ID   BRCA2_MOUSE             Reviewed;        3329 AA.
AC   P97929; F8VPU5; O35922; P97383;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   27-MAR-2024, entry version 199.
DE   RecName: Full=Breast cancer type 2 susceptibility protein homolog {ECO:0000305};
DE   AltName: Full=Fanconi anemia group D1 protein homolog;
GN   Name=Brca2 {ECO:0000312|MGI:MGI:109337}; Synonyms=Fancd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129;
RX   PubMed=9063750; DOI=10.1093/hmg/6.2.291;
RA   Connor F., Smith A., Wooster R., Stratton M., Dixon A., Campbell E.,
RA   Tait T.M., Freeman T., Ashworth A.;
RT   "Cloning, chromosomal mapping and expression pattern of the mouse Brca2
RT   gene.";
RL   Hum. Mol. Genet. 6:291-300(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=9119389; DOI=10.1006/geno.1996.4573;
RA   Sharan S.K., Bradley A.;
RT   "Murine Brca2: sequence, map position, and expression pattern.";
RL   Genomics 40:234-241(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv;
RX   PubMed=9242436;
RA   McAllister K.A., Haugen-Strano A., Hagevik S., Brownlee H.A., Collins N.K.,
RA   Futreal P.A., Bennett L.M., Wiseman R.W.;
RT   "Characterization of the rat and mouse homologues of the BRCA2 breast
RT   cancer susceptibility gene.";
RL   Cancer Res. 57:3121-3125(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 18-200.
RX   PubMed=8917547; DOI=10.1073/pnas.93.23.13078;
RA   Rajan J.V., Wang M., Marquis S.T., Chodosh L.A.;
RT   "Brca2 is coordinately regulated with Brca1 during proliferation and
RT   differentiation in mammary epithelial cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:13078-13083(1996).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 569-625.
RX   PubMed=9196008; DOI=10.1007/s003359900497;
RA   McAllister K.A., Ramachandran S., Haugen-Strano A., Fiedorek F.T. Jr.,
RA   Wiseman R.W.;
RT   "Genetic mapping of the Brca2 breast cancer susceptibility gene on mouse
RT   chromosome 5.";
RL   Mamm. Genome 8:540-541(1997).
RN   [7]
RP   PROTEIN SEQUENCE OF 784-790, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [8]
RP   INTERACTION WITH HSF2BP.
RX   PubMed=31242413; DOI=10.1016/j.celrep.2019.05.096;
RA   Brandsma I., Sato K., van Rossum-Fikkert S.E., van Vliet N., Sleddens E.,
RA   Reuter M., Odijk H., van den Tempel N., Dekkers D.H.W., Bezstarosti K.,
RA   Demmers J.A.A., Maas A., Lebbink J., Wyman C., Essers J., van Gent D.C.,
RA   Baarends W.M., Knipscheer P., Kanaar R., Zelensky A.N.;
RT   "HSF2BP Interacts with a Conserved Domain of BRCA2 and Is Required for
RT   Mouse Spermatogenesis.";
RL   Cell Rep. 27:3790.e7-3798.e7(2019).
RN   [9]
RP   INTERACTION WITH HSF2BP AND RAD51.
RX   PubMed=30760716; DOI=10.1038/s41467-019-08676-2;
RA   Zhang J., Fujiwara Y., Yamamoto S., Shibuya H.;
RT   "A meiosis-specific BRCA2 binding protein recruits recombinases to DNA
RT   double-strand breaks to ensure homologous recombination.";
RL   Nat. Commun. 10:722-722(2019).
RN   [10]
RP   INTERACTION WITH BRME1.
RX   PubMed=32460033; DOI=10.1016/j.celrep.2020.107686;
RA   Takemoto K., Tani N., Takada-Horisawa Y., Fujimura S., Tanno N., Yamane M.,
RA   Okamura K., Sugimoto M., Araki K., Ishiguro K.I.;
RT   "Meiosis-Specific C19orf57/4930432K21Rik/BRME1 Modulates Localization of
RT   RAD51 and DMC1 to DSBs in Mouse Meiotic Recombination.";
RL   Cell Rep. 31:107686-107686(2020).
RN   [11]
RP   INTERACTION WITH HSF2BP AND BRME1.
