Welcome! Click here to login or here to register.
Home
Proteins
DNA damage
Diseases
Homologs
Pathways
Keywords
Publications
Draw a picture
 
Search
 
Links
Help
Contact





Bujnicki Lab Homepage

BRCA1

Protein FULL name:

breast cancer 1, early onset isoform 1 [Homo sapiens].


BRCA1 (Homo sapiens) is product of expression of BRCA1 gene.

Human diseases related to this protein:

BRCA1 is involved in:

DDS in Homo sapiens
     
HRR in Homo sapiens
     





FUNCTION: E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The E3 ubiquitin-protein ligase activity is required for its tumor suppressor function. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for normal cell cycle progression from G2 to mitosis. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation.

ENZYME REGULATION: The E3 ubiquitin-protein ligase activity is inhibited by phosphorylation by STK6/AURKA. Activity is increased by phosphatase treatment.

PATHWAY: Protein modification; protein ubiquitination.

SUBUNIT: Heterodimer with BARD1. Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBN protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1/RAP80, FAM175A/Abraxas, BRCC3/BRCC36, BRE/BRCC45 and MERIT40/NBA1. Interacts (via BRCT domains) with FAM175A/Abraxas and RBBP8. Associates with RNA polymerase II holoenzyme. Interacts with SMC1A and COBRA1/NELFB. Interacts (via BRCT domains) with phosphorylated BRIP1. Interacts with FANCD2 (ubiquitinated). Interacts with BAP1. Interacts with DCLRE1C/Artemis and CLSPN. Interacts with H2AFX (phosphorylated on 'Ser-140'). Interacts with CHEK1/CHK1. Interacts with BRCC3. Interacts (via BRCT domains) with ACACA (phosphorylated); the interaction prevents dephosphorylation of ACACA. Interacts with STK6/AURKA. Interacts with UBXN1.

INTERACTION: Self; NbExp=1; IntAct=EBI-349905, EBI-349905; Q13085:ACACA; NbExp=2; IntAct=EBI-349905, EBI-717681; O14867:BACH1; NbExp=1; IntAct=EBI-349905, EBI-1263541; Q92560:BAP1; NbExp=1; IntAct=EBI-349905, EBI-1791447; Q92560:BAP1; NbExp=1; IntAct=EBI-2015072, EBI-1791447; Q99PU7:Bap1 (xeno); NbExp=2; IntAct=EBI-349905, EBI-1791471; Q99728:BARD1; NbExp=5; IntAct=EBI-349905, EBI-473181; Q7Z569:BRAP; NbExp=1; IntAct=EBI-349905, EBI-349900; P24385:CCND1; NbExp=2; IntAct=EBI-349905, EBI-375001; P24864:CCNE1; NbExp=2; IntAct=EBI-349905, EBI-519526; O14757:CHEK1; NbExp=1; IntAct=EBI-349905, EBI-974488; Q8WX92:COBRA1; NbExp=3; IntAct=EBI-349905, EBI-347721; P03372:ESR1; NbExp=4; IntAct=EBI-349905, EBI-78473; Q6UWZ7:FAM175A; NbExp=4; IntAct=EBI-349905, EBI-1263451; P16104:H2AFX; NbExp=1; IntAct=EBI-349905, EBI-494830; P52292:KPNA2; NbExp=1; IntAct=EBI-349905, EBI-349938; Q14676:MDC1; NbExp=1; IntAct=EBI-349905, EBI-495644; P16333:NCK1; NbExp=1; IntAct=EBI-349905, EBI-389883; Q9UBD5:ORC3L; NbExp=1; IntAct=EBI-349905, EBI-374916; P27986:PIK3R1; NbExp=1; IntAct=EBI-349905, EBI-79464; P62136:PPP1CA; NbExp=2; IntAct=EBI-349905, EBI-357253; P62140:PPP1CB; NbExp=2; IntAct=EBI-349905, EBI-352350; P36873:PPP1CC; NbExp=2; IntAct=EBI-349905, EBI-356283; Q99708:RBBP8; NbExp=5; IntAct=EBI-349905, EBI-1263531; Q14683:SMC1A; NbExp=1; IntAct=EBI-349905, EBI-80690; Q12888:TP53BP1; NbExp=1; IntAct=EBI-349905, EBI-396540; Q9Y4A5:TRRAP; NbExp=2; IntAct=EBI-349905, EBI-399128; Q96RL1:UIMC1; NbExp=4; IntAct=EBI-349905, EBI-725300; Q6NZY4:ZCCHC8; NbExp=2; IntAct=EBI-349905, EBI-1263058; Q9GZX5:ZNF350; NbExp=2; IntAct=EBI-349905, EBI-396421;

