FAH

General Information

Full gene name:fumarylacetoacetate hydrolase (fumarylacetoacetase)
Entrez Gene ID:2184
Location:15q23-q25
Synonyms:
Type:protein-coding

User SNPs

SNPs given by the user that are near or inside this gene:

SNP Distance (bp) Direction
rs11634397 13119 upstream

NCBI Summary

This gene encodes the last enzyme in the tyrosine catabolism pathway. FAH deficiency is associated with Type 1 hereditary tyrosinemia (HT). [provided by RefSeq, Jul 2008]

OMIM

OMIM ID:`OMIM ID 613871 `_

Allelic Variants (Selected Examples)

.0001 TYROSINEMIA, TYPE I

In a French-Canadian patient with type I hereditary tyrosinemia (276700), Phaneuf et al. (1992) demonstrated compound heterozygosity for an FAH allele that appeared not to be expressed in the liver of the proband and a second allele which carried an A-to-T transversion which substituted isoleucine for asparagine-16 (N16I). These findings demonstrated that there are at least 2 different tyrosinemia mutations in the French-Canadian population.

.0002 TYROSINEMIA, TYPE I

In a patient with type I hereditary tyrosinemia (276700) and very low FAH enzymatic activity in the liver, Labelle et al. (1993) found heterozygosity for an ala134-to-asp (A134D) mutation in the FAH gene. The nature of the other allele was not identified.

.0003 TYROSINEMIA, TYPE I

In a patient from eastern Quebec with tyrosinemia type I (276700), Grompe and Al-Dhalimy (1993) demonstrated homozygosity for a splice mutation consisting of a guanine-to-adenine alteration in the donor consensus sequence of intron 12 (IVS12,G-A,+5) of the FAH gene. Two other mutations, glu357-to-ter (E357X) and glu364-to-ter (E364X), were identified. Grompe et al. (1994) designed allele-specific oligonucleotide tests to detect the 3 mutations and used them to demonstrate that all patients with tyrosinemia type I in eastern Quebec carried the splice-donor site mutation, most of them in homozygous state. St-Louis et al. (1995) found the same mutation in a compound heterozygote Norwegian patient. The fact that this is the predominant mutation in French-Canadian cases (having a frequency of 77.6% among Quebec patients with tyrosinemia type I) may indicate its ancient origin. The other mutation in the Norwegian patient was G337S (613871.0007).

The 2 extremes of the clinical phenotype of tyrosinemia type I are the ‘acute’ (a severe disorder with early onset and death), and ‘chronic’ (showing delayed onset and slow course) forms. Allelic heterogeneity and/or mutation reversion in hepatic cells had been proposed to explain the clinical heterogeneity. Poudrier et al. (1998) studied 2 probands from the French-Canadian isolate where type I tyrosinemia is prevalent, one with the acute and the other with the chronic form. Both were found to be germline homozygotes for the IVS12,G-A,+5 splice site mutation. Both showed liver mosaicism for FAH immunoreactivity with evidence for mutation reversion to heterozygosity in FAH-stained nodules as shown by amplification of DNA extracted from microdissected nodules. Western blot analysis of proteins from a reverted FAH-expressing nodule showed 29 +/- 3% FAH immunoreactive material as compared to an average normal liver. This was consistent with the measured FAH hydrolytic activity (25%) in this large regenerating nodule. These findings showed that genotypic heterogeneity is not a sufficient explanation for clinical heterogeneity and implicated epigenetic and other factors modifying the phenotype in this disorder.

.0004 TYROSINEMIA, TYPE I

Grompe and Al-Dhalimy (1993) found that a patient with tyrosinemia type I (276700) was a compound heterozygote for 2 different nonsense mutations in the FAH gene that changed the codon for glutamic acid at positions 357 and 364 of the enzyme to a stop codon (E357X, E364X). One parent was from Quebec and the other from England.

.0005 TYROSINEMIA, TYPE I

See 613871.0004 and Grompe and Al-Dhalimy (1993).

