[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INDUCTION. DOI=10.1006/bbrc.1995.1108; PubMed=7826398 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY, AND INDUCTION. TISSUE=Monocyte; DOI=10.1006/bbrc.2001.5801; PubMed=11676476 [NCBI, ExPASy, EBI, Israel, Japan] Ching A.K.K., Li P.S., Li Q., Chan B.C.L., Chan J.Y.-H., Lim P.L., Pang J.C.S., Chui Y.L.; "Expression of human BRE in multiple isoforms."; Biochem. Biophys. Res. Commun. 288:535-545(2001).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND IDENTIFICATION IN BRCC COMPLEX. DOI=10.1016/S1097-2765(03)00424-6; PubMed=14636569 [NCBI, ExPASy, EBI, Israel, Japan] 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."; Mol. Cell 12:1087-1099(2003).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Keeton K.R., Miles W.M.; Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Colon, and Teratocarcinoma; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; "Complete sequencing and characterization of 21,243 full-length human cDNAs."; Nat. Genet. 36:40-45(2004).
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan] Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.; "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."; Nature 434:724-731(2005).
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.; Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). TISSUE=Cervix; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[9]	FUNCTION, INTERACTION WITH FAS AND TNFRSF1A, AND SUBCELLULAR LOCATION. DOI=10.1074/jbc.M408678200; PubMed=15465831 [NCBI, ExPASy, EBI, Israel, Japan] Li Q., Ching A.K.-K., Chan B.C.-L., Chow S.K.-Y., Lim P.-L., Ho T.C.-Y., Ip W.-K., Wong C.-K., Lam C.W.-K., Lee K.K.-H., Chan J.Y.-H., Chui Y.-L.; "A death receptor-associated anti-apoptotic protein, BRE, inhibits mitochondrial apoptotic pathway."; J. Biol. Chem. 279:52106-52116(2004).
[10]	IDENTIFICATION IN THE BRCA1-A COMPLEX. DOI=10.1126/science.1139516; PubMed=17525341 [NCBI, ExPASy, EBI, Israel, Japan] Sobhian B., Shao G., Lilli D.R., Culhane A.C., Moreau L.A., Xia B., Livingston D.M., Greenberg R.A.; "RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites."; Science 316:1198-1202(2007).
[11]	IDENTIFICATION IN THE BRISC COMPLEX. DOI=10.1038/emboj.2009.27; PubMed=19214193 [NCBI, ExPASy, EBI, Israel, Japan] Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M., Cohen R.E.; "K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1."; EMBO J. 28:621-631(2009).
[12]	IDENTIFICATION IN THE BRCA1-A COMPLEX. DOI=10.1101/gad.1739609; PubMed=19261746 [NCBI, ExPASy, EBI, Israel, Japan] Shao G., Patterson-Fortin J., Messick T.E., Feng D., Shanbhag N., Wang Y., Greenberg R.A.; "MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA double-strand breaks."; Genes Dev. 23:740-754(2009).
[13]	FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, UEV-LIKE DOMAIN, UBIQUITIN-BINDING, AND INTERACTION FAM175A. DOI=10.1101/gad.1770309; PubMed=19261749 [NCBI, ExPASy, EBI, Israel, Japan] Wang B., Hurov K., Hofmann K., Elledge S.J.; "NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control."; Genes Dev. 23:729-739(2009).
[14]	FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION WITH FAM175A; MERIT40 AND BRCC3. DOI=10.1101/gad.1770609; PubMed=19261748 [NCBI, ExPASy, EBI, Israel, Japan] Feng L., Huang J., Chen J.; "MERIT40 facilitates BRCA1 localization and DNA damage repair."; Genes Dev. 23:719-728(2009).

