Atlas of Genetics and Cytogenetics in Oncology and Haematology


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BRCA1 (breast cancer 1, early onset)

Identity

Other namesBRCAI
BRCC1
IRIS
PSCP
RNF53
HGNC (Hugo) BRCA1
LocusID (NCBI) 672
Location 17q21.31
Location_base_pair Starts at 41196312 and ends at 41277500 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Local_order According to NCBI Map Viewer, genes flanking BRCA1 in centromere to telomere direction on 17q21 are: VAT1 17q21 (vesicle amine transport protein 1 homolog (T californica)); RND2 17q21 Rho family GTPase 2; RPL21P4 17q21 ribosomal protein L21 pseudogene 4; BRCA1 17q21 breast cancer 1, early onset; NBR2 17q21 neighbour of BRCA1 gene; BRCA1P1 17q21 BRCA1 pseudogene 1; NBR1 17q21.31 neighbour of BRCA1 gene.
Note BRCA1 is a tumour suppressor phosphoprotein that combines with other tumour suppressors, DNA damage and repair proteins, and signal transducers to form a large multi-subunit protein complex known as BRCA1-associated genome surveillance complex (BASC). Truncating mutations and missence mutations in the BRCA1 gene are found in a large number of familial breast cancer cases. Individuals who inherit a germline mutation of BRCA1 or BRCA2 have a significantly increased lifetime risk for the development of breast and/or ovarian cancer.

DNA/RNA

Note The subcellular localization and physiological function of this gene is greatly modulated by the several alternately splices isoforms that are found. Several of these alternatively spliced transcript variants have been described, however, not all have had their full-length natures identified.
Description According to Entrez-Gene, BRCA1 gene maps to NC_000017.9 in the region between 38449840 and 38530994 on the minus strand and spans across 81.1 kilo bases. According to Spidey (mRNA to genomic sequence alignment tool, http://www.ncbi.nlm.nih.gov/spidey), BRCA1 has 24 exons, the sizes being 181, 99, 54, 78, 89, 140, 105, 47, 77, 89, 172, 127, 191, 311, 88, 78, 41, 84, 55, 74, 61, 1506.
Transcription BRCA1 mRNA NM_007302.3 has 7388bps. The BRCA1 gene contains two separate promoters that induce transcription of mRNAs with different 5' UTRs, a shorter 5'UTRa and a longer 5'UTRb. The downregulation of BRCA1 gene expression in certain breast cancers is caused by a switch from expression of a 5'UTRa, which enables efficient translation, to expression of 5' UTRb, which contains secondary structure and upstream open reading frames that strongly inhibit translation.
Pseudogene According to Entrez Gene the BRCA1 pseudogene 1 (BRCA1P1) is located on 17q21.

Protein

Note BRCA1 sequence is not well conserved between mammals, however, two domains, the C terminal BRCT (BRCA1 C Terminal) motifs and the N-terminal RING domain are highly conserved.
 
