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P97929 (BRCA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Breast cancer type 2 susceptibility protein homolog
Alternative name(s):
Fanconi anemia group D1 protein homolog
Gene names
Name:Brca2
Synonyms:Fancd1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length3329 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication By similarity.

Subunit structure

Monomer and dimer. Interacts with RAD51; regulates RAD51 recruitment and function at sites of DNA repair. Interacts with DSS1, WDR16, USP11, DMC1, ROCK2 and NPM1. Interacts with both nonubiquitinated and monoubiquitinated FANCD2; this complex also includes XRCC3 and phosphorylated FANCG. Part of a BRCA complex containing BRCA1, BRCA2 and PALB2. Interacts directly with PALB2 which may serve as a scaffold for a HR complex containing PALB2, BRCA2, RAD51C, RAD51 and XRCC3. Interacts with BRCA1 only in the presence of PALB2 which serves as the bridging protein. Interacts with POLH; the interaction is direct By similarity.

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Nucleus By similarity.

Tissue specificity

Widely expressed. Highest expression in cerebellum, testis, ileum, appendix, epididymis, ovary and mammary gland. No expression in lung.

Developmental stage

In the mammary gland, expression increases dramatically during pregnancy.

Post-translational modification

Phosphorylation by CHEK1 and CHEK2 regulates interaction with RAD51. Phosphorylation at Ser-3214 by CDK1 and CDK2 is low in S phase when recombination is active, but increases as cells progress towards mitosis; this phosphorylation prevents homologous recombination-dependent repair during S phase and G2 by inhibiting RAD51 binding By similarity.

Ubiquitinated in the absence of DNA damage; this does not lead to proteasomal degradation. In contrast, ubiquitination in response to DNA damage leads to proteasomal degradation By similarity.

Sequence similarities

Contains 7 BRCA2 repeats.

Ontologies

Keywords
   Biological processCell cycle
DNA damage
DNA recombination
DNA repair
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseTumor suppressor
   DomainRepeat
   LigandDNA-binding
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator

Inferred from mutant phenotype PubMed 8738145. Source: MGI

brain development

Inferred from mutant phenotype PubMed 17476307. Source: MGI

cell aging

Inferred from mutant phenotype PubMed 9699678. Source: MGI

cell proliferation

Inferred from mutant phenotype PubMed 16859999PubMed 17476307PubMed 9171368PubMed 9398843PubMed 9660919. Source: MGI

cellular response to DNA damage stimulus

Inferred from direct assay PubMed 12410562. Source: UniProtKB

centrosome duplication

Inferred from Biological aspect of Ancestor. Source: RefGenome

chordate embryonic development

Inferred from mutant phenotype PubMed 9171368. Source: MGI

chromosome organization

Inferred from mutant phenotype PubMed 16859999PubMed 9660919. Source: MGI

cytokinesis

Inferred from electronic annotation. Source: Ensembl

double-strand break repair

Inferred from mutant phenotype PubMed 17476307PubMed 9398843. Source: MGI

double-strand break repair via homologous recombination

Inferred from mutant phenotype PubMed 15485900. Source: MGI

female gonad development

Inferred from mutant phenotype PubMed 9398843. Source: MGI

hemopoiesis

Inferred from mutant phenotype PubMed 16859999. Source: MGI

inner cell mass cell proliferation

Inferred from mutant phenotype PubMed 9171369. Source: MGI

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from genetic interaction PubMed 17476307. Source: MGI

intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from mutant phenotype PubMed 15735671. Source: MGI

male meiosis I

Inferred from mutant phenotype PubMed 14660434. Source: MGI

negative regulation of mammary gland epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

nucleotide-excision repair

Inferred from electronic annotation. Source: Ensembl

oocyte maturation

Inferred from mutant phenotype PubMed 14660434. Source: MGI

positive regulation of mitotic cell cycle

Inferred from mutant phenotype PubMed 9660919. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

regulation of cell proliferation

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of cytokinesis

Inferred from mutant phenotype PubMed 15375219. Source: MGI

replication fork protection

Inferred from mutant phenotype PubMed 14681210. Source: MGI

response to UV-C

Inferred from mutant phenotype PubMed 9660919. Source: MGI

response to X-ray

Inferred from mutant phenotype PubMed 16859999PubMed 9398843PubMed 9660919. Source: MGI

response to gamma radiation

Inferred from mutant phenotype PubMed 9126738PubMed 9699678. Source: MGI

spermatogenesis

Inferred from mutant phenotype PubMed 9398843. Source: MGI

   Cellular_componentBRCA2-MAGE-D1 complex

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 11172592. Source: MGI

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 11172592PubMed 11477095. Source: MGI

secretory granule

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionH3 histone acetyltransferase activity

