Full text data of BRE
BRE
(BRCC45)
[Confidence: low (only semi-automatic identification from reviews)]
BRCA1-A complex subunit BRE (BRCA1/BRCA2-containing complex subunit 45; Brain and reproductive organ-expressed protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
BRCA1-A complex subunit BRE (BRCA1/BRCA2-containing complex subunit 45; Brain and reproductive organ-expressed protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NXR7
ID BRE_HUMAN Reviewed; 383 AA.
AC Q9NXR7; A8K4X1; D6W562; D6W563; Q13880; Q4ZFX8; Q53SD0; Q969X9;
read moreAC Q96P06;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=BRCA1-A complex subunit BRE;
DE AltName: Full=BRCA1/BRCA2-containing complex subunit 45;
DE AltName: Full=Brain and reproductive organ-expressed protein;
GN Name=BRE; Synonyms=BRCC45;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INDUCTION.
RX PubMed=7826398; DOI=10.1006/bbrc.1995.1108;
RA Li L., Yoo H., Becker F.F., Ali-Osman F., Chan J.Y.-H.;
RT "Identification of a brain- and reproductive-organs-specific gene
RT responsive to DNA damage and retinoic acid.";
RL Biochem. Biophys. Res. Commun. 206:764-774(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY, AND
RP INDUCTION.
RC TISSUE=Monocyte;
RX PubMed=11676476; DOI=10.1006/bbrc.2001.5801;
RA Ching A.K.K., Li P.S., Li Q., Chan B.C.L., Chan J.Y.-H., Lim P.L.,
RA Pang J.C.S., Chui Y.L.;
RT "Expression of human BRE in multiple isoforms.";
RL Biochem. Biophys. Res. Commun. 288:535-545(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND IDENTIFICATION
RP IN BRCC COMPLEX.
RX PubMed=14636569; DOI=10.1016/S1097-2765(03)00424-6;
RA Dong Y., Hakimi M.-A., Chen X., Kumaraswamy E., Cooch N.S.,
RA Godwin A.K., Shiekhattar R.;
RT "Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2,
RT by a signalosome-like subunit and its role in DNA repair.";
RL Mol. Cell 12:1087-1099(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Keeton K.R., Miles W.M.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, INTERACTION WITH FAS AND TNFRSF1A, AND SUBCELLULAR LOCATION.
RX PubMed=15465831; DOI=10.1074/jbc.M408678200;
RA Li Q., Ching A.K.-K., Chan B.C.-L., Chow S.K.-Y., Lim P.-L.,
RA Ho T.C.-Y., Ip W.-K., Wong C.-K., Lam C.W.-K., Lee K.K.-H.,
RA Chan J.Y.-H., Chui Y.-L.;
RT "A death receptor-associated anti-apoptotic protein, BRE, inhibits
RT mitochondrial apoptotic pathway.";
RL J. Biol. Chem. 279:52106-52116(2004).
RN [10]
RP IDENTIFICATION IN THE BRCA1-A COMPLEX.
RX PubMed=17525341; DOI=10.1126/science.1139516;
RA Sobhian B., Shao G., Lilli D.R., Culhane A.C., Moreau L.A., Xia B.,
RA Livingston D.M., Greenberg R.A.;
RT "RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage
RT sites.";
RL Science 316:1198-1202(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP IDENTIFICATION IN THE BRISC COMPLEX.
RX PubMed=19214193; DOI=10.1038/emboj.2009.27;
RA Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M.,
RA Cohen R.E.;
RT "K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-
RT associated Brcc36 and proteasomal Poh1.";
RL EMBO J. 28:621-631(2009).
RN [13]
RP IDENTIFICATION IN THE BRCA1-A COMPLEX.
RX PubMed=19261746; DOI=10.1101/gad.1739609;
RA Shao G., Patterson-Fortin J., Messick T.E., Feng D., Shanbhag N.,
RA Wang Y., Greenberg R.A.;
RT "MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA
RT double-strand breaks.";
RL Genes Dev. 23:740-754(2009).
RN [14]
RP FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, DOMAIN UEV-LIKE,
RP UBIQUITIN-BINDING, AND INTERACTION WITH FAM175A.
