| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| FXN | HSCB | ENSP00000366482 | ENSP00000216027 | frataxin; Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown usin [...] | HscB iron-sulfur cluster co-chaperone homolog (E. coli); Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria | 0.969 |
| FXN | HSPA9 | ENSP00000366482 | ENSP00000297185 | frataxin; Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown usin [...] | heat shock 70kDa protein 9 (mortalin) | 0.973 |
| FXN | IBA57 | ENSP00000366482 | ENSP00000355672 | frataxin; Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown usin [...] | IBA57, iron-sulfur cluster assembly homolog (S. cerevisiae); Required for normal heme biosynthesis (By similarity) | 0.595 |
| FXN | ISCU | ENSP00000366482 | ENSP00000310623 | frataxin; Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown usin [...] | iron-sulfur cluster scaffold homolog (E. coli); Involved in the assembly or repair of the [Fe-S] clusters present in iron-sulfur proteins. Binds iron | 0.996 |
| FXN | LYRM4 | ENSP00000366482 | ENSP00000443900 | frataxin; Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown usin [...] | LYR motif containing 4; Required for nuclear and mitochondrial iron-sulfur protein biosynthesis | 0.999 |
| FXN | NFS1 | ENSP00000366482 | ENSP00000363205 | frataxin; Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown usin [...] | NFS1 nitrogen fixation 1 homolog (S. cerevisiae); Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron- sulfur (Fe-S) clusters. May be involved in the biosynthesis of molybdenum cofactor | 0.992 |
| FXN | SCLY | ENSP00000366482 | ENSP00000254663 | frataxin; Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown usin [...] | selenocysteine lyase; Catalyzes the decomposition of L-selenocysteine to L- alanine and elemental selenium (By similarity) | 0.928 |
| FXN | SLC25A28 | ENSP00000366482 | ENSP00000359526 | frataxin; Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown usin [...] | solute carrier family 25 (mitochondrial iron transporter), member 28; Mitochondrial iron transporter that mediates iron uptake. Probably required for heme synthesis of hemoproteins and Fe-S cluster assembly in non-erythroid cells. The iron delivered into the mitochondria, presumably as Fe(2+), is then probably delivered to ferrochelatase to catalyze Fe(2+) incorporation into protoprophyrin IX to make heme (By similarity) | 0.978 |
| FXN | SLC25A37 | ENSP00000366482 | ENSP00000429200 | frataxin; Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown usin [...] | solute carrier family 25 (mitochondrial iron transporter), member 37; Mitochondrial iron transporter that specifically mediates iron uptake in developing erythroid cells, thereby playing an essential role in heme biosynthesis. The iron delivered into the mitochondria, presumably as Fe(2+), is then probably delivered to ferrochelatase to catalyze Fe(2+) incorporation into protoprophyrin IX to make heme (By similarity) | 0.981 |
| HSCB | FXN | ENSP00000216027 | ENSP00000366482 | HscB iron-sulfur cluster co-chaperone homolog (E. coli); Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria | frataxin; Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown usin [...] | 0.969 |
| HSCB | HSPA9 | ENSP00000216027 | ENSP00000297185 | HscB iron-sulfur cluster co-chaperone homolog (E. coli); Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria | heat shock 70kDa protein 9 (mortalin) | 0.838 |
| HSCB | IBA57 | ENSP00000216027 | ENSP00000355672 | HscB iron-sulfur cluster co-chaperone homolog (E. coli); Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria | IBA57, iron-sulfur cluster assembly homolog (S. cerevisiae); Required for normal heme biosynthesis (By similarity) | 0.754 |
| HSCB | ISCU | ENSP00000216027 | ENSP00000310623 | HscB iron-sulfur cluster co-chaperone homolog (E. coli); Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria | iron-sulfur cluster scaffold homolog (E. coli); Involved in the assembly or repair of the [Fe-S] clusters present in iron-sulfur proteins. Binds iron | 0.999 |
| HSCB | LYRM4 | ENSP00000216027 | ENSP00000443900 | HscB iron-sulfur cluster co-chaperone homolog (E. coli); Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria | LYR motif containing 4; Required for nuclear and mitochondrial iron-sulfur protein biosynthesis | 0.834 |
| HSCB | NFS1 | ENSP00000216027 | ENSP00000363205 | HscB iron-sulfur cluster co-chaperone homolog (E. coli); Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria | NFS1 nitrogen fixation 1 homolog (S. cerevisiae); Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron- sulfur (Fe-S) clusters. May be involved in the biosynthesis of molybdenum cofactor | 0.954 |
| HSCB | SCLY | ENSP00000216027 | ENSP00000254663 | HscB iron-sulfur cluster co-chaperone homolog (E. coli); Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria | selenocysteine lyase; Catalyzes the decomposition of L-selenocysteine to L- alanine and elemental selenium (By similarity) | 0.826 |
| HSCB | SLC25A37 | ENSP00000216027 | ENSP00000429200 | HscB iron-sulfur cluster co-chaperone homolog (E. coli); Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria | solute carrier family 25 (mitochondrial iron transporter), member 37; Mitochondrial iron transporter that specifically mediates iron uptake in developing erythroid cells, thereby playing an essential role in heme biosynthesis. The iron delivered into the mitochondria, presumably as Fe(2+), is then probably delivered to ferrochelatase to catalyze Fe(2+) incorporation into protoprophyrin IX to make heme (By similarity) | 0.439 |
| HSPA9 | FXN | ENSP00000297185 | ENSP00000366482 | heat shock 70kDa protein 9 (mortalin) | frataxin; Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown usin [...] | 0.973 |
| HSPA9 | HSCB | ENSP00000297185 | ENSP00000216027 | heat shock 70kDa protein 9 (mortalin) | HscB iron-sulfur cluster co-chaperone homolog (E. coli); Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria | 0.838 |
| HSPA9 | ISCU | ENSP00000297185 | ENSP00000310623 | heat shock 70kDa protein 9 (mortalin) | iron-sulfur cluster scaffold homolog (E. coli); Involved in the assembly or repair of the [Fe-S] clusters present in iron-sulfur proteins. Binds iron | 0.911 |
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