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P97929

- BRCA2_MOUSE

UniProt

P97929 - BRCA2_MOUSE

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Protein

Breast cancer type 2 susceptibility protein homolog

Gene

Brca2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and DSS1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability, independently of its known role in homologous recombination (By similarity).By similarity

GO - Molecular functioni

  1. gamma-tubulin binding Source: RefGenome
  2. H3 histone acetyltransferase activity Source: Ensembl
  3. H4 histone acetyltransferase activity Source: Ensembl
  4. single-stranded DNA binding Source: RefGenome

GO - Biological processi

  1. brain development Source: MGI
  2. cell aging Source: MGI
  3. cell proliferation Source: MGI
  4. cellular response to DNA damage stimulus Source: UniProtKB
  5. centrosome duplication Source: RefGenome
  6. chordate embryonic development Source: MGI
  7. chromosome organization Source: MGI
  8. cytokinesis Source: Ensembl
  9. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: MGI
  10. double-strand break repair Source: MGI
  11. double-strand break repair via homologous recombination Source: MGI
  12. female gonad development Source: MGI
  13. hemopoiesis Source: MGI
  14. inner cell mass cell proliferation Source: MGI
  15. intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
  16. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: MGI
  17. male meiosis I Source: MGI
  18. negative regulation of mammary gland epithelial cell proliferation Source: Ensembl
  19. nucleotide-excision repair Source: Ensembl
  20. oocyte maturation Source: MGI
  21. positive regulation of mitotic cell cycle Source: MGI
  22. positive regulation of transcription, DNA-templated Source: Ensembl
  23. regulation of cell proliferation Source: RefGenome
  24. regulation of cytokinesis Source: MGI
  25. regulation of transcription, DNA-templated Source: RefGenome
  26. replication fork protection Source: MGI
  27. response to gamma radiation Source: MGI
  28. response to UV-C Source: MGI
  29. response to X-ray Source: MGI
  30. spermatogenesis Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_198629. Meiotic recombination.
REACT_27235. Meiotic Recombination.

Names & Taxonomyi

Protein namesi
Recommended name:
Breast cancer type 2 susceptibility protein homolog
Alternative name(s):
Fanconi anemia group D1 protein homolog
Gene namesi
Name:Brca2
Synonyms:Fancd1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:109337. Brca2.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Nucleus By similarity

GO - Cellular componenti

  1. BRCA2-MAGE-D1 complex Source: Ensembl
  2. centrosome Source: UniProtKB
  3. cytoplasm Source: MGI
  4. nucleoplasm Source: Reactome
  5. nucleus Source: MGI
  6. secretory granule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 33293329Breast cancer type 2 susceptibility protein homologPRO_0000064985Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei735 – 7351PhosphoserineBy similarity
Modified residuei3214 – 32141Phosphoserine; by CDK1 and CDK2By similarity

Post-translational modificationi

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).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).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP97929.

PTM databases

PhosphoSiteiP97929.

Expressioni

Tissue specificityi

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

Developmental stagei

In the mammary gland, expression increases dramatically during pregnancy.

Gene expression databases

CleanExiMM_BRCA2.
ExpressionAtlasiP97929. baseline and differential.
GenevestigatoriP97929.

Interactioni

Subunit structurei

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. Interacts with the TREX-2 complex subunits PCID2 and DSS1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi198384. 5 interactions.
IntActiP97929. 2 interactions.