RX PubMed=19261749; DOI=10.1101/gad.1770309;
RA Wang B., Hurov K., Hofmann K., Elledge S.J.;
RT "NBA1, a new player in the Brca1 A complex, is required for DNA damage
RT resistance and checkpoint control.";
RL Genes Dev. 23:729-739(2009).
RN [15]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
RP BRCA1-A COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION WITH FAM175A;
RP BABAM1 AND BRCC3.
RX PubMed=19261748; DOI=10.1101/gad.1770609;
RA Feng L., Huang J., Chen J.;
RT "MERIT40 facilitates BRCA1 localization and DNA damage repair.";
RL Genes Dev. 23:719-728(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that
CC specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A
CC and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1
CC heterodimer to sites of DNA damage at double-strand breaks (DSBs).
CC The BRCA1-A complex also possesses deubiquitinase activity that
CC specifically removes 'Lys-63'-linked ubiquitin on histones H2A and
CC H2AX. In the BRCA1-A complex, it acts as an adapter that bridges
CC the interaction between BABAM1/NBA1 and the rest of the complex,
CC thereby being required for the complex integrity and modulating
CC the E3 ubiquitin ligase activity of the BRCA1-BARD1 heterodimer.
CC Probably also plays a role as a component of the BRISC complex, a
CC multiprotein complex that specifically cleaves 'Lys-63'-linked
CC ubiquitin. May play a role in homeostasis or cellular
CC differentiation in cells of neural, epithelial and germline
CC origins. May also act as a death receptor-associated anti-
CC apoptotic protein, which inhibits the mitochondrial apoptotic
CC pathway. May regulate TNF-alpha signaling through its interactions
CC with TNFRSF1A; however these effects may be indirect.
CC -!- SUBUNIT: Component of the BRCA1-A complex, at least composed of
CC the BRCA1, BARD1, UIMC1/RAP80, FAM175A/Abraxas, BRCC3/BRCC36,
CC BRE/BRCC45 and BABAM1/NBA1. In the BRCA1-A complex, interacts
CC directly with FAM175A/Abraxas, BRCC3/BRCC36 and BABAM1/NBA1. Binds
CC polyubiquitin. Component of the BRISC complex, at least composed
CC of the FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1.
CC Component of the BRCA1/BRCA2 containing complex (BRCC), which also
CC contains BRCA1, BRCA2, BARD1, BRCC3/BRCC36 and RAD51. BRCC is a
CC ubiquitin E3 ligase complex that enhances cellular survival
CC following DNA damage. May interact with FAS and TNFRSF1A.
CC -!- INTERACTION:
CC Q9NWV8:BABAM1; NbExp=3; IntAct=EBI-949389, EBI-745725;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localizes at sites
CC of DNA damage at double-strand breaks (DSBs).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms may exist;
CC Name=2;
CC IsoId=Q9NXR7-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9NXR7-1; Sequence=VSP_051956;
CC Name=3; Synonyms=Alpha a';
CC IsoId=Q9NXR7-3; Sequence=VSP_051957;
CC Name=4;
CC IsoId=Q9NXR7-4; Sequence=VSP_037261;
CC -!- TISSUE SPECIFICITY: Expressed in all cell lines examined. Highly
CC expressed in placenta.
CC -!- INDUCTION: Down-regulated by DNA-damaging agents in fibroblasts,
CC by retinoic acid in brain glioma U-251MG and promyelocytic HL-60
CC cell lines, and by bacterial lipopolysaccharides (LPS) in
CC peripheral blood mononuclear cells (PBMC).
CC -!- DOMAIN: Contains 2 ubiquitin-conjugating enzyme family-like (UEV-
CC like) regions. These regions lack the critical Cys residues
CC required for ubiquitination but retain the ability to bind
CC ubiquitin.
CC -!- SIMILARITY: Belongs to the BRE family.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BREID839ch2p23.html";
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DR EMBL; L38616; AAA64231.1; -; mRNA.
DR EMBL; AF420605; AAL17818.1; -; mRNA.
DR EMBL; AY438031; AAR30499.1; -; mRNA.
DR EMBL; AF015767; AAB69387.1; -; mRNA.
DR EMBL; AF420602; AAL17814.1; -; mRNA.
DR EMBL; AF420603; AAL17816.1; -; mRNA.
DR EMBL; AK000097; BAA90943.1; -; mRNA.
DR EMBL; AK291086; BAF83775.1; -; mRNA.