  The BRCA1 protein showing the RING finger domain, the Nuclear Localisation Signal domain and the BRCT domains. AA- amino acids.
Description BRCA1 is an 1863 amino acid 220kDa protein with an E3 ubiquitin ligase activity as well as a phospho-peptide binding activity. It has several domains that are essential for its function as depicted in the figure. The RING finger domain of BRCA1, commonly found in many DNA repair proteins, consists of a conserved core of approximately 50 amino acids in a pattern of seven cysteine residues and one histidine residue to form a structure that can bind to two Zn++ ions. This motif aids in mediating protein-protein interaction, as exemplified by the interaction of BRCA1 with BARD1 (BRCA1 associated RING domain). This interaction is critical since mutations in the Zn++ binding regions, crucial for heterodimerization with BARD1, have been found in tumours. BRCA1 accumulates in distinct foci in the nucleus during S phase and this transfer is aided by its Nuclear Localisation Signal (NLS) domain. A further role of BARD1 is also implicated whereby its association with the RING finger domain of BRCA1 is necessary for the transfer of BRCA1 to the nucleus. BRCA1 interacts with Rad50 of the MRN complex through the region AA 341-748 and can directly bind to branched, flap and four way DNA structures through a central domain spanning residues 452-1079. The protein inhibits the nucleolytic activities of the Mre11/Rad50/Nbs1 complex as a result of this direct DNA binding. The C terminus of BRCA1, which can function as a transcriptional activation domain, consists of two tandemly arranged elements called BRCT (BRCA1 C- terminal). This motif specifically binds to phosphorylated proteins, an event that is commonly associated with DNA damage response. BRCA1 is capable of interacting directly with BRCA2 and with Rad51 via BRCA2 through this motif. Another protein that interacts with BRCA1 via BRCT is the BRCA1 associated C-terminal helicase ( BACH1 ). BACH1 is said to aid BRCA1 in the DNA damage response and maintain the protein at the nuclear foci formed after DNA damage response. Other proteins that can interact with BRCA1 through the BRCT domains are C terminal Interacting protein /CtIP), RNA Polymerase II, BACH 1 (a member of DEAH helicase family) and p53 .
Expression BRCA1 is ubiquitously expressed in humans with the highest levels observed in the ovaries, testis and thymus. It is a tumour suppressor and a reduced expression is correlated with the transformation procedure and aetiology of sporadic breast cancer. This reduction is expression is said to be transcriptionally regulated with implications of aberrant promoter methylation at CpG dinucleotides as well as CREB binding sites.
Localisation Located in the nucleus.
Function Role of BRCA1 in DNA repair: BRCA1 is a part of a large complex of proteins, the BASC, which monitors the genome for damage and signals downstream effectors. BRCA1 has been implicated in two pathways of DNA double strand break repair: homologous recombination (HR) and non homologous end joining (NHEJ). Upon exposure to DNA damaging agents, BRCA1 becomes hyperphosphorylated and is rapidly relocated, along with Rad51, to sites of DNA synthesis marked by proliferating cell nuclear antigen (PCNA). Rad51, a homolog of the bacterial RecA, is a central player in HR, catalyzing the invasion of the single stranded DNA in a homologous duplex and facilitating the homology search during the establishment of joint molecules. A recent study, however, has indicated that BRCA1 deficient breast cancer cells compensate for this deficiency by upregulating Rad51. The resultant HR may be erroneous and thereby lead to tumorigenesis. In addition, BRCA1 is said to inhibit the MRN complex which is is implicated in bringing together two DNA strands together for the error prone NHEJ. BRCA1-deficient cells are sensitive to ionizing radiation and DNA damaging drugs, such as mitomycin C.
Transcriptional regulation: BRCA1 is capable of transcriptional regulation and chromatin remodelling when tethered to promoters of genes important in the DNA repair process and breast cancer markers. It is a member of the core RNA polymerase II transcriptional machinery, a feature exploited by the DNA damage recognition process. In addition, BRCA1 interacts with p300/CBP, transcriptional coactivators for CREB. p300/CBP are inhibited by the viral oncoprotein E1A and the functionality of E1A as an oncogene could be in part caused by an obstruction of BRCA1:p300/CBP cooperation resulting in the loss of the tumour-suppressing function of BRCA1. BRCA1 can act as a transcriptional coactivator or co repressor of proteins implicated in chromatin remodelling, such as the histone deacetylase complexes or components of the SWI/SNF-related chromatin-remodelling complex.
Cell Cycle Regulation by BRCA1: BRCA1, based on its phosphorylation status, elicits DNA damage induced cell cycle arrest at several stages through modulation of specific downstream target genes. BRCA1 transactivates p21cip1/WAF1, which contributes to an arrest at the G1/S boundary. ATM phosphorylation of BRCA1 appears to be important for its role in the intra S phase checkpoint activation. BRCA1 is also implicated in the transcriptional regulation of several genes such as cyclinB, 14-3-3sigma, GADD45, wee-1 kinase and PLK1 associated with the G2/M checkpoint.
p53-dependent apoptosis: The BRCA1 protein is capable of physically interacting with the p53 tumour suppressor gene, and can stimulate p53-dependent transcription from the p21WAF1/CIP1 mdm2 and promoters. In addition, the BRCA1-BARD1 complex is required for the phosphorylation of p53 at Ser15 by ATM/ATR following DNA damage by IR or UV radiation. The phosphorylation of p53 at Ser-15 is essential for the G(1)/S cell cycle arrest via transcriptional induction of the cyclin-dependent kinase inhibitor p21 after DNA damage.
Ubiquitination: BRCA1 and BARD1 interact together to form an E3 ubiquitin ligase. RNA polII stalled at sites of DNA damage is a target for this ubiquitin ligase mediated degradation following DNA damage, thereby allowing access to the repair machinery. BRCA1 ubiquitinates the transcriptional preinitiation complex, not for proteasomal degradation, but to prevent a stable association of TFIIE and TFIIH; thereby blocking the initiation of mRNA synthesis.
Homology Dog (Canis familiaris): BRCA1
Chimpanzee(Pan troglodytes): BRCA1
Rat (Rattus norvegicus): Brca1
Mouse(Mus musculus): Brca1
Chicken(Gallus gallus): BRCA1