Structurei

Secondary structure

1
3329
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2404 – 242017
Helixi2430 – 24356
Helixi2446 – 24483
Beta strandi2456 – 24583
Beta strandi2462 – 24643
Beta strandi2468 – 24725
Turni2475 – 24806
Helixi2486 – 24894
Turni2490 – 24923
Beta strandi2495 – 24973
Beta strandi2503 – 25053
Turni2512 – 25143
Helixi2518 – 252710
Helixi2538 – 255417
Turni2560 – 25623
Beta strandi2564 – 25696
Helixi2570 – 258415
Turni2585 – 25873
Helixi2592 – 25976
Beta strandi2606 – 26083
Beta strandi2640 – 26434
Beta strandi2648 – 26536
Helixi2655 – 26628
Beta strandi2671 – 26744
Beta strandi2675 – 26773
Beta strandi2679 – 26813
Beta strandi2696 – 26994
Helixi2701 – 27033
Beta strandi2704 – 27074
Beta strandi2713 – 27153
Helixi2726 – 27283
Beta strandi2731 – 27333
Beta strandi2736 – 274611
Beta strandi2751 – 27544
Beta strandi2756 – 27583
Beta strandi2760 – 27634
Helixi2767 – 277812
Helixi2782 – 279110
Helixi2813 – 28175
Helixi2822 – 28309
Beta strandi2833 – 28353
Turni2836 – 28405
Beta strandi2848 – 28503
Turni2851 – 28533
Helixi2855 – 28584
Helixi2861 – 287111
Helixi2873 – 28764
Turni2877 – 28815
Beta strandi2889 – 290012
Beta strandi2904 – 29107
Helixi2913 – 29186
Beta strandi2924 – 29307
Beta strandi2938 – 29403
Beta strandi2945 – 295713
Helixi2961 – 29644
Turni2965 – 29673
Helixi2977 – 29804
Beta strandi2981 – 29833
Turni2986 – 29894
Beta strandi2990 – 300112
Beta strandi3004 – 30063
Beta strandi3009 – 30135
Beta strandi3015 – 30173
Beta strandi3019 – 30268
Beta strandi3037 – 30448
Beta strandi3050 – 30523
Beta strandi3056 – 30583
Beta strandi3063 – 30675
Turni3071 – 30733
Helixi3074 – 30807
Helixi3082 – 30854
Helixi3090 – 310213

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MIUX-ray3.10A2378-3115[»]
1MJEX-ray3.50A2378-3113[»]
ProteinModelPortaliP97929.
SMRiP97929. Positions 1493-1524, 2399-3103.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP97929.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati981 – 101535BRCA2 1Add
BLAST
Repeati1192 – 122635BRCA2 2Add
BLAST
Repeati1394 – 142835BRCA2 3Add
BLAST
Repeati1491 – 152535BRCA2 4Add
BLAST
Repeati1623 – 165735BRCA2 5Add
BLAST
Repeati1924 – 195835BRCA2 6Add
BLAST
Repeati2004 – 203835BRCA2 7Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4040Interaction with PALB2By similarityAdd
BLAST
Regioni628 – 979352Interaction with NPM1By similarityAdd
BLAST
Regioni2298 – 2466169Interaction with FANCD2By similarityAdd
BLAST

Sequence similaritiesi

Contains 7 BRCA2 repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG331296.
GeneTreeiENSGT00390000003602.
HOGENOMiHOG000139693.
HOVERGENiHBG050731.
InParanoidiP97929.
KOiK08775.
OMAiLGFHTAS.
OrthoDBiEOG75TMB1.
TreeFamiTF105041.

