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 |
| ERG11 | ERG25 | YHR007C | YGR060W | Lanosterol 14-alpha-demethylase; catalyzes C-14 demethylation of lanosterol to form 4,4''-dimethyl cholesta-8,14,24-triene-3-beta-ol in ergosterol biosynthesis pathway; transcriptionally down-regulated when ergosterol is in excess; member of cytochrome P450 family; associated and coordinately regulated with the P450 reductase Ncp1p; human CYP51A1 functionally complements the lethality of the erg11 null mutation | Methylsterol monooxygenase; C-4 methyl sterol oxidase; catalyzes the first of three steps required to remove two C-4 methyl groups from an intermediate in ergosterol biosynthesis; mutants accumulate the sterol intermediate 4,4-dimethylzymosterol; human MSMO1 functionally complements the growth defect caused by repression of ERG25 expression | 0.999 |
| ERG11 | HEM1 | YHR007C | YDR232W | Lanosterol 14-alpha-demethylase; catalyzes C-14 demethylation of lanosterol to form 4,4''-dimethyl cholesta-8,14,24-triene-3-beta-ol in ergosterol biosynthesis pathway; transcriptionally down-regulated when ergosterol is in excess; member of cytochrome P450 family; associated and coordinately regulated with the P450 reductase Ncp1p; human CYP51A1 functionally complements the lethality of the erg11 null mutation | 5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family | 0.538 |
| ERG11 | HEM13 | YHR007C | YDR044W | Lanosterol 14-alpha-demethylase; catalyzes C-14 demethylation of lanosterol to form 4,4''-dimethyl cholesta-8,14,24-triene-3-beta-ol in ergosterol biosynthesis pathway; transcriptionally down-regulated when ergosterol is in excess; member of cytochrome P450 family; associated and coordinately regulated with the P450 reductase Ncp1p; human CYP51A1 functionally complements the lethality of the erg11 null mutation | Oxygen-dependent coproporphyrinogen-III oxidase; Coproporphyrinogen III oxidase; oxygen-requiring enzyme that catalyzes sixth step in heme biosynthetic pathway; transcription is repressed by oxygen and heme (via Rox1p and Hap1p); human homolog CPOX can complement yeast mutant and allow growth of haploid null after sporulation of a heterozygous diploid; Belongs to the aerobic coproporphyrinogen-III oxidase family | 0.878 |
| ERG11 | HEM15 | YHR007C | YOR176W | Lanosterol 14-alpha-demethylase; catalyzes C-14 demethylation of lanosterol to form 4,4''-dimethyl cholesta-8,14,24-triene-3-beta-ol in ergosterol biosynthesis pathway; transcriptionally down-regulated when ergosterol is in excess; member of cytochrome P450 family; associated and coordinately regulated with the P450 reductase Ncp1p; human CYP51A1 functionally complements the lethality of the erg11 null mutation | Ferrochelatase; a mitochondrial inner membrane protein, catalyzes insertion of ferrous iron into protoporphyrin IX, the eighth and final step in the heme biosynthetic pathway; human homolog FECH can complement yeast mutant and allow growth of haploid null after sporulation of a heterozygous diploid | 0.613 |
| ERG11 | HEM2 | YHR007C | YGL040C | Lanosterol 14-alpha-demethylase; catalyzes C-14 demethylation of lanosterol to form 4,4''-dimethyl cholesta-8,14,24-triene-3-beta-ol in ergosterol biosynthesis pathway; transcriptionally down-regulated when ergosterol is in excess; member of cytochrome P450 family; associated and coordinately regulated with the P450 reductase Ncp1p; human CYP51A1 functionally complements the lethality of the erg11 null mutation | Delta-aminolevulinic acid dehydratase; Aminolevulinate dehydratase; a homo-octameric enzyme, catalyzes the conversion of 5-aminolevulinate to porphobilinogen, the second step in heme biosynthesis; enzymatic activity is zinc-dependent; localizes to the cytoplasm and nucleus; human homolog ALAD can complement yeast hem2 mutant | 0.908 |