.0006 FUMARYLACETOACETASE PSEUDODEFICIENCY

Rootwelt et al. (1994) found fumarylacetoacetase pseudodeficiency (see 276700) due to a C-to-T transition in nucleotide 1021 leading to an arg341-to-trp (R341W) amino acid substitution in 2.2% of FAH alleles among 516 healthy Norwegian volunteers.

.0007 TYROSINEMIA, TYPE I

St-Louis et al. (1995) found that a Norwegian patient with hepatorenal tyrosinemia (276700) was a compound heterozygote for the IVS12+5G-A mutation (613871.0003), the most frequent mutation in French-Canadian cases, and a new mutation resulting in substitution of serine for glycine-337 (E337S).

.0008 TYROSINEMIA, TYPE I

In a French-Canadian case of hereditary tyrosinemia type I (276700), St-Louis et al. (1995) found an arg381-to-gly (R381G) mutation in the FAH gene inherited from the father. The other mutation in this compound heterozygote was E357X (613871.0004), inherited from the mother.

.0009 TYROSINEMIA, TYPE I

St-Louis et al. (1994) reported a stop mutation in the FAH gene (W262X) in 5 Finnish hereditary tyrosinemia type I (276700) patients. This mutation seemed to predominate in the Finnish population, where it accounted for 95% of the alleles (19/20) in 10 affected patients tested (St-Louis et al. (1996)), and had not been found in any other population. The remaining allele carried the IVS12+5G-A splice mutation (613871.0003) that is predominant in the French-Canadian population but is also seen in patients of other origins. St-Louis et al. (1996) described a simple test for the ‘Finnish’ mutation.

.0010 TYROSINEMIA, TYPE I

In a study of 62 tyrosinemia type I (276700) patients of various ethnic origins, Rootwelt et al. (1996) found that the second most frequent FAH mutation was a G-to-T transversion in the last nucleotide of exon 6. Encountered in 14 alleles, the mutation was common in Central and Western Europe.

.0011 TYROSINEMIA, TYPE I

In a 37-year-old woman with type I tyrosinemia (276700) whose liver disease in infancy and rickets during childhood resolved with dietary therapy, Kim et al. (2000) reported an A-to-G transition in exon 9 of the FAH gene, resulting in a glu279-to-arg (Q279R) substitution, in compound heterozygosity with the IVS6-1G-T mutation (613871.0010). From 14 years of age the patient resumed an unrestricted diet with the continued presence of the biochemical features of tyrosinemia, yet maintained normal liver function. In adulthood she accumulated only small amounts of succinylacetone. Despite this evolution to a mild biochemical and clinical phenotype, she eventually developed hepatocellular carcinoma.

NCBI Phenotypes

  • Gene Reviews
  • GTR
  • OMIM
  • Tyrosinemia type I

Gene Ontology

  • cellular nitrogen compound metabolic process
  • cytosol
  • arginine catabolic process
  • small molecule metabolic process
  • L-phenylalanine catabolic process
  • fumarylacetoacetase activity
  • metal ion binding
  • tyrosine catabolic process

GeneRIFs

  • Affinity Capture-MS [PMID 21890473]
  • We detected 11 novel and 6 previously described pathogenic mutations in the fumarylacetoacetase gene in a cohort of 43 patients originating from the Middle East with the acute form hereditary tyrosinemia type I [PMID 21764616]
  • Observational study of gene-disease association and gene-environment interaction. (HuGE Navigator) [PMID 18072279]
  • Observational study and genome-wide association study of gene-disease association. (HuGE Navigator) [PMID 20201926]
  • PCA [PMID 20029029]
  • identification of an alternative nonsense transcript of the fah gene, which despite being subjected to nonsense-mediated mRNA decay, produces a protein in different human tissues [PMID 15638932]
  • Data describe the metabolism of fumarylacetoacetate hydrolase mRNA harboring a nonsense mutation, W262X, in lymphoblastoid cell lines derived from hereditary tyrosinemia type I patients. [PMID 15465000]
  • A missense mutation in the fumarylacetoacetate hydrolase gene, responsible for hereditary tyrosinemia, acts as a splicing mutation. [PMID 11476670]
  • An immunopositive liver nodule was found in a patient with tyrosinemia having a mosaic pattern of FAH. [PMID 15759101]