Family and domain databases

Gene3Di2.40.50.140. 4 hits.
InterProiIPR015525. BRCA2.
IPR015252. BRCA2_hlx.
IPR015187. BRCA2_OB_1.
IPR015188. BRCA2_OB_3.
IPR002093. BRCA2_repeat.
IPR012340. NA-bd_OB-fold.
IPR015205. Tower.
[Graphical view]
PANTHERiPTHR11289. PTHR11289. 1 hit.
PfamiPF09169. 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]
PIRSFiPIRSF002397. BRCA2. 1 hit.
SUPFAMiSSF50249. SSF50249. 4 hits.
SSF81872. SSF81872. 1 hit.
PROSITEiPS50138. BRCA2_REPEAT. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P97929-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPVEYKRRPT FWEIFKARCS TADLGPISLN WFEELSSEAP PYNSEPPEES
60 70 80 90 100
EYKPHGYEPQ LFKTPQRNPP YHQFASTPIM FKERSQTLPL DQSPFRELGK
110 120 130 140 150
VVASSKHKTH SKKKTKVDPV VDVASPPLKS CLSESPLTLR CTQAVLQREK
160 170 180 190 200
PVVSGSLFYT PKLKEGQTPK PISESLGVEV DPDMSWTSSL ATPPTLSSTV
210 220 230 240 250
LIARDEEARS SVTPADSPAT LKSCFSNHNE SPQKNDRSVP SVIDSENKNQ
260 270 280 290 300
QEAFSQGLGK MLGDSSGKRN SFKDCLRKPI PNILEDGETA VDTSEEDSFS
310 320 330 340 350
LCFPKRRTRN LQKMRMGKTR KKIFSETRTD ELSEEARRQT DDKNSFVFEM
360 370 380 390 400
ELRESDPLDP GVTSQKPFYS QNEEICNEAV QCSDSRWSQS NLSGLNETQT
410 420 430 440 450
GKITLPHISS HSQNISEDFI DMKKEGTGSI TSEKSLPHIS SLPEPEKMFS
460 470 480 490 500
EETVVDKEHE GQHFESLEDS IAGKQMVSRT SQAACLSPSI RKSIFKMREP
510 520 530 540 550
LDETLGTVFS DSMTNSTFTE EHEASACGLG ILTACSQRED SICPSSVDTG
560 570 580 590 600
SWPTTLTDTS ATVKNAGLIS TLKNKKRKFI YSVSDDASLQ GKKLQTHRQL
610 620 630 640 650
ELTNLSAQLE ASAFEVPLTF TNVNSGIPDS SDKKRCLPND PEEPSLTNSF
660 670 680 690 700
GTATSKEISY IHALISQDLN DKEAIVIEEK PQPYTAREAD FLLCLPERTC
710 720 730 740 750
ENDQKSPKVS NGKEKVLVSA CLPSAVQLSS ISFESQENPL GDHNGTSTLK
760 770 780 790 800
LTPSSKLPLS KADMVSREKM CKMPEKLQCE SCKVNIELSK NILEVNEICI
810 820 830 840 850
LSENSKTPGL LPPGENIIEV ASSMKSQFNQ NAKIVIQKDQ KGSPFISEVA
860 870 880 890 900
VNMNSEELFP DSGNNFAFQV TNKCNKPDLG SSVELQEEDL SHTQGPSLKN
910 920 930 940 950
SPMAVDEDVD DAHAAQVLIT KDSDSLAVVH DYTEKSRNNI EQHQKGTEDK
960 970 980 990 1000
DFKSNSSLNM KSDGNSDCSD KWSEFLDPVL NHNFGGSFRT ASNKEIKLSE
1010 1020 1030 1040 1050
HNVKKSKMFF KDIEEQYPTR LACIDIVNTL PLANQKKLSE PHIFDLKSVT
1060 1070 1080 1090 1100
TVSTQSHNQS SVSHEDTDTA PQMLSSKQDF HSNNLTTSQK AEITELSTIL
1110 1120 1130 1140 1150
EESGSQFEFT QFRKPSHIAQ NTSEVPGNQM VVLSTASKEW KDTDLHLPVD
1160 1170 1180 1190 1200
PSVGQTDHSK QFEGSAGVKQ SFPHLLEDTC NKNTSCFLPN INEMEFGGFC
1210 1220 1230 1240 1250
SALGTKLSVS NEALRKAMKL FSDIENSEEP SAKVGPRGFS SSAHHDSVAS
1260 1270 1280 1290 1300
VFKIKKQNTE KSFDEKSSKC QVTLQNNIEM TTCIFVGRNP EKYIKNTKHE
1310 1320 1330 1340 1350
DSYTSSQRNN LENSDGSMSS TSGPVYIHKG DSDLPADQGS KCPESCTQYA
1360 1370 1380 1390 1400
REENTQIKEN ISDLTCLEIM KAEETCMKSS DKKQLPSDKM EQNIKEFNIS
