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BARD1 (BRCA1 associated RING domain 1)

Identity

Other namesBRCA1-associated RING domain protein 1
HGNC (Hugo) BARD1
LocusID (NCBI) 580
Location 2q35
Location_base_pair Starts at 215590370 and ends at 215674435 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Local_order Antiparallel

DNA/RNA

 
  BARD1 structure is presented with RING finger (green) ankyrin repeats (ANK, blue) and BRCT domains (red). Positions of introns (in) are indicated. Structures of splice variants are shown for BARD1beta from the rat (Feki et al., 2004), BARD1delta (Feki et al., 2005; Tsuzuki et al., 2006).
Description The gene spans 81 kb, composed of 11 exons. Alternatively spliced isoforms are identified.
Insert known isoforms:
BARD1beta (rat testis)
BARD1delta (rat ovarian cancer cells)
BARD1delta (HeLa)
BARD1delta (rat ovarian cancer cells)
Transcription Transcription start is 100 bp upstream of first ATG of the BARD1 ORF. There a two 3¹ends reported and possibly two alternative polyadenylation sites. BARD1 is expressed in most proliferative tissues. Highest expression in testis and spleen. No expression the central nervous system.
Pseudogene No pseudogenes reported.

Protein

 
  Mouse and human BARD1 protein sequences are shown schematically. RING finger domains (gren), Ankyrin repeats (ANK, blue), BRCT domains (red), nulear localization signals (light blue). Homology between human and mouse BARD1 is indicated in perentage of identical amino acids for structural regions.
Description Human BARD1 777 amino acids ; Structural motifs: RING, 5 Ankyrin repeats, 2 BRCT domains
Expression In the mouse BARD1 is expressed in most proliferative tissues. Highest expression in testis and spleen, no expression in nervous system.
During mouse development BARD1 is expressed in early embryogenesis and declines after day 9.
Localisation During S-phase BARD1 localizes to nuclear dots. Partially, BARD1 is also localized to the cytoplasm in response to stress.
Function BARD1 functions as heterodimer with BRCA1 as ubiquitin ligase. Several targets of the BARD1-BRCA1 ubiquitin ligase have been identified and suggest its implication in DNA repair, polyadenylation, cell cycle control, and mitosis.
BARD1 acts as inducer of apoptosis, independently of BRCA1, by binding to p53, and by binding to the stress response kinase DNA-PK, facilitating p53 phosphorylation and stabilization. Thus BARD1 acts as signaling molecule from genotoxic stress towards p53-dependent apoptosis.
Homology BARD1 is homologous to BRCA1, regarding the N-terminal RING finger and the C-terminal BRCT domains. Weak homology between BARD1 and BRCA1 can be found throughout exon 1 to exon 4. and from exon 7 through exon 11, with conserved intron-exon junctions.

Mutations

Note Several mutations of BARD1 have been identified in breast and ovarian cancers. Three mutations have been reported associated with inherited predisposition to breast and ovarian cancer.
 
  BARD1 mutations associated with cancer. Small mutations are not unambiguously identified as cancer causing mutations, long arrows red labeled mutations are accepted as cancer associated. Blue indication maps germ line mutations. Q406R, might be cancer associated.
Germinal Germline mutations were reported for C557S and Q564H.
Somatic Several somatic mutation were reported in addition to C557S and Q564H:

Implicated in

Entity Breast and/or ovarian cancer
Note Upregulated expression of truncated BARD1 in epithelial cancers.
Prognosis Upregulated BARD1 is correlated with poor prognosis in breast and ovarian cancer.
Cytogenetics No determined
Hybrid/Mutated Gene Not determined
Abnormal Protein No fusion proteins reported
  
Entity Ovarian cancer
Prognosis Upregulated BARD1 is correlated with poor prognosis in breast and ovarian cancer.
Hybrid/Mutated Gene No
Abnormal Protein No fusion proteins reported
  
Entity Lung cancer
Prognosis Upregulated BARD1 is correlated with poor prognosis in breast and ovarian cancer.
Hybrid/Mutated Gene No
Abnormal Protein No fusion proteins reported
  