PubMed Articles

Recent articles:

  • Imtiaz F et al. “Identification of mutations causing hereditary tyrosinemia type I in patients of Middle Eastern origin.” Mol Genet Metab. 2011 Dec;104(4):688-90. PMID 21764616
  • Wagner SA et al. “A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.” Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. PMID 21890473
  • Joslyn G et al. “Human variation in alcohol response is influenced by variation in neuronal signaling genes.” Alcohol Clin Exp Res. 2010 May;34(5):800-12. PMID 20201926
  • Sniderman King L et al. “Tyrosinemia Type 1.” None 1993;. PMID 20301688
  • Deribe YL et al. “Regulation of epidermal growth factor receptor trafficking by lysine deacetylase HDAC6.” Sci Signal. 2009 Dec 22;2(102):ra84. PMID 20029029
  • Liu J et al. “Combining fMRI and SNP data to investigate connections between brain function and genetics using parallel ICA.” Hum Brain Mapp. 2009 Jan;30(1):241-55. PMID 18072279
  • Bliksrud YT et al. “Tyrosinaemia type I–de novo mutation in liver tissue suppressing an inborn splicing defect.” J Mol Med (Berl). 2005 May;83(5):406-10. PMID 15759101
  • Dreumont N et al. “A minor alternative transcript of the fumarylacetoacetate hydrolase gene produces a protein despite being likely subjected to nonsense-mediated mRNA decay.” BMC Mol Biol. 2005 Jan 7;6(1):1. PMID 15638932
  • Dreumont N et al. “Cytoplasmic nonsense-mediated mRNA decay for a nonsense (W262X) transcript of the gene responsible for hereditary tyrosinemia, fumarylacetoacetate hydrolase.” Biochem Biophys Res Commun. 2004 Nov 5;324(1):186-92. PMID 15465000
  • Gerhard DS et al. “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).” Genome Res. 2004 Oct;14(10B):2121-7. PMID 15489334

Top Pubmed articles linked to gene FAH matching any search term:

  • Li B et al. “Proteomic profiling of differentially expressed proteins from Bax inhibitor-1 knockout and wild type mice.” Mol Cells. 2012 Jul;34(1):15-23. PMID 22736268
  • Fah A et al. “A comparison of epidural and cerebrospinal fluid glucose in parturients at term: an observational study.” Int J Obstet Anesth. 2012 Jul;21(3):242-4. PMID 22626991
  • Quintos JB et al. “Autoimmune polyglandular syndrome Type 3 and growth hormone deficiency.” Pediatr Diabetes. 2010 Sep;11(6):438-42. PMID 19968812
  • Evert M et al. “Overexpression of fatty acid synthase in chemically and hormonally induced hepatocarcinogenesis of the rat.” Lab Invest. 2005 Jan;85(1):99-108. PMID 15543204
  • Evert M et al. “Apolipoprotein A-IV mRNA overexpression in early preneoplastic hepatic foci induced by low-number pancreatic islet transplants in streptozotocin-diabetic rats.” Pathol Res Pract. 2003;199(6):373-9. PMID 12924437
  • Feitkenhauer H et al. “Microbial desizing using starch as model compound: enzyme properties and desizing efficiency.” Biotechnol Prog. 2003 May-Jun;19(3):874-9. PMID 12790652
  • Roffler B et al. “Intestinal morphology, epithelial cell proliferation, and absorptive capacity in neonatal calves fed milk-born insulin-like growth factor-I or a colostrum extract.” J Dairy Sci. 2003 May;86(5):1797-806. PMID 12778590
  • Bannasch P et al. “Hormonal and hormone-like effects eliciting hepatocarcinogenesis.” Folia Histochem Cytobiol. 2001;39 Suppl 2:28-9. PMID 11820616
  • Bannasch P et al. “Significance of hepatic preneoplasia for cancer chemoprevention.” IARC Sci Publ. 2001;154:223-40. PMID 11220662
  • Ibáñez L et al. “Adrenal hyperandrogenism in adolescent girls with a history of low birthweight and precocious pubarche.” Clin Endocrinol (Oxf). 2000 Oct;53(4):523-7. PMID 11012579

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