P97929 (BRCA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Breast cancer type 2 susceptibility protein homolog

Alternative name(s):
Fanconi anemia group D1 protein homolog

Gene names

Name:	Brca2
Synonyms:	Fancd1

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	3329 AA.
Sequence status	Complete.
Protein existence	Evidence 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. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. 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. Interacts with both nonubiquitinated and monoubiquitinated FANCD2; this complex also includes XRCC3 and phosphorylated FANCG By similarity. Interacts with WDR16. Interacts with USP11. Interacts with DMC1. Part of a trimeric complex containing BRCA1, BRCA2 and PALB2. Interacts with PALB2. Interacts with BRCA1 only in the presence of PALB2 which serves as the bridging protein. Interacts with ROCK2 and NPM1 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 process	Cell cycle DNA damage DNA recombination DNA repair
Coding sequence diversity	Polymorphism
Disease	Tumor suppressor
Domain	Repeat
Ligand	DNA-binding
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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 cycle cytokinesis Inferred from electronic annotation. Source: Compara centrosome duplication Inferred from Biological aspect of Ancestor. Source: RefGenome chromosome organization Inferred from mutant phenotype PubMed 16859999PubMed 9660919. 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 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: Compara nucleotide-excision repair Inferred from electronic annotation. Source: Compara 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-dependent Inferred from electronic annotation. Source: Compara regulation of S phase of mitotic cell cycle Inferred from electronic annotation. Source: InterPro 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_component	BRCA2-MAGE-D1 complex Inferred from electronic annotation. Source: Compara centrosome Inferred from Biological aspect of Ancestor. Source: RefGenome cytoplasm Inferred from direct assay PubMed 11172592. Source: MGI nucleoplasm Traceable author statement. Source: Reactome secretory granule Inferred from electronic annotation. Source: Compara
Molecular_function	H3 histone acetyltransferase activity Inferred from electronic annotation. Source: Compara H4 histone acetyltransferase activity Inferred from electronic annotation. Source: Compara 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 3329

3329

Breast cancer type 2 susceptibility protein homolog

PRO_0000064985

Regions

Repeat

981 – 1015

35

BRCA2 1

Repeat

1192 – 1226

35

BRCA2 2

Repeat

1394 – 1428

35

BRCA2 3

Repeat

1491 – 1525

35

BRCA2 4

Repeat

1623 – 1657

35

BRCA2 5

Repeat

1924 – 1958

35

BRCA2 6

Repeat

2004 – 2038

35

BRCA2 7

Region

1 – 40

40

Interaction with PALB2 By similarity

Region

628 – 979

352

Interaction with NPM1 By similarity

Region

2298 – 2466

169

Interaction with FANCD2 By similarity

Amino acid modifications

Modified residue

735

1

Phosphoserine By similarity

Modified residue

3214

1

Phosphoserine; by CDK1 and CDK2 By similarity

Natural variations

Natural variant

44

1

S → F in strain: C57BL/6 and 129/Sv.

Natural variant

340

1

T → P in strain: 129/Sv.

Natural variant

377

1

N → H in strain: C57BL/6.

Natural variant

407

1

H → P in strain: C57BL/6.

Natural variant

661

1

I → V in strain: C57BL/6.

Natural variant

739

1

P → H in strain: C57BL/6.

Natural variant

1198 – 1199

2

GF → RI in strain: C57BL/6.

Natural variant

1257

1

Q → P in strain: C57BL/6.

Natural variant

1392

1

Q → R in strain: C57BL/6.

Natural variant

1520 – 1521

2

FD → CG in strain: C57BL/6.

Natural variant

1583

1

R → W in strain: C57BL/6.

Natural variant

1613

1

C → W in strain: C57BL/6.

Natural variant

1686

1

S → R in strain: C57BL/6.

Natural variant

1799

1

S → F in strain: 129/Sv.

Natural variant

1881

1

P → L in strain: C57BL/6.

Natural variant

1894

1

S → F in strain: 129/Sv.

Natural variant

2141

1

Q → K in strain: C57BL/6.

Natural variant

2392

1

S → R in strain: C57BL/6.

Natural variant

2605

1

K → Q in strain: C57BL/6.

Natural variant

2648

1

A → P in strain: C57BL/6.

Natural variant

2717

1

R → C in strain: 129/Sv.

Natural variant

2729

1

L → M in strain: 129/Sv.

Natural variant

2814

1

Q → H in strain: C57BL/6.

Natural variant

2827

1

A → P in strain: C57BL/6.

Natural variant

2907

1

S → I in strain: 129/Sv.

Natural variant

2929

1

H → L in strain: 129/Sv.

Natural variant

3058

1

A → G in strain: C57BL/6.

Natural variant

3071

1

A → G in strain: C57BL/6.

Natural variant

3081

1

K → E in strain: C57BL/6.

Natural variant

3089

1

T → S in strain: C57BL/6.

Natural variant

3105 – 3109

5

DSPKW → SQSQV in strain: C57BL/6.

Natural variant

3220

1

A → G in strain: 129/Sv.

Natural variant

3238

1

E → K in strain: 129/Sv.

Natural variant

3243

1

Missing in strain: C57BL/6.

Natural variant

3245

1

R → K in strain: 129/Sv.

