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Q9NXR7 (BRE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
BRCA1-A complex subunit BRE
Alternative name(s):
BRCA1/BRCA2-containing complex subunit 45
Brain and reproductive organ-expressed protein
Gene names
Name:BRE
Synonyms:BRCC45
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length383 AA.
Sequence statusComplete.
Protein existenceEvidence 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 BABAM1/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.14 Ref.15

Subunit structure

Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1/RAP80, FAM175A/Abraxas, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1. In the BRCA1-A complex, interacts directly with FAM175A/Abraxas, BRCC3/BRCC36 and BABAM1/NBA1. Binds polyubiquitin. Component of the BRISC complex, at least composed of the FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/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.3 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15

Subcellular location

Cytoplasm. Nucleus. Note: Localizes at sites of DNA damage at double-strand breaks (DSBs). Ref.9 Ref.15

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-251MG and promyelocytic HL-60 cell lines, and by bacterial lipopolysaccharides (LPS) in peripheral blood mononuclear cells (PBMC). Ref.1 Ref.2

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.14

Sequence similarities

Belongs to the BRE family.

Ontologies

Keywords
   Biological processApoptosis
DNA damage
DNA repair
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   Molecular functionChromatin regulator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2 DNA damage checkpoint

Inferred from mutant phenotype Ref.15. Source: UniProtKB

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to DNA damage stimulus

Inferred from expression pattern Ref.1. Source: UniProtKB

chromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

double-strand break repair

Inferred from mutant phenotype Ref.15. Source: UniProtKB

positive regulation of DNA repair

Inferred from mutant phenotype Ref.15. Source: UniProtKB

response to ionizing radiation

Inferred from mutant phenotype Ref.15Ref.14. Source: UniProtKB

signal transduction

Traceable author statement PubMed 9737713. Source: ProtInc

   Cellular_componentBRCA1-A complex

Inferred from direct assay Ref.10Ref.13Ref.15Ref.14. Source: UniProtKB

BRISC complex

Inferred from direct assay Ref.12. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

nuclear ubiquitin ligase complex

Inferred from direct assay Ref.3. Source: UniProtKB

nucleus

Inferred from direct assay Ref.9Ref.15. Source: UniProtKB

   Molecular_functionperoxisome targeting sequence binding

Traceable author statement Ref.2. Source: UniProtKB

polyubiquitin binding

Inferred from direct assay Ref.14. Source: UniProtKB

tumor necrosis factor receptor binding

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BABAM1Q9NWV83EBI-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.
Isoform 1 Ref.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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 383383BRCA1-A complex subunit BRE
PRO_0000224189

Regions

Region30 – 147118UEV-like 1
Region275 – 36490UEV-like 2

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11 Ref.16 Ref.18
Modified residue21Phosphoserine Ref.16

Natural variations

Alternative sequence363 – 38321KAYFK…ANGKL → NSRRQHLPMESSRKHQS in isoform 3.
VSP_051957
Alternative sequence364 – 38320AYFKT…ANGKL → GCQGSRDACSPWEQVLAFAV AKTGCKLLQPQRNWPSSRGP PWRASEGERTAQ in isoform 1.
VSP_051956
Alternative sequence364 – 38320AYFKT…ANGKL → RESNRDGEESSSA in isoform 4.
VSP_037261

Experimental info

Sequence conflict1921V → L in BAF83775. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: D830226E2B8F2C4B

FASTA38343,552
        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 

« Hide

Isoform 1 [UniParc].

Checksum: 0501C5447AAFB3BA
Show »

FASTA41546,974
Isoform 3 (Alpha a') [UniParc].

Checksum: 2A8816CC439FDFB5
Show »

FASTA37943,224
Isoform 4 [UniParc].

Checksum: 56488D883F2A27AE
Show »

FASTA37642,697

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE BRCA1-A COMPLEX.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE BRISC COMPLEX.
[13]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE BRCA1-A COMPLEX.
[14]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, DOMAIN UEV-LIKE, UBIQUITIN-BINDING, INTERACTION WITH FAM175A.
[15]"MERIT40 facilitates BRCA1 localization and DNA damage repair."
Feng L., Huang J., Chen J.
Genes Dev. 23:719-728(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH FAM175A; BABAM1 AND BRCC3.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CH471053 Genomic DNA. Translation: EAX00546.1.
CH471053 Genomic DNA. Translation: EAX00547.1.
CH471053 Genomic DNA. Translation: EAX00548.1.
BC001251 mRNA. Translation: AAH01251.1.
PIRJC2472.
RefSeqNP_001248769.1. NM_001261840.1.
NP_004890.2. NM_004899.4.
NP_954661.1. NM_199191.2.
NP_954662.1. NM_199192.2.
NP_954663.1. NM_199193.2.
NP_954664.1. NM_199194.2.
UniGeneHs.258314.

3D structure databases

ProteinModelPortalQ9NXR7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114946. 41 interactions.
IntActQ9NXR7. 22 interactions.
MINTMINT-2867020.
STRING9606.ENSP00000343412.

PTM databases

PhosphoSiteQ9NXR7.

Polymorphism databases

DMDM229462810.

Proteomic databases

PaxDbQ9NXR7.
PRIDEQ9NXR7.

Protocols and materials databases

DNASU9577.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342045; ENSP00000339371; ENSG00000158019. [Q9NXR7-2]
ENST00000344773; ENSP00000343412; ENSG00000158019. [Q9NXR7-1]
ENST00000361704; ENSP00000354699; ENSG00000158019. [Q9NXR7-4]
ENST00000379624; ENSP00000368945; ENSG00000158019. [Q9NXR7-2]
ENST00000379632; ENSP00000368953; ENSG00000158019. [Q9NXR7-4]
GeneID9577.
KEGGhsa:9577.
UCSCuc002rlp.2. human. [Q9NXR7-3]
uc002rlq.3. human. [Q9NXR7-4]
uc002rlr.3. human. [Q9NXR7-2]
uc002rls.3. human. [Q9NXR7-1]

Organism-specific databases

CTD9577.
GeneCardsGC02P028025.
HGNCHGNC:1106. BRE.
HPAHPA017926.
MIM610497. gene.
neXtProtNX_Q9NXR7.
PharmGKBPA25419.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG71563.
HOVERGENHBG071492.
InParanoidQ9NXR7.
KOK12173.
OMAHIPAFPS.
PhylomeDBQ9NXR7.
TreeFamTF328507.

Gene expression databases

ArrayExpressQ9NXR7.
BgeeQ9NXR7.
CleanExHS_BRE.
GenevestigatorQ9NXR7.

Family and domain databases

InterProIPR010358. Brain/reproduct-express_prot.
[Graphical view]
PfamPF06113. BRE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBRE. human.
GeneWikiBRE_(gene).
GenomeRNAi9577.
NextBio35917.
PROQ9NXR7.
SOURCESearch...

Entry information

Entry nameBRE_HUMAN
AccessionPrimary (citable) accession number: Q9NXR7
Secondary accession number(s): A8K4X1 expand/collapse secondary AC list , D6W562, D6W563, Q13880, Q4ZFX8, Q53SD0, Q969X9, Q96P06
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: May 5, 2009
Last modified: April 16, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM