Reviewed, UniProtKB/Swiss-Prot Q9NXR7 (BRE_HUMAN)

Names and origin

Protein names

Recommended name:
    BRCA1-A complex subunit BRE
Alternative name(s):
    Brain and reproductive organ-expressed protein
    BRCA1/BRCA2-containing complex subunit 45

Gene names

Name:	BRE
Synonyms:	BRCC45

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	383 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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. Ref.3 Ref.9 Ref.13 Ref.14
Subunit structure	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. Ref.9 Ref.13 Ref.14
Subcellular location	Cytoplasm. Nucleus. Note: Localizes at sites of DNA damage at double-strand breaks (DSBs). Ref.9 Ref.14
Tissue specificity	Expressed in all cell lines examined. Highly expressed in placenta. Ref.2
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). Ref.2 Ref.1
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. Ref.13
Sequence similarities	Belongs to the BRE family.

Ontologies

Keywords
Biological process	Apoptosis DNA damage DNA repair
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Molecular function	Chromatin regulator
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	G2/M transition DNA damage checkpoint Ref.14 Inferred from mutant phenotype. Source: UniProtKB apoptosis Inferred from electronic annotation. Source: UniProtKB-KW chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW double-strand break repair Ref.14 Inferred from mutant phenotype. Source: UniProtKB positive regulation of DNA repair Ref.14 Inferred from mutant phenotype. Source: UniProtKB positive regulation of anti-apoptosis Ref.9 Inferred from direct assay. Source: UniProtKB response to ionizing radiation Ref.13 Ref.14 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	BRCA1-A complex Ref.10 Ref.12 Ref.13 Ref.14 Inferred from direct assay. Source: UniProtKB BRISC complex Ref.11 Inferred from direct assay. Source: UniProtKB cytoplasm Ref.9 Inferred from direct assay. Source: UniProtKB nuclear ubiquitin ligase complex Ref.3 Inferred from direct assay. Source: UniProtKB
Molecular function	peroxisome targeting sequence binding Ref.2 Traceable author statement. Source: UniProtKB polyubiquitin binding Ref.13 Inferred from direct assay. Source: UniProtKB tumor necrosis factor receptor binding Ref.9 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRCC3	P46736	1	EBI-949389,EBI-750352
FAM175B	Q15018	1	EBI-949389,EBI-1056583
MERIT40	Q9NWV8	1	EBI-949389,EBI-745725

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms may exist.

Isoform 2 Ref.3 Ref.4 (identifier: Q9NXR7-2)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation exists.

Isoform 1 (identifier: Q9NXR7-1)

The sequence of this isoform differs from the canonical sequence as follows:
     364-383: AYFKTFVPQFQEAAFANGKL → GCQGSRDACSPWEQVLAFAVAKTGCKLLQPQRNWPSSRGPPWRASEGERTAQ

Isoform 3 Ref.2 (identifier: Q9NXR7-3)

Also known as: Alpha a';

The sequence of this isoform differs from the canonical sequence as follows:
     363-383: KAYFKTFVPQFQEAAFANGKL → NSRRQHLPMESSRKHQS

Isoform 4 (identifier: Q9NXR7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     364-383: AYFKTFVPQFQEAAFANGKL → RESNRDGEESSSA

