Atlas of Genetics and Cytogenetics in Oncology and Haematology


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FANCA (Fanconi anemia, complementation group A)

Identity

Other namesFA
FA1
FAA
FACA
FA-H
FAH
FANCH
HGNC (Hugo) FANCA
LocusID (NCBI) 2175
Location 16q24.3
Location_base_pair Starts at 89803959 and ends at 89883065 bp from pter ( according to hg19-Feb_2009)  [Mapping]
 
  Figure 1. Genomic contex of FANCA gene in chromosome 16. Image adapted from NCBI.

DNA/RNA

Description 43 exons spanning 80 kb with 4365 bp open reading frame (Lo Ten Foe et al., 1996). The 5-prime region upstream of the putative transcription start site of FANCA has a GC-rich region instead of TATA or CAAT boxes, which is typical of housekeeping genes (Ianzano et al., 1997). Numerous Alu repeats are present in the FANCA gene, suggesting that Alu-mediated recombination may be an important mechanism for the generation of Fanconi anemia-producing mutations.
Transcription Multiple transcrips have been described and two types produces proteins; a 5,5 kb mRNA corresponding to NM_000135.2 (5460 bp) and NM_001018112 (1673 bp) by alternative splicing (no experimental confirmation available).
Pseudogene Not described.

Protein

Note Two isoforms with accession number in UniProt; the canonical sequence NP_000126.2 (1455 aa) and NP_001018122.1 (297 aa).
Description 1455 amino acids (163 kDa) conserved in lower vertebrates including zebrafish with 2 nuclear localisation signals (NLS) consensus sequences in N-terminus (Lightfoot et al., 1999), putative peroxidase domain (Ren and Youssoufian, 2001) and a partial leucine zipper in 1069-1090 (Lo Ten Foe et al., 1996), none proven to be functional as such. Despite FANCA protein lack of sequence homologies or motifs that can be assigned to a molecular function, many interactions with other proteins have been described. In this sense, FANCA has a FANCG-binding domain overlapping with NLS region (Waisfisz et al., 1999), a region of interaction with the protein FAAP20 between residues 1095 and 1200 (Ali et al., 2012) or for interaction with BRCA1 through the central part of FANCA protein (aa 740-1083) (Folias et al., 2002).
Through different complexes FANCA can interact with other proteins such as alpha spectrin II, SWI/SNF complex or BLM (DNA-helicase Bloom protein) and other proteins associated with this complex (McMahon et al., 1999; Otsuki et al, 2001; Meetei et al., 2003). FANCA is normally phosphorylated including phosphorylation by ATR-CHK1 on serine 1449 in a process that is required for the formation of the nuclear complex (Collins et al., 2009). FANCA has a consensus sequence for Akt kinase near serine 1149 and its phosphorylation can act as a negative regulator (Otsuki et al., 2002) (Figure 2).
 
