Q8K3W0 (BRE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	383 AA.
Sequence status	Complete.
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 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 By similarity. May regulate TNF-alpha signaling through its interactions with TNFRSF1A. Ref.4
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 By similarity. Interacts with TNFRSF1A. Ref.4
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Note: Localizes at sites of DNA damage at double-strand breaks (DSBs) By similarity.
Tissue specificity	Expressed in brain, heart, kidney, liver, lung, testis, germinal center B-cells and various mouse cell lines. Ref.1 Ref.5
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 By similarity.
Sequence similarities	Belongs to the BRE family.
Sequence caution	The sequence BAC34385.1 differs from that shown. Reason: Probable cloning artifact.

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 Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2 DNA damage checkpoint Inferred from sequence or structural similarity. Source: UniProtKB apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW double-strand break repair Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of DNA repair Inferred from sequence or structural similarity. Source: UniProtKB response to ionizing radiation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	BRCA1-A complex Inferred from sequence or structural similarity. Source: UniProtKB BRISC complex Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nuclear ubiquitin ligase complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	polyubiquitin binding Inferred from sequence or structural similarity. Source: UniProtKB tumor necrosis factor receptor binding Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms may exist.

Isoform 2 Ref.1 (identifier: Q8K3W0-2)

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: Q8K3W0-1)

Also known as: I;

The sequence of this isoform differs from the canonical sequence as follows:
     27-43: VGLDATNCLRITDLKSG → IHEKGPSQKLSFKSCSYHLPMCACNEWYGVPDLEKASYLWRKKENHLPLEKGQN

Isoform 3 (identifier: Q8K3W0-4)

Also known as: II,II3+;

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: Missing.

Isoform 4 Ref.1 (identifier: Q8K3W0-5)

Also known as: IV;

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: MSPEIALNRI...CLRITDLKSG → MCACNEWYGVPDLEKASYLWRKKENHLPLEKGQN

Isoform 5 (identifier: Q8K3W0-6)

Also known as: III;

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: MSPEIALNRISPMLSPFISSVVRNGKVGLDATNCLRITDLKSGCTSLTPGPNCDRFKLHIPYAGETLKW → MCACR