SUBCELLULAR LOCATION: Nucleus. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex.

SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.

SUBCELLULAR LOCATION: Isoform 5: Cytoplasm.

TISSUE SPECIFICITY: Isoform 1 and isoform 3 are widely expressed. Isoform 3 is reduced or absent in several breast and ovarian cancer cell lines.

DOMAIN: The BRCT domains recognize and bind phosphorylated pSXXF motif on proteins. The interaction with the phosphorylated pSXXF motif of FAM175A/Abraxas, recruits BRCA1 at DNA damage sites.

DOMAIN: The RING-type zinc finger domain interacts with BAP1.

PTM: Phosphorylation at Ser-308 by STK6/AURKA is required for normal cell cycle progression from G2 to mitosis. Phosphorylated in response to IR, UV, and various stimuli that cause checkpoint activation, probably by ATM or ATR.

PTM: Autoubiquitinated, undergoes 'Lys-6'-linked polyubiquitination. 'Lys-6'-linked polyubiquitination does not promote degradation.

POLYMORPHISM: There is evidence that the presence of the rare form of Gln-356-Arg and Leu-871-Pro polymorphisms may be associated with an increased risk for developing ovarian cancer.

DISEASE: Defects in BRCA1 are a cause of susceptibility to breast cancer (BC) [MIM:114480]. A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. Note=Mutations in BRCA1 are thought to be responsible for 45% of inherited breast cancer. Moreover, BRCA1 carriers have a 4-fold increased risk of colon cancer, whereas male carriers face a 3-fold increased risk of prostate cancer. Cells lacking BRCA1 show defects in DNA repair by homologous recombination.

DISEASE: Defects in BRCA1 are a cause of susceptibility to breast- ovarian cancer familial type 1 (BROVCA1) [MIM:604370]. A condition associated with familial predisposition to cancer of the breast and ovaries. Characteristic features in affected families are an early age of onset of breast cancer (often before age 50), increased chance of bilateral cancers (cancer that develop in both breasts, or both ovaries, independently), frequent occurrence of breast cancer among men, increased incidence of tumors of other specific organs, such as the prostate. Note=Mutations in BRCA1 are thought to be responsible for more than 80% of inherited breast- ovarian cancer.

DISEASE: Defects in BRCA1 are a cause of genetic susceptibility to ovarian cancer [MIM:113705].

SIMILARITY: Contains 2 BRCT domains.

SIMILARITY: Contains 1 RING-type zinc finger.

WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; [LINK]

WEB RESOURCE: Name=GeneReviews; [LINK]

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]

WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and polymorphism database; [LINK]

WEB RESOURCE: Name=Wikipedia; Note=BRCA1 entry; [LINK]


NCBI GenPept GI number(s): 6552301
6552299
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P38398 P38398
PFAM: - P38398 (Link - using uniprot id)
InterPro: - P38398 (Link - using uniprot id)
CATH: None  
SCOP: None  
PDB: - -


