RAD54_HUMAN
ID RAD54_HUMAN Reviewed; 747 AA.
AC Q92698; Q5TE31; Q6IUY3;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=DNA repair and recombination protein RAD54-like;
DE EC=3.6.4.12 {ECO:0000269|PubMed:9774452};
DE AltName: Full=RAD54 homolog;
DE Short=hHR54;
DE Short=hRAD54;
GN Name=RAD54L; Synonyms=RAD54A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, CELL CYCLE REGULATION,
RP AND MUTAGENESIS OF LYS-189.
RC TISSUE=Testis;
RX PubMed=8805304; DOI=10.1016/s0960-9822(02)00606-1;
RA Kanaar R., Troelstra C., Swagemakers S.M.A., Essers J., Smit B.,
RA Franssen J.-H., Pastink A., Bezzubova O.Y., Buerstedde J.-M., Clever B.,
RA Heyer W.-D., Hoeijmakers J.H.J.;
RT "Human and mouse homologs of the Saccharomyces cerevisiae RAD54 DNA repair
RT gene: evidence for functional conservation.";
RL Curr. Biol. 6:828-838(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-21; MET-74; CYS-202;
RP GLN-380; CYS-534 AND THR-583.
RG NIEHS SNPs program;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9192813;
RA Rasio D., Murakumo Y., Robbins D., Roth T., Silver A., Negrini M.,
RA Schmidt C., Burczak J., Fishel R., Croce C.M.;
RT "Characterization of the human homologue of RAD54: a gene located on
RT chromosome 1p32 at a region of high loss of heterozygosity in breast
RT tumors.";
RL Cancer Res. 57:2378-2383(1997).
RN [6]
RP INTERACTION WITH RAD51.
RX PubMed=9321665; DOI=10.1093/nar/25.20.4106;
RA Golub E.I., Kovalenko O.V., Gupta R.C., Ward D.C., Radding C.M.;
RT "Interaction of human recombination proteins Rad51 and Rad54.";
RL Nucleic Acids Res. 25:4106-4110(1997).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9774452; DOI=10.1074/jbc.273.43.28292;
RA Swagemakers S.M.A., Essers J., de Wit J., Hoeijmakers J.H.J., Kanaar R.;
RT "The human RAD54 recombinational DNA repair protein is a double-stranded
RT DNA-dependent ATPase.";
RL J. Biol. Chem. 273:28292-28297(1998).
RN [8]
RP LACK OF INVOLVEMENT IN PARATHYROID ADENOMAS.
RX PubMed=10449612;
RX DOI=10.1002/(sici)1097-0215(19990924)83:1<80::aid-ijc15>3.0.co;2-e;
RA Carling T., Imanishi Y., Gaz R.D., Arnold A.;
RT "Analysis of the RAD54 gene on chromosome 1p as a potential tumor-
RT suppressor gene in parathyroid adenomas.";
RL Int. J. Cancer 83:80-82(1999).
RN [9]
RP FUNCTION.
RX PubMed=11459989; DOI=10.1073/pnas.151056798;
RA Ristic D., Wyman C., Paulusma C., Kanaar R.;
RT "The architecture of the human Rad54-DNA complex provides evidence for
RT protein translocation along DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8454-8460(2001).
RN [10]
RP FUNCTION.
RX PubMed=12205100; DOI=10.1074/jbc.m208004200;
RA Sigurdsson S., Van Komen S., Petukhova G., Sung P.;
RT "Homologous DNA pairing by human recombination factors Rad51 and Rad54.";
RL J. Biol. Chem. 277:42790-42794(2002).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP FUNCTION, AND INTERACTION WITH NAP1L1.
RX PubMed=24798879; DOI=10.1038/srep04863;
RA Machida S., Takaku M., Ikura M., Sun J., Suzuki H., Kobayashi W.,
RA Kinomura A., Osakabe A., Tachiwana H., Horikoshi Y., Fukuto A., Matsuda R.,
RA Ura K., Tashiro S., Ikura T., Kurumizaka H.;
RT "Nap1 stimulates homologous recombination by RAD51 and RAD54 in higher-
RT ordered chromatin containing histone H1.";
RL Sci. Rep. 4:4863-4863(2014).
RN [13]
RP PHOSPHORYLATION AT SER-572, MUTAGENESIS OF SER-572, AND FUNCTION.
RX PubMed=27264870; DOI=10.1016/j.molcel.2016.04.032;
RA Spies J., Waizenegger A., Barton O., Suerder M., Wright W.D., Heyer W.D.,
RA Loebrich M.;
RT "Nek1 Regulates Rad54 to Orchestrate Homologous Recombination and
RT Replication Fork Stability.";
RL Mol. Cell 62:903-917(2016).
RN [14]
RP ACETYLATION AT LYS-515, INTERACTION WITH BRD9, FUNCTION, AND MUTAGENESIS OF
RP LYS-515.
RX PubMed=32457312; DOI=10.1038/s41467-020-16443-x;
RA Zhou Q., Huang J., Zhang C., Zhao F., Kim W., Tu X., Zhang Y., Nowsheen S.,
RA Zhu Q., Deng M., Chen Y., Qin B., Luo K., Liu B., Lou Z., Mutter R.W.,
RA Yuan J.;
RT "The bromodomain containing protein BRD-9 orchestrates RAD51-RAD54 complex
RT formation and regulates homologous recombination-mediated repair.";
RL Nat. Commun. 11:2639-2639(2020).
RN [15]
RP VARIANTS HIS-63; GLU-151; ARG-325 AND GLU-444.
RX PubMed=10362365; DOI=10.1038/sj.onc.1202692;
RA Matsuda M., Miyagawa K., Takahashi M., Fukuda T., Kataoka T., Asahara T.,
RA Inui H., Watatani M., Yasutomi M., Kamada N., Dohi K., Kamiya K.;
RT "Mutations in the RAD54 recombination gene in primary cancers.";
RL Oncogene 18:3427-3430(1999).
CC -!- FUNCTION: Plays an essential role in homologous recombination (HR)
CC which is a major pathway for repairing DNA double-strand breaks (DSBs),
CC single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication
CC forks (PubMed:9774452, PubMed:24798879, PubMed:32457312,
CC PubMed:11459989, PubMed:12205100, PubMed:27264870). Acts as a molecular
CC motor during the homology search and guides RAD51 ssDNA along a donor
CC dsDNA thereby changing the homology search from the diffusion-based
CC mechanism to a motor-guided mechanism. Also plays an essential role in
CC RAD51-mediated synaptic complex formation which consists of three
CC strands encased in a protein filament formed once homology is
CC recognized. Once DNA strand exchange occured, dissociates RAD51 from
CC nucleoprotein filaments formed on dsDNA (By similarity).
CC {ECO:0000250|UniProtKB:P32863, ECO:0000269|PubMed:11459989,
CC ECO:0000269|PubMed:12205100, ECO:0000269|PubMed:24798879,
CC ECO:0000269|PubMed:27264870, ECO:0000269|PubMed:32457312,
CC ECO:0000269|PubMed:9774452}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000269|PubMed:9774452};
CC -!- SUBUNIT: Homohexamer (By similarity). Interacts (via N-terminus) with
CC RAD51 (PubMed:9321665). Interacts with NAP1L1 (PubMed:24798879).
CC Interacts with BRD9; this interaction orchestrates RAD51-RAD54 complex
CC formation (PubMed:32457312). {ECO:0000250|UniProtKB:Q7ZV09,
CC ECO:0000269|PubMed:24798879, ECO:0000269|PubMed:32457312,
CC ECO:0000269|PubMed:9321665}.
CC -!- INTERACTION:
CC Q92698; Q96HA8: NTAQ1; NbExp=4; IntAct=EBI-5333483, EBI-741158;
CC Q92698; Q9H2K2: TNKS2; NbExp=3; IntAct=EBI-5333483, EBI-4398527;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8805304}.
CC -!- INDUCTION: Expression increases approximately 3-fold in late G1 phase
CC compared to other phases of the cell cycle.
CC -!- PTM: Acetylated. Acetylation promotes interaction with BRD9, and
CC subsequently with RAD54, which is essential for homologous
CC recombination (HR). {ECO:0000269|PubMed:32457312}.
CC -!- PTM: Phosphorylated. Phosphorylation at Ser-572 by NEK1 specifically in
CC G2 phase allows efficient removal of RAD51 filaments from DNA.
CC {ECO:0000269|PubMed:27264870}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rad54l/";
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DR EMBL; X97795; CAA66379.1; -; mRNA.
DR EMBL; AY623117; AAT38113.1; -; Genomic_DNA.
DR EMBL; AL121602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC121059; AAI21060.1; -; mRNA.
DR EMBL; BC121060; AAI21061.1; -; mRNA.
DR CCDS; CCDS532.1; -.
DR RefSeq; NP_001136020.1; NM_001142548.1.
DR RefSeq; NP_003570.2; NM_003579.3.
DR AlphaFoldDB; Q92698; -.
DR SMR; Q92698; -.
DR BioGRID; 114018; 9.
DR DIP; DIP-48628N; -.
DR ELM; Q92698; -.
DR IntAct; Q92698; 9.
DR STRING; 9606.ENSP00000361043; -.
DR BindingDB; Q92698; -.
DR ChEMBL; CHEMBL2146297; -.
DR iPTMnet; Q92698; -.
DR PhosphoSitePlus; Q92698; -.
DR BioMuta; RAD54L; -.
DR DMDM; 51316508; -.
DR EPD; Q92698; -.
DR jPOST; Q92698; -.
DR MassIVE; Q92698; -.
DR MaxQB; Q92698; -.
DR PaxDb; Q92698; -.
DR PeptideAtlas; Q92698; -.
DR PRIDE; Q92698; -.
DR ProteomicsDB; 75414; -.
DR Antibodypedia; 18708; 266 antibodies from 31 providers.
DR DNASU; 8438; -.
DR Ensembl; ENST00000371975.9; ENSP00000361043.4; ENSG00000085999.13.
DR Ensembl; ENST00000442598.5; ENSP00000396113.1; ENSG00000085999.13.
DR Ensembl; ENST00000671528.1; ENSP00000499652.1; ENSG00000085999.13.
DR GeneID; 8438; -.
DR KEGG; hsa:8438; -.
DR MANE-Select; ENST00000371975.9; ENSP00000361043.4; NM_003579.4; NP_003570.2.
DR UCSC; uc001cpl.3; human.
DR CTD; 8438; -.
DR DisGeNET; 8438; -.
DR GeneCards; RAD54L; -.
DR HGNC; HGNC:9826; RAD54L.
DR HPA; ENSG00000085999; Tissue enhanced (lymphoid tissue, testis).
DR MalaCards; RAD54L; -.
DR MIM; 603615; gene.
DR neXtProt; NX_Q92698; -.
DR OpenTargets; ENSG00000085999; -.
DR Orphanet; 227535; Hereditary breast cancer.
DR PharmGKB; PA34181; -.
DR VEuPathDB; HostDB:ENSG00000085999; -.
DR eggNOG; KOG0390; Eukaryota.
DR GeneTree; ENSGT00940000156897; -.
DR HOGENOM; CLU_000315_10_5_1; -.
DR InParanoid; Q92698; -.
DR OMA; YTEHERM; -.
DR OrthoDB; 93727at2759; -.
DR PhylomeDB; Q92698; -.
DR TreeFam; TF101224; -.
DR BRENDA; 3.6.4.B9; 2681.
DR PathwayCommons; Q92698; -.
DR SignaLink; Q92698; -.
DR BioGRID-ORCS; 8438; 43 hits in 1084 CRISPR screens.
DR ChiTaRS; RAD54L; human.
DR GeneWiki; DNA_repair_and_recombination_protein_RAD54-like; -.
DR GenomeRNAi; 8438; -.
DR Pharos; Q92698; Tbio.
DR PRO; PR:Q92698; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q92698; protein.
DR Bgee; ENSG00000085999; Expressed in left testis and 100 other tissues.
DR ExpressionAtlas; Q92698; baseline and differential.
DR Genevisible; Q92698; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0036310; F:ATP-dependent DNA/DNA annealing activity; IDA:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0015616; F:DNA translocase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl.