  Figure 2. Scheme of FANCA protein. The sizes of the regions are only approximate.
Expression Wide: brain, liver, placenta, testis, tonsils (mRNA); in mice: protein expression predominant in lymphoid organs, testis, ovary (Van de Vrugt et al., 2000).
Localisation FANCA can be cytoplasmic and nuclear where it exerts its primary function.
Function FANCA is one of the15 known FA proteins that participate in the FA/BRCA pathway which participates in the repair of DNA interstrand cross-links, probably involving homologous recombination and the coordination for other DNA damage repair events, including nucleotide excision repair (NER) and translesion synthesis (Moldovan and D'Andrea, 2009). The FA/BRCA pathway may be divided in three parts; 1) FA core complex (FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL and FANCM) and six associated factors (FAAP100, FAAP24, FAAP20, HES1, MHF1 and MHF2), 2) ID complex (FANCD2 and FANCI) and 3) downstream FA proteins (FANCD1/BRCA2, FANCN/PALB2, FANCJ/BRIP1, FANCP/SLX4, FANCO/RAD51C) (Moldovan and D'Andrea, 2009; Ali et al., 2012) (Figure 3).
Several subcomplex are formed in the cytoplasm and from here FANCB-FANCL-FAAP100 are transported together to the nucleus (Ling et al., 2007). FANCA and FANCG form a complex in the cytoplasm, through an N-term FANCA (involving the nuclear localization signal) - FANCG interaction; FANCC join the complex and phosphorylation of FANCA would induce its translocation into the nucleus (Garcia-Higuera et al., 2000; Kruyt et al., 1999). The FA subcomplexes translocates into the nucleus, where FANCE and FANCF are present; and join to the complex (de Winter et al., 2000; kee and D'Andrea, 2010). A large FA core complex is generated with FANCM-FAAP24. Interstrand cross-links are recognized by the FANCM-FAAP24-MHF1/2 complex which recruits the rest of the FA core proteins by interaction between FANCM and FANCF. Because of the ubiquitin E3 ligase activity present in FANCL (Hodson et al., 2011) the heterodimer ID complex formed by FANCD2 and FANCI can be monoubiquitinated and then translocated to chromatin, interacting with downstream proteins in the FA pathway such as FANCD1/BRCA2, FANCN/PALB2, FANCJ/BRIP1, FANCP/SLX4, FANCO/RAD51C and with BRCA1 (Garcia-Higuera et al., 2001) and the nuclease FAN1 (Liu et al., 2010). These downstream FA proteins are involved in DNA repair by homologous recombination (Moldovan and D'Andrea, 2009). In addition to DNA damage, the FA pathway can be activated during S phase of cell cycle. After DNA repair, FANCD2 and FANCI return to the non-ubiquinated form by the action of a complex ubiquitin-specific protease USP1/UAF1 (Nijman et al., 2005) (Figure 3).
Biallelic mutations in FANCA (or in any other gene encoding proteins of the FA core complex) prevent the ubiquitin E3 ligase activity and the monoubiquinitation of FANCD2 and FANCI resulting in a defective FA/BRCA pathway.
 
  Figure 3. Overview of the FA/BRCA pathway. Fanconi proteins are shown in yellow. Other proteins in the FA core complex necessary for monoubiquitination of the ID complex are shown in blue (FAAP; fanconi anemia associated protein). Downstream proteins involved in the pathway are shown in pink. (ICL: interstrand cross-link). ATR-CHK1 phosphorylates multiple FA and FA-associated proteins including FANCA, FANCE, FANCD2, FANCI and BRCA1. Not all protein interactions are shown and proximity nor imply direct interaction (Adapted from Valeri et al., 2011).
Homology No known complete homology or functional motifs.

Mutations

Note Epigenetics: Although hypermethylation of the promotor of different FA genes (FANCD1/BRCA2, FANCB, FANCC, FANCL, FANCN and especially in FANCF) has been described in several sporadic malignancies this effect has not been described so far in FANCA (Valeri et al., 2011).
Germinal The number of different pathogenic mutations in FANCA gene is very high. Mutations are heterogeneous; point mutations, splicing mutations, large intragene deletions probably Alu-mediated or insertions have been described (Morgan et al., 1999; Levran et al., 2005). Over 90% of the mutations are private, with about 30% being relatively large deletions. Founder mutations have been described in South Africa and Spanish Gypsies (Tipping et al., 2001; Callen et al., 2005). Unlike mutations in downstream FA genes such as FANCD1/BRCA2 (breast, ovarian, and solid childhood cancer), FANCN/PALB2 (breast cancer) or FANCO/RAD51C (breast and ovarian cancer), FANCJ/BRIP1 (breast cancer and solid childhood cancer), the carriers of monoallelic mutations in FANCA do not seem to have a significant risk of cancer (Garcia and Benitez, 2008). However, It has been recently described in Finnish breast cancer families that FANCA deletions might contribute to breast cancer susceptibility, potentially in combination with other germline mutations (Solyom et al., 2011).
Somatic In FA-A patients, the presence of wild type cells with a restored FANCA function, can be obtained via back mutation, intragenic crossover, compensating deletions/insertions, or gene conversion of either the paternal or maternal allele. This can lead to a selective advantage of corrected cells generating the so-called somatic mosaicism (Gregory et al., 2001; Gross et al., 2002). The clinical significance of this mosaicism is unclear but there are cases that show improvement of their hematological status when the correction involves hematopoietic stem cells. Somatic mutations and epigenetic silencing in some FA genes occur in a variety of cancers in the general population (non-FA patients) (Valeri et al., 2011). In relation to FANCA, deletions or point mutations were found in several sporadic AML (Tischkowitz et al., 2004; Condie et al., 2002).

