RAD52_HUMAN
ID RAD52_HUMAN Reviewed; 418 AA.
AC P43351; Q13205; Q9Y5T7; Q9Y5T8; Q9Y5T9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=DNA repair protein RAD52 homolog;
GN Name=RAD52;
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 ALPHA).
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RC TISSUE=Spleen;
RX PubMed=7797537; DOI=10.1074/jbc.270.26.15467;
RA Park M.S.;
RT "Expression of human RAD52 confers resistance to ionizing radiation in
RT mammalian cells.";
RL J. Biol. Chem. 270:15467-15470(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA; GAMMA AND DELTA), AND
RP ALTERNATIVE SPLICING.
RC TISSUE=Testis;
RX PubMed=10673031; DOI=10.1016/s0167-4781(99)00214-6;
RA Kito K., Wada H., Yeh E.T., Kamitani T.;
RT "Identification of novel isoforms of human RAD52.";
RL Biochim. Biophys. Acta 1489:303-314(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GAMMA AND DELTA).
RC TISSUE=Amygdala, and Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TRP-70; GLU-221 AND
RP ASN-287.
RG NIEHS SNPs program;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION IN HOMOLOGOUS RECOMBINATION, INTERACTION WITH RPA2, AND REGION.
RX PubMed=8702565; DOI=10.1074/jbc.271.31.18996;
RA Park M.S., Ludwig D.L., Stigger E., Lee S.H.;
RT "Physical interaction between human RAD52 and RPA is required for
RT homologous recombination in mammalian cells.";
RL J. Biol. Chem. 271:18996-19000(1996).
RN [10]
RP FUNCTION, INTERACTION WITH ABL1, AND PHOSPHORYLATION AT TYR-104.
RX PubMed=12379650; DOI=10.1074/jbc.m208151200;
RA Kitao H., Yuan Z.M.;
RT "Regulation of ionizing radiation-induced Rad52 nuclear foci formation by
RT c-Abl-mediated phosphorylation.";
RL J. Biol. Chem. 277:48944-48948(2002).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND THR-335, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP IDENTIFICATION BY 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 [14]
RP INTERACTION WITH RAD51AP1.
RX PubMed=31400850; DOI=10.1016/j.molcel.2019.06.043;
RA Barroso-Gonzalez J., Garcia-Exposito L., Hoang S.M., Lynskey M.L.,
RA Roncaioli J.L., Ghosh A., Wallace C.T., de Vitis M., Modesti M.,
RA Bernstein K.A., Sarkar S.N., Watkins S.C., O'Sullivan R.J.;
RT "RAD51AP1 is an essential mediator of alternative lengthening of
RT telomeres.";
RL Mol. Cell 76:11-26(2019).
RN [15]
RP ERRATUM OF PUBMED:31400850.
RX PubMed=31585101; DOI=10.1016/j.molcel.2019.08.009;
RA Barroso-Gonzalez J., Garcia-Exposito L., Hoang S.M., Lynskey M.L.,
RA Roncaioli J.L., Ghosh A., Wallace C.T., Modesti M., Bernstein K.A.,
RA Sarkar S.N., Watkins S.C., O'Sullivan R.J.;
RT "RAD51AP1 is an essential mediator of alternative lengthening of
RT telomeres.";
RL Mol. Cell 76:217-217(2019).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-212, SUBUNIT, DNA-BINDING
RP REGION, AND MUTAGENESIS OF ARG-55; TYR-65; LYS-152; ARG-153 AND ARG-156.
RX PubMed=12191481; DOI=10.1016/s1097-2765(02)00587-7;
RA Kagawa W., Kurumizaka H., Ishitani R., Fukai S., Nureki O., Shibata T.,
RA Yokoyama S.;
RT "Crystal structure of the homologous-pairing domain from the human Rad52
RT recombinase in the undecameric form.";
RL Mol. Cell 10:359-371(2002).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-209.
RX PubMed=12370410; DOI=10.1073/pnas.212449899;
RA Singleton M.R., Wentzell L.M., Liu Y., West S.C., Wigley D.B.;
RT "Structure of the single-strand annealing domain of human RAD52 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13492-13497(2002).
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:0000269|PubMed:12379650, ECO:0000269|PubMed:8702565}.
CC -!- SUBUNIT: The full-length protein forms heptameric rings
CC (PubMed:12191481). Interacts with ABL1 (PubMed:12379650). Interacts
CC with RPA2; the interaction is direct and associates RAD52 with the RPA
CC complex (PubMed:8702565). Interacts with RAD51AP1 (PubMed:31400850).