RX   PubMed=32845237; DOI=10.7554/elife.56996;
RA   Felipe-Medina N., Caburet S., Sanchez-Saez F., Condezo Y.B., de Rooij D.G.,
RA   Gomez-H L., Garcia-Valiente R., Todeschini A.L., Duque P.,
RA   Sanchez-Martin M.A., Shalev S.A., Llano E., Veitia R.A., Pendas A.M.;
RT   "A missense in HSF2BP causing primary ovarian insufficiency affects meiotic
RT   recombination by its novel interactor C19ORF57/BRME1.";
RL   Elife 9:0-0(2020).
RN   [12]
RP   INTERACTION WITH HSF2BP; BRME1; SPATA22; MEIOB AND RAD51, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=32345962; DOI=10.1038/s41467-020-15954-x;
RA   Zhang J., Gurusaran M., Fujiwara Y., Zhang K., Echbarthi M., Vorontsov E.,
RA   Guo R., Pendlebury D.F., Alam I., Livera G., Emmanuelle M., Wang P.J.,
RA   Nandakumar J., Davies O.R., Shibuya H.;
RT   "The BRCA2-MEILB2-BRME1 complex governs meiotic recombination and impairs
RT   the mitotic BRCA2-RAD51 function in cancer cells.";
RL   Nat. Commun. 11:2055-2055(2020).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 2378-3115 IN COMPLEX WITH SEM1,
RP   AND INTERACTION WITH SEM1.
RX   PubMed=12228710; DOI=10.1126/science.297.5588.1837;
RA   Yang H., Jeffrey P.D., Miller J., Kinnucan E., Sun Y., Thoma N.H.,
RA   Zheng N., Chen P.L., Lee W.H., Pavletich N.P.;
RT   "BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA
RT   structure.";
RL   Science 297:1837-1848(2002).
CC   -!- FUNCTION: Involved in double-strand break repair and/or homologous
CC       recombination. Binds RAD51 and potentiates recombinational DNA repair
CC       by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts
CC       by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to
CC       displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-
CC       ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded
CC       HR complex containing RAD51C and which is thought to play a role in DNA
CC       repair by HR. May participate in S phase checkpoint activation. Binds
CC       selectively to ssDNA, and to ssDNA in tailed duplexes and replication
CC       fork structures. May play a role in the extension step after strand
CC       invasion at replication-dependent DNA double-strand breaks; together
CC       with PALB2 is involved in both POLH localization at collapsed
CC       replication forks and DNA polymerization activity. In concert with
CC       NPM1, regulates centrosome duplication. Interacts with the TREX-2
CC       complex (transcription and export complex 2) subunits PCID2 and SEM1,
CC       and is required to prevent R-loop-associated DNA damage and thus
CC       transcription-associated genomic instability, independently of its
CC       known role in homologous recombination (By similarity).
CC       {ECO:0000250|UniProtKB:O35923, ECO:0000250|UniProtKB:P51587}.
CC   -!- SUBUNIT: Monomer and dimer. Interacts with RAD51; regulates RAD51
CC       recruitment and function at sites of DNA repair. Interacts with SEM1,
CC       WDR16, USP11, DMC1, ROCK2 and NPM1. Interacts with both
CC       nonubiquitinated and monoubiquitinated FANCD2; this complex also
CC       includes XRCC3 and phosphorylated FANCG. Part of a BRCA complex
CC       containing BRCA1, BRCA2 and PALB2. Component of the homologous
CC       recombination repair (HR) complex composed of ERCC5/XPG, BRCA2, PALB2,
CC       DSS1 and RAD51 (By similarity). Within the complex, interacts with
CC       ERCC5/XPG and PALB2 (By similarity). Interacts directly with PALB2
CC       which may serve as a scaffold for a HR complex containing PALB2, BRCA2,
CC       RAD51C, RAD51 and XRCC3. Interacts with BRCA1 only in the presence of
CC       PALB2 which serves as the bridging protein. Interacts with POLH; the
CC       interaction is direct. Interacts with the TREX-2 complex subunits PCID2
CC       and SEM1 (By similarity). Interacts with HSF2BP and BRME1; the
CC       interaction with HSF2BP is direct and allows the formation of a ternary
CC       complex (PubMed:32345962, PubMed:32460033, PubMed:31242413,
CC       PubMed:30760716, PubMed:32845237). The complex BRME1:HSF2BP:BRCA2
CC       interacts with SPATA22, MEIOB and RAD51 (PubMed:32345962,
CC       PubMed:30760716). {ECO:0000250|UniProtKB:O35923,
CC       ECO:0000250|UniProtKB:P51587, ECO:0000269|PubMed:12228710,
CC       ECO:0000269|PubMed:30760716, ECO:0000269|PubMed:31242413,
CC       ECO:0000269|PubMed:32345962, ECO:0000269|PubMed:32460033,
CC       ECO:0000269|PubMed:32845237}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51587}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:P51587}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in cerebellum,
CC       testis, ileum, appendix, epididymis, ovary and mammary gland. No
CC       expression in lung. {ECO:0000269|PubMed:32460033}.
CC   -!- DEVELOPMENTAL STAGE: In the mammary gland, expression increases
CC       dramatically during pregnancy.
CC   -!- PTM: Phosphorylated by ATM upon irradiation-induced DNA damage.
CC       Phosphorylation by CHEK1 and CHEK2 regulates interaction with RAD51.
CC       Phosphorylation at Ser-3291 by CDK1 and CDK2 is low in S phase when
CC       recombination is active, but increases as cells progress towards
CC       mitosis; this phosphorylation prevents homologous recombination-
CC       dependent repair during S phase and G2 by inhibiting RAD51 binding.
CC       {ECO:0000250|UniProtKB:P51587}.
CC   -!- PTM: Ubiquitinated in the absence of DNA damage; this does not lead to
CC       proteasomal degradation. In contrast, ubiquitination in response to DNA
CC       damage leads to proteasomal degradation.
CC       {ECO:0000250|UniProtKB:P51587}.
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DR   EMBL; U82270; AAB48306.1; -; mRNA.
DR   EMBL; U65594; AAC23702.1; -; mRNA.
DR   EMBL; U89652; AAB71377.1; -; mRNA.
DR   EMBL; AC154885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U72947; AAB40720.1; -; mRNA.
DR   EMBL; U89503; AAC53276.1; -; Genomic_DNA.
DR   CCDS; CCDS39411.1; -.
DR   PIR; T30835; T30835.
DR   PIR; T30904; T30904.
DR   PIR; T42205; T42205.
DR   RefSeq; NP_001074470.1; NM_001081001.2.
DR   RefSeq; NP_033895.2; NM_009765.3.
DR   RefSeq; XP_017176117.1; XM_017320628.1.
DR   PDB; 1MIU; X-ray; 3.10 A; A=2378-3115.
DR   PDB; 1MJE; X-ray; 3.50 A; A=2378-3113.
DR   PDBsum; 1MIU; -.
DR   PDBsum; 1MJE; -.
DR   SMR; P97929; -.
DR   BioGRID; 198384; 26.
DR   ComplexPortal; CPX-972; BRCC ubiquitin ligase complex.
DR   IntAct; P97929; 2.
DR   MINT; P97929; -.
DR   STRING; 10090.ENSMUSP00000038576; -.
DR   iPTMnet; P97929; -.
DR   PhosphoSitePlus; P97929; -.
DR   EPD; P97929; -.
DR   MaxQB; P97929; -.
DR   PaxDb; 10090-ENSMUSP00000038576; -.
DR   PeptideAtlas; P97929; -.
DR   ProteomicsDB; 273841; -.
DR   Antibodypedia; 7788; 387 antibodies from 42 providers.
DR   DNASU; 12190; -.
DR   Ensembl; ENSMUST00000044620.11; ENSMUSP00000038576.8; ENSMUSG00000041147.11.
DR   Ensembl; ENSMUST00000202313.2; ENSMUSP00000144150.2; ENSMUSG00000041147.11.
DR   GeneID; 12190; -.
DR   KEGG; mmu:12190; -.
DR   UCSC; uc009aty.2; mouse.
DR   AGR; MGI:109337; -.
DR   CTD; 675; -.
DR   MGI; MGI:109337; Brca2.
DR   VEuPathDB; HostDB:ENSMUSG00000041147; -.
DR   eggNOG; KOG4751; Eukaryota.
DR   GeneTree; ENSGT00390000003602; -.
DR   HOGENOM; CLU_000344_0_0_1; -.
DR   InParanoid; P97929; -.
DR   OMA; CWYTKLG; -.
DR   OrthoDB; 5484321at2759; -.
DR   PhylomeDB; P97929; -.
DR   TreeFam; TF105041; -.
DR   Reactome; R-MMU-5685939; HDR through MMEJ (alt-NHEJ).
DR   Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR   Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR   Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
DR   Reactome; R-MMU-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR   BioGRID-ORCS; 12190; 22 hits in 120 CRISPR screens.
