FANCA

From Wikipedia, the free encyclopedia

Fanconi anemia, complementation group A

Identifiers

FANCA; FA; FA-H; FA1; FAA; FACA; FAH; FANCH; MGC75158

External IDs

OMIM: 607139 MGI: 1341823 HomoloGene: 108

Gene ontology
Molecular Function:	• protein binding
Cellular Component:	• nucleus • cytoplasm
Biological Process:	• DNA repair • protein complex assembly • male meiosis • male gonad development • female gonad development • regulation of cell proliferation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000135 (mRNA)
NP_000126 (protein)

NM_016925 (mRNA)
NP_058621 (protein)

Location

Chr 16: 88.33 - 88.41 Mb

Chr 8: 126.15 - 126.2 Mb

Pubmed search

[1]

[2]

Fanconi anemia, complementation group A, also known as FANCA, is a human gene.^[1]

The Fanconi anemia complementation group (FANC) currently includes FANCA, FANCB, FANCC, FANCD1 (also called BRCA2), FANCD2, FANCE, FANCF, FANCG, and FANCL. The previously defined group FANCH is the same as FANCA. Fanconi anemia is a genetically heterogeneous recessive disorder characterized by cytogenetic instability, hypersensitivity to DNA crosslinking agents, increased chromosomal breakage, and defective DNA repair. The members of the Fanconi anemia complementation group do not share sequence similarity; they are related by their assembly into a common nuclear protein complex. This gene encodes the protein for complementation group A. Alternative splicing results in multiple transcript variants encoding different isoforms. Mutations in this gene are the most common cause of Fanconi anemia.^[1]

[edit] References

^ ^a ^b Entrez Gene: FANCA Fanconi anemia, complementation group A.

[edit] Further reading

Marmo E (1976). "[Beta-adrenolytic agents in the treatment of hypertension]". La Clinica terapeutica 74 (3): 209–29. PMID 6186.
Pronk JC, Gibson RA, Savoia A, et al. (1995). "Localisation of the Fanconi anaemia complementation group A gene to chromosome 16q24.3.". Nat. Genet. 11 (3): 338–40. doi:10.1038/ng1195-338. PMID 7581462.
Gschwend M, Levran O, Kruglyak L, et al. (1996). "A locus for Fanconi anemia on 16q determined by homozygosity mapping.". Am. J. Hum. Genet. 59 (2): 377–84. PMID 8755924.
Lo Ten Foe JR, Rooimans MA, Bosnoyan-Collins L, et al. (1996). "Expression cloning of a cDNA for the major Fanconi anaemia gene, FAA.". Nat. Genet. 14 (3): 320–3. doi:10.1038/ng1196-320. PMID 8896563.
"Positional cloning of the Fanconi anaemia group A gene. The Fanconi anaemia/breast cancer consortium." (1996). Nat. Genet. 14 (3): 324–8. doi:10.1038/ng1196-324. PMID 8896564.
Ianzano L, D'Apolito M, Centra M, et al. (1997). "The genomic organization of the Fanconi anemia group A (FAA) gene.". Genomics 41 (3): 309–14. doi:10.1006/geno.1997.4675. PMID 9169126.
Levran O, Erlich T, Magdalena N, et al. (1998). "Sequence variation in the Fanconi anemia gene FAA.". Proc. Natl. Acad. Sci. U.S.A. 94 (24): 13051–6. PMID 9371798.
Joenje H, Oostra AB, Wijker M, et al. (1997). "Evidence for at least eight Fanconi anemia genes.". Am. J. Hum. Genet. 61 (4): 940–4. PMID 9382107.
Kupfer GM, Näf D, Suliman A, et al. (1997). "The Fanconi anaemia proteins, FAA and FAC, interact to form a nuclear complex.". Nat. Genet. 17 (4): 487–90. doi:10.1038/ng1297-487. PMID 9398857.
Savino M, Ianzano L, Strippoli P, et al. (1998). "Mutations of the Fanconi anemia group A gene (FAA) in Italian patients.". Am. J. Hum. Genet. 61 (6): 1246–53. PMID 9399890.
Levran O, Doggett NA, Auerbach AD (1998). "Identification of Alu-mediated deletions in the Fanconi anemia gene FAA.". Hum. Mutat. 12 (3): 145–52. doi:10.1002/(SICI)1098-1004(1998)12:3<145::AID-HUMU2>3.0.CO;2-G. PMID 9711872.
Centra M, Memeo E, d'Apolito M, et al. (1998). "Fine exon-intron structure of the Fanconi anemia group A (FAA) gene and characterization of two genomic deletions.". Genomics 51 (3): 463–7. doi:10.1006/geno.1998.5353. PMID 9721219.
Näf D, Kupfer GM, Suliman A, et al. (1998). "Functional activity of the fanconi anemia protein FAA requires FAC binding and nuclear localization.". Mol. Cell. Biol. 18 (10): 5952–60. PMID 9742112.
Yamashita T, Kupfer GM, Naf D, et al. (1998). "The fanconi anemia pathway requires FAA phosphorylation and FAA/FAC nuclear accumulation.". Proc. Natl. Acad. Sci. U.S.A. 95 (22): 13085–90. PMID 9789045.
Nakamura A, Matsuura S, Tauchi H, et al. (1999). "Four novel mutations of the Fanconi anemia group A gene (FAA) in Japanese patients.". J. Hum. Genet. 44 (1): 48–51. PMID 9929978.
Wijker M, Morgan NV, Herterich S, et al. (1999). "Heterogeneous spectrum of mutations in the Fanconi anaemia group A gene.". Eur. J. Hum. Genet. 7 (1): 52–9. doi:10.1038/sj.ejhg.5200248. PMID 10094191.
Kupfer G, Naf D, Garcia-Higuera I, et al. (1999). "A patient-derived mutant form of the Fanconi anemia protein, FANCA, is defective in nuclear accumulation.". Exp. Hematol. 27 (4): 587–93. PMID 10210316.
Garcia-Higuera I, Kuang Y, Näf D, et al. (1999). "Fanconi anemia proteins FANCA, FANCC, and FANCG/XRCC9 interact in a functional nuclear complex.". Mol. Cell. Biol. 19 (7): 4866–73. PMID 10373536.
Jelesko JG, Harper R, Furuya M, Gruissem W (1999). "Rare germinal unequal crossing-over leading to recombinant gene formation and gene duplication in Arabidopsis thaliana.". Proc. Natl. Acad. Sci. U.S.A. 96 (18): 10302–7. PMID 10468603.
Waisfisz Q, de Winter JP, Kruyt FA, et al. (1999). "A physical complex of the Fanconi anemia proteins FANCG/XRCC9 and FANCA.". Proc. Natl. Acad. Sci. U.S.A. 96 (18): 10320–5. PMID 10468606.