1410 1420 1430 1440 1450
FQTASGKNTR VSKESLNKSV NIFNRETDEL TVISDSLNSK ILHGINKDKM
1460 1470 1480 1490 1500
HTSCHKKAIS IKKVFEDHFP IVTVSQLPAQ QHPEYEIEST KEPTLLSFHT
1510 1520 1530 1540 1550
ASGKKVKIMQ ESLDKVKNLF DETQYVRKTA SFSQGSKPLK DSKKELTLAY
1560 1570 1580 1590 1600
EKIEVTASKC EEMQNFVSKE TEMLPQQNYH MYRQTENLKT SNGTSSKVQE
1610 1620 1630 1640 1650
NIENNVEKNP RICCICQSSY PVTEDSALAY YTEDSRKTCV RESSLSKGRK
1660 1670 1680 1690 1700
WLREQGDKLG TRNTIKIECV KEHTEDFAGN ASYEHSLVII RTEIDTNHVS
1710 1720 1730 1740 1750
ENQVSTLLSD PNVCHSYLSQ SSFCHCDDMH NDSGYFLKNK IDSDVPPDMK
1760 1770 1780 1790 1800
NAEGNTISPR VSATKERNLH PQTINEYCVQ KLETNTSPHA NKDVAIDPSL
1810 1820 1830 1840 1850
LDSRNCKVGS LVFITAHSQE TERTKEIVTD NCYKIVEQNR QSKPDTCQTS
1860 1870 1880 1890 1900
CHKVLDDSKD FICPSSSGDV CINSRKDSFC PHNEQILQHN QSMSGLKKAA
1910 1920 1930 1940 1950
TPPVGLETWD TSKSIREPPQ AAHPSRTYGI FSTASGKAIQ VSDASLEKAR
1960 1970 1980 1990 2000
QVFSEMDGDA KQLSSMVSLE GNEKPHHSVK RENSVVHSTQ GVLSLPKPLP
2010 2020 2030 2040 2050
GNVNSSVFSG FSTAGGKLVT VSESALHKVK GMLEEFDLIR TEHTLQHSPI
2060 2070 2080 2090 2100
PEDVSKILPQ PCAEIRTPEY PVNSKLQKTY NDKSSLPSNY KESGSSGNTQ
2110 2120 2130 2140 2150
SIEVSLQLSQ MERNQDTQLV LGTKVSHSKA NLLGKEQTLP QNIKVKTDEM
2160 2170 2180 2190 2200
KTFSDVPVKT NVGEYYSKES ENYFETEAVE SAKAFMEDDE LTDSEQTHAK
2210 2220 2230 2240 2250
CSLFTCPQNE TLFNSRTRKR GGVTVDAVGQ PPIKRSLLNE FDRIIESKGK
2260 2270 2280 2290 2300
SLTPSKSTPD GTVKDRSLFT HHMSLEPVTC GPFCSSKERQ GAQRPHLTSP
2310 2320 2330 2340 2350
AQELLSKGHP WRHSALEKSP SSPIVSILPA HDVSATRTER TRHSGKSTKV
2360 2370 2380 2390 2400
FVPPFKMKSQ FHGDEHFNSK NVNLEGKNQK STDGDREDGN DSHVRQFNKD
2410 2420 2430 2440 2450
LMSSLQSARD LQDMRIKNKE RRHLRLQPGS LYLTKSSTLP RISLQAAVGD
2460 2470 2480 2490 2500
RAPSACSPKQ LYIYGVSKEC INVNSKNAEY FQFDIQDHFG KEDLCAGKGF
2510 2520 2530 2540 2550
QLADGGWLIP SNDGKAGKEE FYRALCDTPG VDPKLISSIW VANHYRWIVW
2560 2570 2580 2590 2600
KLAAMEFAFP KEFANRCLNP ERVLLQLKYR YDVEIDNSRR SALKKILERD
2610 2620 2630 2640 2650
DTAAKTLVLC ISDIISPSTK VSETSGGKTS GEDANKVDTI ELTDGWYAVR
2660 2670 2680 2690 2700
AQLDPPLMAL VKSGKLTVGQ KIITQGAELV GSPDACAPLE APDSLRLKIS
2710 2720 2730 2740 2750
ANSTRPARWH SRLGFFRDPR PFPLPLSSLF SDGGNVGCVD IIVQRVYPLQ
2760 2770 2780 2790 2800
WVEKTVSGLY IFRSEREEEK EALRFAEAQQ KKLEALFTKV HTEFKDHEED
2810 2820 2830 2840 2850
TTQRCVLSRT LTRQQVHALQ DGAELYAAVQ YASDPDHLEA CFSEEQLRAL
2860 2870 2880 2890 2900
NNYRQMLNDK KQARIQSEFR KALESAEKEE GLSRDVTTVW KLRVTSYKKK
2910 2920 2930 2940 2950
EKSALLSIWR PSSDLSSLLT EGKRYRIYHL AVSKSKSKFE RPSIQLTATK
2960 2970 2980 2990 3000
RTQYQQLPVS SETLLQVYQP RESLHFSRLS DPAFQPPCSE VDVVGVVVSV
3010 3020 3030 3040 3050
VKPIGLAPLV YLSDECLNLL VVKFGIDLNE DIKPRVLIAA SNLQCQPEST
3060 3070 3080 3090 3100
SGVPTLFAGH FSIFSASPKE AYFQEKVNNL KHAIENIDTF YKEAEKKLIH
3110 3120 3130 3140 3150
VLEGDSPKWS TPNKDPTREP HAASTCCASD LLGSGGQFLR ISPTGQQSYQ
3160 3170 3180 3190 3200
SPLSHCTLKG KSMPLAHSAQ MAAKSWSGEN EIDDPKTCRK RRALDFLSRL
3210 3220 3230 3240 3250
PLPSPVSPIC TFVSPAAQKA FQPPRSCGTK YATPIKKEPS SPRRRTPFQK
3260 3270 3280 3290 3300
TSGVSLPDCD SVADEELALL STQALTPDSV GGNEQAFPGD STRNPQPAQR
3310 3320
PDQQVGPRSR KESLRDCRGD SSEKLAVES
Length:3,329
Mass (Da):370,664
Last modified:October 3, 2012 - v2
Checksum:i50A32E8BADE2CF7E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1038 – 10381L → I in AAB48306. (PubMed:9063750)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti44 – 441S → F in strain: C57BL/6 and 129/Sv.
Natural varianti340 – 3401T → P in strain: 129/Sv.
Natural varianti377 – 3771N → H in strain: C57BL/6.
Natural varianti407 – 4071H → P in strain: C57BL/6.
Natural varianti661 – 6611I → V in strain: C57BL/6.
Natural varianti739 – 7391P → H in strain: C57BL/6.
Natural varianti1198 – 11992GF → RI in strain: C57BL/6.
Natural varianti1257 – 12571Q → P in strain: C57BL/6.
Natural varianti1392 – 13921Q → R in strain: C57BL/6.
Natural varianti1520 – 15212FD → CG in strain: C57BL/6.
Natural varianti1583 – 15831R → W in strain: C57BL/6.
Natural varianti1613 – 16131C → W in strain: C57BL/6.
Natural varianti1686 – 16861S → R in strain: C57BL/6.
Natural varianti1799 – 17991S → F in strain: 129/Sv.
Natural varianti1881 – 18811P → L in strain: C57BL/6.
Natural varianti1894 – 18941S → F in strain: 129/Sv.
Natural varianti2141 – 21411Q → K in strain: C57BL/6.
Natural varianti2392 – 23921S → R in strain: C57BL/6.
Natural varianti2605 – 26051K → Q in strain: C57BL/6.
Natural varianti2648 – 26481A → P in strain: C57BL/6.
Natural varianti2717 – 27171R → C in strain: 129/Sv.
Natural varianti2729 – 27291L → M in strain: 129/Sv.
Natural varianti2814 – 28141Q → H in strain: C57BL/6.
Natural varianti2827 – 28271A → P in strain: C57BL/6.
Natural varianti2907 – 29071S → I in strain: 129/Sv.
Natural varianti2929 – 29291H → L in strain: 129/Sv.
Natural varianti3058 – 30581A → G in strain: C57BL/6.
Natural varianti3071 – 30711A → G in strain: C57BL/6.
Natural varianti3081 – 30811K → E in strain: C57BL/6.
Natural varianti3089 – 30891T → S in strain: C57BL/6.
Natural varianti3105 – 31095DSPKW → SQSQV in strain: C57BL/6.
Natural varianti3220 – 32201A → G in strain: 129/Sv.
Natural varianti3238 – 32381E → K in strain: 129/Sv.
Natural varianti3243 – 32431Missing in strain: C57BL/6.
Natural varianti3245 – 32451R → K in strain: 129/Sv.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS39411.1.
PIRiT30835.
T30904.
T42205.
RefSeqiNP_001074470.1. NM_001081001.2.
NP_033895.2. NM_009765.3.
UniGeneiMm.236256.