DR EMBL; AC021171; AAY24156.1; -; Genomic_DNA.
DR EMBL; AC093690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096552; AAX88935.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00545.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00546.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00547.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00548.1; -; Genomic_DNA.
DR EMBL; BC001251; AAH01251.1; -; mRNA.
DR PIR; JC2472; JC2472.
DR RefSeq; NP_001248769.1; NM_001261840.1.
DR RefSeq; NP_004890.2; NM_004899.4.
DR RefSeq; NP_954661.1; NM_199191.2.
DR RefSeq; NP_954662.1; NM_199192.2.
DR RefSeq; NP_954663.1; NM_199193.2.
DR RefSeq; NP_954664.1; NM_199194.2.
DR RefSeq; XP_005264708.1; XM_005264651.1.
DR UniGene; Hs.258314; -.
DR ProteinModelPortal; Q9NXR7; -.
DR IntAct; Q9NXR7; 22.
DR MINT; MINT-2867020; -.
DR STRING; 9606.ENSP00000343412; -.
DR PhosphoSite; Q9NXR7; -.
DR DMDM; 229462810; -.
DR PaxDb; Q9NXR7; -.
DR PRIDE; Q9NXR7; -.
DR DNASU; 9577; -.
DR Ensembl; ENST00000342045; ENSP00000339371; ENSG00000158019.
DR Ensembl; ENST00000344773; ENSP00000343412; ENSG00000158019.
DR Ensembl; ENST00000361704; ENSP00000354699; ENSG00000158019.
DR Ensembl; ENST00000379624; ENSP00000368945; ENSG00000158019.
DR Ensembl; ENST00000379632; ENSP00000368953; ENSG00000158019.
DR GeneID; 9577; -.
DR KEGG; hsa:9577; -.
DR UCSC; uc002rlr.3; human.
DR CTD; 9577; -.
DR GeneCards; GC02P028025; -.
DR HGNC; HGNC:1106; BRE.
DR HPA; HPA017926; -.
DR MIM; 610497; gene.
DR neXtProt; NX_Q9NXR7; -.
DR PharmGKB; PA25419; -.
DR eggNOG; NOG71563; -.
DR HOVERGEN; HBG071492; -.
DR InParanoid; Q9NXR7; -.
DR KO; K12173; -.
DR OMA; HIPAFPS; -.
DR ChiTaRS; BRE; human.
DR GeneWiki; BRE_(gene); -.
DR GenomeRNAi; 9577; -.
DR NextBio; 35917; -.
DR PRO; PR:Q9NXR7; -.
DR ArrayExpress; Q9NXR7; -.
DR Bgee; Q9NXR7; -.
DR CleanEx; HS_BRE; -.
DR Genevestigator; Q9NXR7; -.
DR GO; GO:0070531; C:BRCA1-A complex; IDA:UniProtKB.
DR GO; GO:0070552; C:BRISC complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000152; C:nuclear ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0000268; F:peroxisome targeting sequence binding; TAS:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin binding; IDA:UniProtKB.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR GO; GO:0031572; P:G2 DNA damage checkpoint; IMP:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR010358; Brain/reproduct-express_prot.
DR Pfam; PF06113; BRE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Chromatin regulator;
KW Complete proteome; Cytoplasm; DNA damage; DNA repair; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1 383 BRCA1-A complex subunit BRE.
FT /FTId=PRO_0000224189.
FT REGION 30 147 UEV-like 1.
FT REGION 275 364 UEV-like 2.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 2 2 Phosphoserine.
FT VAR_SEQ 363 383 KAYFKTFVPQFQEAAFANGKL -> NSRRQHLPMESSRKHQ
FT S (in isoform 3).
FT /FTId=VSP_051957.
FT VAR_SEQ 364 383 AYFKTFVPQFQEAAFANGKL -> GCQGSRDACSPWEQVLA
FT FAVAKTGCKLLQPQRNWPSSRGPPWRASEGERTAQ (in
FT isoform 1).
FT /FTId=VSP_051956.
FT VAR_SEQ 364 383 AYFKTFVPQFQEAAFANGKL -> RESNRDGEESSSA (in
FT isoform 4).
FT /FTId=VSP_037261.
FT CONFLICT 192 192 V -> L (in Ref. 5; BAF83775).
