RA54B_HUMAN
ID RA54B_HUMAN Reviewed; 910 AA.
AC Q9Y620; F6WBS8;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=DNA repair and recombination protein RAD54B;
DE EC=3.6.4.-;
DE AltName: Full=RAD54 homolog B;
GN Name=RAD54B;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS
RP TYR-418 AND SER-593.
RX PubMed=10362364; DOI=10.1038/sj.onc.1202691;
RA Hiramoto T., Nakanishi T., Sumiyoshi T., Fukuda T., Matsuura S., Tauchi H.,
RA Komatsu K., Shibasaki Y., Inui H., Watatani M., Yasutomi M., Sumii K.,
RA Kajiyama G., Kamada N., Miyagawa K., Kamiya K.;
RT "Mutations of a novel human RAD54 homologue, RAD54B, in primary cancer.";
RL Oncogene 18:3422-3426(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 INTERACTION WITH RAD51.
RX PubMed=10851248; DOI=10.1074/jbc.m910306199;
RA Tanaka K., Hiramoto T., Fukuda T., Miyagawa K.;
RT "A novel human Rad54 homologue, Rad54B, associates with Rad51.";
RL J. Biol. Chem. 275:26316-26321(2000).
RN [6]
RP FUNCTION.
RX PubMed=11782437; DOI=10.1093/emboj/21.1.175;
RA Miyagawa K., Tsuruga T., Kinomura A., Usui K., Katsura M., Tashiro S.,
RA Mishima H., Tanaka K.;
RT "A role for RAD54B in homologous recombination in human cells.";
RL EMBO J. 21:175-180(2002).
RN [7]
RP FUNCTION, AND CHARACTERIZATION.
RX PubMed=11884632; DOI=10.1093/nar/30.6.1346;
RA Tanaka K., Kagawa W., Kinebuchi T., Kurumizaka H., Miyagawa K.;
RT "Human Rad54B is a double-stranded DNA-dependent ATPase and has biochemical
RT properties different from its structural homolog in yeast, Tid1/Rdh54.";
RL Nucleic Acids Res. 30:1346-1353(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [9]
RP VARIANTS GLU-833 AND VAL-899.
RX PubMed=25930971; DOI=10.1111/cge.12605;
RA Srour M., Hamdan F.F., Gan-Or Z., Labuda D., Nassif C., Oskoui M.,
RA Gana-Weisz M., Orr-Urtreger A., Rouleau G.A., Michaud J.L.;
RT "A homozygous mutation in SLC1A4 in siblings with severe intellectual
RT disability and microcephaly.";
RL Clin. Genet. 88:E1-E4(2015).
CC -!- FUNCTION: Involved in DNA repair and mitotic recombination. May play an
CC active role in recombination processes in concert with other members of
CC the RAD52 epistasis group. {ECO:0000269|PubMed:11782437,
CC ECO:0000269|PubMed:11884632}.
CC -!- SUBUNIT: Interacts with RAD51 through the NH2-terminal domain.
CC Immunoprecipitation experiments show that the interaction is
CC constitutive and not induced by ionizing radiation. The interaction may
CC be indirect. {ECO:0000269|PubMed:10851248}.
CC -!- INTERACTION:
CC Q9Y620; P54253: ATXN1; NbExp=3; IntAct=EBI-740830, EBI-930964;
CC Q9Y620; Q8TBB1: LNX1; NbExp=4; IntAct=EBI-740830, EBI-739832;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y620-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y620-2; Sequence=VSP_045956, VSP_045957;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in testis and spleen.
CC Relatively low levels observed in thymus, prostate, ovary and colon.
CC {ECO:0000269|PubMed:10362364}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AF112481; AAD34331.1; -; mRNA.
DR EMBL; AL523600; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC023632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001965; AAH01965.1; -; mRNA.
DR CCDS; CCDS56546.1; -. [Q9Y620-2]
DR CCDS; CCDS6262.1; -. [Q9Y620-1]
DR RefSeq; NP_001192192.1; NM_001205263.1.
DR RefSeq; NP_036547.1; NM_012415.3. [Q9Y620-1]
DR AlphaFoldDB; Q9Y620; -.
DR SMR; Q9Y620; -.
DR BioGRID; 117321; 45.
DR IntAct; Q9Y620; 18.
DR MINT; Q9Y620; -.
DR STRING; 9606.ENSP00000336606; -.
DR GlyGen; Q9Y620; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y620; -.
DR PhosphoSitePlus; Q9Y620; -.
DR BioMuta; RAD54B; -.
DR DMDM; 51316548; -.
DR EPD; Q9Y620; -.
DR jPOST; Q9Y620; -.
DR MassIVE; Q9Y620; -.
DR MaxQB; Q9Y620; -.
DR PaxDb; Q9Y620; -.
DR PeptideAtlas; Q9Y620; -.
DR PRIDE; Q9Y620; -.
DR ProteomicsDB; 28103; -.
DR ProteomicsDB; 86588; -. [Q9Y620-1]
DR Antibodypedia; 1882; 214 antibodies from 27 providers.
DR DNASU; 25788; -.
DR Ensembl; ENST00000297592.5; ENSP00000430153.2; ENSG00000197275.14. [Q9Y620-2]
DR Ensembl; ENST00000336148.10; ENSP00000336606.5; ENSG00000197275.14. [Q9Y620-1]
DR GeneID; 25788; -.
DR KEGG; hsa:25788; -.
DR MANE-Select; ENST00000336148.10; ENSP00000336606.5; NM_012415.3; NP_036547.1.