Comments

FUNCTION: Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it acts as an adapter that bridges the interaction between MERIT40/NBA1 and the rest of the complex, thereby being required for the complex integrity and modulating the E3 ubiquitin ligase activity of the BRCA1-BARD1 heterodimer. Probably also plays a role as a component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin. May play a role in homeostasis or cellular differentiation in cells of neural, epithelial and germline origins. May also act as a death receptor-associated anti-apoptotic protein, which inhibits the mitochondrial apoptotic pathway. May regulate TNF-alpha signaling through its interactions with TNFRSF1A; however these effects may be indirect.
SUBUNIT: Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1/RAP80, FAM175A/Abraxas, BRCC3/BRCC36, BRE/BRCC45 and MERIT40/NBA1. In the BRCA1-A complex, interacts directly with FAM175A/Abraxas, BRCC3/BRCC36 and MERIT40/NBA1. Binds polyubiquitin. Component of the BRISC complex, at least composed of the FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 and MERIT40/NBA1. Component of the BRCA1/BRCA2 containing complex (BRCC), which also contains BRCA1, BRCA2, BARD1, BRCC3/BRCC36 and RAD51. BRCC is a ubiquitin E3 ligase complex that enhances cellular survival following DNA damage. May interact with FAS and TNFRSF1A.
INTERACTION:
P46736:BRCC3; NbExp=1; IntAct=EBI-949389, EBI-750352;
Q15018:FAM175B; NbExp=1; IntAct=EBI-949389, EBI-1056583;
Q9NWV8:MERIT40; NbExp=1; IntAct=EBI-949389, EBI-745725;
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs).

ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing. Additional isoforms may exist.

Name	2
Isoform ID	Q9NXR7-2
Note: No experimental confirmation exists.
This is the isoform sequence displayed in this entry.

Name	1
Isoform ID	Q9NXR7-1
Features which should be applied to build the isoform sequence: VSP_051956.

Name	3
Synonyms	Alpha a'
Isoform ID	Q9NXR7-3
Features which should be applied to build the isoform sequence: VSP_051957.

Name	4
Isoform ID	Q9NXR7-4
Features which should be applied to build the isoform sequence: VSP_037261.

TISSUE SPECIFICITY: Expressed in all cell lines examined. Highly expressed in placenta.
INDUCTION: Down-regulated by DNA-damaging agents in fibroblasts, by retinoic acid in brain glioma U-251 and promyelocytic HL-60 cell lines, and by LPS in peripheral blood mononuclear cells (PBMC).
DOMAIN: Contains 2 ubiquitin-conjugating enzyme family-like (UEV-like) regions. These regions lack the critical Cys residues required for ubiquitination but retain the ability to bind ubiquitin.
SIMILARITY: Belongs to the BRE family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L38616; AAA64231.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF420605; AAL17818.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY438031; AAR30499.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF015767; AAB69387.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF420602; AAL17814.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF420603; AAL17816.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK000097; BAA90943.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291086; BAF83775.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC021171; AAY24156.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC093690; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
AC096552; AAX88935.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471053; EAX00545.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001251; AAH01251.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00149276; -.
IPI00164724; -.
IPI00719447; -.

PIR

JC2472; JC2472.

RefSeq

NP_004890.2; -.
NP_954661.1; -.
NP_954662.1; -.
NP_954663.1; -.
NP_954664.1; -.

UniGene

Hs.11916

3D structure databases

ModBase

Q9NXR7.

Protein-protein interaction databases

IntAct

Q9NXR7; 4.

PTM databases

PhosphoSite

Q9NXR7; -.

Organism-specific databases

GC02P028025; -.

HIX0001933; -.

HGNC:1106; BRE.

BRE.

HPA017926; -.

610497; gene. [NCBI / EBI]

PharmGKB

PA25419; -.

Gene expression databases

Q9NXR7; -.

Q9NXR7; -.

HS_BRE; -.

ENSG00000158019; Homo sapiens.