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

Leukemias t0817q24q22ID1494

External links

Nomenclature
HGNC (Hugo)BARD1   952
Cards
AtlasBARD1ID756ch2q35
Entrez_Gene (NCBI)BARD1  580  BRCA1 associated RING domain 1
GeneCards (Weizmann)BARD1
Ensembl (Hinxton)ENSG00000138376 [Gene_View]  chr2:215590370-215674435 [Contig_View]  BARD1 [Vega]
ICGC DataPortalENSG00000138376
cBioPortalBARD1
AceView (NCBI)BARD1
Genatlas (Paris)BARD1
WikiGenes580
SOURCE (Princeton)NM_000465 NM_001282543 NM_001282545 NM_001282548 NM_001282549
Genomic and cartography
GoldenPath (UCSC)BARD1  -  2q35   chr2:215590370-215674435 -  2q34-q35   [Description]    (hg19-Feb_2009)
EnsemblBARD1 - 2q34-q35 [CytoView]
Mapping of homologs : NCBIBARD1 [Mapview]
OMIM114480   601593   
Gene and transcription
Genbank (Entrez)AK223409 AK301843 AK310759 AK314260 AX794378
RefSeq transcript (Entrez)NM_000465 NM_001282543 NM_001282545 NM_001282548 NM_001282549
RefSeq genomic (Entrez)AC_000134 NC_000002 NC_018913 NG_012047 NT_005403 NW_001838863 NW_004929305
Consensus coding sequences : CCDS (NCBI)BARD1
Cluster EST : UnigeneHs.597413 [ NCBI ]
CGAP (NCI)Hs.597413
Alternative Splicing : Fast-db (Paris)GSHG0018325
Alternative Splicing GalleryENSG00000138376
Gene ExpressionBARD1 [ NCBI-GEO ]     BARD1 [ SEEK ]   BARD1 [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ99728 (Uniprot)
NextProtQ99728  [Medical]
With graphics : InterProQ99728
Splice isoforms : SwissVarQ99728 (Swissvar)
Domaine pattern : Prosite (Expaxy)ANK_REP_REGION (PS50297)    ANK_REPEAT (PS50088)    BRCT (PS50172)    ZF_RING_1 (PS00518)    ZF_RING_2 (PS50089)   
Domains : Interpro (EBI)Ankyrin_rpt [organisation]   Ankyrin_rpt-contain_dom [organisation]   BRCT_dom [organisation]   Znf_RING [organisation]   Znf_RING/FYVE/PHD [organisation]   Znf_RING_CS [organisation]  
Related proteins : CluSTrQ99728
Domain families : Pfam (Sanger)Ank (PF00023)    BRCT (PF00533)   
Domain families : Pfam (NCBI)pfam00023    pfam00533   
Domain families : Smart (EMBL)ANK (SM00248)  BRCT (SM00292)  RING (SM00184)  
DMDM Disease mutations580
Blocks (Seattle)Q99728
PDB (SRS)1JM7    2NTE    2R1Z    3C5R    3FA2   
PDB (PDBSum)1JM7    2NTE    2R1Z    3C5R    3FA2   
PDB (IMB)1JM7    2NTE    2R1Z    3C5R    3FA2   
PDB (RSDB)1JM7    2NTE    2R1Z    3C5R    3FA2   
Human Protein AtlasENSG00000138376 [gene] [tissue] [antibody] [cell] [cancer]
Peptide AtlasQ99728
HPRD03354
IPIIPI00017746   IPI00909828   IPI00927763   IPI00925400   IPI00927562   
Protein Interaction databases
DIP (DOE-UCLA)Q99728
IntAct (EBI)Q99728
FunCoupENSG00000138376
BioGRIDBARD1
InParanoidQ99728
Interologous Interaction database Q99728
IntegromeDBBARD1
STRING (EMBL)BARD1
Ontologies - Pathways