Experimental info

Sequence conflict

1038

1

L → I in AAB48306. Ref.1

Secondary structure

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3329

Helix Strand Turn

Details...

Helix

2404 – 2420

17

Helix

2430 – 2435

6

Helix

2446 – 2448

3

Beta strand

2456 – 2458

3

Beta strand

2462 – 2464

3

Beta strand

2468 – 2472

5

Turn

2475 – 2480

6

Helix

2486 – 2489

4

Turn

2490 – 2492

3

Beta strand

2495 – 2497

3

Beta strand

2503 – 2505

3

Turn

2512 – 2514

3

Helix

2518 – 2527

10

Helix

2538 – 2554

17

Turn

2560 – 2562

3

Beta strand

2564 – 2569

6

Helix

2570 – 2584

15

Turn

2585 – 2587

3

Helix

2592 – 2597

6

Beta strand

2606 – 2608

3

Beta strand

2640 – 2643

4

Beta strand

2648 – 2653

6

Helix

2655 – 2662

8

Beta strand

2671 – 2674

4

Beta strand

2675 – 2677

3

Beta strand

2679 – 2681

3

Beta strand

2696 – 2699

4

Helix

2701 – 2703

3

Beta strand

2704 – 2707

4

Beta strand

2713 – 2715

3

Helix

2726 – 2728

3

Beta strand

2731 – 2733

3

Beta strand

2736 – 2746

11

Beta strand

2751 – 2754

4

Beta strand

2756 – 2758

3

Beta strand

2760 – 2763

4

Helix

2767 – 2778

12

Helix

2782 – 2791

10

Helix

2813 – 2817

5

Helix

2822 – 2830

9

Beta strand

2833 – 2835

3

Turn

2836 – 2840

5

Beta strand

2848 – 2850

3

Turn

2851 – 2853

3

Helix

2855 – 2858

4

Helix

2861 – 2871

11

Helix

2873 – 2876

4

Turn

2877 – 2881

5

Beta strand

2889 – 2900

12

Beta strand

2904 – 2910

7

Helix

2913 – 2918

6

Beta strand

2924 – 2930

7

Beta strand

2938 – 2940

3

Beta strand

2945 – 2957

13

Helix

2961 – 2964

4

Turn

2965 – 2967

3

Helix

2977 – 2980

4

Beta strand

2981 – 2983

3

Turn

2986 – 2989

4

Beta strand

2990 – 3001

12

Beta strand

3004 – 3006

3

Beta strand

3009 – 3013

5

Beta strand

3015 – 3017

3

Beta strand

3019 – 3026

8

Beta strand

3037 – 3044

8

Beta strand

3050 – 3052

3

Beta strand

3056 – 3058

3

Beta strand

3063 – 3067

5

Turn

3071 – 3073

3

Helix

3074 – 3080

7

Helix

3082 – 3085

4

Helix

3090 – 3102

13

Sequences

	Sequence		Length	Mass (Da)
	P97929 [UniParc]. Last modified October 3, 2012. Version 2. Checksum: 50A32E8BADE2CF7E	FASTA	3,329	370,664
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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.

IPI

IPI00314969.

PIR

T30835.
T30904.
T42205.

RefSeq

NP_001074470.1. NM_001081001.1.
NP_033895.2. NM_009765.2.

UniGene

Mm.236256.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MIU	X-ray	3.10	A	2378-3115	[»]
1MJE	X-ray	3.50	A	2378-3113	[»]

ProteinModelPortal

P97929.

SMR

P97929. Positions 1493-1524, 2399-3103.

ModBase

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Protein-protein interaction databases

IntAct

P97929. 1 interaction.

MINT

MINT-205603.

PTM databases

PhosphoSite

P97929.

Proteomic databases

PRIDE

P97929.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENSMUST00000044620; ENSMUSP00000038576; ENSMUSG00000041147.

GeneID

12190.

KEGG

mmu:12190.

UCSC

uc009aty.1. mouse.

Organism-specific databases

CTD

675.

MGI

MGI:109337. Brca2.

Phylogenomic databases

eggNOG

NOG331296.

GeneTree

ENSGT00390000003602.

HOGENOM

HOG000139693.

HOVERGEN

HBG050731.

InParanoid

P97929.

KO

K08775.

OMA

LGFHTAS.

OrthoDB

EOG4ZCT3K.

Enzyme and pathway databases

Reactome

REACT_120463. Meiosis.
REACT_27235. Meiotic Recombination (mouse).

Gene expression databases

CleanEx

MM_BRCA2.

Genevestigator

P97929.

GermOnline

ENSMUSG00000041147. Mus musculus.

Family and domain databases

Gene3D

2.40.50.140. 4 hits.

InterPro

IPR015525. 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]

PANTHER

PTHR11289. PTHR11289. 1 hit.

Pfam

PF09169. 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]

PIRSF

PIRSF002397. BRCA2. 1 hit.

SUPFAM

SSF81872. BRCA2_helical. 1 hit.
SSF50249. Nucleic_acid_OB. 3 hits.

PROSITE

PS50138. BRCA2_REPEAT. 6 hits.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

P97929.

NextBio

280585.

SOURCE

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Entry information

Entry name

BRCA2_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program