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O35923

- BRCA2_RAT

UniProt

O35923 - BRCA2_RAT

Protein

Breast cancer type 2 susceptibility protein homolog

Gene

Brca2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      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. protein binding Source: RGD
    3. single-stranded DNA binding Source: RGD

    GO - Biological processi

    1. centrosome duplication Source: RefGenome
    2. chromosome organization Source: RefGenome
    3. DNA recombination Source: RGD
    4. double-strand break repair via homologous recombination Source: UniProtKB
    5. homologous chromosome orientation involved in meiotic metaphase I plate congression Source: RGD
    6. mammary gland development Source: RGD
    7. multicellular organism growth Source: RGD
    8. regulation of cell proliferation Source: RefGenome
    9. regulation of transcription, DNA-templated Source: RefGenome
    10. response to estradiol Source: RGD
    11. response to nutrient Source: RGD
    12. spermatogenesis Source: RGD

    Keywords - Biological processi

    Cell cycle, DNA damage, DNA recombination, DNA repair

    Keywords - Ligandi

    DNA-binding

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2219. Brca2.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB-KW
    3. nucleus Source: RefGenome

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 33433343Breast cancer type 2 susceptibility protein homologPRO_0000064986Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei736 – 7361PhosphoserineBy similarity
    Modified residuei3222 – 32221Phosphoserine; by CDK1 and CDK2By similarity

    Post-translational modificationi

    Phosphorylation by CHEK1 and CHEK2 regulates interaction with RAD51. Phosphorylation at Ser-3222 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

    PaxDbiO35923.
    PRIDEiO35923.

    Expressioni

    Tissue specificityi

    Highest expression in testis. Also expressed in spleen, skeletal muscle, thymus, mammary gland, heart, ovary, prostate, liver, lung, kidney and brain.

    Gene expression databases

    GenevestigatoriO35923.

    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.1 Publication

    Structurei

    Secondary structure

    1
    3343
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni2407 – 24093
    Helixi2410 – 242819
    Turni2441 – 24433
    Beta strandi2444 – 24463
    Helixi2453 – 24575
    Beta strandi2467 – 24693
    Helixi2470 – 24734
    Helixi2479 – 24813
    Turni2484 – 24896
    Helixi2494 – 24985
    Turni2500 – 25023
    Beta strandi2503 – 25053
    Beta strandi2509 – 25113
    Helixi2512 – 25143
    Beta strandi2515 – 25173
    Helixi2527 – 25359
    Helixi2542 – 25443
    Helixi2547 – 256721
    Turni2569 – 25713
    Turni2573 – 25753
    Beta strandi2576 – 25783
    Helixi2579 – 259315
    Helixi2601 – 26066
    Beta strandi2615 – 26228
    Beta strandi2649 – 26524
    Beta strandi2657 – 26604
    Helixi2664 – 26718
    Beta strandi2680 – 26845
    Beta strandi2687 – 26904
    Helixi2697 – 26993
    Beta strandi2705 – 27073
    Turni2710 – 27123
    Beta strandi2713 – 27153
    Beta strandi2718 – 27203
    Beta strandi2722 – 27243
    Beta strandi2746 – 27483
    Beta strandi2759 – 27635
    Beta strandi2765 – 27728
    Helixi2774 – 27829
    Beta strandi2895 – 29039
    Beta strandi2905 – 29095
    Beta strandi2913 – 29197
    Turni2922 – 29276
    Beta strandi2934 – 29385
    Beta strandi2962 – 29654
    Helixi2970 – 29734
    Turni2974 – 29763
    Helixi2985 – 29895
    Helixi2996 – 29983
    Beta strandi2999 – 30057
    Beta strandi3008 – 30103
    Beta strandi3013 – 30153
    Beta strandi3018 – 30225
    Beta strandi3028 – 30358
    Beta strandi3046 – 30549
    Beta strandi3064 – 307613
    Helixi3080 – 309718
    Helixi3101 – 311010