DR GO; GO:0006310; P:DNA recombination; TAS:ProtInc.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; TAS:ProtInc.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..747
FT /note="DNA repair and recombination protein RAD54-like"
FT /id="PRO_0000074337"
FT DOMAIN 170..345
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 500..653
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..9
FT /note="Required for chromatin remodeling, strand pairing
FT activities and coupling of ATPase activity"
FT /evidence="ECO:0000250"
FT MOTIF 296..299
FT /note="DEGH box"
FT COMPBIAS 14..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 183..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 515
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:32457312"
FT MOD_RES 572
FT /note="Phosphoserine; by NEK1"
FT /evidence="ECO:0000269|PubMed:27264870"
FT VARIANT 21
FT /note="D -> G (in dbSNP:rs28363192)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_055363"
FT VARIANT 63
FT /note="P -> H (in a colon adenocarcinoma sample;
FT dbSNP:rs121908688)"
FT /evidence="ECO:0000269|PubMed:10362365"
FT /id="VAR_019559"
FT VARIANT 74
FT /note="I -> M (in dbSNP:rs28363209)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_055364"
FT VARIANT 151
FT /note="K -> E (in dbSNP:rs2295466)"
FT /evidence="ECO:0000269|PubMed:10362365"
FT /id="VAR_019560"
FT VARIANT 202
FT /note="R -> C (in dbSNP:rs28363218)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_055365"
FT VARIANT 325
FT /note="G -> R (in a breast cancer sample; invasive ductal;
FT dbSNP:rs121908690)"
FT /evidence="ECO:0000269|PubMed:10362365"
FT /id="VAR_019561"
FT VARIANT 380
FT /note="R -> Q (in dbSNP:rs28363234)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_055366"
FT VARIANT 444
FT /note="V -> E (in a non-Hodgkin lymphoma sample;
FT dbSNP:rs121908689)"
FT /evidence="ECO:0000269|PubMed:10362365"
FT /id="VAR_019562"
FT VARIANT 534
FT /note="R -> C (in dbSNP:rs28363240)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_055367"
FT VARIANT 583
FT /note="I -> T (in dbSNP:rs28363243)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_055368"
FT MUTAGEN 189
FT /note="K->R: Unable to rescue the MMS-sensitive phenotype
FT of S cerevisiae rad54delta cells."
FT /evidence="ECO:0000269|PubMed:8805304"
FT MUTAGEN 515
FT /note="K->R: Loss of acetylation."
FT /evidence="ECO:0000269|PubMed:32457312"
FT MUTAGEN 572
FT /note="S->A: Defect in homologous recombination (HR)."
FT /evidence="ECO:0000269|PubMed:27264870"
FT MUTAGEN 572
FT /note="S->E: Promotes homologous recombination (HR), but
FT causes RAD51 removal from chromatin."
FT /evidence="ECO:0000269|PubMed:27264870"
FT CONFLICT 738
FT /note="R -> H (in Ref. 1; CAA66379)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 747 AA; 84352 MW; 718100974CA6687B CRC64;
MRRSLAPSQL AKRKPEGRSC DDEDWQPGLV TPRKRKSSSE TQIQECFLSP FRKPLSQLTN
QPPCLDSSQH EAFIRSILSK PFKVPIPNYQ GPLGSRALGL KRAGVRRALH DPLEKDALVL
YEPPPLSAHD QLKLDKEKLP VHVVVDPILS KVLRPHQREG VKFLWECVTS RRIPGSHGCI
MADEMGLGKT LQCITLMWTL LRQSPECKPE IDKAVVVSPS SLVKNWYNEV GKWLGGRIQP
LAIDGGSKDE IDQKLEGFMN QRGARVSSPI LIISYETFRL HVGVLQKGSV GLVICDEGHR
LKNSENQTYQ ALDSLNTSRR VLISGTPIQN DLLEYFSLVH FVNSGILGTA HEFKKHFELP
ILKGRDAAAS EADRQLGEER LRELTSIVNR CLIRRTSDIL SKYLPVKIEQ VVCCRLTPLQ
TELYKRFLRQ AKPAEELLEG KMSVSSLSSI TSLKKLCNHP ALIYDKCVEE EDGFVGALDL
FPPGYSSKAL EPQLSGKMLV LDYILAVTRS RSSDKVVLVS NYTQTLDLFE KLCRARRYLY
VRLDGTMSIK KRAKVVERFN SPSSPDFVFM LSSKAGGCGL NLIGANRLVM FDPDWNPAND
EQAMARVWRD GQKKTCYIYR LLSAGTIEEK IFQRQSHKKA LSSCVVDEEQ DVERHFSLGE
LKELFILDEA SLSDTHDRLH CRRCVNSRQI RPPPDGSDCT SDLAGWNHCT DKWGLRDEVL
QAAWDAASTA ITFVFHQRSH EEQRGLR