Ontology : AmiGOubiquitin ligase complex  tissue homeostasis  RNA binding  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  protein binding  nucleus  nucleus  nucleolus  nucleolus  cytoplasm  DNA repair  cellular response to DNA damage stimulus  cell cycle arrest  zinc ion binding  protein ubiquitination  ligase activity  kinase binding  BRCA1-BARD1 complex  negative regulation of mRNA 3'-end processing  regulation of phosphorylation  protein homodimerization activity  positive regulation of apoptotic process  negative regulation of apoptotic process  intracellular membrane-bounded organelle  positive regulation of protein catabolic process  negative regulation of protein export from nucleus  protein heterodimerization activity  BRCA1-A complex  protein K6-linked ubiquitination  
Ontology : EGO-EBIubiquitin ligase complex  tissue homeostasis  RNA binding  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  protein binding  nucleus  nucleus  nucleolus  nucleolus  cytoplasm  DNA repair  cellular response to DNA damage stimulus  cell cycle arrest  zinc ion binding  protein ubiquitination  ligase activity  kinase binding  BRCA1-BARD1 complex  negative regulation of mRNA 3'-end processing  regulation of phosphorylation  protein homodimerization activity  positive regulation of apoptotic process  negative regulation of apoptotic process  intracellular membrane-bounded organelle  positive regulation of protein catabolic process  negative regulation of protein export from nucleus  protein heterodimerization activity  BRCA1-A complex  protein K6-linked ubiquitination  
Pathways : BIOCARTABRCA1-dependent Ub-ligase activity [Genes]   
Protein Interaction DatabaseBARD1
Wikipedia pathwaysBARD1
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)BARD1
snp3D : Map Gene to Disease580
SNP (GeneSNP Utah)BARD1
SNP : HGBaseBARD1
Genetic variants : HAPMAPBARD1
Exome VariantBARD1
1000_GenomesBARD1 
ICGC programENSG00000138376 
Somatic Mutations in Cancer : COSMICBARD1 
CONAN: Copy Number AnalysisBARD1 
Mutations and Diseases : HGMDBARD1
Genomic VariantsBARD1  BARD1 [DGVbeta]
dbVarBARD1
ClinVarBARD1
Pred. of missensesPolyPhen-2  SIFT(SG)  SIFT(JCVI)  Align-GVGD  MutAssessor  Mutanalyser  
Pred. splicesGeneSplicer  Human Splicing Finder  MaxEntScan  
Diseases
OMIM114480    601593   
MedgenBARD1
GENETestsBARD1
Disease Genetic AssociationBARD1
Huge Navigator BARD1 [HugePedia]  BARD1 [HugeCancerGEM]
General knowledge
Homologs : HomoloGeneBARD1
Homology/Alignments : Family Browser (UCSC)BARD1
Phylogenetic Trees/Animal Genes : TreeFamBARD1
Chemical/Protein Interactions : CTD580
Chemical/Pharm GKB GenePA25256
Clinical trialBARD1
Cancer Resource (Charite)ENSG00000138376
Other databases
Probes
Litterature
PubMed163 Pubmed reference(s) in Entrez
CoreMineBARD1
iHOPBARD1
OncoSearchBARD1