Ontologies

GO:0070531;	Cellular component: BRCA1-A complex (inferred from direct assay from UniProtKB).
GO:0070552;	Cellular component: BRISC complex (inferred from direct assay from UniProtKB).
GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
GO:0000152;	Cellular component: nuclear ubiquitin ligase complex (inferred from direct assay from UniProtKB).
GO:0000268;	Molecular function: peroxisome targeting sequence binding (traceable author statement from UniProtKB).
GO:0031593;	Molecular function: polyubiquitin binding (inferred from direct assay from UniProtKB).
GO:0005164;	Molecular function: tumor necrosis factor receptor binding (inferred from direct assay from UniProtKB).
GO:0006915;	Biological process: apoptosis (inferred from electronic annotation from UniProtKB-KW).
GO:0016568;	Biological process: chromatin modification (inferred from electronic annotation from UniProtKB-KW).
GO:0006302;	Biological process: double-strand break repair (inferred from mutant phenotype from UniProtKB).
GO:0031572;	Biological process: G2/M transition DNA damage checkpoint (inferred from mutant phenotype from UniProtKB).
GO:0045768;	Biological process: positive regulation of anti-apoptosis (inferred from direct assay from UniProtKB).
GO:0045739;	Biological process: positive regulation of DNA repair (inferred from mutant phenotype from UniProtKB).
GO:0010212;	Biological process: response to ionizing radiation (inferred from mutant phenotype from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR010358; BRE.
Graphical view of domain structure.

Pfam

PF06113; BRE; 1.
Pfam graphical view of domain structure.

Proteomic databases

PRIDE

Q9NXR7; -.

Genome annotation databases

Ensembl

ENSG00000158019; Homo sapiens. [Contig view]

GeneID

9577; -.

KEGG

hsa:9577; -.

Phylogenomic databases

HOGENOM

Q9NXR7; -.

HOVERGEN

Q9NXR7; -.

OMA

Q9NXR7; HIDLPLY.

Other

35917; -.

BRE; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Apoptosis; Chromatin regulator; Cytoplasm; DNA damage; DNA repair; Nucleus; Repeat.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 383`	`383`	`BRCA1-A complex subunit BRE.`	`PRO_0000224189`
`REGION`	`30 147`	`118`	`UEV-like 1.`
`REGION`	`275 364`	`90`	`UEV-like 2.`
`VAR_SEQ`	`363 383`		`KAYFKTFVPQFQEAAFANGKL -> NSRRQHLPMESSRKHQS (in isoform 3).`	`VSP_051957`
`VAR_SEQ`	`364 383`		`AYFKTFVPQFQEAAFANGKL -> GCQGSRDACSPWEQVLAFAVAKTGCKLLQPQRNWPSSRGP` `PWRASEGERTAQ (in isoform 1).`	`VSP_051956`
`VAR_SEQ`	`364 383`		`AYFKTFVPQFQEAAFANGKL -> RESNRDGEESSSA (in isoform 4).`	`VSP_037261`
`CONFLICT`	`192 192`		`V -> L (in Ref. 5; BAF83775).`

Sequence information

Length: 383 AA [This is the length of the unprocessed precursor]

Molecular weight: 43552 Da [This is the MW of the unprocessed precursor]

CRC64: D830226E2B8F2C4B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSPEVALNRI SPMLSPFISS VVRNGKVGLD ATNCLRITDL KSGCTSLTPG PNCDRFKLHI 

        70         80         90        100        110        120 
PYAGETLKWD IIFNAQYPEL PPDFIFGEDA EFLPDPSALQ NLASWNPSNP ECLLLVVKEL 

       130        140        150        160        170        180 
VQQYHQFQCS RLRESSRLMF EYQTLLEEPQ YGENMEIYAG KKNNWTGEFS ARFLLKLPVD 

       190        200        210        220        230        240 
FSNIPTYLLK DVNEDPGEDV ALLSVSFEDT EATQVYPKLY LSPRIEHALG GSSALHIPAF 

       250        260        270        280        290        300 
PGGGCLIDYV PQVCHLLTNK VQYVIQGYHK RREYIAAFLS HFGTGVVEYD AEGFTKLTLL 

       310        320        330        340        350        360 
LMWKDFCFLV HIDLPLFFPR DQPTLTFQSV YHFTNSGQLY SQAQKNYPYS PRWDGNEMAK 

       370        380 
RAKAYFKTFV PQFQEAAFAN GKL

Q9NXR7 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools