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MGI:Fech
Contents |
| Species (Taxon ID) | Mus musculus (house mouse) (taxon:10090) | |
| Gene Name(s) | Fech ( synonyms: fch, Fcl ) | |
| Protein Name(s) | ferrochelatase, | |
| External Links | ||
| MGI | MGI:95513 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004325 |
ferrochelatase activity |
MGI:MGI:1327758 |
IMP: Inferred from Mutant Phenotype |
MGI:MGI:2384729 |
F |
From MGI |
||
| GO:0004325 |
ferrochelatase activity |
MGI:MGI:2384247 |
IDA: Inferred from Direct Assay |
F |
From MGI |
|||
| GO:0004325 |
ferrochelatase activity |
MGI:MGI:3041718 |
IDA: Inferred from Direct Assay |
F |
From MGI |
|||
| GO:0004325 |
ferrochelatase activity |
MGI:MGI:3620268 |
IDA: Inferred from Direct Assay |
F |
From MGI |
|||
| GO:0004325 |
ferrochelatase activity |
MGI:MGI:3620268 |
IDA: Inferred from Direct Assay |
F |
From MGI |
|||
| GO:0004325 |
ferrochelatase activity |
MGI:MGI:3696634 |
IDA: Inferred from Direct Assay |
F |
From MGI |
|||
| GO:0004325 |
ferrochelatase activity |
MGI:MGI:3794459 |
IMP: Inferred from Mutant Phenotype |
MGI:MGI:1858114 |
F |
From MGI |
||
| GO:0004325 |
ferrochelatase activity |
MGI:MGI:3818407 |
IMP: Inferred from Mutant Phenotype |
MGI:MGI:1858114 |
F |
From MGI |
||
| GO:0004325 |
ferrochelatase activity |
MGI:MGI:4417868 |
ISO: Inferred from Sequence Orthology |
NCBI:NP_001101904 |
F |
From MGI |
||
| GO:0004325 |
ferrochelatase activity |
MGI:MGI:4834177 |
ISO: Inferred from Sequence Orthology |
F |
From MGI |
|||
| GO:0004325 |
ferrochelatase activity |
MGI:MGI:60976 |
IMP: Inferred from Mutant Phenotype |
MGI:MGI:1858114 |
F |
From MGI |
||
| GO:0004325 |
ferrochelatase activity |
MGI:MGI:84753 |
ISO: Inferred from Sequence Orthology |
F |
From MGI |
|||
| GO:0005506 |
iron ion binding |
MGI:MGI:3041718 |
IDA: Inferred from Direct Assay |
F |
From MGI |
|||
| GO:0005739 |
mitochondrion |
MGI:MGI:2682130 |
IDA: Inferred from Direct Assay |
C |
From MGI |
|||
| GO:0005739 |
mitochondrion |
MGI:MGI:3852644 |
IDA: Inferred from Direct Assay |
C |
From MGI |
|||
| GO:0005739 |
mitochondrion |
MGI:MGI:4417868 |
ISO: Inferred from Sequence Orthology |
NCBI:NP_001101904 |
C |
From MGI |
||
| GO:0005743 |
mitochondrial inner membrane |
MGI:MGI:2384247 |
TAS: Traceable Author Statement |
C |
From MGI |
|||
| GO:0006779 |
porphyrin-containing compound biosynthetic process |
MGI:MGI:2384247 |
IMP: Inferred from Mutant Phenotype |
MGI:MGI:2384729 |
P |
From MGI |
||
| GO:0006783 |
heme biosynthetic process |
MGI:MGI:1327758 |
IMP: Inferred from Mutant Phenotype |
MGI:MGI:2384729 |
P |
From MGI |
||
| GO:0006783 |
heme biosynthetic process |
MGI:MGI:2384247 |
TAS: Traceable Author Statement |
P |
From MGI |
|||
| GO:0006783 |
heme biosynthetic process |
MGI:MGI:3620268 |
IDA: Inferred from Direct Assay |
P |
From MGI |
|||
| GO:0006783 |
heme biosynthetic process |
MGI:MGI:3696634 |
IDA: Inferred from Direct Assay |
P |
From MGI |
|||
| GO:0006783 |
heme biosynthetic process |
MGI:MGI:3794459 |
IMP: Inferred from Mutant Phenotype |
MGI:MGI:1858114 |
P |
From MGI |
||
| GO:0006783 |
heme biosynthetic process |
MGI:MGI:4417868 |
ISO: Inferred from Sequence Orthology |
NCBI:NP_001101904 |
P |
From MGI |
||
| GO:0006783 |
heme biosynthetic process |
MGI:MGI:79136 |
IMP: Inferred from Mutant Phenotype |
P |
From MGI |
|||
| GO:0008152 |
metabolic process |
MGI:MGI:1354194 |
IEA: Inferred from Electronic Annotation |
UniProtKB-KW:KW-0456 |
P |
From MGI |
||
| GO:0008203 |
cholesterol metabolic process |
MGI:MGI:1930023 |
IMP: Inferred from Mutant Phenotype |
MGI:MGI:1858114 |
P |
From MGI |
||
| GO:0009416 |
response to light stimulus |
MGI:MGI:50545 |
IMP: Inferred from Mutant Phenotype |
MGI:MGI:1858114 |
P |
From MGI |
||
| GO:0009589 |
detection of UV |
MGI:MGI:2384247 |
IMP: Inferred from Mutant Phenotype |
MGI:MGI:2384729 |
P |
From MGI |
||
| GO:0010999 |
regulation of eIF2 alpha phosphorylation by heme |
MGI:MGI:3581470 |
IGI: Inferred from Genetic Interaction |
MGI:MGI:95513 |
P |
From MGI |
||
| GO:0010999 |
regulation of eIF2 alpha phosphorylation by heme |
MGI:MGI:3581470 |
IMP: Inferred from Mutant Phenotype |
MGI:MGI:1858114 |
P |
From MGI |
||
| GO:0016829 |
lyase activity |
MGI:MGI:1354194 |
IEA: Inferred from Electronic Annotation |
UniProtKB-KW:KW-0456 |
F |
From MGI |
||
| GO:0020037 |
heme binding |
MGI:MGI:3620268 |
IDA: Inferred from Direct Assay |
F |
From MGI |
|||
| GO:0030218 |
erythrocyte differentiation |
MGI:MGI:50545 |
IMP: Inferred from Mutant Phenotype |
MGI:MGI:1858114 |
P |
From MGI |
||
| GO:0030350 |
iron-responsive element binding |
MGI:MGI:76464 |
IDA: Inferred from Direct Assay |
F |
From MGI |
|||
| GO:0034379 |
very-low-density lipoprotein particle assembly |
MGI:MGI:1930023 |
IMP: Inferred from Mutant Phenotype |
MGI:MGI:1858114 |
P |
From MGI |
||
| GO:0046501 |
protoporphyrinogen IX metabolic process |
MGI:MGI:3581470 |
IGI: Inferred from Genetic Interaction |
MGI:MGI:95513 |
P |
From MGI |
||
| GO:0046501 |
protoporphyrinogen IX metabolic process |
MGI:MGI:4834177 |
ISO: Inferred from Sequence Orthology |
P |
From MGI |
|||
| GO:0046906 |
tetrapyrrole binding |
MGI:MGI:3041718 |
IDA: Inferred from Direct Assay |
F |
From MGI |
|||
| GO:0046906 |
tetrapyrrole binding |
MGI:MGI:3620268 |
IDA: Inferred from Direct Assay |
F |
From MGI |
|||
| GO:0046906 |
tetrapyrrole binding |
MGI:MGI:3620268 |
IDA: Inferred from Direct Assay |
F |
From MGI |
|||
| GO:0046906 |
tetrapyrrole binding |
MGI:MGI:3696634 |
IDA: Inferred from Direct Assay |
F |
From MGI |
|||
| GO:0046984 |
regulation of hemoglobin biosynthetic process |
MGI:MGI:3581470 |
IGI: Inferred from Genetic Interaction |
MGI:MGI:95513 |
P |
From MGI |
||
| GO:0055072 |
iron ion homeostasis |
MGI:MGI:3818407 |
IMP: Inferred from Mutant Phenotype |
MGI:MGI:1858114 |
P |
From MGI |
| |
| edit table |