DR   ChiTaRS; Brca2; mouse.
DR   EvolutionaryTrace; P97929; -.
DR   PRO; PR:P97929; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; P97929; Protein.
DR   Bgee; ENSMUSG00000041147; Expressed in cleaving embryo and 196 other cell types or tissues.
DR   ExpressionAtlas; P97929; baseline and differential.
DR   GO; GO:0033593; C:BRCA2-MAGE-D1 complex; ISO:MGI.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR   GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:1990391; C:DNA repair complex; ISO:MGI.
DR   GO; GO:0000800; C:lateral element; ISO:MGI.
DR   GO; GO:0000152; C:nuclear ubiquitin ligase complex; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0030141; C:secretory granule; ISO:MGI.
DR   GO; GO:0043015; F:gamma-tubulin binding; ISO:MGI.
DR   GO; GO:0010484; F:histone H3 acetyltransferase activity; ISO:MGI.
DR   GO; GO:0010485; F:histone H4 acetyltransferase activity; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0002020; F:protease binding; ISO:MGI.
DR   GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR   GO; GO:0071479; P:cellular response to ionizing radiation; ISO:MGI.
DR   GO; GO:0090398; P:cellular senescence; IMP:MGI.
DR   GO; GO:0051298; P:centrosome duplication; ISO:MGI.
DR   GO; GO:0043009; P:chordate embryonic development; IMP:MGI.
DR   GO; GO:0051276; P:chromosome organization; IMP:MGI.
DR   GO; GO:0006974; P:DNA damage response; IDA:UniProtKB.
DR   GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IMP:MGI.
DR   GO; GO:0006310; P:DNA recombination; ISO:MGI.
DR   GO; GO:0006302; P:double-strand break repair; IMP:MGI.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:MGI.
DR   GO; GO:0070200; P:establishment of protein localization to telomere; IDA:BHF-UCL.
DR   GO; GO:0008585; P:female gonad development; IMP:MGI.
DR   GO; GO:0071425; P:hematopoietic stem cell proliferation; IMP:MGI.
DR   GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR   GO; GO:0031619; P:homologous chromosome orientation in meiotic metaphase I; ISO:MGI.
DR   GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IGI:MGI.
DR   GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:MGI.
DR   GO; GO:0007141; P:male meiosis I; IDA:UniProtKB.
DR   GO; GO:0030879; P:mammary gland development; ISO:MGI.
DR   GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; ISO:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; ISO:MGI.
DR   GO; GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; ISO:MGI.
DR   GO; GO:0006289; P:nucleotide-excision repair; ISO:MGI.
DR   GO; GO:0001556; P:oocyte maturation; IMP:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0032465; P:regulation of cytokinesis; IMP:MGI.
DR   GO; GO:2000001; P:regulation of DNA damage checkpoint; NAS:ComplexPortal.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:0031297; P:replication fork processing; IMP:MGI.
DR   GO; GO:0010332; P:response to gamma radiation; IMP:MGI.
DR   GO; GO:0010225; P:response to UV-C; IMP:MGI.
DR   GO; GO:0010165; P:response to X-ray; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR   GO; GO:0000722; P:telomere maintenance via recombination; IGI:BHF-UCL.
DR   CDD; cd04493; BRCA2DBD_OB1; 1.
DR   CDD; cd04494; BRCA2DBD_OB2; 1.
DR   CDD; cd04495; BRCA2DBD_OB3; 1.
DR   Gene3D; 6.10.70.10; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 3.
DR   IDEAL; IID50324; -.
DR   InterPro; IPR015525; BRCA2.
DR   InterPro; IPR015252; BRCA2_hlx.
DR   InterPro; IPR036315; BRCA2_hlx_sf.
DR   InterPro; IPR015187; BRCA2_OB_1.
DR   InterPro; IPR048262; BRCA2_OB_2_dom.
DR   InterPro; IPR015188; BRCA2_OB_3.
DR   InterPro; IPR002093; BRCA2_repeat.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR015205; Tower_dom.
DR   PANTHER; PTHR11289:SF0; BREAST CANCER TYPE 2 SUSCEPTIBILITY PROTEIN; 1.
DR   PANTHER; PTHR11289; BREAST CANCER TYPE 2 SUSCEPTIBILITY PROTEIN BRCA2; 1.
DR   Pfam; PF09169; BRCA-2_helical; 1.
DR   Pfam; PF09103; BRCA-2_OB1; 1.
DR   Pfam; PF09104; BRCA-2_OB3; 1.
DR   Pfam; PF00634; BRCA2; 7.
DR   Pfam; PF21318; BRCA2DBD_OB2; 1.
DR   Pfam; PF09121; Tower; 1.
DR   PIRSF; PIRSF002397; BRCA2; 1.
DR   SMART; SM01341; Tower; 1.
DR   SUPFAM; SSF81872; BRCA2 helical domain; 1.
DR   SUPFAM; SSF81878; BRCA2 tower domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
DR   PROSITE; PS50138; BRCA2_REPEAT; 6.
DR   Genevisible; P97929; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; DNA damage; DNA recombination; DNA repair;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Tumor suppressor; Ubl conjugation.
FT   CHAIN           1..3329
FT                   /note="Breast cancer type 2 susceptibility protein homolog"
FT                   /id="PRO_0000064985"
FT   REPEAT          981..1015
FT                   /note="BRCA2 1"
FT   REPEAT          1192..1226
FT                   /note="BRCA2 2"
FT   REPEAT          1394..1428
FT                   /note="BRCA2 3"
FT   REPEAT          1491..1525
FT                   /note="BRCA2 4"
FT   REPEAT          1623..1657
FT                   /note="BRCA2 5"
FT   REPEAT          1924..1958
FT                   /note="BRCA2 6"
FT   REPEAT          2004..2038
FT                   /note="BRCA2 7"
FT   REGION          1..40
FT                   /note="Interaction with PALB2"
FT                   /evidence="ECO:0000250"
FT   REGION          37..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          628..979
FT                   /note="Interaction with NPM1"
FT                   /evidence="ECO:0000250"
FT   REGION          628..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          934..965
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          982..2035
FT                   /note="Interaction with RAD51"
FT                   /evidence="ECO:0000269|PubMed:30760716"
FT   REGION          1296..1340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2073..2099
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2219..2285
FT                   /note="Interaction with HSF2BP"
FT                   /evidence="ECO:0000269|PubMed:30760716,
FT                   ECO:0000269|PubMed:32345962"
FT   REGION          2298..2466
FT                   /note="Interaction with FANCD2"
FT                   /evidence="ECO:0000250"
FT   REGION          2361..2393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2402..2753
FT                   /note="Interaction with SEM1"
FT                   /evidence="ECO:0000250|UniProtKB:P51587"
FT   REGION          3221..3257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3273..3329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           2603..2619
FT                   /note="Nuclear export signal; masked by interaction with
FT                   SEM1"
FT                   /evidence="ECO:0000250|UniProtKB:P51587"
FT   COMPBIAS        213..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..956
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1303..1326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2379..2393
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3273..3303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3305..3329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         435
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51587"
FT   MOD_RES         481
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51587"
FT   MOD_RES         735
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51587"
FT   MOD_RES         2048
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51587"
FT   MOD_RES         3214
FT                   /note="Phosphoserine; by CDK1 and CDK2"
FT                   /evidence="ECO:0000250|UniProtKB:P51587"
FT   MOD_RES         3241
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51587"
FT   VARIANT         44
FT                   /note="S -> F (in strain: C57BL/6 and 129/Sv)"
FT   VARIANT         340
FT                   /note="T -> P (in strain: 129/Sv)"
FT   VARIANT         377
FT                   /note="N -> H (in strain: C57BL/6)"
FT   VARIANT         407