Genome annotation databases

EnsembliENSMUST00000044620; ENSMUSP00000038576; ENSMUSG00000041147.
GeneIDi12190.
KEGGimmu:12190.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS39411.1.
PIRi T30835.
T30904.
T42205.
RefSeqi NP_001074470.1. NM_001081001.2.
NP_033895.2. NM_009765.3.
UniGenei Mm.236256.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MIU X-ray 3.10 A 2378-3115 [» ]
1MJE X-ray 3.50 A 2378-3113 [» ]
ProteinModelPortali P97929.
SMRi P97929. Positions 1493-1524, 2399-3103.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198384. 5 interactions.
IntActi P97929. 2 interactions.

PTM databases

PhosphoSitei P97929.

Proteomic databases

PRIDEi P97929.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000044620 ; ENSMUSP00000038576 ; ENSMUSG00000041147 .
GeneIDi 12190.
KEGGi mmu:12190.

Organism-specific databases

CTDi 675.
MGIi MGI:109337. Brca2.

Phylogenomic databases

eggNOGi NOG331296.
GeneTreei ENSGT00390000003602.
HOGENOMi HOG000139693.
HOVERGENi HBG050731.
InParanoidi P97929.
KOi K08775.
OMAi LGFHTAS.
OrthoDBi EOG75TMB1.
TreeFami TF105041.

Enzyme and pathway databases

Reactomei REACT_198629. Meiotic recombination.
REACT_27235. Meiotic Recombination.

Miscellaneous databases

EvolutionaryTracei P97929.
NextBioi 280585.
PROi P97929.
SOURCEi Search...

Gene expression databases

CleanExi MM_BRCA2.
ExpressionAtlasi P97929. baseline and differential.
Genevestigatori P97929.

Family and domain databases

Gene3Di 2.40.50.140. 4 hits.
InterProi IPR015525. BRCA2.
IPR015252. BRCA2_hlx.
IPR015187. BRCA2_OB_1.
IPR015188. BRCA2_OB_3.
IPR002093. BRCA2_repeat.
IPR012340. NA-bd_OB-fold.
IPR015205. Tower.
[Graphical view ]
PANTHERi PTHR11289. PTHR11289. 1 hit.
Pfami 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 ]
PIRSFi PIRSF002397. BRCA2. 1 hit.
SUPFAMi SSF50249. SSF50249. 4 hits.
SSF81872. SSF81872. 1 hit.
PROSITEi PS50138. BRCA2_REPEAT. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiBRCA2_MOUSE
AccessioniPrimary (citable) accession number: P97929
Secondary accession number(s): F8VPU5, O35922, P97383
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: October 3, 2012
Last modified: October 29, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3