Inferred from electronic annotation. Source: Ensembl

H4 histone acetyltransferase activity

Inferred from electronic annotation. Source: Ensembl

gamma-tubulin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

single-stranded DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 33293329Breast cancer type 2 susceptibility protein homolog
PRO_0000064985

Regions

Repeat981 – 101535BRCA2 1
Repeat1192 – 122635BRCA2 2
Repeat1394 – 142835BRCA2 3
Repeat1491 – 152535BRCA2 4
Repeat1623 – 165735BRCA2 5
Repeat1924 – 195835BRCA2 6
Repeat2004 – 203835BRCA2 7
Region1 – 4040Interaction with PALB2 By similarity
Region628 – 979352Interaction with NPM1 By similarity
Region2298 – 2466169Interaction with FANCD2 By similarity

Amino acid modifications

Modified residue7351Phosphoserine By similarity
Modified residue32141Phosphoserine; by CDK1 and CDK2 By similarity

Natural variations

Natural variant441S → F in strain: C57BL/6 and 129/Sv.
Natural variant3401T → P in strain: 129/Sv.
Natural variant3771N → H in strain: C57BL/6.
Natural variant4071H → P in strain: C57BL/6.
Natural variant6611I → V in strain: C57BL/6.
Natural variant7391P → H in strain: C57BL/6.
Natural variant1198 – 11992GF → RI in strain: C57BL/6.
Natural variant12571Q → P in strain: C57BL/6.
Natural variant13921Q → R in strain: C57BL/6.
Natural variant1520 – 15212FD → CG in strain: C57BL/6.
Natural variant15831R → W in strain: C57BL/6.
Natural variant16131C → W in strain: C57BL/6.
Natural variant16861S → R in strain: C57BL/6.
Natural variant17991S → F in strain: 129/Sv.
Natural variant18811P → L in strain: C57BL/6.
Natural variant18941S → F in strain: 129/Sv.
Natural variant21411Q → K in strain: C57BL/6.
Natural variant23921S → R in strain: C57BL/6.
Natural variant26051K → Q in strain: C57BL/6.
Natural variant26481A → P in strain: C57BL/6.
Natural variant27171R → C in strain: 129/Sv.
Natural variant27291L → M in strain: 129/Sv.
Natural variant28141Q → H in strain: C57BL/6.
Natural variant28271A → P in strain: C57BL/6.
Natural variant29071S → I in strain: 129/Sv.
Natural variant29291H → L in strain: 129/Sv.
Natural variant30581A → G in strain: C57BL/6.
Natural variant30711A → G in strain: C57BL/6.
Natural variant30811K → E in strain: C57BL/6.
Natural variant30891T → S in strain: C57BL/6.
Natural variant3105 – 31095DSPKW → SQSQV in strain: C57BL/6.
Natural variant32201A → G in strain: 129/Sv.
Natural variant32381E → K in strain: 129/Sv.
Natural variant32431Missing in strain: C57BL/6.
Natural variant32451R → K in strain: 129/Sv.

Experimental info

Sequence conflict10381L → I in AAB48306. Ref.1

Secondary structure

..................................................................................................................................... 3329
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P97929 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 50A32E8BADE2CF7E

FASTA3,329370,664
        10         20         30         40         50         60 
MPVEYKRRPT FWEIFKARCS TADLGPISLN WFEELSSEAP PYNSEPPEES EYKPHGYEPQ 

        70         80         90        100        110        120 
LFKTPQRNPP YHQFASTPIM FKERSQTLPL DQSPFRELGK VVASSKHKTH SKKKTKVDPV 

       130        140        150        160        170        180 
VDVASPPLKS CLSESPLTLR CTQAVLQREK PVVSGSLFYT PKLKEGQTPK PISESLGVEV 

       190        200        210        220        230        240 
DPDMSWTSSL ATPPTLSSTV LIARDEEARS SVTPADSPAT LKSCFSNHNE SPQKNDRSVP 

       250        260        270        280        290        300 
SVIDSENKNQ QEAFSQGLGK MLGDSSGKRN SFKDCLRKPI PNILEDGETA VDTSEEDSFS 

       310        320        330        340        350        360 
LCFPKRRTRN LQKMRMGKTR KKIFSETRTD ELSEEARRQT DDKNSFVFEM ELRESDPLDP 

       370        380        390        400        410        420 
GVTSQKPFYS QNEEICNEAV QCSDSRWSQS NLSGLNETQT GKITLPHISS HSQNISEDFI 