SQ SEQUENCE 383 AA; 43552 MW; D830226E2B8F2C4B CRC64;
MSPEVALNRI SPMLSPFISS VVRNGKVGLD ATNCLRITDL KSGCTSLTPG PNCDRFKLHI
PYAGETLKWD IIFNAQYPEL PPDFIFGEDA EFLPDPSALQ NLASWNPSNP ECLLLVVKEL
VQQYHQFQCS RLRESSRLMF EYQTLLEEPQ YGENMEIYAG KKNNWTGEFS ARFLLKLPVD
FSNIPTYLLK DVNEDPGEDV ALLSVSFEDT EATQVYPKLY LSPRIEHALG GSSALHIPAF
PGGGCLIDYV PQVCHLLTNK VQYVIQGYHK RREYIAAFLS HFGTGVVEYD AEGFTKLTLL
LMWKDFCFLV HIDLPLFFPR DQPTLTFQSV YHFTNSGQLY SQAQKNYPYS PRWDGNEMAK
RAKAYFKTFV PQFQEAAFAN GKL
//
ID BRE_HUMAN Reviewed; 383 AA.
AC Q9NXR7; A8K4X1; D6W562; D6W563; Q13880; Q4ZFX8; Q53SD0; Q969X9;
read moreAC Q96P06;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=BRCA1-A complex subunit BRE;
DE AltName: Full=BRCA1/BRCA2-containing complex subunit 45;
DE AltName: Full=Brain and reproductive organ-expressed protein;
GN Name=BRE; Synonyms=BRCC45;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INDUCTION.
RX PubMed=7826398; DOI=10.1006/bbrc.1995.1108;
RA Li L., Yoo H., Becker F.F., Ali-Osman F., Chan J.Y.-H.;
RT "Identification of a brain- and reproductive-organs-specific gene
RT responsive to DNA damage and retinoic acid.";
RL Biochem. Biophys. Res. Commun. 206:764-774(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY, AND
RP INDUCTION.
RC TISSUE=Monocyte;
RX PubMed=11676476; DOI=10.1006/bbrc.2001.5801;
RA Ching A.K.K., Li P.S., Li Q., Chan B.C.L., Chan J.Y.-H., Lim P.L.,
RA Pang J.C.S., Chui Y.L.;
RT "Expression of human BRE in multiple isoforms.";
RL Biochem. Biophys. Res. Commun. 288:535-545(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND IDENTIFICATION
RP IN BRCC COMPLEX.
RX PubMed=14636569; DOI=10.1016/S1097-2765(03)00424-6;
RA Dong Y., Hakimi M.-A., Chen X., Kumaraswamy E., Cooch N.S.,
RA Godwin A.K., Shiekhattar R.;
RT "Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2,
RT by a signalosome-like subunit and its role in DNA repair.";
RL Mol. Cell 12:1087-1099(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Keeton K.R., Miles W.M.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, INTERACTION WITH FAS AND TNFRSF1A, AND SUBCELLULAR LOCATION.
RX PubMed=15465831; DOI=10.1074/jbc.M408678200;
RA Li Q., Ching A.K.-K., Chan B.C.-L., Chow S.K.-Y., Lim P.-L.,
RA Ho T.C.-Y., Ip W.-K., Wong C.-K., Lam C.W.-K., Lee K.K.-H.,
RA Chan J.Y.-H., Chui Y.-L.;
RT "A death receptor-associated anti-apoptotic protein, BRE, inhibits
RT mitochondrial apoptotic pathway.";
RL J. Biol. Chem. 279:52106-52116(2004).
RN [10]
RP IDENTIFICATION IN THE BRCA1-A COMPLEX.
RX PubMed=17525341; DOI=10.1126/science.1139516;
RA Sobhian B., Shao G., Lilli D.R., Culhane A.C., Moreau L.A., Xia B.,
RA Livingston D.M., Greenberg R.A.;
RT "RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage
RT sites.";
RL Science 316:1198-1202(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP IDENTIFICATION IN THE BRISC COMPLEX.
RX PubMed=19214193; DOI=10.1038/emboj.2009.27;
RA Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M.,
RA Cohen R.E.;
RT "K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-
RT associated Brcc36 and proteasomal Poh1.";
RL EMBO J. 28:621-631(2009).
RN [13]
RP IDENTIFICATION IN THE BRCA1-A COMPLEX.
