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P97929

- BRCA2_MOUSE

UniProt

P97929 - BRCA2_MOUSE

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
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (03 Oct 2012)
      Previous versions | rss
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    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 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. protein binding Source: MGI
    5. 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

    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

    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

    ArrayExpressiP97929.
    CleanExiMM_BRCA2.
    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 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

    MPVEYKRRPT FWEIFKARCS TADLGPISLN WFEELSSEAP PYNSEPPEES     50
    EYKPHGYEPQ LFKTPQRNPP YHQFASTPIM FKERSQTLPL DQSPFRELGK 100
    VVASSKHKTH SKKKTKVDPV VDVASPPLKS CLSESPLTLR CTQAVLQREK 150
    PVVSGSLFYT PKLKEGQTPK PISESLGVEV DPDMSWTSSL ATPPTLSSTV 200
    LIARDEEARS SVTPADSPAT LKSCFSNHNE SPQKNDRSVP SVIDSENKNQ 250
    QEAFSQGLGK MLGDSSGKRN SFKDCLRKPI PNILEDGETA VDTSEEDSFS 300
    LCFPKRRTRN LQKMRMGKTR KKIFSETRTD ELSEEARRQT DDKNSFVFEM 350
    ELRESDPLDP GVTSQKPFYS QNEEICNEAV QCSDSRWSQS NLSGLNETQT 400
    GKITLPHISS HSQNISEDFI DMKKEGTGSI TSEKSLPHIS SLPEPEKMFS 450
    EETVVDKEHE GQHFESLEDS IAGKQMVSRT SQAACLSPSI RKSIFKMREP 500
    LDETLGTVFS DSMTNSTFTE EHEASACGLG ILTACSQRED SICPSSVDTG 550
    SWPTTLTDTS ATVKNAGLIS TLKNKKRKFI YSVSDDASLQ GKKLQTHRQL 600
    ELTNLSAQLE ASAFEVPLTF TNVNSGIPDS SDKKRCLPND PEEPSLTNSF 650
    GTATSKEISY IHALISQDLN DKEAIVIEEK PQPYTAREAD FLLCLPERTC 700
    ENDQKSPKVS NGKEKVLVSA CLPSAVQLSS ISFESQENPL GDHNGTSTLK 750
    LTPSSKLPLS KADMVSREKM CKMPEKLQCE SCKVNIELSK NILEVNEICI 800
    LSENSKTPGL LPPGENIIEV ASSMKSQFNQ NAKIVIQKDQ KGSPFISEVA 850
    VNMNSEELFP DSGNNFAFQV TNKCNKPDLG SSVELQEEDL SHTQGPSLKN 900
    SPMAVDEDVD DAHAAQVLIT KDSDSLAVVH DYTEKSRNNI EQHQKGTEDK 950
    DFKSNSSLNM KSDGNSDCSD KWSEFLDPVL NHNFGGSFRT ASNKEIKLSE 1000
    HNVKKSKMFF KDIEEQYPTR LACIDIVNTL PLANQKKLSE PHIFDLKSVT 1050
    TVSTQSHNQS SVSHEDTDTA PQMLSSKQDF HSNNLTTSQK AEITELSTIL 1100
    EESGSQFEFT QFRKPSHIAQ NTSEVPGNQM VVLSTASKEW KDTDLHLPVD 1150
    PSVGQTDHSK QFEGSAGVKQ SFPHLLEDTC NKNTSCFLPN INEMEFGGFC 1200
    SALGTKLSVS NEALRKAMKL FSDIENSEEP SAKVGPRGFS SSAHHDSVAS 1250
    VFKIKKQNTE KSFDEKSSKC QVTLQNNIEM TTCIFVGRNP EKYIKNTKHE 1300
    DSYTSSQRNN LENSDGSMSS TSGPVYIHKG DSDLPADQGS KCPESCTQYA 1350
    REENTQIKEN ISDLTCLEIM KAEETCMKSS DKKQLPSDKM EQNIKEFNIS 1400
    FQTASGKNTR VSKESLNKSV NIFNRETDEL TVISDSLNSK ILHGINKDKM 1450
    HTSCHKKAIS IKKVFEDHFP IVTVSQLPAQ QHPEYEIEST KEPTLLSFHT 1500