Protein sequence:
MDLSALRVEEVQNVINAMQKILECPICLELIKEPVSTKCDHIFCKFCMLK
LLNQKKGPSQCPLCKNDITKRSLQESTRFSQLVEELLKIICAFQLDTGLE
YANSYNFAKKENNSPEHLKDEVSIIQSMGYRNRAKRLLQSEPENPSLQET
SLSVQLSNLGTVRTLRTKQRIQPQKTSVYIELGSDSSEDTVNKATYCSVG
DQELLQITPQGTRDEISLDSAKKAACEFSETDVTNTEHHQPSNNDLNTTE
KRAAERHPEKYQGSSVSNLHVEPCGTNTHASSLQHENSSLLLTKDRMNVE
KAEFCNKSKQPGLARSQHNRWAGSKETCNDRRTPSTEKKVDLNADPLCER
KEWNKQKLPCSENPRDTEDVPWITLNSSIQKVNEWFSRSDELLGSDDSHD
GESESNAKVADVLDVLNEVDEYSGSSEKIDLLASDPHEALICKSERVHSK
SVESNIEDKIFGKTYRKKASLPNLSHVTENLIIGAFVTEPQIIQERPLTN
KLKRKRRPTSGLHPEDFIKKADLAVQKTPEMINQGTNQTEQNGQVMNITN
SGHENKTKGDSIQNEKNPNPIESLEKESAFKTKAEPISSSISNMELELNI
HNSKAPKKNRLRRKSSTRHIHALELVVSRNLSPPNCTELQIDSCSSSEEI
KKKKYNQMPVRHSRNLQLMEGKEPATGAKKSNKPNEQTSKRHDSDTFPEL
KLTNAPGSFTKCSNTSELKEFVNPSLPREEKEEKLETVKVSNNAEDPKDL
MLSGERVLQTERSVESSSISLVPGTDYGTQESISLLEVSTLGKAKTEPNK
CVSQCAAFENPKGLIHGCSKDNRNDTEGFKYPLGHEVNHSRETSIEMEES
ELDAQYLQNTFKVSKRQSFAPFSNPGNAEEECATFSAHSGSLKKQSPKVT
FECEQKEENQGKNESNIKPVQTVNITAGFPVVGQKDKPVDNAKCSIKGGS
RFCLSSQFRGNETGLITPNKHGLLQNPYRIPPLFPIKSFVKTKCKKNLLE
ENFEEHSMSPEREMGNENIPSTVSTISRNNIRENVFKEASSSNINEVGSS
TNEVGSSINEIGSSDENIQAELGRNRGPKLNAMLRLGVLQPEVYKQSLPG
SNCKHPEIKKQEYEEVVQTVNTDFSPYLISDNLEQPMGSSHASQVCSETP
DDLLDDGEIKEDTSFAENDIKESSAVFSKSVQKGELSRSPSPFTHTHLAQ
GYRRGAKKLESSEENLSSEDEELPCFQHLLFGKVNNIPSQSTRHSTVATE
CLSKNTEENLLSLKNSLNDCSNQVILAKASQEHHLSEETKCSASLFSSQC
SELEDLTANTNTQDPFLIGSSKQMRHQSESQGVGLSDKELVSDDEERGTG
LEENNQEEQSMDSNLGEAASGCESETSVSEDCSGLSSQSDILTTQQRDTM
QHNLIKLQQEMAELEAVLEQHGSQPSNSYPSIISDSSALEDLRNPEQSTS
EKAVLTSQKSSEYPISQNPEGLSADKFEVSADSSTSKNKEPGVERSSPSK
CPSLDDRWYMHSCSGSLQNRNYPSQEELIKVVDVEEQQLEESGPHDLTET
SYLPRQDLEGTPYLESGISLFSDDPESDPSEDRAPESARVGNIPSSTSAL
KVPQLKVAESAQSPAAAHTTDTAGYNAMEESVSREKPELTASTERVNKRM
SMVVSGLTPEEFMLVYKFARKHHITLTNLITEETTHVVMKTDAEFVCERT
LKYFLGIAGGKWVVSYFWVTQSIKERKMLNEHDFEVRGDVVNGRNHQGPK
RARESQDRKIFRGLEICCYGPFTNMPTDQLEWMVQLCGASVVKELSSFTL
GTGVHPIVVVQPDAWTEDNGFHAIGQMCEAPVVTREWVLDSVALYQCQEL
DTYLIPQIPHSHY

BRCA1 (Homo sapiens) is able to recognize following damages:
References:

Title Authors Journal
A strong candidate for the breast and ovarian cancer susceptibility gene BRCA1. Miki Y, Swensen J, Shattuck-Eidens D, Futreal PA, Harshman K, Tavtigian S, Liu Q, Cochran C, Bennett LM, Ding W, et al. Science Oct. 7, 1994
BRCA1 mutations in primary breast and ovarian carcinomas. Futreal PA, Liu Q, Shattuck-Eidens D, Cochran C, Harshman K, Tavtigian S, Bennett LM, Haugen-Strano A, Swensen J, Miki Y, et al. Science Oct. 7, 1994
Mutations in the BRCA1 gene in families with early-onset breast and ovarian cancer. Castilla LH, Couch FJ, Erdos MR, Hoskins KF, Calzone K, Garber JE, Boyd J, Lubin MB, Deshano ML, Brody LC, et al. Nat Genet Dec. 1, 1994
Confirmation of BRCA1 by analysis of germline mutations linked to breast and ovarian cancer in ten families. Friedman LS, Ostermeyer EA, Szabo CI, Dowd P, Lynch ED, Rowell SE, King MC Nat Genet Dec. 1, 1994
Mutations and polymorphisms in the familial early-onset breast cancer (BRCA1) gene. Breast Cancer Information Core. Couch FJ, Weber BL Hum Mutat Jan. 1, 1996
BRCA1 R841W: a strong candidate for a common mutation with moderate phenotype. Barker DF, Almeida ER, Casey G, Fain PR, Liao SY, Masunaka I, Noble B, Kurosaki T, Anton-Culver H Genet Epidemiol Jan. 1, 1996
Mutations in the BRCA1 gene in Japanese breast cancer patients. Katagiri T, Emi M, Ito I, Kobayashi K, Yoshimoto M, Iwase T, Kasumi F, Miki Y, Skolnick MH, Nakamura Y Hum Mutat Jan. 1, 1996
A high incidence of BRCA1 mutations in 20 breast-ovarian cancer families. Serova O, Montagna M, Torchard D, Narod SA, Tonin P, Sylla B, Lynch HT, Feunteun J, Lenoir GM Am J Hum Genet Feb. 1, 1996
Comparison of BRCA1 polymorphisms, rare sequence variants and/or missense mutations in unaffected and breast/ovarian cancer populations. Durocher F, Shattuck-Eidens D, McClure M, Labrie F, Skolnick MH, Goldgar DE, Simard J Hum Mol Genet June 1, 1996
Complete genomic sequence and analysis of 117 kb of human DNA containing the gene BRCA1. Smith TM, Lee MK, Szabo CI, Jerome N, McEuen M, Taylor M, Hood L, King MC Genome Res Nov. 1, 1996
Localization of BRCA1 and a splice variant identifies the nuclear localization signal. Thakur S, Zhang HB, Peng Y, Le H, Carroll B, Ward T, Yao J, Farid LM, Couch FJ, Wilson RB, Weber BL Mol Cell Biol Feb. 1, 1997
Differential subcellular localization, expression and biological toxicity of BRCA1 and the splice variant BRCA1-delta11b. Wilson CA, Payton MN, Elliott GS, Buaas FW, Cajulis EE, Grosshans D, Ramos L, Reese DM, Slamon DJ, Calzone FJ Oncogene Feb. 9, 1997
Constant denaturant gel electrophoresis (CDGE) in BRCA1 mutation screening. Andersen TI, Eiken HG, Couch F, Kaada G, Skrede M, Johnsen H, Aloysius TA, Tveit KM, Tranebjaerg L, Dorum A, Moller P, Weber BL, Borresen-Dale AL Hum Mutat Jan. 1, 1998
High proportion of missense mutations of the BRCA1 and BRCA2 genes in Japanese breast cancer families. Katagiri T, Kasumi F, Yoshimoto M, Nomizu T, Asaishi K, Abe R, Tsuchiya A, Sugano M, Takai S, Yoneda M, Fukutomi T, Nanba K, Makita M, Okazaki H, Hirata K, Okazaki M, Furutsuma Y, Morishita Y, Iino Y, Karino T, Ayabe H, Hara S, Kajiwara T, Houga S, Miki Y, et al. J Hum Genet Jan. 1, 1998
BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression. Jensen DE, Proctor M, Marquis ST, Gardner HP, Ha SI, Chodosh LA, Ishov AM, Tommerup N, Vissing H, Sekido Y, Minna J, Borodovsky A, Schultz DC, Wilkinson KD, Maul GG, Barlev N, Berger SL, Prendergast GC, Rauscher FJ 3rd Oncogene March 5, 1998
A high proportion of mutations in the BRCA1 gene in German breast/ovarian cancer families with clustering of mutations in the 3' third of the gene. Dong J, Chang-Claude J, Wu Y, Schumacher V, Debatin I, Tonin P, Royer-Pokora B Hum Genet Aug. 1, 1998
Characterization of a carboxy-terminal BRCA1 interacting protein. Wong AK, Ormonde PA, Pero R, Chen Y, Lian L, Salada G, Berry S, Lawrence Q, Dayananth P, Ha P, Tavtigian SV, Teng DH, Bartel PL Oncogene Nov. 5, 1998
Molecular characterization of germline mutations in the BRCA1 and BRCA2 genes from breast cancer families in Taiwan. Li SS, Tseng HM, Yang TP, Liu CH, Teng SJ, Huang HW, Chen LM, Kao HW, Chen JH, Tseng JN, Chen A, Hou MF, Huang TJ, Chang HT, Mok KT, Tsai JH Hum Genet March 1, 1999
Germline BRCA1 alterations in a population-based series of ovarian cancer cases. Janezic SA, Ziogas A, Krumroy LM, Krasner M, Plummer SJ, Cohen P, Gildea M, Barker D, Haile R, Casey G, Anton-Culver H Hum Mol Genet May 1, 1999
RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination. Lorick KL, Jensen JP, Fang S, Ong AM, Hatakeyama S, Weissman AM Proc Natl Acad Sci U S A Sept. 28, 1999
The contribution of germline BRCA1 and BRCA2 mutations to familial ovarian cancer: no evidence for other ovarian cancer-susceptibility genes. Gayther SA, Russell P, Harrington P, Antoniou AC, Easton DF, Ponder BA Am J Hum Genet Oct. 1, 1999
BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures. Wang Y, Cortez D, Yazdi P, Neff N, Elledge SJ, Qin J Genes Dev April 15, 2000
Initiation of translation from a downstream in-frame AUG codon on BRCA1 can generate the novel isoform protein DeltaBRCA1(17aa). Liu J, Prolla G, Rostagno A, Chiarle R, Feiner H, Inghirami G Oncogene May 25, 2000
Functional interactions between BRCA1 and the checkpoint kinase ATR during genotoxic stress. Tibbetts RS, Cortez D, Brumbaugh KM, Scully R, Livingston D, Elledge SJ, Abraham RT Genes Dev Dec. 1, 2000
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 Jan. 1, 2001
BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function. Cantor SB, Bell DW, Ganesan S, Kass EM, Drapkin R, Grossman S, Wahrer DC, Sgroi DC, Lane WS, Haber DA, Livingston DM Cell April 6, 2001
Structure of a BRCA1-BARD1 heterodimeric RING-RING complex. Brzovic PS, Rajagopal P, Hoyt DW, King MC, Klevit RE Nat Struct Biol Oct. 1, 2001
Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1. Williams RS, Green R, Glover JN Nat Struct Biol Oct. 1, 2001
BRCA1-induced large-scale chromatin unfolding and allele-specific effects of cancer-predisposing mutations. Ye Q, Hu YF, Zhong H, Nye AC, Belmont AS, Li R J Cell Biol Dec. 10, 2001
Characterization of common BRCA1 and BRCA2 variants. Deffenbaugh AM, Frank TS, Hoffman M, Cannon-Albright L, Neuhausen SL Genet Test Jan. 1, 2002
SMC1 is a downstream effector in the ATM/NBS1 branch of the human S-phase checkpoint. Yazdi PT, Wang Y, Zhao S, Patel N, Lee EY, Qin J Genes Dev March 1, 2002
BRCA1 regulates the G2/M checkpoint by activating Chk1 kinase upon DNA damage. Yarden RI, Pardo-Reoyo S, Sgagias M, Cowan KH, Brody LC Nat Genet March 1, 2002
Phosphorylation of serine 1387 in Brca1 is specifically required for the Atm-mediated S-phase checkpoint after ionizing irradiation. Xu B, O'Donnell AH, Kim ST, Kastan MB Cancer Res Aug. 15, 2002
NBS1 localizes to gamma-H2AX foci through interaction with the FHA/BRCT domain. Kobayashi J, Tauchi H, Sakamoto S, Nakamura A, Morishima K, Matsuura S, Kobayashi T, Tamai K, Tanimoto K, Komatsu K Curr Biol Oct. 1, 2002
BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains. Magnard C, Bachelier R, Vincent A, Jaquinod M, Kieffer S, Lenoir GM, Venezia ND Oncogene Oct. 3, 2002
BRCA1 and BRCA2 sequence variants in Chinese breast cancer families. Zhi X, Szabo C, Chopin S, Suter N, Wang QS, Ostrander EA, Sinilnikova OM, Lenoir GM, Goldgar D, Shi YR Hum Mutat Dec. 1, 2002
BRCA1 and BRCA2 mutation analysis of early-onset and familial breast cancer cases in Mexico. Ruiz-Flores P, Sinilnikova OM, Badzioch M, Calderon-Garciduenas AL, Chopin S, Fabrice O, Gonzalez-Guerrero JF, Szabo C, Lenoir G, Goldgar DE, Barrera-Saldana HA Hum Mutat Dec. 1, 2002
Structural consequences of a cancer-causing BRCA1-BRCT missense mutation. Williams RS, Glover JN J Biol Chem Feb. 24, 2003
BRCA1-independent ubiquitination of FANCD2. Vandenberg CJ, Gergely F, Ong CY, Pace P, Mallery DL, Hiom K, Patel KJ Mol Cell July 1, 2003
Twenty-three novel BRCA1 and BRCA2 sequence alterations in breast and/or ovarian cancer families in Southern Germany. Meyer P, Voigtlaender T, Bartram CR, Klaes R Hum Mutat Sept. 1, 2003
The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin. Wu-Baer F, Lagrazon K, Yuan W, Baer R J Biol Chem Sept. 12, 2003
Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair. Dong Y, Hakimi MA, Chen X, Kumaraswamy E, Cooch NS, Godwin AK, Shiekhattar R Mol Cell Nov. 1, 2003
One in 10 ovarian cancer patients carry germ line BRCA1 or BRCA2 mutations: results of a prospective study in Southern Sweden. Malander S, Ridderheim M, Masback A, Loman N, Kristoffersson U, Olsson H, Nilbert M, Borg A Eur J Cancer Jan. 1, 2004
Novel germline mutations in the BRCA1 and BRCA2 genes in Indian breast and breast-ovarian cancer families. Valarmathi MT, Sawhney M, Deo SS, Shukla NK, Das SN Hum Mutat Jan. 1, 2004
BRCA1 and BRCA2 germline mutation spectrum and frequencies in Belgian breast/ovarian cancer families. Claes K, Poppe B, Coene I, Paepe AD, Messiaen L Br J Cancer March 22, 2004
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 Hum Mol Genet April 15, 2004
Human Claspin works with BRCA1 to both positively and negatively regulate cell proliferation. Lin SY, Li K, Stewart GS, Elledge SJ Proc Natl Acad Sci U S A April 27, 2004
BRCA1 phosphorylation by Aurora-A in the regulation of G2 to M transition. Ouchi M, Fujiuchi N, Sasai K, Katayama H, Minamishima YA, Ongusaha PP, Deng C, Sen S, Lee SW, Ouchi T J Biol Chem May 7, 2004
Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer. Clapperton JA, Manke IA, Lowery DM, Ho T, Haire LF, Yaffe MB, Smerdon SJ Nat Struct Mol Biol June 1, 2004
Artemis is a phosphorylation target of ATM and ATR and is involved in the G2/M DNA damage checkpoint response. Zhang X, Succi J, Feng Z, Prithivirajsingh S, Story MD, Legerski RJ Mol Cell Biol Oct. 1, 2004
BRCA1 and BRCA2 germline mutations in Korean patients with sporadic breast cancer. Seo JH, Cho DY, Ahn SH, Yoon KS, Kang CS, Cho HM, Lee HS, Choe JJ, Choi CW, Kim BS, Shin SW, Kim YH, Kim JS, Son GS, Lee JB, Koo BH Hum Mutat Oct. 1, 2004