FT                   /note="H -> P (in strain: C57BL/6)"
FT   VARIANT         661
FT                   /note="I -> V (in strain: C57BL/6)"
FT   VARIANT         739
FT                   /note="P -> H (in strain: C57BL/6)"
FT   VARIANT         1198..1199
FT                   /note="GF -> RI (in strain: C57BL/6)"
FT   VARIANT         1257
FT                   /note="Q -> P (in strain: C57BL/6)"
FT   VARIANT         1392
FT                   /note="Q -> R (in strain: C57BL/6)"
FT   VARIANT         1520..1521
FT                   /note="FD -> CG (in strain: C57BL/6)"
FT   VARIANT         1583
FT                   /note="R -> W (in strain: C57BL/6)"
FT   VARIANT         1613
FT                   /note="C -> W (in strain: C57BL/6)"
FT   VARIANT         1686
FT                   /note="S -> R (in strain: C57BL/6)"
FT   VARIANT         1799
FT                   /note="S -> F (in strain: 129/Sv)"
FT   VARIANT         1881
FT                   /note="P -> L (in strain: C57BL/6)"
FT   VARIANT         1894
FT                   /note="S -> F (in strain: 129/Sv)"
FT   VARIANT         2141
FT                   /note="Q -> K (in strain: C57BL/6)"
FT   VARIANT         2392
FT                   /note="S -> R (in strain: C57BL/6)"
FT   VARIANT         2605
FT                   /note="K -> Q (in strain: C57BL/6)"
FT   VARIANT         2648
FT                   /note="A -> P (in strain: C57BL/6)"
FT   VARIANT         2717
FT                   /note="R -> C (in strain: 129/Sv)"
FT   VARIANT         2729
FT                   /note="L -> M (in strain: 129/Sv)"
FT   VARIANT         2814
FT                   /note="Q -> H (in strain: C57BL/6)"
FT   VARIANT         2827
FT                   /note="A -> P (in strain: C57BL/6)"
FT   VARIANT         2907
FT                   /note="S -> I (in strain: 129/Sv)"
FT   VARIANT         2929
FT                   /note="H -> L (in strain: 129/Sv)"
FT   VARIANT         3058
FT                   /note="A -> G (in strain: C57BL/6)"
FT   VARIANT         3071
FT                   /note="A -> G (in strain: C57BL/6)"
FT   VARIANT         3081
FT                   /note="K -> E (in strain: C57BL/6)"
FT   VARIANT         3089
FT                   /note="T -> S (in strain: C57BL/6)"
FT   VARIANT         3105..3109
FT                   /note="DSPKW -> SQSQV (in strain: C57BL/6)"
FT   VARIANT         3220
FT                   /note="A -> G (in strain: 129/Sv)"
FT   VARIANT         3238
FT                   /note="E -> K (in strain: 129/Sv)"
FT   VARIANT         3243
FT                   /note="Missing (in strain: C57BL/6)"
FT   VARIANT         3245
FT                   /note="R -> K (in strain: 129/Sv)"
FT   CONFLICT        1038
FT                   /note="L -> I (in Ref. 1; AAB48306)"
FT                   /evidence="ECO:0000305"
FT   HELIX           2404..2420
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           2430..2435
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           2446..2448
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2456..2458
FT                   /evidence="ECO:0007829|PDB:1MJE"
FT   STRAND          2462..2464
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2468..2472
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   TURN            2475..2480
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           2486..2489
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   TURN            2490..2492
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2495..2497
FT                   /evidence="ECO:0007829|PDB:1MJE"
FT   STRAND          2503..2505
FT                   /evidence="ECO:0007829|PDB:1MJE"
FT   TURN            2512..2514
FT                   /evidence="ECO:0007829|PDB:1MJE"
FT   HELIX           2518..2527
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           2538..2554
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   TURN            2560..2562
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2564..2569
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           2570..2584