       430        440        450        460        470        480 
DMKKEGTGSI TSEKSLPHIS SLPEPEKMFS EETVVDKEHE GQHFESLEDS IAGKQMVSRT 

       490        500        510        520        530        540 
SQAACLSPSI RKSIFKMREP LDETLGTVFS DSMTNSTFTE EHEASACGLG ILTACSQRED 

       550        560        570        580        590        600 
SICPSSVDTG SWPTTLTDTS ATVKNAGLIS TLKNKKRKFI YSVSDDASLQ GKKLQTHRQL 

       610        620        630        640        650        660 
ELTNLSAQLE ASAFEVPLTF TNVNSGIPDS SDKKRCLPND PEEPSLTNSF GTATSKEISY 

       670        680        690        700        710        720 
IHALISQDLN DKEAIVIEEK PQPYTAREAD FLLCLPERTC ENDQKSPKVS NGKEKVLVSA 

       730        740        750        760        770        780 
CLPSAVQLSS ISFESQENPL GDHNGTSTLK LTPSSKLPLS KADMVSREKM CKMPEKLQCE 

       790        800        810        820        830        840 
SCKVNIELSK NILEVNEICI LSENSKTPGL LPPGENIIEV ASSMKSQFNQ NAKIVIQKDQ 

       850        860        870        880        890        900 
KGSPFISEVA VNMNSEELFP DSGNNFAFQV TNKCNKPDLG SSVELQEEDL SHTQGPSLKN 

       910        920        930        940        950        960 
SPMAVDEDVD DAHAAQVLIT KDSDSLAVVH DYTEKSRNNI EQHQKGTEDK DFKSNSSLNM 

       970        980        990       1000       1010       1020 
KSDGNSDCSD KWSEFLDPVL NHNFGGSFRT ASNKEIKLSE HNVKKSKMFF KDIEEQYPTR 

      1030       1040       1050       1060       1070       1080 
LACIDIVNTL PLANQKKLSE PHIFDLKSVT TVSTQSHNQS SVSHEDTDTA PQMLSSKQDF 

      1090       1100       1110       1120       1130       1140 
HSNNLTTSQK AEITELSTIL EESGSQFEFT QFRKPSHIAQ NTSEVPGNQM VVLSTASKEW 

      1150       1160       1170       1180       1190       1200 
KDTDLHLPVD PSVGQTDHSK QFEGSAGVKQ SFPHLLEDTC NKNTSCFLPN INEMEFGGFC 

      1210       1220       1230       1240       1250       1260 
SALGTKLSVS NEALRKAMKL FSDIENSEEP SAKVGPRGFS SSAHHDSVAS VFKIKKQNTE 

      1270       1280       1290       1300       1310       1320 
KSFDEKSSKC QVTLQNNIEM TTCIFVGRNP EKYIKNTKHE DSYTSSQRNN LENSDGSMSS 

      1330       1340       1350       1360       1370       1380 
TSGPVYIHKG DSDLPADQGS KCPESCTQYA REENTQIKEN ISDLTCLEIM KAEETCMKSS 

      1390       1400       1410       1420       1430       1440 
DKKQLPSDKM EQNIKEFNIS FQTASGKNTR VSKESLNKSV NIFNRETDEL TVISDSLNSK 

      1450       1460       1470       1480       1490       1500 
ILHGINKDKM HTSCHKKAIS IKKVFEDHFP IVTVSQLPAQ QHPEYEIEST KEPTLLSFHT 

      1510       1520       1530       1540       1550       1560 
ASGKKVKIMQ ESLDKVKNLF DETQYVRKTA SFSQGSKPLK DSKKELTLAY EKIEVTASKC 

      1570       1580       1590       1600       1610       1620 
EEMQNFVSKE TEMLPQQNYH MYRQTENLKT SNGTSSKVQE NIENNVEKNP RICCICQSSY 

      1630       1640       1650       1660       1670       1680 
PVTEDSALAY YTEDSRKTCV RESSLSKGRK WLREQGDKLG TRNTIKIECV KEHTEDFAGN 

      1690       1700       1710       1720       1730       1740 
ASYEHSLVII RTEIDTNHVS ENQVSTLLSD PNVCHSYLSQ SSFCHCDDMH NDSGYFLKNK 

      1750       1760       1770       1780       1790       1800 
IDSDVPPDMK NAEGNTISPR VSATKERNLH PQTINEYCVQ KLETNTSPHA NKDVAIDPSL 

      1810       1820       1830       1840       1850       1860 
LDSRNCKVGS LVFITAHSQE TERTKEIVTD NCYKIVEQNR QSKPDTCQTS CHKVLDDSKD 