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_0000224190
Regions
	Region	30 – 147	118	UEV-like 1
	Region	275 – 364	90	UEV-like 2
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	2	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 138	138	Missing in isoform 3.		VSP_051952
	Alternative sequence	1 – 69	69	MSPEI…ETLKW → MCACR in isoform 5.		VSP_037262
	Alternative sequence	1 – 43	43	MSPEI…DLKSG → MCACNEWYGVPDLEKASYLW RKKENHLPLEKGQN in isoform 4.		VSP_037263
	Alternative sequence	27 – 43	17	VGLDA…DLKSG → IHEKGPSQKLSFKSCSYHLP MCACNEWYGVPDLEKASYLW RKKENHLPLEKGQN in isoform 1.		VSP_051953
Experimental info
	Sequence conflict	105	1	W → R in AAH61000. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 7BABA837A8AF82E6	FASTA	383	43,545
	10 20 30 40 50 60 MSPEIALNRI SPMLSPFISS VVRNGKVGLD ATNCLRITDL KSGCTSLTPG PNCDRFKLHI 70 80 90 100 110 120 PYAGETLKWD IIFNAQYPEL PPDFIFGEDA EFLPDPSALH NLASWNPSNP ECLLLVVKEL 130 140 150 160 170 180 VQQYHQFQCG 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 (I) [UniParc]. Checksum: 1A9D634D162CE2A8	FASTA	420	48,089
	10 20 30 40 50 60 MSPEIALNRI SPMLSPFISS VVRNGKIHEK GPSQKLSFKS CSYHLPMCAC NEWYGVPDLE 70 80 90 100 110 120 KASYLWRKKE NHLPLEKGQN CTSLTPGPNC DRFKLHIPYA GETLKWDIIF NAQYPELPPD 130 140 150 160 170 180 FIFGEDAEFL PDPSALHNLA SWNPSNPECL LLVVKELVQQ YHQFQCGRLR ESSRLMFEYQ 190 200 210 220 230 240 TLLEEPQYGE NMEIYAGKKN NWTGEFSARF LLKLPVDFSN IPTYLLKDVN EDPGEDVALL 250 260 270 280 290 300 SVSFEDTEAT QVYPKLYLSP RIEHALGGSS ALHIPAFPGG GCLIDYVPQV CHLLTNKVQY 310 320 330 340 350 360 VIQGYHKRRE YIAAFLSHFG TGVVEYDAEG FTKLTLLLMW KDFCFLVHID LPLFFPRDQP 370 380 390 400 410 420 TLTFQSVYHF TNSGQLYSQA QKNYPYSPRW DGNEMAKRAK AYFKTFVPQF QEAAFANGKL
	Isoform 3 (II,II3+) [UniParc]. Checksum: 2F77E99B644BD4B4	FASTA	245	28,090
	10 20 30 40 50 60 MFEYQTLLEE PQYGENMEIY AGKKNNWTGE FSARFLLKLP VDFSNIPTYL LKDVNEDPGE 70 80 90 100 110 120 DVALLSVSFE DTEATQVYPK LYLSPRIEHA LGGSSALHIP AFPGGGCLID YVPQVCHLLT 130 140 150 160 170 180 NKVQYVIQGY HKRREYIAAF LSHFGTGVVE YDAEGFTKLT LLLMWKDFCF LVHIDLPLFF 190 200 210 220 230 240 PRDQPTLTFQ SVYHFTNSGQ LYSQAQKNYP YSPRWDGNEM AKRAKAYFKT FVPQFQEAAF ANGKL
	Isoform 4 (IV) [UniParc]. Checksum: 6A60137DAF657C78	FASTA	374	42,994
	10 20 30 40 50 60 MCACNEWYGV PDLEKASYLW RKKENHLPLE KGQNCTSLTP GPNCDRFKLH IPYAGETLKW 70 80 90 100 110 120 DIIFNAQYPE LPPDFIFGED AEFLPDPSAL HNLASWNPSN PECLLLVVKE LVQQYHQFQC 130 140 150 160 170 180 GRLRESSRLM FEYQTLLEEP QYGENMEIYA GKKNNWTGEF SARFLLKLPV DFSNIPTYLL 190 200 210 220 230 240 KDVNEDPGED VALLSVSFED TEATQVYPKL YLSPRIEHAL GGSSALHIPA FPGGGCLIDY 250 260 270 280 290 300 VPQVCHLLTN KVQYVIQGYH KRREYIAAFL SHFGTGVVEY DAEGFTKLTL LLMWKDFCFL 310 320 330 340 350 360 VHIDLPLFFP RDQPTLTFQS VYHFTNSGQL YSQAQKNYPY SPRWDGNEMA KRAKAYFKTF 370 VPQFQEAAFA NGKL
	Isoform 5 (III) [UniParc]. Checksum: 2AE2865E15A82E37	FASTA	319	36,595