RX PubMed=19261746; DOI=10.1101/gad.1739609;
RA Shao G., Patterson-Fortin J., Messick T.E., Feng D., Shanbhag N.,
RA Wang Y., Greenberg R.A.;
RT "MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA
RT double-strand breaks.";
RL Genes Dev. 23:740-754(2009).
RN [14]
RP FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, DOMAIN UEV-LIKE,
RP UBIQUITIN-BINDING, AND INTERACTION WITH FAM175A.
RX PubMed=19261749; DOI=10.1101/gad.1770309;
RA Wang B., Hurov K., Hofmann K., Elledge S.J.;
RT "NBA1, a new player in the Brca1 A complex, is required for DNA damage
RT resistance and checkpoint control.";
RL Genes Dev. 23:729-739(2009).
RN [15]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
RP BRCA1-A COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION WITH FAM175A;
RP BABAM1 AND BRCC3.
RX PubMed=19261748; DOI=10.1101/gad.1770609;
RA Feng L., Huang J., Chen J.;
RT "MERIT40 facilitates BRCA1 localization and DNA damage repair.";
RL Genes Dev. 23:719-728(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that
CC specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A
CC and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1
CC heterodimer to sites of DNA damage at double-strand breaks (DSBs).
CC The BRCA1-A complex also possesses deubiquitinase activity that
CC specifically removes 'Lys-63'-linked ubiquitin on histones H2A and
CC H2AX. In the BRCA1-A complex, it acts as an adapter that bridges
CC the interaction between BABAM1/NBA1 and the rest of the complex,
CC thereby being required for the complex integrity and modulating
CC the E3 ubiquitin ligase activity of the BRCA1-BARD1 heterodimer.
CC Probably also plays a role as a component of the BRISC complex, a
CC multiprotein complex that specifically cleaves 'Lys-63'-linked
CC ubiquitin. May play a role in homeostasis or cellular
CC differentiation in cells of neural, epithelial and germline
CC origins. May also act as a death receptor-associated anti-
CC apoptotic protein, which inhibits the mitochondrial apoptotic
CC pathway. May regulate TNF-alpha signaling through its interactions
CC with TNFRSF1A; however these effects may be indirect.
CC -!- SUBUNIT: Component of the BRCA1-A complex, at least composed of
CC the BRCA1, BARD1, UIMC1/RAP80, FAM175A/Abraxas, BRCC3/BRCC36,
CC BRE/BRCC45 and BABAM1/NBA1. In the BRCA1-A complex, interacts
CC directly with FAM175A/Abraxas, BRCC3/BRCC36 and BABAM1/NBA1. Binds
CC polyubiquitin. Component of the BRISC complex, at least composed
CC of the FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1.
CC Component of the BRCA1/BRCA2 containing complex (BRCC), which also
CC contains BRCA1, BRCA2, BARD1, BRCC3/BRCC36 and RAD51. BRCC is a
CC ubiquitin E3 ligase complex that enhances cellular survival
CC following DNA damage. May interact with FAS and TNFRSF1A.
CC -!- INTERACTION:
CC Q9NWV8:BABAM1; NbExp=3; IntAct=EBI-949389, EBI-745725;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localizes at sites
CC of DNA damage at double-strand breaks (DSBs).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms may exist;
CC Name=2;
CC IsoId=Q9NXR7-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9NXR7-1; Sequence=VSP_051956;
CC Name=3; Synonyms=Alpha a';
CC IsoId=Q9NXR7-3; Sequence=VSP_051957;
CC Name=4;
CC IsoId=Q9NXR7-4; Sequence=VSP_037261;
CC -!- TISSUE SPECIFICITY: Expressed in all cell lines examined. Highly
CC expressed in placenta.
CC -!- INDUCTION: Down-regulated by DNA-damaging agents in fibroblasts,
CC by retinoic acid in brain glioma U-251MG and promyelocytic HL-60
CC cell lines, and by bacterial lipopolysaccharides (LPS) in
CC peripheral blood mononuclear cells (PBMC).
CC -!- DOMAIN: Contains 2 ubiquitin-conjugating enzyme family-like (UEV-
CC like) regions. These regions lack the critical Cys residues
CC required for ubiquitination but retain the ability to bind
CC ubiquitin.