DR UCSC; uc003ygk.4; human. [Q9Y620-1]
DR CTD; 25788; -.
DR DisGeNET; 25788; -.
DR GeneCards; RAD54B; -.
DR HGNC; HGNC:17228; RAD54B.
DR HPA; ENSG00000197275; Tissue enhanced (retina).
DR MalaCards; RAD54B; -.
DR MIM; 604289; gene.
DR neXtProt; NX_Q9Y620; -.
DR OpenTargets; ENSG00000197275; -.
DR PharmGKB; PA134927202; -.
DR VEuPathDB; HostDB:ENSG00000197275; -.
DR eggNOG; KOG0390; Eukaryota.
DR GeneTree; ENSGT00940000156966; -.
DR InParanoid; Q9Y620; -.
DR OMA; QFLYECV; -.
DR OrthoDB; 93727at2759; -.
DR PhylomeDB; Q9Y620; -.
DR TreeFam; TF101223; -.
DR BRENDA; 3.6.4.B9; 2681.
DR PathwayCommons; Q9Y620; -.
DR SignaLink; Q9Y620; -.
DR BioGRID-ORCS; 25788; 14 hits in 1083 CRISPR screens.
DR ChiTaRS; RAD54B; human.
DR GenomeRNAi; 25788; -.
DR Pharos; Q9Y620; Tbio.
DR PRO; PR:Q9Y620; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9Y620; protein.
DR Bgee; ENSG00000197275; Expressed in right uterine tube and 127 other tissues.
DR ExpressionAtlas; Q9Y620; baseline and differential.
DR Genevisible; Q9Y620; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; TAS:ProtInc.
DR GO; GO:0015616; F:DNA translocase activity; IDA:MGI.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; TAS:ProtInc.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:MGI.
DR GO; GO:0006312; P:mitotic recombination; 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 Alternative splicing; ATP-binding; DNA damage; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..910
FT /note="DNA repair and recombination protein RAD54B"
FT /id="PRO_0000074340"
FT DOMAIN 313..480
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 649..810
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 431..434
FT /note="DEGH box"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 326..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 103..117
FT /note="HSAPKEVAVSKEQEE -> QTWMRRHRLVPVHYR (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_045956"
FT VAR_SEQ 118..910
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_045957"
FT VARIANT 30
FT /note="L -> V (in dbSNP:rs28910279)"
FT /id="VAR_034430"
FT VARIANT 97
FT /note="D -> H (in dbSNP:rs2919661)"
FT /id="VAR_037885"
FT VARIANT 418
FT /note="D -> Y (in a colon cancer sample;
FT dbSNP:rs119490107)"
FT /evidence="ECO:0000269|PubMed:10362364"
FT /id="VAR_019563"
FT VARIANT 593
FT /note="N -> S (in a non-Hodgkin lymphoma sample;
FT dbSNP:rs114216685)"
FT /evidence="ECO:0000269|PubMed:10362364"
FT /id="VAR_019564"
FT VARIANT 833
FT /note="G -> E (in dbSNP:rs752511501)"
FT /evidence="ECO:0000269|PubMed:25930971"
FT /id="VAR_075089"
FT VARIANT 899
FT /note="I -> V (in dbSNP:rs150017319)"
FT /evidence="ECO:0000269|PubMed:25930971"
FT /id="VAR_075090"
SQ SEQUENCE 910 AA; 102967 MW; 0167288FBA95FBC5 CRC64;
MRRSAAPSQL QGNSFKKPKF IPPGRSNPGL NEEITKLNPD IKLFEGVAIN NTFLPSQNDL
RICSLNLPSE ESTREINNRD NCSGKYCFEA PTLATLDPPH TVHSAPKEVA VSKEQEEKSD
SLVKYFSVVW CKPSKKKHKK WEGDAVLIVK GKSFILKNLE GKDIGRGIGY KFKELEKIEE
GQTLMICGKE IEVMGVISPD DFSSGRCFQL GGGSTAISHS SQVARKCFSN PFKSVCKPSS
KENRQNDFQN CKPRHDPYTP NSLVMPRPDK NHQWVFNKNC FPLVDVVIDP YLVYHLRPHQ
KEGIIFLYEC VMGMRMNGRC GAILADEMGL GKTLQCISLI WTLQCQGPYG GKPVIKKTLI
VTPGSLVNNW KKEFQKWLGS ERIKIFTVDQ DHKVEEFIKS IFYSVLIISY EMLLRSLDQI
KNIKFDLLIC DEGHRLKNSA IKTTTALISL SCEKRIILTG TPIQNDLQEF FALIDFVNPG
ILGSLSSYRK IYEEPIILSR EPSASEEEKE LGERRAAELT CLTGLFILRR TQEIINKYLP
PKIENVVFCR PGALQIELYR KLLNSQVVRF CLQGLLENSP HLICIGALKK LCNHPCLLFN
SIKEKECSST CDKNEEKSLY KGLLSVFPAD YNPLLFTEKE SGKLQVLSKL LAVIHELRPT
EKVVLVSNYT QTLNILQEVC KRHGYAYTRL DGQTPISQRQ QIVDGFNSQH SSFFIFLLSS
KAGGVGLNLI GGSHLILYDI DWNPATDIQA MSRVWRDGQK YPVHIYRLLT TGTIEEKIYQ
RQISKQGLCG AVVDLTKTSE HIQFSVEELK NLFTLHESSD CVTHDLLDCE CTGEEVHTGD
SLEKFIVSRD CQLGPHHQKS NSLKPLSMSQ LKQWKHFSGD HLNLTDPFLE RITENVSFIF
QNITTQATGT