Bibliography

Identification of a RING protein that can interact in vivo with the BRCA1 gene product.
Wu LC, Wang ZW, Tsan JT, Spillman MA, Phung A, Xu XL, Yang MC, Hwang LY, Bowcock AM, Baer R
Nature genetics. 1996 ; 14 (4) : 430-440.
PMID 8944023
 
BRCA1 is a component of the RNA polymerase II holoenzyme.
Scully R, Anderson SF, Chao DM, Wei W, Ye L, Young RA, Livingston DM, Parvin JD
Proceedings of the National Academy of Sciences of the United States of America. 1997 ; 94 (11) : 5605-5610.
PMID 9159119
 
Dynamic changes of BRCA1 subnuclear location and phosphorylation state are initiated by DNA damage.
Scully R, Chen J, Ochs RL, Keegan K, Hoekstra M, Feunteun J, Livingston DM
Cell. 1997 ; 90 (3) : 425-435.
PMID 9267023
 
Conservation of function and primary structure in the BRCA1-associated RING domain (BARD1) protein.
Ayi TC, Tsan JT, Hwang LY, Bowcock AM, Baer R
Oncogene. 1998 ; 17 (16) : 2143-2148.
PMID 9798686
 
Stable interaction between the products of the BRCA1 and BRCA2 tumor suppressor genes in mitotic and meiotic cells.
Chen J, Silver DP, Walpita D, Cantor SB, Gazdar AF, Tomlinson G, Couch FJ, Weber BL, Ashley T, Livingston DM, Scully R
Molecular cell. 1998 ; 2 (3) : 317-328.
PMID 9774970
 
In vitro repression of Brca1-associated RING domain gene, Bard1, induces phenotypic changes in mammary epithelial cells.
Irminger-Finger I, Soriano JV, Vaudan G, Montesano R, Sappino AP
The Journal of cell biology. 1998 ; 143 (5) : 1329-1339.
PMID 9832560
 
Mutations in the BRCA1-associated RING domain (BARD1) gene in primary breast, ovarian and uterine cancers.
Thai TH, Du F, Tsan JT, Jin Y, Phung A, Spillman MA, Massa HF, Muller CY, Ashfaq R, Mathis JM, Miller DS, Trask BJ, Baer R, Bowcock AM
Human molecular genetics. 1998 ; 7 (2) : 195-202.
PMID 9425226
 
The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators.
Dechend R, Hirano F, Lehmann K, Heissmeyer V, Ansieau S, Wulczyn FG, Scheidereit C, Leutz A
Oncogene. 1999 ; 18 (22) : 3316-3323.
PMID 10362352
 
Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50.
Kleiman FE, Manley JL
Science (New York, N.Y.). 1999 ; 285 (5433) : 1576-1579.
PMID 10477523
 
Identification of an apoptotic cleavage product of BARD1 as an autoantigen: a potential factor in the antitumoral response mediated by apoptotic bodies.
Gautier F, Irminger-Finger I, Grˆ©goire M, Meflah K, Harb J
Cancer research. 2000 ; 60 (24) : 6895-6900.
PMID 11156388
 
Structure of a BRCA1-BARD1 heterodimeric RING-RING complex.
Brzovic PS, Rajagopal P, Hoyt DW, King MC, Klevit RE
Nature structural biology. 2001 ; 8 (10) : 833-837.
PMID 11573085
 
The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation.
Hashizume R, Fukuda M, Maeda I, Nishikawa H, Oyake D, Yabuki Y, Ogata H, Ohta T
The Journal of biological chemistry. 2001 ; 276 (18) : 14537-14540.
PMID 11278247
 
The BARD1-CstF-50 interaction links mRNA 3' end formation to DNA damage and tumor suppression.
Kleiman FE, Manley JL
Cell. 2001 ; 104 (5) : 743-753.
PMID 11257228
 
Identification of BARD1 as mediator between proapoptotic stress and p53-dependent apoptosis.
Irminger-Finger I, Leung WC, Li J, Dubois-Dauphin M, Harb J, Feki A, Jefford CE, Soriano JV, Jaconi M, Montesano R, Krause KH
Molecular cell. 2001 ; 8 (6) : 1255-1266.
PMID 11779501
 
Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase.
Chen A, Kleiman FE, Manley JL, Ouchi T, Pan ZQ
The Journal of biological chemistry. 2002 ; 277 (24) : 22085-22092.
PMID 11927591
 
The BRCA1 and BARD1 association with the RNA polymerase II holoenzyme.
Chiba N, Parvin JD
Cancer research. 2002 ; 62 (15) : 4222-4228.
PMID 12154023
 
BARD1 induces BRCA1 intranuclear foci formation by increasing RING-dependent BRCA1 nuclear import and inhibiting BRCA1 nuclear export.
Fabbro M, Rodriguez JA, Baer R, Henderson BR
The Journal of biological chemistry. 2002 ; 277 (24) : 21315-21324.
PMID 11925436
 