Mutations

Note BRCA1 germline mutations contribute significantly to the development of familial/hereditary breast and ovarian cancer. However, each gene carries as many as 1000 different disease associated mutations, many of which are rare. These mutations are distributed uniformly along the entire coding region and intronic sequences flanking each exon. The mutations are at a high penetrance therefore women who carry these mutations have a lifetime risk of 80-90% to develop breast cancer. Founder mutations such as the BRCA1-185delAG and 5382insC are found among Ashkenazi Jews. Larger and complex genomic rearrangements in the exons 21 and 22 of the BRCA1 gene, resulting in a lack of the BRCT motif have been reported.

Implicated in

Entity Breast Cancer
Disease Heterozygous carriers of high-risk mutations in the general Caucasian population have been estimated to be about one in 1000 for the BRCA1 gene. The lifetime risk of the development of hereditary breast cancer with the presence of BRCA1 mutations is very high. In addition, for sporadic breast cancer, a reduction in the expression of BRCA1 rather than the presence of mutations has been observed. The lack of a functional BRCA1 leads to impaired repair of DNA double strand breaks, cell cycle progression and transcriptional regulation, thereby causing the development of neoplasms.
  
Entity Ovarian Cancer
Disease Mutations of the BRCA1 gene is the major cause for familial breast and ovarian cancer incidence. The lifetime risks of ovarian cancer associated with a BRCA1 gene mutation carrier has been estimated as 40 to 50%. The most common mutations are frameshift and nonsense mutations that are predicted to cause premature truncation of the BRCA1 protein. In addition, mutations that are predicted to affect splice-site consensus sequences as well as missense mutation have also been seen in ovarian cancer. Large genomic alterations, such as the gains in copy number of exon 13 as well as deletion of exons in the BRCA1 gene is also associated with the development of ovarian cancer.
  
Entity Other cancers
Disease An increased relative risk to the development of cancer of the colon, cervix, uterus, pancreas and prostate has been suggested in BRCA1-mutation carriers.
  

Other Leukemias implicated (Data extracted from papers in the Atlas)

Leukemias 11q23ChildAMLID1615

Other Solid tumors implicated (Data extracted from papers in the Atlas)

Solid Tumors AmeloblastomID5945 MedulloblastomaID5065 rhab5004 rhabID5004 blad5001