Implicated in

Entity Fanconi anaemia (FA)
Note FANCA is implicated in the FA complementation group A (FA-A) that is the most frequent complementation group accounting for about 70% of FA cases, although geographical variations may alter the prevalence in some complementation groups (Casado et al., 2007).
Disease Fanconi anaemia is a chromosome instability syndrome/cancer prone disease (at risk of leukaemia and squamous cell carcinoma), progressive bone marrow failure (pancytopenia), and several congenital abnormalities mainly: skin hiperpigmentation, skeletal malformation, small stature or urogenital abnormalities (Auerbach, 2009).
Prognosis Fanconi anaemia's prognosis is poor; mean survival is 20 years: patients die of bone marrow failure (infections, haemorrhages), leukaemia, or solid cancer specially squamous carcinomas (SCC) in adult patients. Hematopoietic stem cell transplantation with a suitable HLA-matched donor is currently the best treatment to cure the aplastic anemia or leukaemia (Gluckman and Wagner, 2008).
It has been shown that significant phenotypic differences were found between the various complementation groups. In FA group A, patients homozygous for null mutations had an earlier onset of anemia and a higher incidence of leukemia than those with mutations producing an altered protein. Patients homozygous for null mutations in FANCA are high-risk groups with a poor hematologic outcome and should be considered as candidates both for frequent monitoring and early therapeutic intervention (Faivre et al., 2000). However, in another recent study, no clinical differences in terms of onset of hematologic disease and number of congenital anomalies were found in patients with expression of a mutant form of FANCA protein compared with patients without expression of the protein (Castella et al., 2011).
Cytogenetics Compared to control cells, an increase of chromatid-type aberrations (breaks, gaps, interchanges; increased rate of breaks) is observed in FA cells when samples are treated with specific clastogens known as DNA inter-strand cross-linking agents (e.g. mitomycin C, diepoxybutane). Theses agents are widely used for FA diagnosis (Auerbach, 1993).
  

External links

Nomenclature
HGNC (Hugo)FANCA   3582
Cards
AtlasFA1ID102
Entrez_Gene (NCBI)FANCA  2175  Fanconi anemia, complementation group A
GeneCards (Weizmann)FANCA
Ensembl (Hinxton)ENSG00000187741 [Gene_View]  chr16:89803959-89883065 [Contig_View]  FANCA [Vega]
AceView (NCBI)FANCA
Genatlas (Paris)FANCA
WikiGenes2175
SOURCE (Princeton)NM_000135 NM_001018112 NM_001286167
Genomic and cartography
GoldenPath (UCSC)FANCA  -  16q24.3   chr16:89803959-89883065 -  16q24.3   [Description]    (hg19-Feb_2009)
EnsemblFANCA - 16q24.3 [CytoView]
Mapping of homologs : NCBIFANCA [Mapview]
OMIM227650   607139   
Gene and transcription
Genbank (Entrez)AK299282 AK301168 BC008979 BC022498 BC064540
RefSeq transcript (Entrez)NM_000135 NM_001018112 NM_001286167
RefSeq genomic (Entrez)AC_000148 NC_000016 NC_018927 NG_011706 NT_010542 NW_001838336 NW_004929403
Consensus coding sequences : CCDS (NCBI)FANCA
Cluster EST : UnigeneHs.744083 [ NCBI ]
CGAP (NCI)Hs.744083
Alternative Splicing : Fast-db (Paris)GSHG0012092
Alternative Splicing GalleryENSG00000187741
Gene ExpressionFANCA [ NCBI-GEO ]     FANCA [ SEEK ]   FANCA [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtO15360 (Uniprot)
NextProtO15360  [Medical]
With graphics : InterProO15360
Splice isoforms : SwissVarO15360 (Swissvar)
Domains : Interpro (EBI)Fanconia   
Related proteins : CluSTrO15360
Domain families : Pfam (Sanger)Fanconi_A (PF03511)   
Domain families : Pfam (NCBI)pfam03511   
DMDM Disease mutations2175
Blocks (Seattle)O15360
Human Protein AtlasENSG00000187741
Peptide AtlasO15360
HPRD06186
IPIIPI00006170   IPI00219337   IPI00922440   IPI01014803   IPI00785107   IPI00816416   IPI00816196   
Protein Interaction databases
DIP (DOE-UCLA)O15360
IntAct (EBI)O15360
FunCoupENSG00000187741
BioGRIDFANCA
InParanoidO15360
Interologous Interaction database O15360
IntegromeDBFANCA
STRING (EMBL)FANCA
Ontologies - Pathways
Ontology : AmiGOprotein binding  nucleus  nucleoplasm  cytoplasm  DNA repair  protein complex assembly  male meiosis  male gonad development  female gonad development  regulation of cell proliferation  Fanconi anaemia nuclear complex  
Ontology : EGO-EBIprotein binding  nucleus  nucleoplasm  cytoplasm  DNA repair  protein complex assembly  male meiosis  male gonad development  female gonad development  regulation of cell proliferation  Fanconi anaemia nuclear complex  
Pathways : BIOCARTABRCA1-dependent Ub-ligase activity [Genes]    Role of BRCA1, BRCA2 and ATR in Cancer Susceptibility [Genes]   
Pathways : KEGGFanconi anemia pathway   
REACTOMEFANCA
Protein Interaction DatabaseFANCA
Wikipedia pathwaysFANCA
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)FANCA
SNP (GeneSNP Utah)FANCA
SNP : HGBaseFANCA
Genetic variants : HAPMAPFANCA
1000_GenomesFANCA 
ICGC programENSG00000187741 
Cancer Gene: CensusFANCA 
Somatic Mutations in Cancer : COSMICFANCA 
CONAN: Copy Number AnalysisFANCA 
Mutations and Diseases : HGMDFANCA
OMIM227650    607139   
GENETestsFANCA
Disease Genetic AssociationFANCA
Huge Navigator FANCA [HugePedia]  FANCA [HugeCancerGEM]
Genomic VariantsFANCA  FANCA [DGVbeta]
Exome VariantFANCA
dbVarFANCA
ClinVarFANCA
snp3D : Map Gene to Disease2175
General knowledge
Homologs : HomoloGeneFANCA
Homology/Alignments : Family Browser (UCSC)FANCA
Phylogenetic Trees/Animal Genes : TreeFamFANCA
Chemical/Protein Interactions : CTD2175
Chemical/Pharm GKB GenePA27995
Clinical trialFANCA
Cancer Resource (Charite)ENSG00000187741
Other databases
Probes
Litterature
PubMed146 Pubmed reference(s) in Entrez
CoreMineFANCA
iHOPFANCA

Bibliography

Fanconi anemia diagnosis and the diepoxybutane (DEB) test.
Auerbach AD.
Exp Hematol. 1993 Jun;21(6):731-3.
PMID 8500573
 
Expression cloning of a cDNA for the major Fanconi anaemia gene, FAA.
Lo Ten Foe JR, Rooimans MA, Bosnoyan-Collins L, Alon N, Wijker M, Parker L, Lightfoot J, Carreau M, Callen DF, Savoia A, Cheng NC, van Berkel CG, Strunk MH, Gille JJ, Pals G, Kruyt FA, Pronk JC, Arwert F, Buchwald M, Joenje H.
Nat Genet. 1996 Nov;14(3):320-3.
PMID 8896563
 