| ERG11 | HEM3 | YHR007C | YDL205C | Lanosterol 14-alpha-demethylase; catalyzes C-14 demethylation of lanosterol to form 4,4''-dimethyl cholesta-8,14,24-triene-3-beta-ol in ergosterol biosynthesis pathway; transcriptionally down-regulated when ergosterol is in excess; member of cytochrome P450 family; associated and coordinately regulated with the P450 reductase Ncp1p; human CYP51A1 functionally complements the lethality of the erg11 null mutation | Porphobilinogen deaminase; catalyzes the conversion of 4-porphobilinogen to hydroxymethylbilane, the third step in heme biosynthesis; localizes to the cytoplasm and nucleus; expression is regulated by Hap2p-Hap3p, but not by levels of heme; human homolog HMBS can complement yeast mutant and allow growth of haploid null after sporulation of a heterozygous diploid | 0.406 |
| ERG11 | HEM4 | YHR007C | YOR278W | Lanosterol 14-alpha-demethylase; catalyzes C-14 demethylation of lanosterol to form 4,4''-dimethyl cholesta-8,14,24-triene-3-beta-ol in ergosterol biosynthesis pathway; transcriptionally down-regulated when ergosterol is in excess; member of cytochrome P450 family; associated and coordinately regulated with the P450 reductase Ncp1p; human CYP51A1 functionally complements the lethality of the erg11 null mutation | Uroporphyrinogen III synthase; catalyzes the conversion of hydroxymethylbilane to uroporphyrinogen III, the fourth step in heme biosynthesis; deficiency in the human homolog can result in the disease congenital erythropoietic porphyria | 0.912 |
| ERG25 | ERG11 | YGR060W | YHR007C | Methylsterol monooxygenase; C-4 methyl sterol oxidase; catalyzes the first of three steps required to remove two C-4 methyl groups from an intermediate in ergosterol biosynthesis; mutants accumulate the sterol intermediate 4,4-dimethylzymosterol; human MSMO1 functionally complements the growth defect caused by repression of ERG25 expression | Lanosterol 14-alpha-demethylase; catalyzes C-14 demethylation of lanosterol to form 4,4''-dimethyl cholesta-8,14,24-triene-3-beta-ol in ergosterol biosynthesis pathway; transcriptionally down-regulated when ergosterol is in excess; member of cytochrome P450 family; associated and coordinately regulated with the P450 reductase Ncp1p; human CYP51A1 functionally complements the lethality of the erg11 null mutation | 0.999 |
| ERG25 | HEM13 | YGR060W | YDR044W | Methylsterol monooxygenase; C-4 methyl sterol oxidase; catalyzes the first of three steps required to remove two C-4 methyl groups from an intermediate in ergosterol biosynthesis; mutants accumulate the sterol intermediate 4,4-dimethylzymosterol; human MSMO1 functionally complements the growth defect caused by repression of ERG25 expression | Oxygen-dependent coproporphyrinogen-III oxidase; Coproporphyrinogen III oxidase; oxygen-requiring enzyme that catalyzes sixth step in heme biosynthetic pathway; transcription is repressed by oxygen and heme (via Rox1p and Hap1p); human homolog CPOX can complement yeast mutant and allow growth of haploid null after sporulation of a heterozygous diploid; Belongs to the aerobic coproporphyrinogen-III oxidase family | 0.890 |
| ERG25 | HEM2 | YGR060W | YGL040C | Methylsterol monooxygenase; C-4 methyl sterol oxidase; catalyzes the first of three steps required to remove two C-4 methyl groups from an intermediate in ergosterol biosynthesis; mutants accumulate the sterol intermediate 4,4-dimethylzymosterol; human MSMO1 functionally complements the growth defect caused by repression of ERG25 expression | Delta-aminolevulinic acid dehydratase; Aminolevulinate dehydratase; a homo-octameric enzyme, catalyzes the conversion of 5-aminolevulinate to porphobilinogen, the second step in heme biosynthesis; enzymatic activity is zinc-dependent; localizes to the cytoplasm and nucleus; human homolog ALAD can complement yeast hem2 mutant | 0.932 |
| ERG25 | HEM4 | YGR060W | YOR278W | Methylsterol monooxygenase; C-4 methyl sterol oxidase; catalyzes the first of three steps required to remove two C-4 methyl groups from an intermediate in ergosterol biosynthesis; mutants accumulate the sterol intermediate 4,4-dimethylzymosterol; human MSMO1 functionally complements the growth defect caused by repression of ERG25 expression | Uroporphyrinogen III synthase; catalyzes the conversion of hydroxymethylbilane to uroporphyrinogen III, the fourth step in heme biosynthesis; deficiency in the human homolog can result in the disease congenital erythropoietic porphyria | 0.932 |