Germline mutations of the BRCA1-associated ring domain (BARD1) gene in breast and breast/ovarian families negative for BRCA1 and BRCA2 alterations.
Ghimenti C, Sensi E, Presciuttini S, Brunetti IM, Conte P, Bevilacqua G, Caligo MA
Genes, chromosomes & cancer. 2002 ; 33 (3) : 235-242.
PMID 11807980
 
BRCA1-dependent and independent functions of BARD1.
Irminger-Finger I, Leung WC
The international journal of biochemistry & cell biology. 2002 ; 34 (6) : 582-587.
PMID 11943588
 
Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains.
Mallery DL, Vandenberg CJ, Hiom K
The EMBO journal. 2002 ; 21 (24) : 6755-6762.
PMID 12485996
 
Identification of residues required for the interaction of BARD1 with BRCA1.
Morris JR, Keep NH, Solomon E
The Journal of biological chemistry. 2002 ; 277 (11) : 9382-9386.
PMID 11773071
 
E2F integrates cell cycle progression with DNA repair, replication, and G(2)/M checkpoints.
Ren B, Cam H, Takahashi Y, Volkert T, Terragni J, Young RA, Dynlacht BD
Genes & development. 2002 ; 16 (2) : 245-256.
PMID 11799067
 
Interaction of the EWS NH2 terminus with BARD1 links the Ewing's sarcoma gene to a common tumor suppressor pathway.
Spahn L, Petermann R, Siligan C, Schmid JA, Aryee DN, Kovar H
Cancer research. 2002 ; 62 (16) : 4583-4587.
PMID 12183411
 
Mutational analysis of BARD1 in familial breast cancer patients in Japan.
Ishitobi M, Miyoshi Y, Hasegawa S, Egawa C, Tamaki Y, Monden M, Noguchi S
Cancer letters. 2003 ; 200 (1) : 1-7.
PMID 14550946
 
Loss of Bard1, the heterodimeric partner of the Brca1 tumor suppressor, results in early embryonic lethality and chromosomal instability.
McCarthy EE, Celebi JT, Baer R, Ludwig T
Molecular and cellular biology. 2003 ; 23 (14) : 5056-5063.
PMID 12832489
 
BARD1 participates with BRCA1 in homology-directed repair of chromosome breaks.
Westermark UK, Reyngold M, Olshen AB, Baer R, Jasin M, Moynahan ME
Molecular and cellular biology. 2003 ; 23 (21) : 7926-7936.
PMID 14560035
 
Ubiquitination and proteasomal degradation of the BRCA1 tumor suppressor is regulated during cell cycle progression.
Choudhury AD, Xu H, Baer R
The Journal of biological chemistry. 2004 ; 279 (32) : 33909-33918.
PMID 15166217
 
BRCA1-BARD1 complexes are required for p53Ser-15 phosphorylation and a G1/S arrest following ionizing radiation-induced DNA damage.
Fabbro M, Savage K, Hobson K, Deans AJ, Powell SN, McArthur GA, Khanna KK
The Journal of biological chemistry. 2004 ; 279 (30) : 31251-31258.
PMID 15159397
 
BARD1 regulates BRCA1 apoptotic function by a mechanism involving nuclear retention.
Fabbro M, Schuechner S, Au WW, Henderson BR
Experimental cell research. 2004 ; 298 (2) : 661-673.
PMID 15265711
 
BARD1 expression during spermatogenesis is associated with apoptosis and hormonally regulated.
Feki A, Jefford CE, Durand P, Harb J, Lucas H, Krause KH, Irminger-Finger I
Biology of reproduction. 2004 ; 71 (5) : 1614-1624.
PMID 15240424
 
Nuclear-cytoplasmic translocation of BARD1 is linked to its apoptotic activity.
Jefford CE, Feki A, Harb J, Krause KH, Irminger-Finger I
Oncogene. 2004 ; 23 (20) : 3509-3520.
PMID 15077185
 