The genomic organization of the Fanconi anemia group A (FAA) gene.
Ianzano L, D'Apolito M, Centra M, Savino M, Levran O, Auerbach AD, Cleton-Jansen AM, Doggett NA, Pronk JC, Tipping AJ, Gibson RA, Mathew CG, Whitmore SA, Apostolou S, Callen DF, Zelante L, Savoia A.
Genomics. 1997 May 1;41(3):309-14.
PMID 9169126
 
Fanconi anemia proteins FANCA, FANCC, and FANCG/XRCC9 interact in a functional nuclear complex.
Garcia-Higuera I, Kuang Y, Naf D, Wasik J, D'Andrea AD.
Mol Cell Biol. 1999 Jul;19(7):4866-73.
PMID 10373536
 
Resistance to mitomycin C requires direct interaction between the Fanconi anemia proteins FANCA and FANCG in the nucleus through an arginine-rich domain.
Kruyt FA, Abou-Zahr F, Mok H, Youssoufian H.
J Biol Chem. 1999 Nov 26;274(48):34212-8.
PMID 10567393
 
Characterization of regions functional in the nuclear localization of the Fanconi anemia group A protein.
Lightfoot J, Alon N, Bosnoyan-Collins L, Buchwald M.
Hum Mol Genet. 1999 Jun;8(6):1007-15.
PMID 10332032
 
Human alpha spectrin II and the Fanconi anemia proteins FANCA and FANCC interact to form a nuclear complex.
McMahon LW, Walsh CE, Lambert MW.
J Biol Chem. 1999 Nov 12;274(46):32904-8.
PMID 10551855
 
High frequency of large intragenic deletions in the Fanconi anemia group A gene.
Morgan NV, Tipping AJ, Joenje H, Mathew CG.
Am J Hum Genet. 1999 Nov;65(5):1330-41.
PMID 10521298
 
A physical complex of the Fanconi anemia proteins FANCG/XRCC9 and FANCA.
Waisfisz Q, de Winter JP, Kruyt FA, de Groot J, van der Weel L, Dijkmans LM, Zhi Y, Arwert F, Scheper RJ, Youssoufian H, Hoatlin ME, Joenje H.
Proc Natl Acad Sci U S A. 1999 Aug 31;96(18):10320-5.
PMID 10468606
 
The Fanconi anemia protein FANCF forms a nuclear complex with FANCA, FANCC and FANCG.
de Winter JP, van der Weel L, de Groot J, Stone S, Waisfisz Q, Arwert F, Scheper RJ, Kruyt FA, Hoatlin ME, Joenje H.
Hum Mol Genet. 2000 Nov 1;9(18):2665-74.
PMID 11063725
 
Association of complementation group and mutation type with clinical outcome in fanconi anemia. European Fanconi Anemia Research Group.
Faivre L, Guardiola P, Lewis C, Dokal I, Ebell W, Zatterale A, Altay C, Poole J, Stones D, Kwee ML, van Weel-Sipman M, Havenga C, Morgan N, de Winter J, Digweed M, Savoia A, Pronk J, de Ravel T, Jansen S, Joenje H, Gluckman E, Mathew CG.
Blood. 2000 Dec 15;96(13):4064-70.
PMID 11110674
 
The fanconi anemia proteins FANCA and FANCG stabilize each other and promote the nuclear accumulation of the Fanconi anemia complex.
Garcia-Higuera I, Kuang Y, Denham J, D'Andrea AD.
Blood. 2000 Nov 1;96(9):3224-30.
PMID 11050007
 
Cloning and characterization of murine fanconi anemia group A gene: Fanca protein is expressed in lymphoid tissues, testis, and ovary.
van de Vrugt HJ, Cheng NC, de Vries Y, Rooimans MA, de Groot J, Scheper RJ, Zhi Y, Hoatlin ME, Joenje H, Arwert F.
Mamm Genome. 2000 Apr;11(4):326-31.
PMID 10754110
 
Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway.
Garcia-Higuera I, Taniguchi T, Ganesan S, Meyn MS, Timmers C, Hejna J, Grompe M, D'Andrea AD.
Mol Cell. 2001 Feb;7(2):249-62.
PMID 11239454
 
Somatic mosaicism in Fanconi anemia: evidence of genotypic reversion in lymphohematopoietic stem cells.
Gregory JJ Jr, Wagner JE, Verlander PC, Levran O, Batish SD, Eide CR, Steffenhagen A, Hirsch B, Auerbach AD.
Proc Natl Acad Sci U S A. 2001 Feb 27;98(5):2532-7. Epub 2001 Feb 13.
PMID 11226273
 
Fanconi anemia and DNA repair.
Grompe M, D'Andrea A.
Hum Mol Genet. 2001 Oct 1;10(20):2253-9. (REVIEW)
PMID 11673408
 
Fanconi anemia protein, FANCA, associates with BRG1, a component of the human SWI/SNF complex.
Otsuki T, Furukawa Y, Ikeda K, Endo H, Yamashita T, Shinohara A, Iwamatsu A, Ozawa K, Liu JM.
Hum Mol Genet. 2001 Nov 1;10(23):2651-60.
PMID 11726552
 
Functional analysis of the putative peroxidase domain of FANCA, the Fanconi anemia complementation group A protein.
Ren J, Youssoufian H.
Mol Genet Metab. 2001 Jan;72(1):54-60.
PMID 11161829
 
Molecular and genealogical evidence for a founder effect in Fanconi anemia families of the Afrikaner population of South Africa.
Tipping AJ, Pearson T, Morgan NV, Gibson RA, Kuyt LP, Havenga C, Gluckman E, Joenje H, de Ravel T, Jansen S, Mathew CG.
Proc Natl Acad Sci U S A. 2001 May 8;98(10):5734-9.
PMID 11344308
 
Analysis of the Fanconi anaemia complementation group A gene in acute myeloid leukaemia.
Condie A, Powles RL, Hudson CD, Shepherd V, Bevan S, Yuille MR, Houlston RS.
Leuk Lymphoma. 2002 Sep;43(9):1849-53.
PMID 12685843
 
BRCA1 interacts directly with the Fanconi anemia protein FANCA.
Folias A, Matkovic M, Bruun D, Reid S, Hejna J, Grompe M, D'Andrea A, Moses R.
Hum Mol Genet. 2002 Oct 1;11(21):2591-7.
PMID 12354784
 
Reverse mosaicism in Fanconi anemia: natural gene therapy via molecular self-correction.
Gross M, Hanenberg H, Lobitz S, Friedl R, Herterich S, Dietrich R, Gruhn B, Schindler D, Hoehn H.
Cytogenet Genome Res. 2002;98(2-3):126-35.
PMID 12697994
 
Phosphorylation of Fanconi anemia protein, FANCA, is regulated by Akt kinase.
Otsuki T, Nagashima T, Komatsu N, Kirito K, Furukawa Y, Kobayashi Si S, Liu JM, Ozawa K.
Biochem Biophys Res Commun. 2002 Mar 1;291(3):628-34.
PMID 11855836
 
A multiprotein nuclear complex connects Fanconi anemia and Bloom syndrome.
Meetei AR, Sechi S, Wallisch M, Yang D, Young MK, Joenje H, Hoatlin ME, Wang W.
Mol Cell Biol. 2003 May;23(10):3417-26.
PMID 12724401
 
Deletion and reduced expression of the Fanconi anemia FANCA gene in sporadic acute myeloid leukemia.
Tischkowitz MD, Morgan NV, Grimwade D, Eddy C, Ball S, Vorechovsky I, Langabeer S, Stoger R, Hodgson SV, Mathew CG.
Leukemia. 2004 Mar;18(3):420-5.
PMID 14749703
 
A common founder mutation in FANCA underlies the world's highest prevalence of Fanconi anemia in Gypsy families from Spain.
Callen E, Casado JA, Tischkowitz MD, Bueren JA, Creus A, Marcos R, Dasi A, Estella JM, Munoz A, Ortega JJ, de Winter J, Joenje H, Schindler D, Hanenberg H, Hodgson SV, Mathew CG, Surralles J.
Blood. 2005 Mar 1;105(5):1946-9. Epub 2004 Nov 2.
PMID 15522956
 