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 383	383	BRCA1-A complex subunit BRE		PRO_0000224189
Regions
	Region	30 – 147	118	UEV-like 1
	Region	275 – 364	90	UEV-like 2
Amino acid modifications
	Modified residue	270	1	N6-acetyllysine Ref.15
Natural variations
	Alternative sequence	363 – 383	21	KAYFK…ANGKL → NSRRQHLPMESSRKHQS in isoform 3.		VSP_051957
	Alternative sequence	364 – 383	20	AYFKT…ANGKL → GCQGSRDACSPWEQVLAFAV AKTGCKLLQPQRNWPSSRGP PWRASEGERTAQ in isoform 1.		VSP_051956
	Alternative sequence	364 – 383	20	AYFKT…ANGKL → RESNRDGEESSSA in isoform 4.		VSP_037261
Experimental info
	Sequence conflict	192	1	V → L in BAF83775. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: D830226E2B8F2C4B	FASTA	383	43,552
	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
	Isoform 1. Checksum: 0501C5447AAFB3BA	FASTA	415	46,974
	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 370 380 390 400 410 RAKGCQGSRD ACSPWEQVLA FAVAKTGCKL LQPQRNWPSS RGPPWRASEG ERTAQ
	Isoform 3 (Alpha a'). Checksum: 2A8816CC439FDFB5	FASTA	379	43,224
	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 RANSRRQHLP MESSRKHQS
	Isoform 4. Checksum: 56488D883F2A27AE	FASTA	376	42,697
	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 RAKRESNRDG EESSSA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a brain- and reproductive-organs-specific gene responsive to DNA damage and retinoic acid." Li L., Yoo H., Becker F.F., Ali-Osman F., Chan J.Y.-H. Biochem. Biophys. Res. Commun. 206:764-774(1995) [PubMed: 7826398] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION.
[2]	"Expression of human BRE in multiple isoforms." 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. Biochem. Biophys. Res. Commun. 288:535-545(2001) [PubMed: 11676476] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY, INDUCTION. Tissue: Monocyte.
[3]	"Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair." Dong Y., Hakimi M.-A., Chen X., Kumaraswamy E., Cooch N.S., Godwin A.K., Shiekhattar R. Mol. Cell 12:1087-1099(2003) [PubMed: 14636569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, IDENTIFICATION IN BRCC COMPLEX.
[4]	Keeton K.R., Miles W.M. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Colon and Teratocarcinoma.
[6]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." 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. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Cervix.
[9]	"A death receptor-associated anti-apoptotic protein, BRE, inhibits mitochondrial apoptotic pathway." 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. J. Biol. Chem. 279:52106-52116(2004) [PubMed: 15465831] [Abstract] Cited for: FUNCTION, INTERACTION WITH FAS AND TNFRSF1A, SUBCELLULAR LOCATION.
[10]	"RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites." Sobhian B., Shao G., Lilli D.R., Culhane A.C., Moreau L.A., Xia B., Livingston D.M., Greenberg R.A. Science 316:1198-1202(2007) [PubMed: 17525341] [Abstract] Cited for: IDENTIFICATION IN THE BRCA1-A COMPLEX.
[11]	"K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1." Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M., Cohen R.E. EMBO J. 28:621-631(2009) [PubMed: 19214193] [Abstract] Cited for: IDENTIFICATION IN THE BRISC COMPLEX.
[12]	"MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA double-strand breaks." Shao G., Patterson-Fortin J., Messick T.E., Feng D., Shanbhag N., Wang Y., Greenberg R.A. Genes Dev. 23:740-754(2009) [PubMed: 19261746] [Abstract] Cited for: IDENTIFICATION IN THE BRCA1-A COMPLEX.
[13]	"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 S.J. Genes Dev. 23:729-739(2009) [PubMed: 19261749] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, DOMAIN UEV-LIKE, UBIQUITIN-BINDING, INTERACTION WITH FAM175A.
[14]	"MERIT40 facilitates BRCA1 localization and DNA damage repair." Feng L., Huang J., Chen J. Genes Dev. 23:719-728(2009) [PubMed: 19261748] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH FAM175A; MERIT40 AND BRCC3.
[15]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-270, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L38616 mRNA. Translation: AAA64231.1. AF420605 mRNA. Translation: AAL17818.1. AY438031 mRNA. Translation: AAR30499.1. AF015767 mRNA. Translation: AAB69387.1. AF420602 mRNA. Translation: AAL17814.1. AF420603 mRNA. Translation: AAL17816.1. AK000097 mRNA. Translation: BAA90943.1. AK291086 mRNA. Translation: BAF83775.1. AC021171 Genomic DNA. Translation: AAY24156.1. AC093690 Genomic DNA. No translation available. AC096552 Genomic DNA. Translation: AAX88935.1. CH471053 Genomic DNA. Translation: EAX00545.1. BC001251 mRNA. Translation: AAH01251.1.
IPI	IPI00149276. IPI00164724. IPI00446802. IPI00719447.
PIR	JC2472.
RefSeq	NP_004890.2. NP_954661.1. NP_954662.1. NP_954663.1. NP_954664.1.
UniGene	Hs.11916 Hs.258314
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NXR7. 4 interactions.
STRING	Q9NXR7.
PTM databases
PhosphoSite	Q9NXR7.
Proteomic databases
PRIDE	Q9NXR7.
Genome annotation databases
Ensembl	ENST00000296102; ENSP00000296102; ENSG00000158019; Homo sapiens. [Genome view] ENST00000342045; ENSP00000339371; ENSG00000158019; Homo sapiens. [Genome view] ENST00000344773; ENSP00000343412; ENSG00000158019; Homo sapiens. [Genome view] ENST00000359603; ENSP00000352617; ENSG00000158019; Homo sapiens. [Genome view] ENST00000361704; ENSP00000354699; ENSG00000158019; Homo sapiens. [Genome view] ENST00000379623; ENSP00000368944; ENSG00000158019; Homo sapiens. [Genome view] ENST00000379624; ENSP00000368945; ENSG00000158019; Homo sapiens. [Genome view] ENST00000379629; ENSP00000368950; ENSG00000158019; Homo sapiens. [Genome view] ENST00000379632; ENSP00000368953; ENSG00000158019; Homo sapiens. [Genome view] ENST00000379666; ENSP00000368988; ENSG00000158019; Homo sapiens. [Genome view] ENST00000395447; ENSP00000378834; ENSG00000158019; Homo sapiens. [Genome view] ENST00000436924; ENSP00000392345; ENSG00000158019; Homo sapiens. [Genome view] ENST00000448427; ENSP00000407385; ENSG00000158019; Homo sapiens. [Genome view]
GeneID	9577.
KEGG	hsa:9577.
UCSC	uc002rlp.1. human. uc002rlq.1. human. uc002rlr.1. human. uc002rls.1. human.
Organism-specific databases
CTD	9577.
GeneCards	GC02P028025.
H-InvDB	HIX0001933.
HGNC	HGNC:1106. BRE.
HPA	HPA017926.
MIM	610497. gene.
PharmGKB	PA25419.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q9NXR7.
HOVERGEN	Q9NXR7.
OMA	HIDLPLY.
Gene expression databases
ArrayExpress	Q9NXR7.
Bgee	Q9NXR7.
CleanEx	HS_BRE.
Genevestigator	Q9NXR7.
GermOnline	ENSG00000158019. Homo sapiens.
Family and domain databases
InterPro	IPR010358. Brain/reproduct-express_prot. [Graphical view]
Pfam	PF06113. BRE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	35917.
SOURCE	Search...

Entry information

Entry name

BRE_HUMAN

Accession

Primary (citable) accession number: Q9NXR7
Secondary accession number(s): A8K4X1 , Q13880, Q4ZFX8, Q53SD0, Q969X9, Q96P06

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2006
Last sequence update:	May 5, 2009
Last modified:	November 3, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.