CC {ECO:0000269|PubMed:12191481, ECO:0000269|PubMed:12379650,
CC ECO:0000269|PubMed:31400850, ECO:0000269|PubMed:8702565}.
CC -!- INTERACTION:
CC P43351; Q9NPI6: DCP1A; NbExp=5; IntAct=EBI-706448, EBI-374238;
CC P43351; O00505: KPNA3; NbExp=3; IntAct=EBI-706448, EBI-358297;
CC P43351; P50221: MEOX1; NbExp=3; IntAct=EBI-706448, EBI-2864512;
CC P43351; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-706448, EBI-16439278;
CC P43351; Q13952-2: NFYC; NbExp=3; IntAct=EBI-706448, EBI-11956831;
CC P43351; Q02548: PAX5; NbExp=3; IntAct=EBI-706448, EBI-296331;
CC P43351; Q9H4B4: PLK3; NbExp=3; IntAct=EBI-706448, EBI-751877;
CC P43351; Q06609: RAD51; NbExp=3; IntAct=EBI-706448, EBI-297202;
CC P43351; P43351: RAD52; NbExp=7; IntAct=EBI-706448, EBI-706448;
CC P43351; Q8NG50: RDM1; NbExp=5; IntAct=EBI-706448, EBI-10288724;
CC P43351; P35244: RPA3; NbExp=3; IntAct=EBI-706448, EBI-621428;
CC P43351; Q14191: WRN; NbExp=9; IntAct=EBI-706448, EBI-368417;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=alpha;
CC IsoId=P43351-1; Sequence=Displayed;
CC Name=beta;
CC IsoId=P43351-2; Sequence=VSP_047753, VSP_047754;
CC Name=gamma;
CC IsoId=P43351-3; Sequence=VSP_047750, VSP_047752;
CC Name=delta;
CC IsoId=P43351-4; Sequence=VSP_047749, VSP_047751;
CC -!- PTM: Phosphorylated upon DNA damage by ABL1, and probably by ATM or
CC ATR. {ECO:0000269|PubMed:12379650}.
CC -!- MISCELLANEOUS: [Isoform beta]: Unable to interact with isoform alpha,
CC may act as dominant negative. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform gamma]: Unable to interact with isoform alpha,
CC may act as dominant negative. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform delta]: Unable to interact with isoform alpha,
CC may act as dominant negative. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RAD52 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rad52/";
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DR EMBL; U12134; AAA85793.1; -; mRNA.
DR EMBL; L33262; AAB05203.1; -; mRNA.
DR EMBL; U27516; AAA87554.1; -; mRNA.
DR EMBL; AF125948; AAD24575.1; -; mRNA.
DR EMBL; AF125949; AAD24576.1; -; mRNA.
DR EMBL; AF125950; AAD24577.1; -; mRNA.
DR EMBL; AK292160; BAF84849.1; -; mRNA.
DR EMBL; AK312026; BAG34963.1; -; mRNA.
DR EMBL; AY527412; AAS00097.1; -; Genomic_DNA.
DR EMBL; AC004803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471116; EAW88943.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88945.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88946.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88949.1; -; Genomic_DNA.
DR CCDS; CCDS76501.1; -. [P43351-2]
DR CCDS; CCDS8507.2; -. [P43351-1]
DR PIR; A57518; A57518.
DR RefSeq; NP_001284348.1; NM_001297419.1. [P43351-1]
DR RefSeq; NP_001284349.1; NM_001297420.1. [P43351-2]
DR RefSeq; NP_602296.2; NM_134424.3. [P43351-1]
DR RefSeq; XP_005253777.1; XM_005253720.4. [P43351-1]
DR RefSeq; XP_005253778.1; XM_005253721.2. [P43351-1]
DR RefSeq; XP_011519292.1; XM_011520990.2. [P43351-1]
DR RefSeq; XP_011519293.1; XM_011520991.2. [P43351-1]
DR RefSeq; XP_016875258.1; XM_017019769.1. [P43351-1]
DR PDB; 1H2I; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-209.
DR PDB; 1KN0; X-ray; 2.85 A; A/B/C/D/E/F/G/H/I/J/K=1-212.
DR PDB; 5JRB; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K=1-212.
DR PDB; 5XRZ; X-ray; 3.60 A; A/B/C/D/E/F/G/H/I/J/K=1-212.
DR PDB; 5XS0; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-212.
DR PDBsum; 1H2I; -.
DR PDBsum; 1KN0; -.
DR PDBsum; 5JRB; -.