	10 20 30 40 50 60 MCACRDIIFN AQYPELPPDF IFGEDAEFLP DPSALHNLAS WNPSNPECLL LVVKELVQQY 70 80 90 100 110 120 HQFQCGRLRE SSRLMFEYQT LLEEPQYGEN MEIYAGKKNN WTGEFSARFL LKLPVDFSNI 130 140 150 160 170 180 PTYLLKDVNE DPGEDVALLS VSFEDTEATQ VYPKLYLSPR IEHALGGSSA LHIPAFPGGG 190 200 210 220 230 240 CLIDYVPQVC HLLTNKVQYV IQGYHKRREY IAAFLSHFGT GVVEYDAEGF TKLTLLLMWK 250 260 270 280 290 300 DFCFLVHIDL PLFFPRDQPT LTFQSVYHFT NSGQLYSQAQ KNYPYSPRWD GNEMAKRAKA 310 YFKTFVPQFQ EAAFANGKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of a conserved mouse stress-modulating gene, Bre: comparison with the human ortholog." Ching A.K.K., Li Q., Lim P.L., Chan J.Y.-H., Chui Y.L. DNA Cell Biol. 22:497-504(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), TISSUE SPECIFICITY. Strain: BALB/c and C57BL/6 X CBA/N. Tissue: Heart.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J and NOD. Tissue: Embryo, Medulla oblongata and Spleen.
[3]	"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). Strain: Czech II. Tissue: Kidney and Lung.
[4]	"BRE: a modulator of TNF-alpha action." Gu C., Castellino A., Chan J.Y.-H., Chao M.V. FASEB J. 12:1101-1108(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TNFRSF1A.
[5]	"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: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF440752 mRNA. Translation: AAL40809.1. AF527952 mRNA. Translation: AAM92774.1. AF527953 mRNA. Translation: AAM92775.1. AF527954 mRNA. Translation: AAM92776.1. AF527955 mRNA. Translation: AAM92777.1. AF538925 mRNA. Translation: AAN15148.1. AK050695 mRNA. Translation: BAC34385.1. Sequence problems. AK080991 mRNA. Translation: BAC38108.1. AK156929 mRNA. Translation: BAE33900.1. BC061000 mRNA. Translation: AAH61000.1. BC100565 mRNA. Translation: AAI00566.1.
IPI	IPI00128466. IPI00170162. IPI00400095. IPI00400287. IPI00400376.
RefSeq	NP_653124.1. NM_144541.1. NP_851796.1. NM_181279.1. NP_851797.1. NM_181280.1. NP_851798.1. NM_181281.1. NP_851799.1. NM_181282.1.
UniGene	Mm.482126.
3D structure databases
ModBase	Search...
Proteomic databases
PaxDb	Q8K3W0.
PRIDE	Q8K3W0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000063813; ENSMUSP00000069133; ENSMUSG00000052139. ENSMUST00000071531; ENSMUSP00000071462; ENSMUSG00000052139. ENSMUST00000080598; ENSMUSP00000079434; ENSMUSG00000052139. ENSMUST00000114507; ENSMUSP00000110152; ENSMUSG00000052139. ENSMUST00000131995; ENSMUSP00000128351; ENSMUSG00000052139.
GeneID	107976.
KEGG	mmu:107976.
UCSC	uc008wza.1. mouse. uc008wzb.1. mouse. uc008wzc.1. mouse. uc008wze.1. mouse.
Organism-specific databases
CTD	9577.
MGI	MGI:1333875. Bre.
Phylogenomic databases
eggNOG	NOG71563.
GeneTree	ENSGT00390000004208.
HOVERGEN	HBG071492.
InParanoid	Q8CJ13.
KO	K12173.
OMA	FKTFVPQ.
OrthoDB	EOG4G7BZD.
Gene expression databases
ArrayExpress	Q8K3W0.
Bgee	Q8K3W0.
CleanEx	MM_BRE.
Genevestigator	Q8K3W0.
GermOnline	ENSMUSG00000052139. Mus musculus.
Family and domain databases
InterPro	IPR010358. Brain/reproduct-express_prot. [Graphical view]
Pfam	PF06113. BRE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	BRE. mouse.
NextBio	359811.
SOURCE	Search...

Entry information

Entry name

BRE_MOUSE

Accession

Primary (citable) accession number: Q8K3W0
Secondary accession number(s): Q497G6 , Q6P8Z2, Q8BKU1, Q8CJ13, Q8JZP0, Q8K3V9, Q8VHN1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2006
Last sequence update:	May 5, 2009
Last modified:	May 29, 2013
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program