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   TURN            2585..2587
FT                   /evidence="ECO:0007829|PDB:1MJE"
FT   HELIX           2592..2597
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2606..2608
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2640..2643
FT                   /evidence="ECO:0007829|PDB:1MJE"
FT   STRAND          2648..2653
FT                   /evidence="ECO:0007829|PDB:1MJE"
FT   HELIX           2655..2662
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2671..2674
FT                   /evidence="ECO:0007829|PDB:1MJE"
FT   STRAND          2675..2677
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2679..2681
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2696..2699
FT                   /evidence="ECO:0007829|PDB:1MJE"
FT   HELIX           2701..2703
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2704..2707
FT                   /evidence="ECO:0007829|PDB:1MJE"
FT   STRAND          2713..2715
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           2726..2728
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2731..2733
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2736..2746
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2751..2754
FT                   /evidence="ECO:0007829|PDB:1MJE"
FT   STRAND          2756..2758
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2760..2763
FT                   /evidence="ECO:0007829|PDB:1MJE"
FT   HELIX           2767..2778
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           2782..2791
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           2813..2817
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           2822..2830
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2833..2835
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   TURN            2836..2840
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2848..2850
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   TURN            2851..2853
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           2855..2858
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           2861..2871
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           2873..2876
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   TURN            2877..2881
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2889..2900
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2904..2910
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           2913..2918
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2924..2930
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2938..2940
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2945..2957
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           2961..2964
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   TURN            2965..2967
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           2977..2980
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2981..2983
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   TURN            2986..2989
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          2990..3001
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          3004..3006
FT                   /evidence="ECO:0007829|PDB:1MJE"
FT   STRAND          3009..3013
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          3015..3017
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          3019..3026
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          3037..3044
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          3050..3052
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          3056..3058
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   STRAND          3063..3067
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   TURN            3071..3073
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           3074..3080
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           3082..3085
FT                   /evidence="ECO:0007829|PDB:1MIU"
FT   HELIX           3090..3102