Solution structure, backbone dynamics, and association behavior of the C-terminal BRCT domain from the breast cancer-associated protein BRCA1. Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kuhne R, Oschkinat H, Heinemann U Biochemistry Dec. 28, 2004
Structural basis for cell cycle checkpoint control by the BRCA1-CtIP complex. Varma AK, Brown RS, Birrane G, Ladias JA Biochemistry Aug. 23, 2005
BRCA1 affects lipid synthesis through its interaction with acetyl-CoA carboxylase. Moreau K, Dizin E, Ray H, Luquain C, Lefai E, Foufelle F, Billaud M, Lenoir GM, Venezia ND J Biol Chem Jan. 10, 2006
ACCA phosphopeptide recognition by the BRCT repeats of BRCA1. Ray H, Moreau K, Dizin E, Callebaut I, Venezia ND J Mol Biol June 16, 2006
The consensus coding sequences of human breast and colorectal cancers. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE Science Oct. 13, 2006
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M Cell Nov. 3, 2006
ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ Science May 25, 2007
Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response. Wang B, Matsuoka S, Ballif BA, Zhang D, Smogorzewska A, Gygi SP, Elledge SJ Science May 25, 2007
CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA damage response. Kim H, Huang J, Chen J Nat Struct Mol Biol Aug. 1, 2007
CCDC98 targets BRCA1 to DNA damage sites. Liu Z, Wu J, Yu X Nat Struct Mol Biol Aug. 1, 2007
Aurora-A kinase regulates breast cancer associated gene 1 inhibition of centrosome-dependent microtubule nucleation. Sankaran S, Crone DE, Palazzo RE, Parvin JD Cancer Res Dec. 1, 2007
Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd J Proteome Res March 1, 2008
Structural evidence for direct interactions between the BRCT domains of human BRCA1 and a phospho-peptide from human ACC1. Shen Y, Tong L Biochemistry May 27, 2008
Pathogenicity of the BRCA1 missense variant M1775K is determined by the disruption of the BRCT phosphopeptide-binding pocket: a multi-modal approach. Tischkowitz M, Hamel N, Carvalho MA, Birrane G, Soni A, van Beers EH, Joosse SA, Wong N, Novak D, Quenneville LA, Grist SA, Nederlof PM, Goldgar DE, Tavtigian SV, Monteiro AN, Ladias JA, Foulkes WD Eur J Hum Genet July 1, 2008
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A Aug. 5, 2008
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal Jan. 1, 2009
MERIT40 facilitates BRCA1 localization and DNA damage repair. Feng L, Huang J, Chen J Genes Dev March 15, 2009
NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control. Wang B, Hurov K, Hofmann K, Elledge SJ Genes Dev March 15, 2009
MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA double-strand breaks. Shao G, Patterson-Fortin J, Messick TE, Feng D, Shanbhag N, Wang Y, Greenberg RA Genes Dev March 15, 2009
Comparison of the structures and peptide binding specificities of the BRCT domains of MDC1 and BRCA1. Campbell SJ, Edwards RA, Glover JN Structure Jan. 10, 2010
The UBXN1 protein associates with autoubiquitinated forms of the BRCA1 tumor suppressor and inhibits its enzymatic function. Wu-Baer F, Ludwig T, Baer R Mol Cell Biol June 1, 2010


Last modification of this entry: June 19, 2013.

Add your own comment!

There is no comment yet.
Welcome stranger! Click here to login or here to register.
Valid HTML 4.01! This site is Emacs powered. Made with Django.