DR PDBsum; 5XRZ; -.
DR PDBsum; 5XS0; -.
DR AlphaFoldDB; P43351; -.
DR SMR; P43351; -.
DR BioGRID; 111830; 66.
DR CORUM; P43351; -.
DR DIP; DIP-333N; -.
DR IntAct; P43351; 42.
DR MINT; P43351; -.
DR STRING; 9606.ENSP00000351284; -.
DR BindingDB; P43351; -.
DR ChEMBL; CHEMBL2362978; -.
DR iPTMnet; P43351; -.
DR PhosphoSitePlus; P43351; -.
DR BioMuta; RAD52; -.
DR DMDM; 1172823; -.
DR EPD; P43351; -.
DR MassIVE; P43351; -.
DR PaxDb; P43351; -.
DR PeptideAtlas; P43351; -.
DR PRIDE; P43351; -.
DR ProteomicsDB; 55613; -. [P43351-1]
DR ProteomicsDB; 86502; -.
DR ProteomicsDB; 86503; -.
DR ProteomicsDB; 86504; -.
DR Antibodypedia; 10276; 426 antibodies from 35 providers.
DR CPTC; P43351; 3 antibodies.
DR DNASU; 5893; -.
DR Ensembl; ENST00000358495.8; ENSP00000351284.3; ENSG00000002016.18. [P43351-1]
DR Ensembl; ENST00000430095.6; ENSP00000387901.2; ENSG00000002016.18. [P43351-1]
DR Ensembl; ENST00000461568.5; ENSP00000436008.1; ENSG00000002016.18. [P43351-3]
DR Ensembl; ENST00000468231.5; ENSP00000434703.1; ENSG00000002016.18. [P43351-3]
DR Ensembl; ENST00000541619.1; ENSP00000438965.1; ENSG00000002016.18. [P43351-4]
DR Ensembl; ENST00000544742.5; ENSP00000443254.1; ENSG00000002016.18. [P43351-4]
DR Ensembl; ENST00000545564.5; ENSP00000440268.1; ENSG00000002016.18. [P43351-2]
DR GeneID; 5893; -.
DR KEGG; hsa:5893; -.
DR MANE-Select; ENST00000358495.8; ENSP00000351284.3; NM_134424.4; NP_602296.2.
DR UCSC; uc001qiv.2; human. [P43351-1]
DR CTD; 5893; -.
DR DisGeNET; 5893; -.
DR GeneCards; RAD52; -.
DR HGNC; HGNC:9824; RAD52.
DR HPA; ENSG00000002016; Low tissue specificity.
DR MIM; 600392; gene.
DR neXtProt; NX_P43351; -.
DR OpenTargets; ENSG00000002016; -.
DR PharmGKB; PA34180; -.
DR VEuPathDB; HostDB:ENSG00000002016; -.
DR eggNOG; KOG4141; Eukaryota.
DR GeneTree; ENSGT00390000008766; -.
DR HOGENOM; CLU_054400_0_0_1; -.
DR InParanoid; P43351; -.
DR OMA; VTGNWES; -.
DR PhylomeDB; P43351; -.
DR TreeFam; TF101221; -.
DR PathwayCommons; P43351; -.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-HSA-5685939; HDR through MMEJ (alt-NHEJ).
DR SignaLink; P43351; -.
DR SIGNOR; P43351; -.
DR BioGRID-ORCS; 5893; 120 hits in 1073 CRISPR screens.
DR ChiTaRS; RAD52; human.
DR EvolutionaryTrace; P43351; -.
DR GeneWiki; RAD52; -.
DR GenomeRNAi; 5893; -.
DR Pharos; P43351; Tchem.
DR PRO; PR:P43351; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P43351; protein.
DR Bgee; ENSG00000002016; Expressed in right uterine tube and 140 other tissues.
DR ExpressionAtlas; P43351; baseline and differential.
DR Genevisible; P43351; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CAFA.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003697; F:single-stranded DNA binding; IMP:CAFA.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IGI: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; IDA:MGI.
DR GO; GO:0000730; P:DNA recombinase assembly; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IMP:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; TAS:ProtInc.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
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; IDA:MGI.
DR DisProt; DP00437; -.