FT                   /evidence="ECO:0007829|PDB:1MIU"
SQ   SEQUENCE   3329 AA;  370664 MW;  50A32E8BADE2CF7E CRC64;
     MPVEYKRRPT FWEIFKARCS TADLGPISLN WFEELSSEAP PYNSEPPEES EYKPHGYEPQ
     LFKTPQRNPP YHQFASTPIM FKERSQTLPL DQSPFRELGK VVASSKHKTH SKKKTKVDPV
     VDVASPPLKS CLSESPLTLR CTQAVLQREK PVVSGSLFYT PKLKEGQTPK PISESLGVEV
     DPDMSWTSSL ATPPTLSSTV LIARDEEARS SVTPADSPAT LKSCFSNHNE SPQKNDRSVP
     SVIDSENKNQ QEAFSQGLGK MLGDSSGKRN SFKDCLRKPI PNILEDGETA VDTSEEDSFS
     LCFPKRRTRN LQKMRMGKTR KKIFSETRTD ELSEEARRQT DDKNSFVFEM ELRESDPLDP
     GVTSQKPFYS QNEEICNEAV QCSDSRWSQS NLSGLNETQT GKITLPHISS HSQNISEDFI
     DMKKEGTGSI TSEKSLPHIS SLPEPEKMFS EETVVDKEHE GQHFESLEDS IAGKQMVSRT
     SQAACLSPSI RKSIFKMREP LDETLGTVFS DSMTNSTFTE EHEASACGLG ILTACSQRED
     SICPSSVDTG SWPTTLTDTS ATVKNAGLIS TLKNKKRKFI YSVSDDASLQ GKKLQTHRQL
     ELTNLSAQLE ASAFEVPLTF TNVNSGIPDS SDKKRCLPND PEEPSLTNSF GTATSKEISY
     IHALISQDLN DKEAIVIEEK PQPYTAREAD FLLCLPERTC ENDQKSPKVS NGKEKVLVSA
     CLPSAVQLSS ISFESQENPL GDHNGTSTLK LTPSSKLPLS KADMVSREKM CKMPEKLQCE
     SCKVNIELSK NILEVNEICI LSENSKTPGL LPPGENIIEV ASSMKSQFNQ NAKIVIQKDQ
     KGSPFISEVA VNMNSEELFP DSGNNFAFQV TNKCNKPDLG SSVELQEEDL SHTQGPSLKN
     SPMAVDEDVD DAHAAQVLIT KDSDSLAVVH DYTEKSRNNI EQHQKGTEDK DFKSNSSLNM
     KSDGNSDCSD KWSEFLDPVL NHNFGGSFRT ASNKEIKLSE HNVKKSKMFF KDIEEQYPTR
     LACIDIVNTL PLANQKKLSE PHIFDLKSVT TVSTQSHNQS SVSHEDTDTA PQMLSSKQDF
     HSNNLTTSQK AEITELSTIL EESGSQFEFT QFRKPSHIAQ NTSEVPGNQM VVLSTASKEW
     KDTDLHLPVD PSVGQTDHSK QFEGSAGVKQ SFPHLLEDTC NKNTSCFLPN INEMEFGGFC
     SALGTKLSVS NEALRKAMKL FSDIENSEEP SAKVGPRGFS SSAHHDSVAS VFKIKKQNTE
     KSFDEKSSKC QVTLQNNIEM TTCIFVGRNP EKYIKNTKHE DSYTSSQRNN LENSDGSMSS
     TSGPVYIHKG DSDLPADQGS KCPESCTQYA REENTQIKEN ISDLTCLEIM KAEETCMKSS
     DKKQLPSDKM EQNIKEFNIS FQTASGKNTR VSKESLNKSV NIFNRETDEL TVISDSLNSK
     ILHGINKDKM HTSCHKKAIS IKKVFEDHFP IVTVSQLPAQ QHPEYEIEST KEPTLLSFHT
     ASGKKVKIMQ ESLDKVKNLF DETQYVRKTA SFSQGSKPLK DSKKELTLAY EKIEVTASKC
     EEMQNFVSKE TEMLPQQNYH MYRQTENLKT SNGTSSKVQE NIENNVEKNP RICCICQSSY
     PVTEDSALAY YTEDSRKTCV RESSLSKGRK WLREQGDKLG TRNTIKIECV KEHTEDFAGN
     ASYEHSLVII RTEIDTNHVS ENQVSTLLSD PNVCHSYLSQ SSFCHCDDMH NDSGYFLKNK
     IDSDVPPDMK NAEGNTISPR VSATKERNLH PQTINEYCVQ KLETNTSPHA NKDVAIDPSL
     LDSRNCKVGS LVFITAHSQE TERTKEIVTD NCYKIVEQNR QSKPDTCQTS CHKVLDDSKD
     FICPSSSGDV CINSRKDSFC PHNEQILQHN QSMSGLKKAA TPPVGLETWD TSKSIREPPQ
     AAHPSRTYGI FSTASGKAIQ VSDASLEKAR QVFSEMDGDA KQLSSMVSLE GNEKPHHSVK
     RENSVVHSTQ GVLSLPKPLP GNVNSSVFSG FSTAGGKLVT VSESALHKVK GMLEEFDLIR
     TEHTLQHSPI PEDVSKILPQ PCAEIRTPEY PVNSKLQKTY NDKSSLPSNY KESGSSGNTQ
     SIEVSLQLSQ MERNQDTQLV LGTKVSHSKA NLLGKEQTLP QNIKVKTDEM KTFSDVPVKT
     NVGEYYSKES ENYFETEAVE SAKAFMEDDE LTDSEQTHAK CSLFTCPQNE TLFNSRTRKR
     GGVTVDAVGQ PPIKRSLLNE FDRIIESKGK SLTPSKSTPD GTVKDRSLFT HHMSLEPVTC
     GPFCSSKERQ GAQRPHLTSP AQELLSKGHP WRHSALEKSP SSPIVSILPA HDVSATRTER
     TRHSGKSTKV FVPPFKMKSQ FHGDEHFNSK NVNLEGKNQK STDGDREDGN DSHVRQFNKD
     LMSSLQSARD LQDMRIKNKE RRHLRLQPGS LYLTKSSTLP RISLQAAVGD RAPSACSPKQ
     LYIYGVSKEC INVNSKNAEY FQFDIQDHFG KEDLCAGKGF QLADGGWLIP SNDGKAGKEE
     FYRALCDTPG VDPKLISSIW VANHYRWIVW KLAAMEFAFP KEFANRCLNP ERVLLQLKYR
     YDVEIDNSRR SALKKILERD DTAAKTLVLC ISDIISPSTK VSETSGGKTS GEDANKVDTI
     ELTDGWYAVR AQLDPPLMAL VKSGKLTVGQ KIITQGAELV GSPDACAPLE APDSLRLKIS
     ANSTRPARWH SRLGFFRDPR PFPLPLSSLF SDGGNVGCVD IIVQRVYPLQ WVEKTVSGLY
     IFRSEREEEK EALRFAEAQQ KKLEALFTKV HTEFKDHEED TTQRCVLSRT LTRQQVHALQ
     DGAELYAAVQ YASDPDHLEA CFSEEQLRAL NNYRQMLNDK KQARIQSEFR KALESAEKEE
     GLSRDVTTVW KLRVTSYKKK EKSALLSIWR PSSDLSSLLT EGKRYRIYHL AVSKSKSKFE
     RPSIQLTATK RTQYQQLPVS SETLLQVYQP RESLHFSRLS DPAFQPPCSE VDVVGVVVSV
     VKPIGLAPLV YLSDECLNLL VVKFGIDLNE DIKPRVLIAA SNLQCQPEST SGVPTLFAGH
     FSIFSASPKE AYFQEKVNNL KHAIENIDTF YKEAEKKLIH VLEGDSPKWS TPNKDPTREP
     HAASTCCASD LLGSGGQFLR ISPTGQQSYQ SPLSHCTLKG KSMPLAHSAQ MAAKSWSGEN
     EIDDPKTCRK RRALDFLSRL PLPSPVSPIC TFVSPAAQKA FQPPRSCGTK YATPIKKEPS
     SPRRRTPFQK TSGVSLPDCD SVADEELALL STQALTPDSV GGNEQAFPGD STRNPQPAQR
     PDQQVGPRSR KESLRDCRGD SSEKLAVES
//