| HEM1 | ERG11 | YDR232W | YHR007C | 5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family | Lanosterol 14-alpha-demethylase; catalyzes C-14 demethylation of lanosterol to form 4,4''-dimethyl cholesta-8,14,24-triene-3-beta-ol in ergosterol biosynthesis pathway; transcriptionally down-regulated when ergosterol is in excess; member of cytochrome P450 family; associated and coordinately regulated with the P450 reductase Ncp1p; human CYP51A1 functionally complements the lethality of the erg11 null mutation | 0.538 |
| HEM1 | HEM12 | YDR232W | YDR047W | 5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family | Uroporphyrinogen decarboxylase; catalyzes the fifth step in the heme biosynthetic pathway; localizes to both the cytoplasm and nucleus; a hem12 mutant has phenotypes similar to patients with porphyria cutanea tarda | 0.951 |
| HEM1 | HEM13 | YDR232W | YDR044W | 5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family | Oxygen-dependent coproporphyrinogen-III oxidase; Coproporphyrinogen III oxidase; oxygen-requiring enzyme that catalyzes sixth step in heme biosynthetic pathway; transcription is repressed by oxygen and heme (via Rox1p and Hap1p); human homolog CPOX can complement yeast mutant and allow growth of haploid null after sporulation of a heterozygous diploid; Belongs to the aerobic coproporphyrinogen-III oxidase family | 0.976 |
| HEM1 | HEM14 | YDR232W | YER014W | 5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family | Protoporphyrinogen oxidase; a mitochondrial enzyme that catalyzes the seventh step in the heme biosynthetic pathway, converting protoporphyrinogen IX to protoporphyrin IX; inhibited by diphenyl ether-type herbicides | 0.972 |
| HEM1 | HEM15 | YDR232W | YOR176W | 5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family | Ferrochelatase; a mitochondrial inner membrane protein, catalyzes insertion of ferrous iron into protoporphyrin IX, the eighth and final step in the heme biosynthetic pathway; human homolog FECH can complement yeast mutant and allow growth of haploid null after sporulation of a heterozygous diploid | 0.988 |
| HEM1 | HEM2 | YDR232W | YGL040C | 5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family | Delta-aminolevulinic acid dehydratase; Aminolevulinate dehydratase; a homo-octameric enzyme, catalyzes the conversion of 5-aminolevulinate to porphobilinogen, the second step in heme biosynthesis; enzymatic activity is zinc-dependent; localizes to the cytoplasm and nucleus; human homolog ALAD can complement yeast hem2 mutant | 0.998 |
| HEM1 | HEM3 | YDR232W | YDL205C | 5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family | Porphobilinogen deaminase; catalyzes the conversion of 4-porphobilinogen to hydroxymethylbilane, the third step in heme biosynthesis; localizes to the cytoplasm and nucleus; expression is regulated by Hap2p-Hap3p, but not by levels of heme; human homolog HMBS can complement yeast mutant and allow growth of haploid null after sporulation of a heterozygous diploid | 0.992 |
| HEM1 | HEM4 | YDR232W | YOR278W | 5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family | Uroporphyrinogen III synthase; catalyzes the conversion of hydroxymethylbilane to uroporphyrinogen III, the fourth step in heme biosynthesis; deficiency in the human homolog can result in the disease congenital erythropoietic porphyria | 0.991 |
| HEM12 | HEM1 | YDR047W | YDR232W | Uroporphyrinogen decarboxylase; catalyzes the fifth step in the heme biosynthetic pathway; localizes to both the cytoplasm and nucleus; a hem12 mutant has phenotypes similar to patients with porphyria cutanea tarda | 5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family | 0.951 |
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