External links

Nomenclature
HGNC (Hugo)BRCA1   1100
Cards
AtlasBRCA1ID163ch17q21
Entrez_Gene (NCBI)BRCA1  672  breast cancer 1, early onset
GeneCards (Weizmann)BRCA1
Ensembl (Hinxton)ENSG00000012048 [Gene_View]  chr17:41196312-41277500 [Contig_View]  BRCA1 [Vega]
ICGC DataPortalENSG00000012048
cBioPortalBRCA1
AceView (NCBI)BRCA1
Genatlas (Paris)BRCA1
WikiGenes672
SOURCE (Princeton)NM_007294 NM_007295 NM_007296 NM_007297 NM_007298 NM_007299 NM_007300 NM_007301 NM_007302 NM_007303 NM_007305 NM_007306
Genomic and cartography
GoldenPath (UCSC)BRCA1  -  17q21.31   chr17:41196312-41277500 -  17q21.31   [Description]    (hg19-Feb_2009)
EnsemblBRCA1 - 17q21.31 [CytoView]
Mapping of homologs : NCBIBRCA1 [Mapview]
OMIM113705   114480   604370   614320   
Gene and transcription
Genbank (Entrez)AB621825 AF005068 AF274503 AK307553 AK308084
RefSeq transcript (Entrez)NM_007294 NM_007295 NM_007296 NM_007297 NM_007298 NM_007299 NM_007300 NM_007301 NM_007302 NM_007303 NM_007305 NM_007306
RefSeq genomic (Entrez)AC_000149 NC_000017 NC_018928 NG_005905 NT_010783 NW_001838436 NW_004929407
Consensus coding sequences : CCDS (NCBI)BRCA1
Cluster EST : UnigeneHs.194143 [ NCBI ]
CGAP (NCI)Hs.194143
Alternative Splicing : Fast-db (Paris)GSHG0013437
Alternative Splicing GalleryENSG00000012048
Gene ExpressionBRCA1 [ NCBI-GEO ]     BRCA1 [ SEEK ]   BRCA1 [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP38398 (Uniprot)
NextProtP38398  [Medical]
With graphics : InterProP38398
Splice isoforms : SwissVarP38398 (Swissvar)
Catalytic activity : Enzyme6.3.2.- [ Enzyme-Expasy ]   6.3.2.-6.3.2.- [ IntEnz-EBI ]   6.3.2.- [ BRENDA ]   6.3.2.- [ KEGG ]   
Domaine pattern : Prosite (Expaxy)BRCT (PS50172)    ZF_RING_1 (PS00518)    ZF_RING_2 (PS50089)   
Domains : Interpro (EBI)BRCA1 [organisation]   BRCA1_serine_dom [organisation]   BRCT_dom [organisation]   Znf_C3HC4_RING-type [organisation]   Znf_RING [organisation]   Znf_RING/FYVE/PHD [organisation]   Znf_RING_CS [organisation]  
Related proteins : CluSTrP38398
Domain families : Pfam (Sanger)BRCT (PF00533)    BRCT_assoc (PF12820)    zf-C3HC4 (PF00097)   
Domain families : Pfam (NCBI)pfam00533    pfam12820    pfam00097   
Domain families : Smart (EMBL)BRCT (SM00292)  RING (SM00184)  
DMDM Disease mutations672
Blocks (Seattle)P38398
PDB (SRS)1JM7    1JNX    1N5O    1OQA    1T15    1T29    1T2U    1T2V    1Y98    2ING    3COJ    3K0H    3K0K    3K15    3K16    3PXA    3PXB    3PXC    3PXD    3PXE    4IFI    4IGK   
PDB (PDBSum)1JM7    1JNX    1N5O    1OQA    1T15    1T29    1T2U    1T2V    1Y98    2ING    3COJ    3K0H    3K0K    3K15    3K16    3PXA    3PXB    3PXC    3PXD    3PXE    4IFI    4IGK   
PDB (IMB)1JM7    1JNX    1N5O    1OQA    1T15    1T29    1T2U    1T2V    1Y98    2ING    3COJ    3K0H    3K0K    3K15    3K16    3PXA    3PXB    3PXC    3PXD    3PXE    4IFI    4IGK   
PDB (RSDB)1JM7    1JNX    1N5O    1OQA    1T15    1T29    1T2U    1T2V    1Y98    2ING    3COJ    3K0H    3K0K    3K15    3K16    3PXA    3PXB    3PXC    3PXD    3PXE    4IFI    4IGK   
Human Protein AtlasENSG00000012048 [gene] [tissue] [antibody] [cell] [cancer]
Peptide AtlasP38398
HPRD00218
IPIIPI00218982   IPI00027277   IPI00909467   IPI00185298   IPI00956512   IPI00930496   IPI01008775   IPI00930098   IPI00930103   IPI00930608   IPI00930528   IPI00946422   IPI00945744   IPI00946923   IPI00945613   IPI00946348   IPI00945705   IPI01014513   IPI00027272   IPI00945236   IPI00946315   IPI00946108   IPI00946665   IPI00947541   IPI00946834   IPI00945166   
Protein Interaction databases
DIP (DOE-UCLA)P38398
IntAct (EBI)P38398
FunCoupENSG00000012048
BioGRIDBRCA1
InParanoidP38398
Interologous Interaction database P38398
IntegromeDBBRCA1
STRING (EMBL)BRCA1
Ontologies - Pathways
Ontology : AmiGOubiquitin ligase complex  double-strand break repair via homologous recombination  double-strand break repair via homologous recombination  ruffle  DNA binding  transcription coactivator activity  RNA binding  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  protein binding  nucleus  nucleoplasm  chromosome  cytoplasm  plasma membrane  focal adhesion  DNA repair  postreplication repair  double-strand break repair  double-strand break repair  regulation of transcription from RNA polymerase II promoter  regulation of transcription from RNA polymerase III promoter  fatty acid biosynthetic process  apoptotic process  cellular response to DNA damage stimulus  DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator  chromosome segregation  zinc ion binding  gamma-tubulin ring complex  intrinsic apoptotic signaling pathway in response to DNA damage  response to ionizing radiation  tubulin binding  protein ubiquitination  ligase activity  enzyme binding  androgen receptor signaling pathway  ribonucleoprotein complex  positive regulation of protein ubiquitination  BRCA1-BARD1 complex  G2 DNA damage checkpoint  ubiquitin protein ligase binding  filamentous actin  substrate adhesion-dependent cell spreading  positive regulation of histone acetylation  regulation of cell proliferation  regulation of apoptotic process  protein