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FECH protein (human) - STRING interaction network
"FECH" - Ferrochelatase, mitochondrial in Homo sapiens
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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FECHFerrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX; Belongs to the ferrochelatase family (429 aa)    
Predicted Functional Partners:
PPOX
Protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX (477 aa)
   
 
  0.994
FXN
Frataxin, mitochondrial; 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 [...] (210 aa)
     
  0.988
HMOX1
Heme oxygenase 1; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis (288 aa)
         
  0.969
CPOX
Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial; Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX (454 aa)
   
   
  0.963
HMOX2
Heme oxygenase 2; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter (370 aa)
         
  0.961
HEPH
Hephaestin; May function as a ferroxidase for ferrous (II) to ferric ion (III) conversion and may be involved in copper transport and homeostasis. Implicated in iron homeostasis and may mediate iron efflux associated to ferroportin 1 (1212 aa)
         
  0.952
COX10
Protoheme IX farnesyltransferase, mitochondrial; Converts protoheme IX and farnesyl diphosphate to heme O; Mitochondrial respiratory chain complex assembly factors (443 aa)
     
 
  0.950
UROD
Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III (367 aa)
 
   
  0.947
ABCB7
ATP-binding cassette sub-family B member 7, mitochondrial; Could be involved in the transport of heme from the mitochondria to the cytosol. Plays a central role in the maturation of cytosolic iron-sulfur (Fe/S) cluster-containing proteins; ATP binding cassette subfamily B (753 aa)
     
 
  0.946
ALAD
Delta-aminolevulinic acid dehydratase; Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen; Belongs to the ALAD family (330 aa)
   
   
  0.941
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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