      1870       1880       1890       1900       1910       1920 
FICPSSSGDV CINSRKDSFC PHNEQILQHN QSMSGLKKAA TPPVGLETWD TSKSIREPPQ 

      1930       1940       1950       1960       1970       1980 
AAHPSRTYGI FSTASGKAIQ VSDASLEKAR QVFSEMDGDA KQLSSMVSLE GNEKPHHSVK 

      1990       2000       2010       2020       2030       2040 
RENSVVHSTQ GVLSLPKPLP GNVNSSVFSG FSTAGGKLVT VSESALHKVK GMLEEFDLIR 

      2050       2060       2070       2080       2090       2100 
TEHTLQHSPI PEDVSKILPQ PCAEIRTPEY PVNSKLQKTY NDKSSLPSNY KESGSSGNTQ 

      2110       2120       2130       2140       2150       2160 
SIEVSLQLSQ MERNQDTQLV LGTKVSHSKA NLLGKEQTLP QNIKVKTDEM KTFSDVPVKT 

      2170       2180       2190       2200       2210       2220 
NVGEYYSKES ENYFETEAVE SAKAFMEDDE LTDSEQTHAK CSLFTCPQNE TLFNSRTRKR 

      2230       2240       2250       2260       2270       2280 
GGVTVDAVGQ PPIKRSLLNE FDRIIESKGK SLTPSKSTPD GTVKDRSLFT HHMSLEPVTC 

      2290       2300       2310       2320       2330       2340 
GPFCSSKERQ GAQRPHLTSP AQELLSKGHP WRHSALEKSP SSPIVSILPA HDVSATRTER 

      2350       2360       2370       2380       2390       2400 
TRHSGKSTKV FVPPFKMKSQ FHGDEHFNSK NVNLEGKNQK STDGDREDGN DSHVRQFNKD 

      2410       2420       2430       2440       2450       2460 
LMSSLQSARD LQDMRIKNKE RRHLRLQPGS LYLTKSSTLP RISLQAAVGD RAPSACSPKQ 

      2470       2480       2490       2500       2510       2520 
LYIYGVSKEC INVNSKNAEY FQFDIQDHFG KEDLCAGKGF QLADGGWLIP SNDGKAGKEE 

      2530       2540       2550       2560       2570       2580 
FYRALCDTPG VDPKLISSIW VANHYRWIVW KLAAMEFAFP KEFANRCLNP ERVLLQLKYR 

      2590       2600       2610       2620       2630       2640 
YDVEIDNSRR SALKKILERD DTAAKTLVLC ISDIISPSTK VSETSGGKTS GEDANKVDTI 

      2650       2660       2670       2680       2690       2700 
ELTDGWYAVR AQLDPPLMAL VKSGKLTVGQ KIITQGAELV GSPDACAPLE APDSLRLKIS 

      2710       2720       2730       2740       2750       2760 
ANSTRPARWH SRLGFFRDPR PFPLPLSSLF SDGGNVGCVD IIVQRVYPLQ WVEKTVSGLY 

      2770       2780       2790       2800       2810       2820 
IFRSEREEEK EALRFAEAQQ KKLEALFTKV HTEFKDHEED TTQRCVLSRT LTRQQVHALQ 

      2830       2840       2850       2860       2870       2880 
DGAELYAAVQ YASDPDHLEA CFSEEQLRAL NNYRQMLNDK KQARIQSEFR KALESAEKEE 

      2890       2900       2910       2920       2930       2940 
GLSRDVTTVW KLRVTSYKKK EKSALLSIWR PSSDLSSLLT EGKRYRIYHL AVSKSKSKFE 

      2950       2960       2970       2980       2990       3000 
RPSIQLTATK RTQYQQLPVS SETLLQVYQP RESLHFSRLS DPAFQPPCSE VDVVGVVVSV 

      3010       3020       3030       3040       3050       3060 
VKPIGLAPLV YLSDECLNLL VVKFGIDLNE DIKPRVLIAA SNLQCQPEST SGVPTLFAGH 

      3070       3080       3090       3100       3110       3120 
FSIFSASPKE AYFQEKVNNL KHAIENIDTF YKEAEKKLIH VLEGDSPKWS TPNKDPTREP 

      3130       3140       3150       3160       3170       3180 
HAASTCCASD LLGSGGQFLR ISPTGQQSYQ SPLSHCTLKG KSMPLAHSAQ MAAKSWSGEN 

      3190       3200       3210       3220       3230       3240 
EIDDPKTCRK RRALDFLSRL PLPSPVSPIC TFVSPAAQKA FQPPRSCGTK YATPIKKEPS 