complex  response to estrogen  transcription regulatory region DNA binding  negative regulation of fatty acid biosynthetic process  positive regulation of DNA repair  negative regulation of transcription, DNA-templated  positive regulation of transcription, DNA-templated  positive regulation of transcription, DNA-templated  positive regulation of transcription from RNA polymerase II promoter  positive regulation of transcription from RNA polymerase II promoter  negative regulation of centriole replication  androgen receptor binding  positive regulation of histone H3-K4 methylation  negative regulation of histone H3-K9 methylation  protein autoubiquitination  positive regulation of histone H4-K20 methylation  BRCA1-A complex  positive regulation of cell cycle arrest  cellular response to indole-3-methanol  protein K6-linked ubiquitination  regulation of cell motility  positive regulation of histone H3-K9 acetylation  positive regulation of histone H4-K16 acetylation  
Ontology : EGO-EBIubiquitin ligase complex  double-strand break repair via homologous recombination  double-strand break repair via homologous recombination  ruffle  DNA binding  transcription coactivator activity  RNA binding  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  protein binding  nucleus  nucleoplasm  chromosome  cytoplasm  plasma membrane  focal adhesion  DNA repair  postreplication repair  double-strand break repair  double-strand break repair  regulation of transcription from RNA polymerase II promoter  regulation of transcription from RNA polymerase III promoter  fatty acid biosynthetic process  apoptotic process  cellular response to DNA damage stimulus  DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator  chromosome segregation  zinc ion binding  gamma-tubulin ring complex  intrinsic apoptotic signaling pathway in response to DNA damage  response to ionizing radiation  tubulin binding  protein ubiquitination  ligase activity  enzyme binding  androgen receptor signaling pathway  ribonucleoprotein complex  positive regulation of protein ubiquitination  BRCA1-BARD1 complex  G2 DNA damage checkpoint  ubiquitin protein ligase binding  filamentous actin  substrate adhesion-dependent cell spreading  positive regulation of histone acetylation  regulation of cell proliferation  regulation of apoptotic process  protein complex  response to estrogen  transcription regulatory region DNA binding  negative regulation of fatty acid biosynthetic process  positive regulation of DNA repair  negative regulation of transcription, DNA-templated  positive regulation of transcription, DNA-templated  positive regulation of transcription, DNA-templated  positive regulation of transcription from RNA polymerase II promoter  positive regulation of transcription from RNA polymerase II promoter  negative regulation of centriole replication  androgen receptor binding  positive regulation of histone H3-K4 methylation  negative regulation of histone H3-K9 methylation  protein autoubiquitination  positive regulation of histone H4-K20 methylation  BRCA1-A complex  positive regulation of cell cycle arrest  cellular response to indole-3-methanol  protein K6-linked ubiquitination  regulation of cell motility  positive regulation of histone H3-K9 acetylation  positive regulation of histone H4-K16 acetylation  
Pathways : BIOCARTARole of BRCA1, BRCA2 and ATR in Cancer Susceptibility [Genes]    BRCA1-dependent Ub-ligase activity [Genes]    Cell Cycle: G2/M Checkpoint [Genes]    CARM1 and Regulation of the Estrogen Receptor [Genes]    ATM Signaling Pathway [Genes]   
Pathways : KEGGFanconi anemia pathway    Ubiquitin mediated proteolysis    PI3K-Akt signaling pathway    MicroRNAs in cancer   
Protein Interaction DatabaseBRCA1
Wikipedia pathwaysBRCA1
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)BRCA1
snp3D : Map Gene to Disease672
SNP (GeneSNP Utah)BRCA1
SNP : HGBaseBRCA1
Genetic variants : HAPMAPBRCA1
Exome VariantBRCA1
1000_GenomesBRCA1 
ICGC programENSG00000012048 
Cancer Gene: CensusBRCA1 
Somatic Mutations in Cancer : COSMICBRCA1 
CONAN: Copy Number AnalysisBRCA1 
Mutations and Diseases : HGMDBRCA1
Genomic VariantsBRCA1  BRCA1 [DGVbeta]
dbVarBRCA1
ClinVarBRCA1
Pred. of missensesPolyPhen-2  SIFT(SG)  SIFT(JCVI)  Align-GVGD  MutAssessor  Mutanalyser  
Pred. splicesGeneSplicer  Human Splicing Finder  MaxEntScan  
Diseases
OMIM113705    114480    604370    614320   
MedgenBRCA1
GENETestsBRCA1
Disease Genetic AssociationBRCA1
Huge Navigator BRCA1 [HugePedia]  BRCA1 [HugeCancerGEM]
General knowledge
Homologs : HomoloGeneBRCA1
Homology/Alignments : Family Browser (UCSC)BRCA1
Phylogenetic Trees/Animal Genes : TreeFamBRCA1
Chemical/Protein Interactions : CTD672
Chemical/Pharm GKB GenePA25411
Drug Sensitivity BRCA1
Clinical trialBRCA1
Cancer Resource (Charite)ENSG00000012048
Other databases
Other databaseUMD-BRCA1 (breast cancer 1). Curators: E. Rouleau and S. Caputo
Other databasehttp://cancergenome.broadinstitute.org/index.php?tgene=BRCA1
Probes
Litterature
PubMed499 Pubmed reference(s) in Entrez
CoreMineBRCA1
iHOPBRCA1
OncoSearchBRCA1