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IYJX-ray3.40B/D2335-3151[»]
    ProteinModelPortaliO35923.
    SMRiO35923. Positions 1505-1536, 2403-3112.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO35923.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati984 – 101835BRCA2 1Add
    BLAST
    Repeati1197 – 123135BRCA2 2Add
    BLAST
    Repeati1405 – 143935BRCA2 3Add
    BLAST
    Repeati1503 – 153735BRCA2 4Add
    BLAST
    Repeati1645 – 166925BRCA2 5Add
    BLAST
    Repeati1828 – 184518BRCA2 6Add
    BLAST
    Repeati1939 – 197335BRCA2 7Add
    BLAST
    Repeati2019 – 205335BRCA2 8Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 4040Interaction with PALB2By similarityAdd
    BLAST
    Regioni622 – 982361Interaction with NPM1By similarityAdd
    BLAST
    Regioni2313 – 2475163Interaction with FANCD2By similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 8 BRCA2 repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG331296.
    HOGENOMiHOG000139693.
    HOVERGENiHBG050731.
    InParanoidiO35923.
    PhylomeDBiO35923.

    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.

    O35923-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTVEYKRRPT FWEIFKARCS TADLGPISLN WFEELFSEAP PYNTEHPEES     50
    EYKPQGHEPQ LFKTPQRNPS YHQFASTPIM FKEQSQTLPL DQSPFKELGN 100
    VVANSKRKHH SKKKARKDPV VDVASLPLKA CPSESPCTPR CTQVAPQRRK 150
    PVVSGSLFYT PKLEETPKHI SESLGVEVDP DMSWTSSLAT PPTLSSTVLI 200
    ARDEEAHRNA FPADSPASLK SYFSNHNESL KKNDRFIPSV SDSENKSQQE 250
    AFSQGLEKML GDSSSKINRF RDCLRKPIPN VLEDGETAVD TSGEDSFSLC 300
    FPKRRTRNLQ KTRMGKMKKK IFSETRTDGL SEEARGQADD KNSFALEIEP 350
    RDSEPLDPSV TNQKPLYSQS GDISSEAGQC SDSIWSQPDP SGLNGTQTRK 400
    IPLLHISFHK QSILEDFIDM KKEGTGSITF PHISSLPEPE KMFSEETLVD 450
    KEHEGQHLES LEDSISGKQM VSGTSQTACL SPSIRKSIVK MREPLEETLD 500
    TVFSDSMTSS AFTEELDASA GGLEIHTACS QREDSLCPSS VDTGSWPTTL 550
    TDTSATVKNA GLITTLKNKR RKFIYSVSDD ASHQGKKLQT QRQSELTNLS 600
    APFEASAFEV PFPFTNVDSG IPDSSIKRSN LPNDPEEPSL SLTNSFVTAA 650
    SKEISYIHAL ISQDLNDKEA ILSEEKPQPY TALEADFLSC LPERSCENDQ 700
    KSPKVSDRKE KVLVSACRPS GRLAAAVQLS SISFDSQENP LGSHNVTSTL 750
    KLTPSPKTPL SKPVVVSRGK MCKMPEKLQC KSCKDNIELS KNIPLGVNEM 800
    CVLSENSETP ELLPPLEYIT EVSSSVKSQF NQNTKIAVVQ KDQKDSTFIS 850
    EVTVHMNSEE LFPEKENNFA FQVTNESNKP NIGSTVEFQE EDLSHAKGHS 900
    LKNSPMTVDR DLDDEQAGQV LITEDSDSLA VVHDCTKKSR NTIEQHQKGT 950
    ADKDFKSNSS LYLKSDGNND YLDKWSEFLD PLMNHKLGGS FRTASNKEIK 1000
    LSEDNVKKSK MFFKDIEEQY PTSLDCIDTV STLQLANKKR LSEPHTFDLK 1050
    SGTTVSTQCH SQSSVSHEDT HTAPQMLSSK QDFHSSHNLT PSQKAEITEL 1100
    STILEESGSQ FEFTQFKNPS HIAQNNTSAV LGNQMAVVRT ASEEWKDVDL 1150
    HLPLNPSSVG QIDHNKKFEC LVGVKQSSSH LLEDTCNQNT SCFLPIKEME 1200
    FGGFCSALGT KLSVSNEALR KAMKLFSDIE NISEEPSTKV GPRGFSSCAH 1250
    HDSVASVFKI KKQNTDKSFD EKSSKCQVTV QNNKEMTTCI LVDENPENYV 1300
    KNIKQDNNYT GSQRNAYKLE NSDVSKSSTS GTVYINKGDS DLPFAAEKGN 1350
    KYPESCTQYV REENAQIKES VSDLTCLEVM KAEETCHMKS SDKEQLPSDK 1400
    MEQNMKEFNI SFQTASGKNI RVSKESLNKS VNILDQETED LTVTSDSLNS 1450
    KILCGINKDK MHISCHKKSI NIKKVFEEHF PIGTVSQLPA LQQYPEYEIE 1500
    SIKEPTLLSF HTASGKKVKI MQESLDKVKN LFDETQYVRK TTNFGHQESK 1550
    PLKDREDYKE RLTLAYEKIE VTASKCEEMQ NFVSKQTEML PQQNDHMYRQ 1600
    TENLTSNGSS PKVHGNIENK IEKNPRICCI CQSSYFVTED SALACYTGDS 1650
    RKTCVGESSL SKGKKWLREQ SDKLGTRNTI EIQCVKEHTE DFAGNALYEH 1700
    SLVIIRTEID TSHVSENQAS TLFSDPNVCH SYLSHSSFCH HDDMHNDSGY 1750
    FLKDKIDSDV QPDMKNTEGN AIFPKISATK EIKLHPQTVN EECVQKLETN 1800
    ASPYANKNIA IDSAMLDLRN CKVGSPVFIT THSQETVRMK EIFTDNCSKI 1850
    VEQNRESKPD TCQTSCHKAL DNSEDFICPS SSGDVCINSP MAIFYPQSEQ 1900
    ILQHNQSVSG LKKAATPPVS LETWDTCKSI RGSPQEVHPS RTYGFFSTAS 1950
    GKAVQVSDAS LEKARQVFSE IDGDAKQLAS MVSLEGNEKS HHSVKRESSV 2000
    VHNTHGVLSL RKTLPGNVSS FVFSGFSTAG GKLVTVSESA LHKVKGMLEE 2050
    FDLIRTEHTL QHSPTPEDVS KIPPQPCLES RTPEYSVSSK LQKTYNDKSR 2100
    SPSNYKESGS SGNTQSLEVS PQLSQMERKQ ETQSVLGTKV SQRKTNILEK 2150
    KQNLPQNIKI ESNKMETFSD VSMKTNVGEY YSKEPENYFE TEAVEIAKAF 2200
    MEDDELTDSE QTHAKCSLFA CPQNEALLNS RTRKRGGMAG VAVGQPPIKR 2250
    SLLNEFDRII ESKGKSLTPS KSTPDGTIKD RRLFTHHMSL EPVTCGPFCS 2300
    SKERQETQSP HVTSPAQGLQ SKEHPSRHSA VGKSSSNPTV SALRSERTRH 2350
    SVSDKSTKVF VPPFKVKSRF HRDEHFDSKN VNLEGKNQKS ADGVSEDGND 2400
    SDFPQFNKDL MSSLQNARDL QDIRIKNKER HHLCPQPGSL YLTKSSTLPR 2450
    ISLQAAVGDS VPSACSPKQL YMYGVSKACI SVNSKNAEYF QFAIEDHFGK 2500
    EALCAGKGFR LADGGWLIPS DDGKAGKEEF YRALCDTPGV DPKLISSVWV 2550
    SNHYRWIVWK LAAMEFAFPK EFANRCLNPE RVLLQLKYRY DVEIDNSSRS 2600
    ALKKILERDD TAAKTLVLCV SDIISLSTNV SETSGSKASS EDSNKVDTIE 2650
    LTDGWYAVKA QLDPPLLALV KSGRLTVGQK IITQGAELVG SPDACAPLEA 2700
    PDSLRLKISA NSTRPARWHS KLGFFHDPRP FPLPLSSLFS DGGNVGCVDV 2750
    IVQRVYPLQW VEKTVSGSYI FRNEREEEKE ALRFAEAQQK KLEALFTKVH 2800
    TELKEHEEDI AQRRVLSRAL TRQQVHALQD GAELYAAVQD ASDPEHLETC 2850
    FSEEQLRALN NYRQMLSDKK QARIQSEFRK ALEAAEKEEG LSRDVSTVWK 2900
    LRVTSYKKRE KSALLSIWRP SSDLPSLLTE GQRYRIYHLS VSKSKNKFEW 2950
    PSIQLTATKR TQYQQLPVSS ETLLQLYQPR ELLPFSKLSD PAFQPPCSEV 3000
    DVVGVVVSVV KPIGLAPLVY LSDECLHLLV VKFGIDLNED IKPRVLIAAS 3050
    NLQWRPESTS RVPTLFAGNF SVFSASPKEA HFQERVTNMK HAIENIDTFY 3100
    KEAEKKLIQV LKGDSPKWST PNKDPTREPY PASTCSASDL ASGGQLPRSS 3150
    PTDQQSYRSP LSCCTPTGKS TPLAHSAWMA AKSCSGENEI EDPKTCRKKR 3200
    ALDLLSRLPL PPPLSPVCTF VSPAAQKAFQ PPRSCGTKYP TPLKKEGPSS 3250
    PWSRAPFQKA SGVSLLDCDS VADEELALLS TQALVPHSVG GSEQVFPSDS 3300
    TRTEGPSAST EARPANRSKR ESLRDCRDDS DGKLAAETVP DYS 3343
    Length:3,343
    Mass (Da):372,216
    Last modified:January 1, 1998 - v1
    Checksum:i653DB110D2302A8D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U89653 mRNA. Translation: AAB71378.1.
    PIRiT42207.
    UniGeneiRn.103225.