CC -!- SIMILARITY: Belongs to the BRE family.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BREID839ch2p23.html";
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DR EMBL; L38616; AAA64231.1; -; mRNA.
DR EMBL; AF420605; AAL17818.1; -; mRNA.
DR EMBL; AY438031; AAR30499.1; -; mRNA.
DR EMBL; AF015767; AAB69387.1; -; mRNA.
DR EMBL; AF420602; AAL17814.1; -; mRNA.
DR EMBL; AF420603; AAL17816.1; -; mRNA.
DR EMBL; AK000097; BAA90943.1; -; mRNA.
DR EMBL; AK291086; BAF83775.1; -; mRNA.
DR EMBL; AC021171; AAY24156.1; -; Genomic_DNA.
DR EMBL; AC093690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096552; AAX88935.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00545.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00546.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00547.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00548.1; -; Genomic_DNA.
DR EMBL; BC001251; AAH01251.1; -; mRNA.
DR PIR; JC2472; JC2472.
DR RefSeq; NP_001248769.1; NM_001261840.1.
DR RefSeq; NP_004890.2; NM_004899.4.
DR RefSeq; NP_954661.1; NM_199191.2.
DR RefSeq; NP_954662.1; NM_199192.2.
DR RefSeq; NP_954663.1; NM_199193.2.
DR RefSeq; NP_954664.1; NM_199194.2.
DR RefSeq; XP_005264708.1; XM_005264651.1.
DR UniGene; Hs.258314; -.
DR ProteinModelPortal; Q9NXR7; -.
DR IntAct; Q9NXR7; 22.
DR MINT; MINT-2867020; -.
DR STRING; 9606.ENSP00000343412; -.
DR PhosphoSite; Q9NXR7; -.
DR DMDM; 229462810; -.
DR PaxDb; Q9NXR7; -.
DR PRIDE; Q9NXR7; -.
DR DNASU; 9577; -.
DR Ensembl; ENST00000342045; ENSP00000339371; ENSG00000158019.
DR Ensembl; ENST00000344773; ENSP00000343412; ENSG00000158019.
DR Ensembl; ENST00000361704; ENSP00000354699; ENSG00000158019.
DR Ensembl; ENST00000379624; ENSP00000368945; ENSG00000158019.
DR Ensembl; ENST00000379632; ENSP00000368953; ENSG00000158019.
DR GeneID; 9577; -.
DR KEGG; hsa:9577; -.
DR UCSC; uc002rlr.3; human.
DR CTD; 9577; -.
DR GeneCards; GC02P028025; -.
DR HGNC; HGNC:1106; BRE.
DR HPA; HPA017926; -.
DR MIM; 610497; gene.
DR neXtProt; NX_Q9NXR7; -.
DR PharmGKB; PA25419; -.
DR eggNOG; NOG71563; -.
DR HOVERGEN; HBG071492; -.
DR InParanoid; Q9NXR7; -.
DR KO; K12173; -.
DR OMA; HIPAFPS; -.
DR ChiTaRS; BRE; human.
DR GeneWiki; BRE_(gene); -.
DR GenomeRNAi; 9577; -.
DR NextBio; 35917; -.
DR PRO; PR:Q9NXR7; -.
DR ArrayExpress; Q9NXR7; -.
DR Bgee; Q9NXR7; -.
DR CleanEx; HS_BRE; -.
DR Genevestigator; Q9NXR7; -.
DR GO; GO:0070531; C:BRCA1-A complex; IDA:UniProtKB.
DR GO; GO:0070552; C:BRISC complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000152; C:nuclear ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0000268; F:peroxisome targeting sequence binding; TAS:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin binding; IDA:UniProtKB.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR GO; GO:0031572; P:G2 DNA damage checkpoint; IMP:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR010358; Brain/reproduct-express_prot.
DR Pfam; PF06113; BRE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Chromatin regulator;
KW Complete proteome; Cytoplasm; DNA damage; DNA repair; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1 383 BRCA1-A complex subunit BRE.
FT /FTId=PRO_0000224189.
FT REGION 30 147 UEV-like 1.
FT REGION 275 364 UEV-like 2.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 2 2 Phosphoserine.
FT VAR_SEQ 363 383 KAYFKTFVPQFQEAAFANGKL -> NSRRQHLPMESSRKHQ
FT S (in isoform 3).
FT /FTId=VSP_051957.
