RAD52_MOUSE
ID RAD52_MOUSE Reviewed; 420 AA.
AC P43352;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=DNA repair protein RAD52 homolog;
GN Name=Rad52;
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=C57BL/6J;
RX PubMed=7829098; DOI=10.1006/geno.1994.1503;
RA Bendixen C., Sunjevaric I., Bauchwitz R., Rothstein R.;
RT "Identification of a mouse homologue of the Saccharomyces cerevisiae
RT recombination and repair gene, RAD52.";
RL Genomics 23:300-303(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/HeJ;
RX PubMed=7774919; DOI=10.1016/0888-7543(95)80126-7;
RA Shen Z., Denison K., Lobb R., Gatewood J.M., Chen D.J.;
RT "The human and mouse homologs of the yeast RAD52 gene: cDNA cloning,
RT sequence analysis, assignment to human chromosome 12p12.2-p13, and mRNA
RT expression in mouse tissues.";
RL Genomics 25:199-206(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Thymus;
RX PubMed=7526206; DOI=10.1016/0921-8777(94)90040-x;
RA Muris D.F., Bezzubova O., Buerstedde J.-M., Vreeken K., Balajee A.S.,
RA Osgood C.J., Troelstra C., Hoeijmakers J.H., Ostermann K., Schmidt H.,
RA Natarajan A.T., Eeken J.C.J., Lohman P.H.M., Pastink A.;
RT "Cloning of human and mouse genes homologous to RAD52, a yeast gene
RT involved in DNA repair and recombination.";
RL Mutat. Res. 315:295-305(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J;
RA Sunjevaric I., Bendixen C., Mortensen U.H., Miljkovic V., Rothstein R.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in double-stranded break repair. Plays a central
CC role in genetic recombination and DNA repair by promoting the annealing
CC of complementary single-stranded DNA and by stimulation of the RAD51
CC recombinase. {ECO:0000250|UniProtKB:P43351}.
CC -!- SUBUNIT: The full-length protein forms heptameric rings. Interacts with
CC ABL1. Interacts with RPA2; the interaction is direct and associates
CC RAD52 with the RPA complex. Interacts with RAD51AP1.
CC {ECO:0000250|UniProtKB:P43351}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: Phosphorylated upon DNA damage by ABL1, and probably by ATM or
CC ATR. {ECO:0000250|UniProtKB:P43351}.
CC -!- SIMILARITY: Belongs to the RAD52 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U06837; AAA75441.1; -; mRNA.
DR EMBL; U12135; AAA85794.1; -; mRNA.
DR EMBL; Z32767; CAA83659.1; -; mRNA.
DR EMBL; AF004854; AAB69174.1; -; Genomic_DNA.
DR CCDS; CCDS51887.1; -.
DR PIR; A55727; A55727.
DR PIR; A56529; A56529.
DR RefSeq; NP_001159853.1; NM_001166381.1.
DR AlphaFoldDB; P43352; -.
DR SMR; P43352; -.
DR STRING; 10090.ENSMUSP00000125502; -.
DR iPTMnet; P43352; -.
DR PhosphoSitePlus; P43352; -.
DR PaxDb; P43352; -.
DR PRIDE; P43352; -.
DR ProteomicsDB; 255072; -.
DR Antibodypedia; 10276; 426 antibodies from 35 providers.
DR DNASU; 19365; -.
DR Ensembl; ENSMUST00000162461; ENSMUSP00000125502; ENSMUSG00000030166.
DR GeneID; 19365; -.
DR KEGG; mmu:19365; -.
DR UCSC; uc009dmq.2; mouse.
DR CTD; 5893; -.
DR MGI; MGI:101949; Rad52.
DR VEuPathDB; HostDB:ENSMUSG00000030166; -.
DR eggNOG; KOG4141; Eukaryota.
DR GeneTree; ENSGT00390000008766; -.
DR InParanoid; P43352; -.
DR PhylomeDB; P43352; -.
DR TreeFam; TF101221; -.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-MMU-5685939; HDR through MMEJ (alt-NHEJ).
DR BioGRID-ORCS; 19365; 7 hits in 110 CRISPR screens.
DR PRO; PR:P43352; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P43352; protein.
DR Bgee; ENSMUSG00000030166; Expressed in ascending aorta and 232 other tissues.
DR ExpressionAtlas; P43352; baseline and differential.
DR Genevisible; P43352; MM.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:MGI.
DR GO; GO:0010792; P:DNA double-strand break processing involved in repair via single-strand annealing; IMP:CACAO.
DR GO; GO:0000730; P:DNA recombinase assembly; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:MGI.
DR GO; GO:0045002; P:double-strand break repair via single-strand annealing; IBA:GO_Central.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; ISO:MGI.
DR Gene3D; 3.30.390.80; -; 1.
DR InterPro; IPR004585; DNA_recomb/repair_Rad52.
DR InterPro; IPR041247; Rad52_fam.
DR InterPro; IPR007232; Rad52_Rad59_Rad22.
DR InterPro; IPR042525; Rad52_Rad59_Rad22_sf.
DR PANTHER; PTHR12132; PTHR12132; 1.
DR Pfam; PF04098; Rad52_Rad22; 1.
DR TIGRFAMs; TIGR00607; rad52; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA recombination; DNA repair; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..420
FT /note="DNA repair protein RAD52 homolog"
FT /id="PRO_0000173882"
FT DNA_BIND 153..157
FT /evidence="ECO:0000250"
FT REGION 222..291
FT /note="Mediates interaction with RPA2"
FT /evidence="ECO:0000250"
FT REGION 357..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 105
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:P43351"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43351"
FT MOD_RES 339
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P43351"
FT CONFLICT 195
FT /note="E -> K (in Ref. 2; AAA85794)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="Missing (in Ref. 2; AAA85794)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="A -> G (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="Missing (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="D -> N (in Ref. 3; CAA83659)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 46910 MW; 84514C8579072F98 CRC64;
MAGPEEAVHR GCDNHPPFVG GKSVLLFGQS QYTADEYQAI QKALRQRLGP EYISSRMAGG
GQKVCYIEGH RVINLANEMF GYNGWAHSIT QQNVDFVDLN NGKFYVGVCA FVKVQLKDGS
YHEDVGYGVS EGLRSKALSL EKARKEAVTD GLKRALRSFG NALGNCILDK DYLRSLNKLP
RQLPLDVDLT KTKREDFEPS VEQARYNSCR QNEALGLPKP QEVTSPCRSS PPHDSNIKLQ
GAKDISSSCS LAATLESDAT HQRKLRKLRQ KQLQQQFREQ METRRQSHAP AEEVAAKHAA
VLPAPPKHST PVTAASELLQ EKVVFPDNLE ENLEMWDLTP DLEDIIKPLC RAEPAQTSAT
RTFNNQDSVP HIHCHQKPQE KPGPGHLQTC NTNQHVLGSR EDSEPHRKSQ DLKKRKLDPS