Mutation screening of the BARD1 gene: evidence for involvement of the Cys557Ser allele in hereditary susceptibility to breast cancer.
Karppinen SM, Heikkinen K, Rapakko K, Winqvist R
Journal of medical genetics. 2004 ; 41 (9) : page e114.
PMID 15342711
 
BRCA1 : BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair.
Morris JR, Solomon E
Human molecular genetics. 2004 ; 13 (8) : 807-817.
PMID 14976165
 
Nuclear-cytoplasmic shuttling of BARD1 contributes to its proapoptotic activity and is regulated by dimerization with BRCA1.
Rodriguez JA, Schˆºchner S, Au WW, Fabbro M, Henderson BR
Oncogene. 2004 ; 23 (10) : 1809-1820.
PMID 14647430
 
Nucleophosmin/B23 is a candidate substrate for the BRCA1-BARD1 ubiquitin ligase.
Sato K, Hayami R, Wu W, Nishikawa T, Nishikawa H, Okuda Y, Ogata H, Fukuda M, Ohta T
The Journal of biological chemistry. 2004 ; 279 (30) : 30919-30922.
PMID 15184379
 
BRCA1-dependent ubiquitination of gamma-tubulin regulates centrosome number.
Starita LM, Machida Y, Sankaran S, Elias JE, Griffin K, Schlegel BP, Gygi SP, Parvin JD
Molecular and cellular biology. 2004 ; 24 (19) : 8457-8466.
PMID 15367667
 
Genetic steps of mammalian homologous repair with distinct mutagenic consequences.
Stark JM, Pierce AJ, Oh J, Pastink A, Jasin M
Molecular and cellular biology. 2004 ; 24 (21) : 9305-9316.
PMID 15485900
 
Hyperphosphorylation of the BARD1 tumor suppressor in mitotic cells.
Choudhury AD, Xu H, Modi AP, Zhang W, Ludwig T, Baer R
The Journal of biological chemistry. 2005 ; 280 (26) : 24669-24679.
PMID 15855157
 
BARD1 induces apoptosis by catalysing phosphorylation of p53 by DNA-damage response kinase.
Feki A, Jefford CE, Berardi P, Wu JY, Cartier L, Krause KH, Irminger-Finger I
Oncogene. 2005 ; 24 (23) : 3726-3736.
PMID 15782130
 
Role of nucleophosmin in embryonic development and tumorigenesis.
Grisendi S, Bernardi R, Rossi M, Cheng K, Khandker L, Manova K, Pandolfi PP
Nature. 2005 ; 437 (7055) : 147-153.
PMID 16007073
 
Down-regulation of BRCA1-BARD1 ubiquitin ligase by CDK2.
Hayami R, Sato K, Wu W, Nishikawa T, Hiroi J, Ohtani-Kaneko R, Fukuda M, Ohta T
Cancer research. 2005 ; 65 (1) : 6-10.
PMID 15665273
 
BRCA1/BARD1 inhibition of mRNA 3' processing involves targeted degradation of RNA polymerase II.
Kleiman FE, Wu-Baer F, Fonseca D, Kaneko S, Baer R, Manley JL
Genes & development. 2005 ; 19 (10) : 1227-1237.
PMID 15905410
 
Nuclear targeting and cell cycle regulatory function of human BARD1.
Schˆºchner S, Tembe V, Rodriguez JA, Henderson BR
The Journal of biological chemistry. 2005 ; 280 (10) : 8855-8861.
PMID 15632137
 
BRCA1/BARD1 ubiquitinate phosphorylated RNA polymerase II.
Starita LM, Horwitz AA, Keogh MC, Ishioka C, Parvin JD, Chiba N
The Journal of biological chemistry. 2005 ; 280 (26) : 24498-24505.
PMID 15886201
 
BARD1 content correlates with increased DNA fragmentation associated with muscle wasting in tumour-bearing rats.
Irminger-Finger I, Busquets S, Calabrio F, Lˆ„pez-Soriano FJ, Argilˆ©s JM
Oncology reports. 2006 ; 15 (6) : 1425-1428.
PMID 16685375
 