FT VAR_SEQ 364 383 AYFKTFVPQFQEAAFANGKL -> GCQGSRDACSPWEQVLA
FT FAVAKTGCKLLQPQRNWPSSRGPPWRASEGERTAQ (in
FT isoform 1).
FT /FTId=VSP_051956.
FT VAR_SEQ 364 383 AYFKTFVPQFQEAAFANGKL -> RESNRDGEESSSA (in
FT isoform 4).
FT /FTId=VSP_037261.
FT CONFLICT 192 192 V -> L (in Ref. 5; BAF83775).
SQ SEQUENCE 383 AA; 43552 MW; D830226E2B8F2C4B CRC64;
MSPEVALNRI SPMLSPFISS VVRNGKVGLD ATNCLRITDL KSGCTSLTPG PNCDRFKLHI
PYAGETLKWD IIFNAQYPEL PPDFIFGEDA EFLPDPSALQ NLASWNPSNP ECLLLVVKEL
VQQYHQFQCS RLRESSRLMF EYQTLLEEPQ YGENMEIYAG KKNNWTGEFS ARFLLKLPVD
FSNIPTYLLK DVNEDPGEDV ALLSVSFEDT EATQVYPKLY LSPRIEHALG GSSALHIPAF
PGGGCLIDYV PQVCHLLTNK VQYVIQGYHK RREYIAAFLS HFGTGVVEYD AEGFTKLTLL
LMWKDFCFLV HIDLPLFFPR DQPTLTFQSV YHFTNSGQLY SQAQKNYPYS PRWDGNEMAK
RAKAYFKTFV PQFQEAAFAN GKL
//
MIM
610497
*RECORD*
*FIELD* NO
610497
*FIELD* TI
*610497 BRAIN AND REPRODUCTIVE ORGAN-EXPRESSED PROTEIN; BRE
;;BRCC4;;
BRCC45
*FIELD* TX
read more
CLONING
Li et al. (1995) cloned BRE from a placenta cDNA library. The deduced
protein contains 383 amino acids. Northern blot analysis of normal human
fibroblasts detected a single BRE mRNA at 1.7 to 1.9 kb. Northern blot
analysis of several rat tissues detected highest expression in testis
and intermediate expression in brain and ovary. Using the juxtamembrane
domain of the p55 TNF receptor (TNFRSF1A; 191190) as bait in a yeast
2-hybrid screen, Gu et al. (1998) cloned Bre from a mouse cerebellum
cDNA library.
GENE FUNCTION
Li et al. (1995) found that the expression of BRE decreased following
DNA damage in normal human fibroblasts caused by UV irradiation or
4-nitroquinoline-1-oxide (4NQO) exposure. Similar decreased BRE
expression was observed in retinoic acid-treated human brain glioma
cells and promyelocytic cells. BRE expression was unchanged in cells
following growth inhibition.
Using protein-binding assays and immunoprecipitation analysis in HEK293
cells, Gu et al. (1998) confirmed the interaction between mouse Bre and
Tnfrsf1a. Bre specifically interacted with Tnfrsf1a but not with other
TNF family members. Overexpression of Bre inhibited TNF-induced
NF-kappa-B activation.
Dong et al. (2003) demonstrated that in human cell lines BRE and BRCC3
(300617) are components of a holoenzyme complex containing BRCA1
(113705), BRCA2 (600185), BARD1 (601593), and RAD51 (179617), which they
called the BRCA1- and BRCA2-containing complex (BRCC). The complex
showed UBC5 (see UBE2D1; 602961)-dependent ubiquitin E3 ligase activity.
Inclusion of BRE and BRCC3 enhanced ubiquitination by the complex, and
cancer-associated truncations in BRCA1 reduced the association of BRE
and BRCC3 with the complex. RNA interference of BRE and BRCC3 in HeLa
cells increased cell sensitivity to ionizing radiation and resulted in a
defect in G2/M checkpoint arrest. Dong et al. (2003) concluded that the
BRCC is a ubiquitin E3 ligase that enhances cellular survival following
DNA damage.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the BRE
gene to chromosome 2 (TMAP RH66226).
