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Q8K3W0 (BRE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 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 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 sequence or structural similarity. Source: UniProtKB

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

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_componentBRCA1-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

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionpolyubiquitin 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 383383BRCA1-A complex subunit BRE
PRO_0000224190

Regions

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

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue21Phosphoserine By similarity

Natural variations

Alternative sequence1 – 138138Missing in isoform 3.
VSP_051952
Alternative sequence1 – 6969MSPEI…ETLKW → MCACR in isoform 5.
VSP_037262
Alternative sequence1 – 4343MSPEI…DLKSG → MCACNEWYGVPDLEKASYLW RKKENHLPLEKGQN in isoform 4.
VSP_037263
Alternative sequence27 – 4317VGLDA…DLKSG → IHEKGPSQKLSFKSCSYHLP MCACNEWYGVPDLEKASYLW RKKENHLPLEKGQN in isoform 1.
VSP_051953

Experimental info

Sequence conflict1051W → R in AAH61000. Ref.3

Sequences

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

Last modified May 5, 2009. Version 2.
Checksum: 7BABA837A8AF82E6

FASTA38343,545
        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 

« Hide

Isoform 1 (I) [UniParc].

Checksum: 1A9D634D162CE2A8
Show »

FASTA42048,089
Isoform 3 (II) (II3+) [UniParc].

Checksum: 2F77E99B644BD4B4
Show »

FASTA24528,090
Isoform 4 (IV) [UniParc].

Checksum: 6A60137DAF657C78
Show »

FASTA37442,994
Isoform 5 (III) [UniParc].

Checksum: 2AE2865E15A82E37
Show »

FASTA31936,595

References

« Hide '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. expand/collapse author list , 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.
CCDSCCDS19188.1. [Q8K3W0-2]
CCDS19189.1. [Q8K3W0-1]
CCDS39058.1. [Q8K3W0-5]
CCDS39059.1. [Q8K3W0-4]
CCDS51461.1. [Q8K3W0-6]
RefSeqNP_653124.1. NM_144541.1. [Q8K3W0-2]
NP_851796.1. NM_181279.1. [Q8K3W0-1]
NP_851797.1. NM_181280.1. [Q8K3W0-5]
NP_851798.1. NM_181281.1. [Q8K3W0-6]
NP_851799.1. NM_181282.1. [Q8K3W0-4]
UniGeneMm.482126.

3D structure databases

ProteinModelPortalQ8K3W0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid223733. 3 interactions.

Proteomic databases

MaxQBQ8K3W0.
PaxDbQ8K3W0.
PRIDEQ8K3W0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000063813; ENSMUSP00000069133; ENSMUSG00000052139. [Q8K3W0-1]
ENSMUST00000071531; ENSMUSP00000071462; ENSMUSG00000052139. [Q8K3W0-5]
ENSMUST00000080598; ENSMUSP00000079434; ENSMUSG00000052139. [Q8K3W0-2]
ENSMUST00000114507; ENSMUSP00000110152; ENSMUSG00000052139. [Q8K3W0-6]
ENSMUST00000131995; ENSMUSP00000128351; ENSMUSG00000052139. [Q8K3W0-4]
GeneID107976.
KEGGmmu:107976.
UCSCuc008wza.1. mouse. [Q8K3W0-2]
uc008wzb.1. mouse. [Q8K3W0-1]
uc008wzc.1. mouse. [Q8K3W0-5]
uc008wze.1. mouse. [Q8K3W0-6]

Organism-specific databases

CTD9577.
MGIMGI:1333875. Bre.

Phylogenomic databases

eggNOGNOG71563.
GeneTreeENSGT00390000004208.
HOVERGENHBG071492.
InParanoidQ8CJ13.
KOK12173.
OMAHIPAFPS.
OrthoDBEOG7TJ3J9.
PhylomeDBQ8K3W0.
TreeFamTF328507.

Gene expression databases

BgeeQ8K3W0.
CleanExMM_BRE.
GenevestigatorQ8K3W0.

Family and domain databases

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

Other

ChiTaRSBRE. mouse.
NextBio359811.
PROQ8K3W0.
SOURCESearch...

Entry information

Entry nameBRE_MOUSE
AccessionPrimary (citable) accession number: Q8K3W0
Secondary accession number(s): Q497G6 expand/collapse secondary AC list , Q6P8Z2, Q8BKU1, Q8CJ13, Q8JZP0, Q8K3V9, Q8VHN1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot