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 |
| ACOT8 | BAAT | ENSP00000217455 | ENSP00000259407 | Acyl-coenzyme A thioesterase 8; Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Acyl-coenzyme A thioesterase 8/ACOT8 display no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs (By similarity). Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains. More [...] | Bile acid-CoA:amino acid N-acyltransferase; Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine. More than 95% of the BAs are N-acyl amidates with glycine and taurine. Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism. This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin abs [...] | 0.942 |
| ACOT8 | SCP2 | ENSP00000217455 | ENSP00000360569 | Acyl-coenzyme A thioesterase 8; Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Acyl-coenzyme A thioesterase 8/ACOT8 display no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs (By similarity). Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains. More [...] | Non-specific lipid-transfer protein; Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis. | 0.947 |
| ACOT8 | SLC27A5 | ENSP00000217455 | ENSP00000263093 | Acyl-coenzyme A thioesterase 8; Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Acyl-coenzyme A thioesterase 8/ACOT8 display no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs (By similarity). Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains. More [...] | Bile acyl-CoA synthetase; Acyl-CoA synthetase that catalyzes the activation of bile acids via formation of bile acid CoA thioesters which is necessary for their subsequent conjugation with glycine or taurine. Both primary bile acids (cholic acid and chenodeoxycholic acid) and secondary bile acids (deoxycholic acid and lithocholic acid) are the principal substrates. Also exhibits acyl CoA synthetase activity that activates very long-chain fatty acids (VLCFAs) by catalyzing the formation of fatty acyl-CoA. In vitro, also activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate ( [...] | 0.935 |
| BAAT | ACOT8 | ENSP00000259407 | ENSP00000217455 | Bile acid-CoA:amino acid N-acyltransferase; Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine. More than 95% of the BAs are N-acyl amidates with glycine and taurine. Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism. This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin abs [...] | Acyl-coenzyme A thioesterase 8; Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Acyl-coenzyme A thioesterase 8/ACOT8 display no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs (By similarity). Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains. More [...] | 0.942 |
| BAAT | CSAD | ENSP00000259407 | ENSP00000267085 | Bile acid-CoA:amino acid N-acyltransferase; Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine. More than 95% of the BAs are N-acyl amidates with glycine and taurine. Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism. This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin abs [...] | Cysteine sulfinic acid decarboxylase; Catalyzes the decarboxylation of L-aspartate, 3-sulfino-L- alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine and taurine, respectively. The preferred substrate is 3- sulfino-L-alanine. Does not exhibit any decarboxylation activity toward glutamate. | 0.929 |
| BAAT | GAD1 | ENSP00000259407 | ENSP00000350928 | Bile acid-CoA:amino acid N-acyltransferase; Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine. More than 95% of the BAs are N-acyl amidates with glycine and taurine. Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism. This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin abs [...] | Glutamate decarboxylase 1; Catalyzes the production of GABA. | 0.905 |
| BAAT | GAD2 | ENSP00000259407 | ENSP00000365437 | Bile acid-CoA:amino acid N-acyltransferase; Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine. More than 95% of the BAs are N-acyl amidates with glycine and taurine. Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism. This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin abs [...] | Glutamate decarboxylase 2; Catalyzes the production of GABA. | 0.904 |
| BAAT | GGT1 | ENSP00000259407 | ENSP00000248923 | Bile acid-CoA:amino acid N-acyltransferase; Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine. More than 95% of the BAs are N-acyl amidates with glycine and taurine. Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism. This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin abs [...] | Glutathione hydrolase 1 heavy chain; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione [...] | 0.914 |
| BAAT | GGT5 | ENSP00000259407 | ENSP00000381340 | Bile acid-CoA:amino acid N-acyltransferase; Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine. More than 95% of the BAs are N-acyl amidates with glycine and taurine. Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism. This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin abs [...] | Glutathione hydrolase 5 heavy chain; Cleaves the gamma-glutamyl peptide bond of glutathione conjugates, but maybe not glutathione itself. Converts leukotriene C4 (LTC4) to leukotriene D4 (LTD4). | 0.900 |
| BAAT | GGT6 | ENSP00000259407 | ENSP00000370962 | Bile acid-CoA:amino acid N-acyltransferase; Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine. More than 95% of the BAs are N-acyl amidates with glycine and taurine. Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism. This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin abs [...] | Glutathione hydrolase 6 heavy chain; Cleaves glutathione conjugates; Belongs to the gamma-glutamyltransferase family. | 0.906 |
| BAAT | GGT7 | ENSP00000259407 | ENSP00000338964 | Bile acid-CoA:amino acid N-acyltransferase; Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine. More than 95% of the BAs are N-acyl amidates with glycine and taurine. Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism. This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin abs [...] | Glutathione hydrolase 7 heavy chain; Cleaves glutathione conjugates; Belongs to the gamma-glutamyltransferase family. | 0.900 |
| BAAT | SCP2 | ENSP00000259407 | ENSP00000360569 | Bile acid-CoA:amino acid N-acyltransferase; Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine. More than 95% of the BAs are N-acyl amidates with glycine and taurine. Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism. This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin abs [...] | Non-specific lipid-transfer protein; Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis. | 0.956 |
| BAAT | SLC27A5 | ENSP00000259407 | ENSP00000263093 | Bile acid-CoA:amino acid N-acyltransferase; Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine. More than 95% of the BAs are N-acyl amidates with glycine and taurine. Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism. This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin abs [...] | Bile acyl-CoA synthetase; Acyl-CoA synthetase that catalyzes the activation of bile acids via formation of bile acid CoA thioesters which is necessary for their subsequent conjugation with glycine or taurine. Both primary bile acids (cholic acid and chenodeoxycholic acid) and secondary bile acids (deoxycholic acid and lithocholic acid) are the principal substrates. Also exhibits acyl CoA synthetase activity that activates very long-chain fatty acids (VLCFAs) by catalyzing the formation of fatty acyl-CoA. In vitro, also activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate ( [...] | 0.987 |
| CSAD | BAAT | ENSP00000267085 | ENSP00000259407 | Cysteine sulfinic acid decarboxylase; Catalyzes the decarboxylation of L-aspartate, 3-sulfino-L- alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine and taurine, respectively. The preferred substrate is 3- sulfino-L-alanine. Does not exhibit any decarboxylation activity toward glutamate. | Bile acid-CoA:amino acid N-acyltransferase; Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine. More than 95% of the BAs are N-acyl amidates with glycine and taurine. Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism. This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin abs [...] | 0.929 |
| CSAD | GAD1 | ENSP00000267085 | ENSP00000350928 | Cysteine sulfinic acid decarboxylase; Catalyzes the decarboxylation of L-aspartate, 3-sulfino-L- alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine and taurine, respectively. The preferred substrate is 3- sulfino-L-alanine. Does not exhibit any decarboxylation activity toward glutamate. | Glutamate decarboxylase 1; Catalyzes the production of GABA. | 0.904 |
| CSAD | GAD2 | ENSP00000267085 | ENSP00000365437 | Cysteine sulfinic acid decarboxylase; Catalyzes the decarboxylation of L-aspartate, 3-sulfino-L- alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine and taurine, respectively. The preferred substrate is 3- sulfino-L-alanine. Does not exhibit any decarboxylation activity toward glutamate. | Glutamate decarboxylase 2; Catalyzes the production of GABA. | 0.914 |
| CSAD | GGT1 | ENSP00000267085 | ENSP00000248923 | Cysteine sulfinic acid decarboxylase; Catalyzes the decarboxylation of L-aspartate, 3-sulfino-L- alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine and taurine, respectively. The preferred substrate is 3- sulfino-L-alanine. Does not exhibit any decarboxylation activity toward glutamate. | Glutathione hydrolase 1 heavy chain; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione [...] | 0.907 |
| CSAD | GGT5 | ENSP00000267085 | ENSP00000381340 | Cysteine sulfinic acid decarboxylase; Catalyzes the decarboxylation of L-aspartate, 3-sulfino-L- alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine and taurine, respectively. The preferred substrate is 3- sulfino-L-alanine. Does not exhibit any decarboxylation activity toward glutamate. | Glutathione hydrolase 5 heavy chain; Cleaves the gamma-glutamyl peptide bond of glutathione conjugates, but maybe not glutathione itself. Converts leukotriene C4 (LTC4) to leukotriene D4 (LTD4). | 0.908 |
| CSAD | GGT6 | ENSP00000267085 | ENSP00000370962 | Cysteine sulfinic acid decarboxylase; Catalyzes the decarboxylation of L-aspartate, 3-sulfino-L- alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine and taurine, respectively. The preferred substrate is 3- sulfino-L-alanine. Does not exhibit any decarboxylation activity toward glutamate. | Glutathione hydrolase 6 heavy chain; Cleaves glutathione conjugates; Belongs to the gamma-glutamyltransferase family. | 0.907 |
| CSAD | GGT7 | ENSP00000267085 | ENSP00000338964 | Cysteine sulfinic acid decarboxylase; Catalyzes the decarboxylation of L-aspartate, 3-sulfino-L- alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine and taurine, respectively. The preferred substrate is 3- sulfino-L-alanine. Does not exhibit any decarboxylation activity toward glutamate. | Glutathione hydrolase 7 heavy chain; Cleaves glutathione conjugates; Belongs to the gamma-glutamyltransferase family. | 0.908 |
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