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 3D-structure; Alternative splicing; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..418
FT /note="DNA repair protein RAD52 homolog"
FT /id="PRO_0000173881"
FT DNA_BIND 152..156
FT REGION 219..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..280
FT /note="Mediates interaction with RPA2"
FT /evidence="ECO:0000269|PubMed:8702565"
FT REGION 368..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:12379650"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 318
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 94..118
FT /note="DFVDLNNGKFYVGVCAFVRVQLKDG -> GEYALQQWGLLHCPAPAESLLWV
FT RR (in isoform delta)"
FT /evidence="ECO:0000303|PubMed:10673031,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_047749"
FT VAR_SEQ 117..139
FT /note="DGSYHEDVGYGVSEGLKSKALSL -> VRGWSRPAARKDQWVVGEGWFIS
FT (in isoform gamma)"
FT /evidence="ECO:0000303|PubMed:10673031,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_047750"
FT VAR_SEQ 119..418
FT /note="Missing (in isoform delta)"
FT /evidence="ECO:0000303|PubMed:10673031,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_047751"
FT VAR_SEQ 140..418
FT /note="Missing (in isoform gamma)"
FT /evidence="ECO:0000303|PubMed:10673031,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_047752"
FT VAR_SEQ 157..226
FT /note="SFGNALGNCILDKDYLRSLNKLPRQLPLEVDLTKAKRQDLEPSVEEARYNSC
FT RPNMALGHPQLQQVTSPS -> LPLLGVSGRILYSLFSVHSVMCAGGLPTPTASAQTAP
FT SSPCSSAVLRYAQEFWECTWKLYSGQRLPEITK (in isoform beta)"
FT /evidence="ECO:0000303|PubMed:10673031"
FT /id="VSP_047753"
FT VAR_SEQ 227..418
FT /note="Missing (in isoform beta)"
FT /evidence="ECO:0000303|PubMed:10673031"
FT /id="VSP_047754"
FT VARIANT 70
FT /note="R -> W (in dbSNP:rs11571421)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_019218"
FT VARIANT 221
FT /note="Q -> E (in dbSNP:rs4987206)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_019219"
FT VARIANT 287
FT /note="S -> N (in dbSNP:rs11571463)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_019220"
FT MUTAGEN 55
FT /note="R->A: Abolishes ssDNA-binding."
FT /evidence="ECO:0000269|PubMed:12191481"
FT MUTAGEN 65
FT /note="Y->A: Moderately defective in both ss and dsDNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:12191481"
FT MUTAGEN 152
FT /note="K->A: Abolishes ssDNA-binding."
FT /evidence="ECO:0000269|PubMed:12191481"
FT MUTAGEN 153
FT /note="R->A: Moderately defective in both ss and dsDNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:12191481"
FT MUTAGEN 156
FT /note="R->A: Moderately defective in both ss and dsDNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:12191481"
FT CONFLICT 100
FT /note="N -> K (in Ref. 3; AAA87554)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="S -> SY (in Ref. 3; AAA87554)"
FT /evidence="ECO:0000305"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:1KN0"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:5JRB"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:5JRB"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:5JRB"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:5JRB"
FT HELIX 68..79
FT /evidence="ECO:0007829|PDB:5JRB"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:5JRB"
FT STRAND 84..99
FT /evidence="ECO:0007829|PDB:5JRB"
FT STRAND 102..115
FT /evidence="ECO:0007829|PDB:5JRB"
FT STRAND 120..131
FT /evidence="ECO:0007829|PDB:5JRB"
FT HELIX 135..155
FT /evidence="ECO:0007829|PDB:5JRB"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:5JRB"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:5JRB"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:5JRB"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:5JRB"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:5JRB"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:5JRB"
SQ SEQUENCE 418 AA; 46169 MW; 7E1BBCAF0B9CD4AF CRC64;
MSGTEEAILG GRDSHPAAGG GSVLCFGQCQ YTAEEYQAIQ KALRQRLGPE YISSRMAGGG
QKVCYIEGHR VINLANEMFG YNGWAHSITQ QNVDFVDLNN GKFYVGVCAF VRVQLKDGSY
HEDVGYGVSE GLKSKALSLE KARKEAVTDG LKRALRSFGN ALGNCILDKD YLRSLNKLPR
QLPLEVDLTK AKRQDLEPSV EEARYNSCRP NMALGHPQLQ QVTSPSRPSH AVIPADQDCS
SRSLSSSAVE SEATHQRKLR QKQLQQQFRE RMEKQQVRVS TPSAEKSEAA PPAPPVTHST
PVTVSEPLLE KDFLAGVTQE LIKTLEDNSE KWAVTPDAGD GVVKPSSRAD PAQTSDTLAL
NNQMVTQNRT PHSVCHQKPQ AKSGSWDLQT YSADQRTTGN WESHRKSQDM KKRKYDPS