      3250       3260       3270       3280       3290       3300 
SPRRRTPFQK TSGVSLPDCD SVADEELALL STQALTPDSV GGNEQAFPGD STRNPQPAQR 

      3310       3320 
PDQQVGPRSR KESLRDCRGD SSEKLAVES 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, chromosomal mapping and expression pattern of the mouse Brca2 gene."
Connor F., Smith A., Wooster R., Stratton M., Dixon A., Campbell E., Tait T.M., Freeman T., Ashworth A.
Hum. Mol. Genet. 6:291-300(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129.
[2]"Murine Brca2: sequence, map position, and expression pattern."
Sharan S.K., Bradley A.
Genomics 40:234-241(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[3]"Characterization of the rat and mouse homologues of the BRCA2 breast cancer susceptibility gene."
McAllister K.A., Haugen-Strano A., Hagevik S., Brownlee H.A., Collins N.K., Futreal P.A., Bennett L.M., Wiseman R.W.
Cancer Res. 57:3121-3125(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129/Sv.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"Brca2 is coordinately regulated with Brca1 during proliferation and differentiation in mammary epithelial cells."
Rajan J.V., Wang M., Marquis S.T., Chodosh L.A.
Proc. Natl. Acad. Sci. U.S.A. 93:13078-13083(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-200.
[6]"Genetic mapping of the Brca2 breast cancer susceptibility gene on mouse chromosome 5."
McAllister K.A., Ramachandran S., Haugen-Strano A., Fiedorek F.T. Jr., Wiseman R.W.
Mamm. Genome 8:540-541(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 569-625.
[7]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 784-790, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U82270 mRNA. Translation: AAB48306.1.
U65594 mRNA. Translation: AAC23702.1.
U89652 mRNA. Translation: AAB71377.1.
AC154885 Genomic DNA. No translation available.
U72947 mRNA. Translation: AAB40720.1.
U89503 Genomic DNA. Translation: AAC53276.1.
PIRT30835.
T30904.
T42205.
RefSeqNP_001074470.1. NM_001081001.2.
NP_033895.2. NM_009765.3.
UniGeneMm.236256.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MIUX-ray3.10A2378-3115[»]
1MJEX-ray3.50A2378-3113[»]
ProteinModelPortalP97929.
SMRP97929. Positions 1493-1524, 2399-3103.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198384. 5 interactions.
IntActP97929. 2 interactions.

PTM databases

PhosphoSiteP97929.

Proteomic databases

PRIDEP97929.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000044620; ENSMUSP00000038576; ENSMUSG00000041147.
GeneID12190.
KEGGmmu:12190.

Organism-specific databases

CTD675.
MGIMGI:109337. Brca2.

Phylogenomic databases

eggNOGNOG331296.
GeneTreeENSGT00390000003602.
HOGENOMHOG000139693.
HOVERGENHBG050731.
InParanoidP97929.
KOK08775.
OMALGFHTAS.
OrthoDBEOG75TMB1.
TreeFamTF105041.

Enzyme and pathway databases

ReactomeREACT_198624. Meiosis.
REACT_27235. Meiotic Recombination.

Gene expression databases

ArrayExpressP97929.
CleanExMM_BRCA2.
GenevestigatorP97929.

Family and domain databases

Gene3D2.40.50.140. 4 hits.
InterProIPR015525. BRCA2.
IPR015187. BRCA2_OB_1.
IPR015188. BRCA2_OB_3.
IPR002093. BRCA2_repeat.
IPR015252. DNA_recomb/repair_BRCA2_hlx.
IPR012340. NA-bd_OB-fold.
IPR015205. Tower.
[Graphical view]
PANTHERPTHR11289. PTHR11289. 1 hit.
PfamPF09169. BRCA-2_helical. 1 hit.
PF09103. BRCA-2_OB1. 1 hit.
PF09104. BRCA-2_OB3. 1 hit.
PF00634. BRCA2. 7 hits.
PF09121. Tower. 1 hit.
[Graphical view]
PIRSFPIRSF002397. BRCA2. 1 hit.
SUPFAMSSF50249. SSF50249. 4 hits.
SSF81872. SSF81872. 1 hit.
PROSITEPS50138. BRCA2_REPEAT. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP97929.
NextBio280585.
PROP97929.
SOURCESearch...

Entry information

Entry nameBRCA2_MOUSE
AccessionPrimary (citable) accession number: P97929
Secondary accession number(s): F8VPU5, O35922, P97383
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: October 3, 2012
Last modified: April 16, 2014
This is version 129 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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