Bibliography

A strong candidate for the breast and ovarian cancer susceptibility gene BRCA1.
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Transcriptional activation by BRCA1.
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BRCA1 is a component of the RNA polymerase II holoenzyme.
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A CREB site in the BRCA1 proximal promoter acts as a constitutive transcriptional element.
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The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation.
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BRCA1-BARD1 complexes are required for p53Ser-15 phosphorylation and a G1/S arrest following ionizing radiation-induced DNA damage.
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Spectrum of mutations in BRCA1, BRCA2, CHEK2, and TP53 in families at high risk of breast cancer.
Walsh T, Casadei S, Coats KH, Swisher E, Stray SM, Higgins J, Roach KC, Mandell J, Lee MK, Ciernikova S, Foretova L, Soucek P, King MC
JAMA : the journal of the American Medical Association. 2006 ; 295 (12) : 1379-1388.
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Founder mutations in BRCA1 and BRCA2 genes.
Ferla R, Calˆ¾ V, Cascio S, Rinaldi G, Badalamenti G, Carreca I, Surmacz E, Colucci G, Bazan V, Russo A
Annals of oncology : official journal of the European Society for Medical Oncology / ESMO. 2007 ; 18 Suppl 6 : vi93-vi98.
PMID 17591843
 
A mechanism for transcriptional repression dependent on the BRCA1 E3 ubiquitin ligase.
Horwitz AA, Affar el B, Heine GF, Shi Y, Parvin JD
Proceedings of the National Academy of Sciences of the United States of America. 2007 ; 104 (16) : 6614-6619.
PMID 17420471
 
RAD51 up-regulation bypasses BRCA1 function and is a common feature of BRCA1-deficient breast tumors.
Martin RW, Orelli BJ, Yamazoe M, Minn AJ, Takeda S, Bishop DK
Cancer research. 2007 ; 67 (20) : 9658-9665.
PMID 17942895
 
Genetic susceptibility for breast cancer: how many more genes to be found?
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Critical reviews in oncology/hematology. 2007 ; 63 (2) : 125-149.
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Contribution of BRCA1 and BRCA2 mutations to inherited ovarian cancer.
Ramus SJ, Harrington PA, Pye C, DiCioccio RA, Cox MJ, Garlinghouse-Jones K, Oakley-Girvan I, Jacobs IJ, Hardy RM, Whittemore AS, Ponder BA, Piver MS, Pharoah PD, Gayther SA
Human mutation. 2007 ; 28 (12) : 1207-1215.
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Novel complex genomic rearrangement of the BRCA1 gene.
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Written10-2007Sreeparna Banerjee
Department of Biology, Middle East Technical University, Ankara 06531, Turkey

Citation

This paper should be referenced as such :
Banerjee, S
BRCA1 (breast cancer 1, early onset)
Atlas Genet Cytogenet Oncol Haematol. 2008;12(3):197-200.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/BRCA1ID163ch17q21.html

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