RAD52_YEAST
ID RAD52_YEAST Reviewed; 471 AA.
AC P06778; D6VZE2;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=DNA repair and recombination protein RAD52;
GN Name=RAD52; OrderedLocusNames=YML032C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6098821; DOI=10.1128/mcb.4.12.2735-2744.1984;
RA Adzuma K., Ogawa T., Ogawa H.;
RT "Primary structure of the RAD52 gene in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 4:2735-2744(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP INTERACTION WITH RAD51 AND RAD59.
RX PubMed=13679150; DOI=10.1016/s1568-7864(03)00121-6;
RA Davis A.P., Symington L.S.;
RT "The Rad52-Rad59 complex interacts with Rad51 and replication protein A.";
RL DNA Repair 2:1127-1134(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP IDENTIFICATION OF INITIATION SITES, AND PHOSPHORYLATION.
RX PubMed=16707661; DOI=10.1093/nar/gkl280;
RA Antunez de Mayolo A., Lisby M., Erdeniz N., Thybo T., Mortensen U.H.,
RA Rothstein R.;
RT "Multiple start codons and phosphorylation result in discrete Rad52 protein
RT species.";
RL Nucleic Acids Res. 34:2587-2597(2006).
RN [8]
RP INTERACTION WITH SAW1.
RX PubMed=18471978; DOI=10.1016/j.molcel.2008.02.028;
RA Li F., Dong J., Pan X., Oum J.-H., Boeke J.D., Lee S.E.;
RT "Microarray-based genetic screen defines SAW1, a gene required for
RT Rad1/Rad10-dependent processing of recombination intermediates.";
RL Mol. Cell 30:325-335(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Involved in DNA double-strand break (DSB) repair and
CC recombination. Promotes the annealing of complementary single-stranded
CC DNA and by stimulation of the RAD51 recombinase.
CC -!- SUBUNIT: Part of a complex that includes RAD51, RAD52 and RAD59.
CC Interacts with SAW1. {ECO:0000269|PubMed:13679150,
CC ECO:0000269|PubMed:18471978}.
CC -!- INTERACTION:
CC P06778; P25694: CDC48; NbExp=4; IntAct=EBI-14719, EBI-4308;
CC P06778; P25454: RAD51; NbExp=9; IntAct=EBI-14719, EBI-14709;
CC P06778; Q12306: SMT3; NbExp=2; IntAct=EBI-14719, EBI-17490;
CC P06778; P53044: UFD1; NbExp=4; IntAct=EBI-14719, EBI-19997;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=1;
CC IsoId=P06778-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P06778-2; Sequence=VSP_019612;
CC Name=3;
CC IsoId=P06778-3; Sequence=VSP_019613;
CC -!- MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met-5
CC of isoform 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative initiation at Met-7
CC of isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RAD52 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA50352.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT93163.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA86623.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M10249; AAA50352.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z46659; CAA86623.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY693144; AAT93163.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006946; DAA09866.1; -; Genomic_DNA.
DR PIR; A23282; A23282.
DR RefSeq; NP_013680.2; NM_001182390.1. [P06778-1]
DR AlphaFoldDB; P06778; -.
DR SMR; P06778; -.
DR BioGRID; 35137; 578.
DR DIP; DIP-3N; -.
DR IntAct; P06778; 32.
DR MINT; P06778; -.
DR STRING; 4932.YML032C; -.
DR iPTMnet; P06778; -.
DR MaxQB; P06778; -.
DR PaxDb; P06778; -.
DR PRIDE; P06778; -.
DR EnsemblFungi; YML032C_mRNA; YML032C; YML032C. [P06778-1]
DR GeneID; 854976; -.
DR KEGG; sce:YML032C; -.
DR SGD; S000004494; RAD52.
DR VEuPathDB; FungiDB:YML032C; -.
DR eggNOG; KOG4141; Eukaryota.
DR GeneTree; ENSGT00390000008766; -.
DR HOGENOM; CLU_011431_3_2_1; -.
DR InParanoid; P06778; -.
DR OMA; LDDSFMF; -.
DR BioCyc; YEAST:G3O-32633-MON; -.
DR Reactome; R-SCE-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-SCE-5685938; HDR through Single Strand Annealing (SSA).
DR PRO; PR:P06778; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P06778; protein.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0000228; C:nuclear chromosome; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000150; F:DNA strand exchange activity; IDA:SGD.
DR GO; GO:1990814; F:DNA/DNA annealing activity; IDA:SGD.
DR GO; GO:0006277; P:DNA amplification; IMP:SGD.
DR GO; GO:0000730; P:DNA recombinase assembly; IDA:SGD.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:SGD.
DR GO; GO:0045002; P:double-strand break repair via single-strand annealing; IGI:SGD.
DR GO; GO:0000709; P:meiotic joint molecule formation; IMP:SGD.
DR GO; GO:0043504; P:mitochondrial DNA repair; IMP:SGD.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:1904877; P:positive regulation of DNA ligase activity; IDA:SGD.
DR GO; GO:0006301; P:postreplication repair; IMP:SGD.
DR GO; GO:0000722; P:telomere maintenance via recombination; IMP:SGD.
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 1: Evidence at protein level;
KW Alternative initiation; DNA damage; DNA recombination; DNA repair; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..471
FT /note="DNA repair and recombination protein RAD52"
FT /id="PRO_0000173892"
FT REGION 166..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..6
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_019613"
FT VAR_SEQ 1..4
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_019612"
SQ SEQUENCE 471 AA; 52404 MW; 4F5D07480A05B564 CRC64;
MNEIMDMDEK KPVFGNHSED IQTKLDKKLG PEYISKRVGF GTSRIAYIEG WRVINLANQI
FGYNGWSTEV KSVVIDFLDE RQGKFSIGCT AIVRVTLTSG TYREDIGYGT VENERRKPAA
FERAKKSAVT DALKRSLRGF GNALGNCLYD KDFLAKIDKV KFDPPDFDEN NLFRPTDEIS
ESSRTNTLHE NQEQQQYPNK RRQLTKVTNT NPDSTKNLVK IENTVSRGTP MMAAPAEANS
KNSSNKDTDL KSLDASKQDQ DDLLDDSLMF SDDFQDDDLI NMGNTNSNVL TTEKDPVVAK
QSPTASSNPE AEQITFVTAK AATSVQNERY IGEESIFDPK YQAQSIRHTV DQTTSKHIPA
SVLKDKTMTT ARDSVYEKFA PKGKQLSMKN NDKELGPHML EGAGNQVPRE TTPIKTNATA
FPPAAAPRFA PPSKVVHPNG NGAVPAVPQQ RSTRREVGRP KINPLHARKP T