    ASGKKVKIMQ ESLDKVKNLF DETQYVRKTA SFSQGSKPLK DSKKELTLAY 1550
    EKIEVTASKC EEMQNFVSKE TEMLPQQNYH MYRQTENLKT SNGTSSKVQE 1600
    NIENNVEKNP RICCICQSSY PVTEDSALAY YTEDSRKTCV RESSLSKGRK 1650
    WLREQGDKLG TRNTIKIECV KEHTEDFAGN ASYEHSLVII RTEIDTNHVS 1700
    ENQVSTLLSD PNVCHSYLSQ SSFCHCDDMH NDSGYFLKNK IDSDVPPDMK 1750
    NAEGNTISPR VSATKERNLH PQTINEYCVQ KLETNTSPHA NKDVAIDPSL 1800
    LDSRNCKVGS LVFITAHSQE TERTKEIVTD NCYKIVEQNR QSKPDTCQTS 1850
    CHKVLDDSKD FICPSSSGDV CINSRKDSFC PHNEQILQHN QSMSGLKKAA 1900
    TPPVGLETWD TSKSIREPPQ AAHPSRTYGI FSTASGKAIQ VSDASLEKAR 1950
    QVFSEMDGDA KQLSSMVSLE GNEKPHHSVK RENSVVHSTQ GVLSLPKPLP 2000
    GNVNSSVFSG FSTAGGKLVT VSESALHKVK GMLEEFDLIR TEHTLQHSPI 2050
    PEDVSKILPQ PCAEIRTPEY PVNSKLQKTY NDKSSLPSNY KESGSSGNTQ 2100
    SIEVSLQLSQ MERNQDTQLV LGTKVSHSKA NLLGKEQTLP QNIKVKTDEM 2150
    KTFSDVPVKT NVGEYYSKES ENYFETEAVE SAKAFMEDDE LTDSEQTHAK 2200
    CSLFTCPQNE TLFNSRTRKR GGVTVDAVGQ PPIKRSLLNE FDRIIESKGK 2250
    SLTPSKSTPD GTVKDRSLFT HHMSLEPVTC GPFCSSKERQ GAQRPHLTSP 2300
    AQELLSKGHP WRHSALEKSP SSPIVSILPA HDVSATRTER TRHSGKSTKV 2350
    FVPPFKMKSQ FHGDEHFNSK NVNLEGKNQK STDGDREDGN DSHVRQFNKD 2400
    LMSSLQSARD LQDMRIKNKE RRHLRLQPGS LYLTKSSTLP RISLQAAVGD 2450
    RAPSACSPKQ LYIYGVSKEC INVNSKNAEY FQFDIQDHFG KEDLCAGKGF 2500
    QLADGGWLIP SNDGKAGKEE FYRALCDTPG VDPKLISSIW VANHYRWIVW 2550
    KLAAMEFAFP KEFANRCLNP ERVLLQLKYR YDVEIDNSRR SALKKILERD 2600
    DTAAKTLVLC ISDIISPSTK VSETSGGKTS GEDANKVDTI ELTDGWYAVR 2650
    AQLDPPLMAL VKSGKLTVGQ KIITQGAELV GSPDACAPLE APDSLRLKIS 2700
    ANSTRPARWH SRLGFFRDPR PFPLPLSSLF SDGGNVGCVD IIVQRVYPLQ 2750
    WVEKTVSGLY IFRSEREEEK EALRFAEAQQ KKLEALFTKV HTEFKDHEED 2800
    TTQRCVLSRT LTRQQVHALQ DGAELYAAVQ YASDPDHLEA CFSEEQLRAL 2850
    NNYRQMLNDK KQARIQSEFR KALESAEKEE GLSRDVTTVW KLRVTSYKKK 2900
    EKSALLSIWR PSSDLSSLLT EGKRYRIYHL AVSKSKSKFE RPSIQLTATK 2950
    RTQYQQLPVS SETLLQVYQP RESLHFSRLS DPAFQPPCSE VDVVGVVVSV 3000
    VKPIGLAPLV YLSDECLNLL VVKFGIDLNE DIKPRVLIAA SNLQCQPEST 3050
    SGVPTLFAGH FSIFSASPKE AYFQEKVNNL KHAIENIDTF YKEAEKKLIH 3100
    VLEGDSPKWS TPNKDPTREP HAASTCCASD LLGSGGQFLR ISPTGQQSYQ 3150
    SPLSHCTLKG KSMPLAHSAQ MAAKSWSGEN EIDDPKTCRK RRALDFLSRL 3200
    PLPSPVSPIC TFVSPAAQKA FQPPRSCGTK YATPIKKEPS SPRRRTPFQK 3250
    TSGVSLPDCD SVADEELALL STQALTPDSV GGNEQAFPGD STRNPQPAQR 3300
    PDQQVGPRSR KESLRDCRGD SSEKLAVES 3329
    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

    ArrayExpressi P97929.
    CleanExi MM_BRCA2.
    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

    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 1, 2014
    This is version 134 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