RA54B_MOUSE
ID RA54B_MOUSE Reviewed; 886 AA.
AC Q6PFE3; A2AIV0;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=DNA repair and recombination protein RAD54B;
DE EC=3.6.4.-;
DE AltName: Full=RAD54 homolog B;
GN Name=Rad54b;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain;
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 [3]
RP FUNCTION.
RX PubMed=12548566; DOI=10.1002/immu.200310009;
RA Bross L., Wesoly J., Buerstedde J.-M., Kanaar R., Jacobs H.;
RT "Somatic hypermutation does not require Rad54 and Rad54B-mediated
RT homologous recombination.";
RL Eur. J. Immunol. 33:352-357(2003).
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:12548566}.
CC -!- SUBUNIT: Interacts with RAD51 through the NH2-terminal domain.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AL732538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057604; AAH57604.1; -; mRNA.
DR CCDS; CCDS17970.1; -.
DR RefSeq; NP_001034645.1; NM_001039556.3.
DR AlphaFoldDB; Q6PFE3; -.
DR SMR; Q6PFE3; -.
DR BioGRID; 550136; 4.
DR IntAct; Q6PFE3; 1.
DR MINT; Q6PFE3; -.
DR STRING; 10090.ENSMUSP00000066977; -.
DR iPTMnet; Q6PFE3; -.
DR PhosphoSitePlus; Q6PFE3; -.
DR EPD; Q6PFE3; -.
DR MaxQB; Q6PFE3; -.
DR PaxDb; Q6PFE3; -.
DR PRIDE; Q6PFE3; -.
DR ProteomicsDB; 300340; -.
DR Antibodypedia; 1882; 214 antibodies from 27 providers.
DR Ensembl; ENSMUST00000070755; ENSMUSP00000066977; ENSMUSG00000078773.
DR GeneID; 623474; -.
DR KEGG; mmu:623474; -.
DR UCSC; uc008rzs.2; mouse.
DR CTD; 25788; -.
DR MGI; MGI:3605986; Rad54b.
DR VEuPathDB; HostDB:ENSMUSG00000078773; -.
DR eggNOG; KOG0390; Eukaryota.
DR GeneTree; ENSGT00940000156966; -.
DR HOGENOM; CLU_000315_10_1_1; -.
DR InParanoid; Q6PFE3; -.
DR OMA; QFLYECV; -.
DR OrthoDB; 93727at2759; -.
DR PhylomeDB; Q6PFE3; -.
DR TreeFam; TF101223; -.
DR BioGRID-ORCS; 623474; 3 hits in 111 CRISPR screens.
DR ChiTaRS; Rad54b; mouse.
DR PRO; PR:Q6PFE3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6PFE3; protein.
DR Bgee; ENSMUSG00000078773; Expressed in dorsal pancreas and 167 other tissues.
DR ExpressionAtlas; Q6PFE3; baseline and differential.
DR Genevisible; Q6PFE3; MM.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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:0015616; F:DNA translocase activity; ISO:MGI.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0008340; P:determination of adult lifespan; IGI:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:MGI.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
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 2: Evidence at transcript level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..886
FT /note="DNA repair and recombination protein RAD54B"
FT /id="PRO_0000074341"
FT DOMAIN 291..458
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 627..788
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 409..412
FT /note="DEGH box"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 304..311
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:0000250|UniProtKB:Q9Y620"
SQ SEQUENCE 886 AA; 99338 MW; A723501E5D5723A6 CRC64;
MRRSAAPSQV QGKSFKKTRF IPPGRSNADV SKEITKMSPD PKLFQGAEQS QNDPGVCSSN
PCPSEGIPRE VGDGTRVDPL PPVHSASKEI TESKAQEEEA SSLLKYFSVV WCKASKKKHK
KWEGDAILIV RGRSFTLKDL EGKDIGRGIG YKFKDLENVE EGQTLIIGGK EIEILGTISS
DDFNSGKCFQ HGSGSPAVPS SQAARKCFSN PFKSVCQSTQ AQGKRWNDCR PRHNPCTPNA
LVMPRPDENH QRMFNRHCSP IVDVVIDPHL VHHLRPHQKD GIIFLYECVM GMRAVGKCGA
ILADEMGLGK TLQCISLIWT LQCQGPYGGK PVIKKTLIVT PGSLVNNWRK EFQKWLGSER
IKIFTVDQDH KVEEFINSTF HSVLIISYEM LLRSLDQIKT IPFGLLICDE GHRLKNSSIK
TTTALSSLSC EKTVILTGTP VQNDLQEFFA LVDFVNPGIL GSLSSYRKIY EEPIIISREP
SSSKEERELG ERRATELTRL TGRFILRRTQ EVINKYLPPK IENVVFCRPG ALQIELYRKL
LRSQSVRFCL QGLLENSAHL ICIGALKKLC NHPCLLFSSV KGKEFSSSCE ENEERNLCQG
LLSVFPAGYN PLQFSEEESG KLQVLVKLLA VIHELRPTEK VILVSNYRQT LNVLEEVCKR
HGYACARLDG QTPVSQRQHI VDSFNSKYST DFIFLLSSKA GGVGLNLIGG SHLILYDIDW
NPATDIQAMS RVWRDGQKHP VHIYRLLTTG TIEEKIYQRQ ISKQGLSGAV VDLTRSSEHI
QFSVEELKNL FTLHESSHCV THDLLDCECT GEKGHTEDAS EGPVASRQCQ FGPQKSDALR
PLSMSQLKQW KHFSGDHLNL PDPFLERIRE NVSFFFQNIT NQAPAV