Spectrum of sequence variations in the FANCA gene: an International Fanconi Anemia Registry (IFAR) study.
Levran O, Diotti R, Pujara K, Batish SD, Hanenberg H, Auerbach AD.
Hum Mutat. 2005 Feb;25(2):142-9.
PMID 15643609
 
The deubiquitinating enzyme USP1 regulates the Fanconi anemia pathway.
Nijman SM, Huang TT, Dirac AM, Brummelkamp TR, Kerkhoven RM, D'Andrea AD, Bernards R.
Mol Cell. 2005 Feb 4;17(3):331-9.
PMID 15694335
 
A comprehensive strategy for the subtyping of patients with Fanconi anaemia: conclusions from the Spanish Fanconi Anemia Research Network.
Antonio Casado J, Callen E, Jacome A, Rio P, Castella M, Lobitz S, Ferro T, Munoz A, Sevilla J, Cantalejo A, Cela E, Cervera J, Sanchez-Calero J, Badell I, Estella J, Dasi A, Olive T, Jose Ortega J, Rodriguez-Villa A, Tapia M, Molines A, Madero L, Segovia JC, Neveling K, Kalb R, Schindler D, Hanenberg H, Surralles J, Bueren JA.
J Med Genet. 2007 Apr;44(4):241-9. Epub 2006 Nov 14.
PMID 17105750
 
FAAP100 is essential for activation of the Fanconi anemia-associated DNA damage response pathway.
Ling C, Ishiai M, Ali AM, Medhurst AL, Neveling K, Kalb R, Yan Z, Xue Y, Oostra AB, Auerbach AD, Hoatlin ME, Schindler D, Joenje H, de Winter JP, Takata M, Meetei AR, Wang W.
EMBO J. 2007 Apr 18;26(8):2104-14. Epub 2007 Mar 29.
PMID 17396147
 
The Fanconi anaemia/BRCA pathway and cancer susceptibility. Searching for new therapeutic targets.
Garcia MJ, Benitez J.
Clin Transl Oncol. 2008 Feb;10(2):78-84. (REVIEW)
PMID 18258506
 
Hematopoietic stem cell transplantation in childhood inherited bone marrow failure syndrome.
Gluckman E, Wagner JE.
Bone Marrow Transplant. 2008 Jan;41(2):127-32. Epub 2007 Dec 17. (REVIEW)
PMID 18084332
 
Fanconi anemia and its diagnosis.
Auerbach AD.
Mutat Res. 2009 Jul 31;668(1-2):4-10. Epub 2009 Feb 28. (REVIEW)
PMID 19622403
 
ATR-dependent phosphorylation of FANCA on serine 1449 after DNA damage is important for FA pathway function.
Collins NB, Wilson JB, Bush T, Thomashevski A, Roberts KJ, Jones NJ, Kupfer GM.
Blood. 2009 Mar 5;113(10):2181-90. Epub 2008 Dec 24.
PMID 19109555
 
How the fanconi anemia pathway guards the genome.
Moldovan GL, D'Andrea AD.
Annu Rev Genet. 2009;43:223-49.
PMID 19686080
 
Expanded roles of the Fanconi anemia pathway in preserving genomic stability.
Kee Y, D'Andrea AD.
Genes Dev. 2010 Aug 15;24(16):1680-94. (REVIEW)
PMID 20713514
 
FAN1 acts with FANCI-FANCD2 to promote DNA interstrand cross-link repair.
Liu T, Ghosal G, Yuan J, Chen J, Huang J.
Science. 2010 Aug 6;329(5992):693-6. Epub 2010 Jul 29.
PMID 20671156
 
