BRCA2_MOUSE
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 03-AUG-2022, entry version 190.
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; P97929; -.
DR PeptideAtlas; P97929; -.
DR PRIDE; P97929; -.
DR ProteomicsDB; 273841; -.
DR Antibodypedia; 7788; 332 antibodies from 41 providers.
DR DNASU; 12190; -.
DR Ensembl; ENSMUST00000044620; ENSMUSP00000038576; ENSMUSG00000041147.
DR Ensembl; ENSMUST00000202313; ENSMUSP00000144150; ENSMUSG00000041147.
DR GeneID; 12190; -.
DR KEGG; mmu:12190; -.
DR UCSC; uc009aty.2; mouse.
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; PYGSLFC; -.
DR OrthoDB; 257485at2759; -.
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 114 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 193 other tissues.
DR ExpressionAtlas; P97929; baseline and differential.
DR Genevisible; P97929; MM.
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:H3 histone acetyltransferase activity; ISO:MGI.
DR GO; GO:0010485; F:H4 histone 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:0008022; F:protein C-terminus 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:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
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: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:0035518; P:histone H2A monoubiquitination; IC:ComplexPortal.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0043967; P:histone H4 acetylation; ISO:MGI.
DR GO; GO:0031619; P:homologous chromosome orientation involved in meiotic metaphase I plate congression; 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:0045931; P:positive regulation of mitotic cell cycle; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; IC:ComplexPortal.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:MGI.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0048478; P:replication fork protection; 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; cd04495; BRCA2DBD_OB3; 1.
DR Gene3D; 2.40.50.140; -; 3.
DR InterPro; IPR015525; BRCA2.
DR InterPro; IPR015252; BRCA2_hlx.
DR InterPro; IPR036315; BRCA2_hlx_sf.
DR InterPro; IPR015187; BRCA2_OB_1.
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; PTHR11289; 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; PF09121; Tower; 1.
DR PIRSF; PIRSF002397; BRCA2; 1.
DR SMART; SM01341; Tower; 1.
DR SUPFAM; SSF50249; SSF50249; 3.
DR SUPFAM; SSF81872; SSF81872; 1.
DR PROSITE; PS50138; BRCA2_REPEAT; 6.
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