Is there more to BARD1 than BRCA1?
Irminger-Finger I, Jefford CE
Nature reviews. Cancer. 2006 ; 6 (5) : 382-391.
PMID 16633366
 
The BRCA1/BARD1 heterodimer modulates ran-dependent mitotic spindle assembly.
Joukov V, Groen AC, Prokhorova T, Gerson R, White E, Rodriguez A, Walter JC, Livingston DM
Cell. 2006 ; 127 (3) : 539-552.
PMID 17081976
 
Nordic collaborative study of the BARD1 Cys557Ser allele in 3956 patients with cancer: enrichment in familial BRCA1/BRCA2 mutation-negative breast cancer but not in other malignancies.
Karppinen SM, Barkardottir RB, Backenhorn K, Sydenham T, Syrjˆ§koski K, Schleutker J, Ikonen T, Pylkˆ§s K, Rapakko K, Erkko H, Johannesdottir G, Gerdes AM, Thomassen M, Agnarsson BA, Grip M, Kallioniemi A, Kere J, Aaltonen LA, Arason A, Mˆ½ller P, Kruse TA, Borg A, Winqvist R
Journal of medical genetics. 2006 ; 43 (11) : 856-862.
PMID 16825437
 
The BARD1 Cys557Ser variant and breast cancer risk in Iceland.
Stacey SN, Sulem P, Johannsson OT, Helgason A, Gudmundsson J, Kostic JP, Kristjansson K, Jonsdottir T, Sigurdsson H, Hrafnkelsson J, Johannsson J, Sveinsson T, Myrdal G, Grimsson HN, Bergthorsson JT, Amundadottir LT, Gulcher JR, Thorsteinsdottir U, Kong A, Stefansson K
PLoS medicine. 2006 ; 3 (7) : page e217.
PMID 16768547
 
A truncated splice variant of human BARD1 that lacks the RING finger and ankyrin repeats.
Tsuzuki M, Wu W, Nishikawa H, Hayami R, Oyake D, Yabuki Y, Fukuda M, Ohta T
Cancer letters. 2006 ; 233 (1) : 108-116.
PMID 15878232
 
BARD1 variants Cys557Ser and Val507Met in breast cancer predisposition.
Vahteristo P, Syrjˆ§koski K, Heikkinen T, Eerola H, Aittomˆ§ki K, von Smitten K, Holli K, Blomqvist C, Kallioniemi OP, Nevanlinna H
European journal of human genetics : EJHG. 2006 ; 14 (2) : 167-172.
PMID 16333312
 
Aberrant expression of BARD1 in breast and ovarian cancers with poor prognosis.
Wu JY, Vlastos AT, Pelte MF, Caligo MA, Bianco A, Krause KH, Laurent GJ, Irminger-Finger I
International journal of cancer. Journal international du cancer. 2006 ; 118 (5) : 1215-1226.
PMID 16152612
 
Ubiquitination and proteasome-mediated degradation of BRCA1 and BARD1 during steroidogenesis in human ovarian granulosa cells.
Lu Y, Amleh A, Sun J, Jin X, McCullough SD, Baer R, Ren D, Li R, Hu Y
Molecular endocrinology (Baltimore, Md.). 2007 ; 21 (3) : 651-663.
PMID 17185394
 
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Contributor(s)

Written02-2007Irmgard Irminger-Finger
Biology of Aging Laboratory, Dept of Geriatrics and Dept of Gynecology and Obstetrics, Geneva University and University Hospitals, 30, Bloulevard de la Cluse, CH-1211 Geneva, Switzerland

Citation

This paper should be referenced as such :
Irminger-Finger, I
BARD1 (BRCA1 associated RING domain 1)
Atlas Genet Cytogenet Oncol Haematol. 2007;11(3):173-176.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/BARD1ID756ch2q35.html

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indexed on : Sat Jul 26 14:59:08 CEST 2014

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