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 |
| GLY1 | HEM1 | YEL046C | YDR232W | Low specificity L-threonine aldolase; Threonine aldolase; catalyzes the cleavage of L-allo-threonine and L-threonine to glycine; involved in glycine biosynthesis. | 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. | 0.938 |
| GLY1 | HEM25 | YEL046C | YDL119C | Low specificity L-threonine aldolase; Threonine aldolase; catalyzes the cleavage of L-allo-threonine and L-threonine to glycine; involved in glycine biosynthesis. | Mitochondrial glycine transporter; required for the transport of glycine into mitochondria for initiation of heme biosynthesis, with YMC1 acting as a secondary transporter; homolog of human SLC25A38, a mitochondrial glycine transporter associated with nonsyndromic autosomal recessive congenital sideroblastic anemia; human SLC25A38 can complement the heme deficiency associated with the null mutant; GFP-fusion protein is induced in response to the DNA-damaging agent MMS. | 0.533 |
| HEM1 | GLY1 | YDR232W | YEL046C | 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. | Low specificity L-threonine aldolase; Threonine aldolase; catalyzes the cleavage of L-allo-threonine and L-threonine to glycine; involved in glycine biosynthesis. | 0.938 |
| 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. | 0.872 |
| 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. | 0.895 |
| HEM1 | HEM25 | YDR232W | YDL119C | 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. | Mitochondrial glycine transporter; required for the transport of glycine into mitochondria for initiation of heme biosynthesis, with YMC1 acting as a secondary transporter; homolog of human SLC25A38, a mitochondrial glycine transporter associated with nonsyndromic autosomal recessive congenital sideroblastic anemia; human SLC25A38 can complement the heme deficiency associated with the null mutant; GFP-fusion protein is induced in response to the DNA-damaging agent MMS. | 0.747 |
| 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 |
| HEM1 | MCX1 | YDR232W | YBR227C | 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. | ATP-dependent clpX-like chaperone, mitochondrial; Non-proteolytic ATPase of the AAA family; stimulates incorporation of the pyridoxal phosphate cofactor into Hem1p (5-aminolevulinic acid synthase); localized to the mitochondrial matrix; ortholog of vertebrate CLPX, which promotes erythropoiesis. | 0.680 |
| 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. | 0.872 |
| HEM12 | HEM14 | YDR047W | YER014W | 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. | 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. | 0.999 |
| HEM12 | HEM25 | YDR047W | YDL119C | 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. | Mitochondrial glycine transporter; required for the transport of glycine into mitochondria for initiation of heme biosynthesis, with YMC1 acting as a secondary transporter; homolog of human SLC25A38, a mitochondrial glycine transporter associated with nonsyndromic autosomal recessive congenital sideroblastic anemia; human SLC25A38 can complement the heme deficiency associated with the null mutant; GFP-fusion protein is induced in response to the DNA-damaging agent MMS. | 0.696 |
| HEM12 | HEM4 | YDR047W | YOR278W | 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. | 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. | 0.998 |
| HEM12 | MCX1 | YDR047W | YBR227C | 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. | ATP-dependent clpX-like chaperone, mitochondrial; Non-proteolytic ATPase of the AAA family; stimulates incorporation of the pyridoxal phosphate cofactor into Hem1p (5-aminolevulinic acid synthase); localized to the mitochondrial matrix; ortholog of vertebrate CLPX, which promotes erythropoiesis. | 0.657 |
| HEM14 | HEM1 | YER014W | YDR232W | 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. | 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. | 0.895 |
| HEM14 | HEM12 | YER014W | YDR047W | 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. | 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. | 0.999 |
| HEM14 | HEM25 | YER014W | YDL119C | 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. | Mitochondrial glycine transporter; required for the transport of glycine into mitochondria for initiation of heme biosynthesis, with YMC1 acting as a secondary transporter; homolog of human SLC25A38, a mitochondrial glycine transporter associated with nonsyndromic autosomal recessive congenital sideroblastic anemia; human SLC25A38 can complement the heme deficiency associated with the null mutant; GFP-fusion protein is induced in response to the DNA-damaging agent MMS. | 0.776 |
| HEM14 | HEM4 | YER014W | YOR278W | 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. | 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. | 0.929 |
| HEM25 | GLY1 | YDL119C | YEL046C | Mitochondrial glycine transporter; required for the transport of glycine into mitochondria for initiation of heme biosynthesis, with YMC1 acting as a secondary transporter; homolog of human SLC25A38, a mitochondrial glycine transporter associated with nonsyndromic autosomal recessive congenital sideroblastic anemia; human SLC25A38 can complement the heme deficiency associated with the null mutant; GFP-fusion protein is induced in response to the DNA-damaging agent MMS. | Low specificity L-threonine aldolase; Threonine aldolase; catalyzes the cleavage of L-allo-threonine and L-threonine to glycine; involved in glycine biosynthesis. | 0.533 |
| HEM25 | HEM1 | YDL119C | YDR232W | Mitochondrial glycine transporter; required for the transport of glycine into mitochondria for initiation of heme biosynthesis, with YMC1 acting as a secondary transporter; homolog of human SLC25A38, a mitochondrial glycine transporter associated with nonsyndromic autosomal recessive congenital sideroblastic anemia; human SLC25A38 can complement the heme deficiency associated with the null mutant; GFP-fusion protein is induced in response to the DNA-damaging agent MMS. | 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. | 0.747 |
| HEM25 | HEM12 | YDL119C | YDR047W | Mitochondrial glycine transporter; required for the transport of glycine into mitochondria for initiation of heme biosynthesis, with YMC1 acting as a secondary transporter; homolog of human SLC25A38, a mitochondrial glycine transporter associated with nonsyndromic autosomal recessive congenital sideroblastic anemia; human SLC25A38 can complement the heme deficiency associated with the null mutant; GFP-fusion protein is induced in response to the DNA-damaging agent MMS. | 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. | 0.696 |
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