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Magness ST & Brenner DA (1999) Targeted disruption of the mouse ferrochelatase gene producing an exon 10 deletion. Biochim Biophys Acta 1453: 161-74 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 2.3 2.4 Magness ST et al. (2002) An exon 10 deletion in the mouse ferrochelatase gene has a dominant-negative effect and causes mild protoporphyria. Blood 100: 1470-7 PubMed GONUTS page
- ↑ 3.0 3.1 3.2 Shi Z & Ferreira GC (2004) Probing the active site loop motif of murine ferrochelatase by random mutagenesis. J Biol Chem 279: 19977-86 PubMed GONUTS page
- ↑ 4.0 4.1 4.2 4.3 4.4 4.5 Shi Z et al. (2006) The conserved active-site loop residues of ferrochelatase induce porphyrin conformational changes necessary for catalysis. Biochemistry 45: 2904-12 PubMed GONUTS page
- ↑ 5.0 5.1 5.2 Franco R et al. (2005) Porphyrin-substrate binding to murine ferrochelatase: effect on the thermal stability of the enzyme. Biochem J 386: 599-605 PubMed GONUTS page
- ↑ 6.0 6.1 Chernova T et al. (2006) Heme deficiency is associated with senescence and causes suppression of N-methyl-D-aspartate receptor subunits expression in primary cortical neurons. Mol Pharmacol 69: 697-705 PubMed GONUTS page
- ↑ 7.0 7.1 Lyoumi S et al. (2007) Increased plasma transferrin, altered body iron distribution, and microcytic hypochromic anemia in ferrochelatase-deficient mice. Blood 109: 811-8 PubMed GONUTS page
- ↑ Boulechfar S et al. (1993) Ferrochelatase structural mutant (Fechm1Pas) in the house mouse. Genomics 16: 645-8 PubMed GONUTS page
- ↑ Crouse BR et al. (1996) Site-directed mutagenesis and spectroscopic characterization of human ferrochelatase: identification of residues coordinating the [2Fe-2S] cluster. Biochemistry 35: 16222-9 PubMed GONUTS page
- ↑ Mootha VK et al. (2003) Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria. Cell 115: 629-40 PubMed GONUTS page
- ↑ Pagliarini DJ et al. (2008) A mitochondrial protein compendium elucidates complex I disease biology. Cell 134: 112-23 PubMed GONUTS page
- ↑ Sellers VM et al. (1996) Function of the [2FE-2S] cluster in mammalian ferrochelatase: a possible role as a nitric oxide sensor. Biochemistry 35: 2699-704 PubMed GONUTS page
- ↑ 13.0 13.1 Bloks VW et al. (2001) Hyperlipidemia and atherosclerosis associated with liver disease in ferrochelatase-deficient mice. J Lipid Res 42: 41-50 PubMed GONUTS page
- ↑ 14.0 14.1 Tutois S et al. (1991) Erythropoietic protoporphyria in the house mouse. A recessive inherited ferrochelatase deficiency with anemia, photosensitivity, and liver disease. J Clin Invest 88: 1730-6 PubMed GONUTS page
- ↑ 15.0 15.1 15.2 15.3 Han AP et al. (2005) Heme-regulated eIF2alpha kinase modifies the phenotypic severity of murine models of erythropoietic protoporphyria and beta-thalassemia. J Clin Invest 115: 1562-70 PubMed GONUTS page
- ↑ Ferreira GC (1995) Ferrochelatase binds the iron-responsive element present in the erythroid 5-aminolevulinate synthase mRNA. Biochem Biophys Res Commun 214: 875-8 PubMed GONUTS page
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