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BARD1 (BRCA1 associated RING domain 1)

Identity

Other namesBRCA1-associated RING domain protein 1
HGNC BARD1
Location 2q35
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
  

External links

Nomenclature
HGNCBARD1   952
Entrez_GeneBARD1  580  BRCA1 associated RING domain 1
Cards
AtlasBARD1ID756ch2q35
GeneCardsBARD1
EnsemblBARD1 [Search_View]   ENSG00000138376 [Gene_View]
GenatlasBARD1
GeneLynxBARD1
eGenomeBARD1
euGene580
Genomic and cartography
GoldenPathBARD1  -  2q35   chr2:215301520-215382673 -  2q34-q35   [Description]    (hg18-Mar_2006)
EnsemblBARD1 - 2q34-q35 [CytoView]
NCBIMapview
OMIMDisease map [OMIM]
HomoloGeneBARD1
Gene and transcription
GenbankAK223409 [ ENTREZ ]
GenbankAK301843 [ ENTREZ ]
GenbankAK310759 [ ENTREZ ]
GenbankAK314260 [ ENTREZ ]
GenbankBC126426 [ ENTREZ ]
RefSeqNM_000465 [ SRS ]    NM_000465 [ ENTREZ ]
RefSeqAC_000045 [ SRS ]    AC_000045 [ ENTREZ ]
RefSeqAC_000134 [ SRS ]    AC_000134 [ ENTREZ ]
RefSeqNC_000002 [ SRS ]    NC_000002 [ ENTREZ ]
RefSeqNT_005403 [ SRS ]    NT_005403 [ ENTREZ ]
RefSeqNW_001838863 [ SRS ]    NW_001838863 [ ENTREZ ]
RefSeqNW_921618 [ SRS ]    NW_921618 [ ENTREZ ]
AceViewBARD1 AceView - NCBI
UnigeneHs.591642 [ SRS ]    Hs.591642 [ NCBI ]     HS591642 [ spliceNest ]
Fast-db14898 (alternative variants)
Protein : pattern, domain, 3D structure
SwissProtQ53F80 [ SRS]    Q53F80 [ EXPASY ]     Q53F80 [ INTERPRO ]     Q53F80 [ UNIPROT ]
PrositePS50297 ANK_REP_REGION [ SRS ]    PS50297 ANK_REP_REGION [ Expasy ]
PrositePS50088 ANK_REPEAT [ SRS ]    PS50088 ANK_REPEAT [ Expasy ]
PrositePS50172 BRCT [ SRS ]    PS50172 BRCT [ Expasy ]
PrositePS00518 ZF_RING_1 [ SRS ]    PS00518 ZF_RING_1 [ Expasy ]
PrositePS50089 ZF_RING_2 [ SRS ]    PS50089 ZF_RING_2 [ Expasy ]
InterproIPR002110 ANK [ SRS ]    IPR002110 ANK [ EBI ]
InterproIPR001357 BRCT [ SRS ]    IPR001357 BRCT [ EBI ]
InterproIPR001841 Znf_RING [ SRS ]    IPR001841 Znf_RING [ EBI ]
InterproIPR013083 Znf_RING/FYVE/PHD [ SRS ]    IPR013083 Znf_RING/FYVE/PHD [ EBI ]
CluSTrQ53F80
PfamPF00023 Ank [ SRS ]    PF00023 Ank [ Sanger ]    pfam00023 [ NCBI-CDD ]
PfamPF00533 BRCT [ SRS ]    PF00533 BRCT [ Sanger ]    pfam00533 [ NCBI-CDD ]
SmartSM00248 ANK [EMBL]
SmartSM00292 BRCT [EMBL]
SmartSM00184 RING [EMBL]
BlocksQ53F80
HPRD03354
Protein Interaction databases
DIPQ53F80
IntActQ53F80
Polymorphism : SNP, mutations, diseases
OMIM114480;601593    [ map ]   
GENECLINICS114480;601593
SNPBARD1 [dbSNP-NCBI]  
SNPNM_000465 [SNP-NCI]  
SNPBARD1 [GeneSNPs - Utah]  BARD1] [HGBASE - SRS]
HAPMAPBARD1 [HAPMAP]  
COSMICBARD1 [Somatic mutation (COSMIC-CGP-Sanger)]  
HGMDBARD1
General knowledge
Family BrowserBARD1 [UCSC Family Browser]
SOURCENM_000465
SMDHs.591642
SAGEHs.591642
GOubiquitin ligase complex [Amigo]  ubiquitin ligase complex
GOtissue homeostasis [Amigo]  tissue homeostasis
GORNA binding [Amigo]  RNA binding
GOubiquitin-protein ligase activity [Amigo]  ubiquitin-protein ligase activity
GOprotein binding [Amigo]  protein binding
GOintracellular [Amigo]  intracellular
GOnucleus [Amigo]  nucleus
GOnucleus [Amigo]  nucleus
GOcytoplasm [Amigo]  cytoplasm
GOresponse to DNA damage stimulus [Amigo]  response to DNA damage stimulus
GOcell cycle arrest [Amigo]  cell cycle arrest
GOzinc ion binding [Amigo]  zinc ion binding
GOprotein ubiquitination [Amigo]  protein ubiquitination
GOkinase binding [Amigo]  kinase binding
GOBRCA1-BARD1 complex [Amigo]  BRCA1-BARD1 complex
GOnegative regulation of mRNA 3'-end processing [Amigo]  negative regulation of mRNA 3'-end processing
GOregulation of phosphorylation [Amigo]  regulation of phosphorylation
GOprotein homodimerization activity [Amigo]  protein homodimerization activity
GOpositive regulation of apoptosis [Amigo]  positive regulation of apoptosis
GOnegative regulation of apoptosis [Amigo]  negative regulation of apoptosis
GOpositive regulation of protein catabolic process [Amigo]  positive regulation of protein catabolic process
GOnegative regulation of protein export from nucleus [Amigo]  negative regulation of protein export from nucleus
GOmetal ion binding [Amigo]  metal ion binding
GOprotein heterodimerization activity [Amigo]  protein heterodimerization activity
BIOCARTABRCA1-dependent Ub-ligase activity    [Genes]
PubGeneBARD1
TreeFamBARD1
CTD580 [Comparative ToxicoGenomics Database]
Other databases
Probes
ProbeBARD1 Related clones (RZPD - Berlin)
PubMed
PubMed81 Pubmed reference(s) in LocusLink

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. February 2007 .
URL : http://AtlasGeneticsOncology.org/Genes/BARD1ID756ch2q35.html

© Atlas of Genetics and Cytogenetics in Oncology and Haematology
indexed on : Mon Aug 11 21:12:21 2008


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