. | 0.973 |
| AhcyL2 | Eip55E | FBpp0089085 | FBpp0311547 | Adenosylhomocysteinase like 2 (AhcyL2) encodes a protein that, together with the product of AhcyL1, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | Ecdysone-induced protein 55E (Eip55E) encodes a protein involved in glutathione biosynthesis. | 0.938 |
| CG10623 | Ahcy | FBpp0311160 | FBpp0312000 | CG10623 protein; Zinc ion binding; betaine-homocysteine S-methyltransferase activity; S-adenosylmethionine-homocysteine S-methyltransferase activity. It is involved in the biological process described with: S-methylmethionine cycle; methionine biosynthetic process. | Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions. | 0.959 |
| CG10623 | AhcyL1 | FBpp0311160 | FBpp0072886 | CG10623 protein; Zinc ion binding; betaine-homocysteine S-methyltransferase activity; S-adenosylmethionine-homocysteine S-methyltransferase activity. It is involved in the biological process described with: S-methylmethionine cycle; methionine biosynthetic process. | Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | 0.931 |
| CG10623 | AhcyL2 | FBpp0311160 | FBpp0089085 | CG10623 protein; Zinc ion binding; betaine-homocysteine S-methyltransferase activity; S-adenosylmethionine-homocysteine S-methyltransferase activity. It is involved in the biological process described with: S-methylmethionine cycle; methionine biosynthetic process. | Adenosylhomocysteinase like 2 (AhcyL2) encodes a protein that, together with the product of AhcyL1, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...] | 0.935 |
| CG10623 | Cbs | FBpp0311160 | FBpp0076938 | CG10623 protein; Zinc ion binding; betaine-homocysteine S-methyltransferase activity; S-adenosylmethionine-homocysteine S-methyltransferase activity. It is involved in the biological process described with: S-methylmethionine cycle; methionine biosynthetic process. | Cystathionine beta-synthase (Cbs) encodes an enzyme involved in endoplasmic reticulum stress response; Belongs to the cysteine synthase/cystathionine beta- synthase family. | 0.976 |
| CG10623 | Eip55E | FBpp0311160 | FBpp0311547 | CG10623 protein; Zinc ion binding; betaine-homocysteine S-methyltransferase activity; S-adenosylmethionine-homocysteine S-methyltransferase activity. It is involved in the biological process described with: S-methylmethionine cycle; methionine biosynthetic process. | Ecdysone-induced protein 55E (Eip55E) encodes a protein involved in glutathione biosynthesis. | 0.972 |
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