    Genome annotation databases

    UCSCiRGD:2219. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U89653 mRNA. Translation: AAB71378.1 .
    PIRi T42207.
    UniGenei Rn.103225.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IYJ X-ray 3.40 B/D 2335-3151 [» ]
    ProteinModelPortali O35923.
    SMRi O35923. Positions 1505-1536, 2403-3112.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi O35923.
    PRIDEi O35923.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:2219. rat.

    Organism-specific databases

    RGDi 2219. Brca2.

    Phylogenomic databases

    eggNOGi NOG331296.
    HOGENOMi HOG000139693.
    HOVERGENi HBG050731.
    InParanoidi O35923.
    PhylomeDBi O35923.

    Miscellaneous databases

    EvolutionaryTracei O35923.
    NextBioi 21679528.
    PROi O35923.

    Gene expression databases

    Genevestigatori O35923.

    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. "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: Sprague-Dawley.
      Tissue: Testis.
    2. "BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure."
      Yang H., Jeffrey P.D., Miller J., Kinnucan E., Sun Y., Thoma N.H., Zheng N., Chen P.L., Lee W.H., Pavletich N.P.
      Science 297:1837-1848(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 2335-3151 IN COMPLEX WITH DSS1.

    Entry informationi

    Entry nameiBRCA2_RAT
    AccessioniPrimary (citable) accession number: O35923
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 14, 2003
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3