*FIELD* RF
1. Dong, Y.; Hakimi, M.-A.; Chen, X.; Kumaraswamy, E.; Cooch, N. S.;
Godwin, A. K.; Shiekhattar, R.: Regulation of BRCC, a holoenzyme
complex containing BRCA1 and BRCA2, by a signalosome-like subunit
and its role in DNA repair. Molec. Cell 12: 1087-1099, 2003.
2. Gu, C.; Castellino, A.; Chan, J. Y.-H.; Chao, M. V.: BRE: a modulator
of TNF-alpha action. FASEB J. 12: 1101-1108, 1998.
3. Li, L.; Yoo, H.; Becker, F. F.; Ali-Osman, F.; Chan, J. Y. H.:
Identification of a brain- and reproductive-organs-specific gene responsive
to DNA damage and retinoic acid. Biochem. Biophys. Res. Commun. 206:
764-774, 1995.
*FIELD* CD
Patricia A. Hartz: 10/16/2006
*FIELD* ED
wwang: 10/16/2006
*RECORD*
*FIELD* NO
610497
*FIELD* TI
*610497 BRAIN AND REPRODUCTIVE ORGAN-EXPRESSED PROTEIN; BRE
;;BRCC4;;
BRCC45
*FIELD* TX
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CLONING
Li et al. (1995) cloned BRE from a placenta cDNA library. The deduced
protein contains 383 amino acids. Northern blot analysis of normal human
fibroblasts detected a single BRE mRNA at 1.7 to 1.9 kb. Northern blot
analysis of several rat tissues detected highest expression in testis
and intermediate expression in brain and ovary. Using the juxtamembrane
domain of the p55 TNF receptor (TNFRSF1A; 191190) as bait in a yeast
2-hybrid screen, Gu et al. (1998) cloned Bre from a mouse cerebellum
cDNA library.
GENE FUNCTION
Li et al. (1995) found that the expression of BRE decreased following
DNA damage in normal human fibroblasts caused by UV irradiation or
4-nitroquinoline-1-oxide (4NQO) exposure. Similar decreased BRE
expression was observed in retinoic acid-treated human brain glioma
cells and promyelocytic cells. BRE expression was unchanged in cells
following growth inhibition.
Using protein-binding assays and immunoprecipitation analysis in HEK293
cells, Gu et al. (1998) confirmed the interaction between mouse Bre and
Tnfrsf1a. Bre specifically interacted with Tnfrsf1a but not with other
TNF family members. Overexpression of Bre inhibited TNF-induced
NF-kappa-B activation.
Dong et al. (2003) demonstrated that in human cell lines BRE and BRCC3
(300617) are components of a holoenzyme complex containing BRCA1
(113705), BRCA2 (600185), BARD1 (601593), and RAD51 (179617), which they
called the BRCA1- and BRCA2-containing complex (BRCC). The complex
showed UBC5 (see UBE2D1; 602961)-dependent ubiquitin E3 ligase activity.
Inclusion of BRE and BRCC3 enhanced ubiquitination by the complex, and
cancer-associated truncations in BRCA1 reduced the association of BRE
and BRCC3 with the complex. RNA interference of BRE and BRCC3 in HeLa
cells increased cell sensitivity to ionizing radiation and resulted in a
defect in G2/M checkpoint arrest. Dong et al. (2003) concluded that the
BRCC is a ubiquitin E3 ligase that enhances cellular survival following
DNA damage.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the BRE
gene to chromosome 2 (TMAP RH66226).
*FIELD* RF
1. Dong, Y.; Hakimi, M.-A.; Chen, X.; Kumaraswamy, E.; Cooch, N. S.;
Godwin, A. K.; Shiekhattar, R.: Regulation of BRCC, a holoenzyme
complex containing BRCA1 and BRCA2, by a signalosome-like subunit
and its role in DNA repair. Molec. Cell 12: 1087-1099, 2003.
2. Gu, C.; Castellino, A.; Chan, J. Y.-H.; Chao, M. V.: BRE: a modulator
of TNF-alpha action. FASEB J. 12: 1101-1108, 1998.
3. Li, L.; Yoo, H.; Becker, F. F.; Ali-Osman, F.; Chan, J. Y. H.:
Identification of a brain- and reproductive-organs-specific gene responsive
to DNA damage and retinoic acid. Biochem. Biophys. Res. Commun. 206:
764-774, 1995.
*FIELD* CD
Patricia A. Hartz: 10/16/2006
*FIELD* ED
wwang: 10/16/2006