Origin, functional role, and clinical impact of Fanconi anemia FANCA mutations.
Castella M, Pujol R, Callen E, Trujillo JP, Casado JA, Gille H, Lach FP, Auerbach AD, Schindler D, Benitez J, Porto B, Ferro T, Munoz A, Sevilla J, Madero L, Cela E, Belendez C, de Heredia CD, Olive T, de Toledo JS, Badell I, Torrent M, Estella J, Dasi A, Rodriguez-Villa A, Gomez P, Barbot J, Tapia M, Molines A, Figuera A, Bueren JA, Surralles J.
Blood. 2011 Apr 7;117(14):3759-69. Epub 2011 Jan 27.
PMID 21273304
 
Structural analysis of human FANCL, the E3 ligase in the Fanconi anemia pathway.
Hodson C, Cole AR, Lewis LP, Miles JA, Purkiss A, Walden H.
J Biol Chem. 2011 Sep 16;286(37):32628-37. Epub 2011 Jul 20.
PMID 21775430
 
Screening for large genomic rearrangements in the FANCA gene reveals extensive deletion in a Finnish breast cancer family.
Solyom S, Winqvist R, Nikkila J, Rapakko K, Hirvikoski P, Kokkonen H, Pylkas K.
Cancer Lett. 2011 Mar 28;302(2):113-8. Epub 2011 Jan 13.
PMID 21236561
 
Fanconi anaemia: from a monogenic disease to sporadic cancer.
Valeri A, Martinez S, Casado JA, Bueren JA.
Clin Transl Oncol. 2011 Apr;13(4):215-21. (REVIEW)
PMID 21493181
 
FAAP20: a novel ubiquitin-binding FA nuclear core-complex protein required for functional integrity of the FA-BRCA DNA repair pathway.
Ali AM, Pradhan A, Singh TR, Du C, Li J, Wahengbam K, Grassman E, Auerbach AD, Pang Q, Meetei AR.
Blood. 2012 Apr 5;119(14):3285-94. Epub 2012 Feb 17.
PMID 22343915
 
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Written04-1998Jean-Loup Huret
Genetics, Dept Medical Information, University of Poitiers, CHU Poitiers Hospital, F-86021 Poitiers, France
Updated12-2001Hans Joenje
Department of Clinical Genetics and Human Genetics VU University Medical Center Van der Boechorststraat 7, NL-1081 BT Amsterdam, The Netherlands
Updated06-2002Jean-Loup Huret
Genetics, Dept Medical Information, University of Poitiers, CHU Poitiers Hospital, F-86021 Poitiers, France
Updated03-2012Jose Antonio Casado, Juan Antonio Bueren
Hematopoiesis and Gene Therapy, Centro de Investigaciones Energeticas, Medioambientales y Tecnologicas, and Centro de Investigacion Biomedica en Red de Enfermedades Raras (CIBERER), Madrid, Spain

Citation

This paper should be referenced as such :
Huret JL . FANCA (Fanconi anemia, complementation group A). Atlas Genet Cytogenet Oncol Haematol. April 1998 .
Joenje H . FANCA (Fanconi anemia, complementation group A). Atlas Genet Cytogenet Oncol Haematol. December 2001 .
Huret JL . FANCA (Fanconi anemia, complementation group A). Atlas Genet Cytogenet Oncol Haematol. June 2002 .
Casado JA, Bueren JA . FANCA (Fanconi anemia, complementation group A). Atlas Genet Cytogenet Oncol Haematol. March 2012 .
URL : http://AtlasGeneticsOncology.org/Genes/FA1ID102.html

The various updated versions of this paper are referenced and archived by INIST as such :
http://documents.irevues.inist.fr/bitstream/2042/37432/1/04-1998-FA1ID102.pdf   [ Bibliographic record ]
http://documents.irevues.inist.fr/bitstream/2042/37829/1/12-2001-FA1ID102.pdf   [ Bibliographic record ]
http://documents.irevues.inist.fr/bitstream/2042/37891/1/06-2002-FA1ID102.pdf   [ Bibliographic record ]
http://documents.irevues.inist.fr/bitstream/handle/2042/47530/03-2012-FA1ID102.pdf   [ Bibliographic record ]

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