ID RFA2_HUMAN Reviewed; 270 AA. AC P15927; Q52II0; Q5TEI9; Q5TEJ5; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 27-MAR-2024, entry version 234. DE RecName: Full=Replication protein A 32 kDa subunit; DE Short=RP-A p32; DE AltName: Full=Replication factor A protein 2; DE Short=RF-A protein 2; DE AltName: Full=Replication protein A 34 kDa subunit; DE Short=RP-A p34; GN Name=RPA2; Synonyms=REPA2, RPA32, RPA34; 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), PARTIAL PROTEIN SEQUENCE, FUNCTION RP IN DNA REPLICATION, AND IDENTIFICATION IN RPA COMPLEX. RX PubMed=2406247; DOI=10.1016/s0021-9258(19)39750-9; RA Erdile L.F., Wold M.S., Kelly T.J.; RT "The primary structure of the 32-kDa subunit of human replication protein RT A."; RL J. Biol. Chem. 265:3177-3182(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-14; ARG-15 AND SER-203. RG NIEHS SNPs program; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney, Lung, and Muscle; 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 [6] RP CELL CYCLE-DEPENDENT PHOSPHORYLATION. RX PubMed=2200738; DOI=10.1101/gad.4.6.968; RA Din S., Brill S.J., Fairman M.P., Stillman B.; RT "Cell-cycle-regulated phosphorylation of DNA replication factor A from RT human and yeast cells."; RL Genes Dev. 4:968-977(1990). RN [7] RP DNA DAMAGE-INDUCED PHOSPHORYLATION, AND PHOSPHORYLATION AT SER-23 AND RP SER-29. RX PubMed=1318195; DOI=10.1002/j.1460-2075.1992.tb05278.x; RA Dutta A., Stillman B.; RT "cdc2 family kinases phosphorylate a human cell DNA replication factor, RT RPA, and activate DNA replication."; RL EMBO J. 11:2189-2199(1992). RN [8] RP PHOSPHORYLATION AT SER-23 AND SER-29. RX PubMed=8246944; DOI=10.1128/mcb.13.12.7222-7231.1993; RA Liu V.F., Weaver D.T.; RT "The ionizing radiation-induced replication protein A phosphorylation RT response differs between ataxia telangiectasia and normal human cells."; RL Mol. Cell. Biol. 13:7222-7231(1993). RN [9] RP FUNCTION IN NUCLEOTIDE EXCISION REPAIR. RX PubMed=7697716; DOI=10.1016/0092-8674(95)90289-9; RA Aboussekhra A., Biggerstaff M., Shivji M.K., Vilpo J.A., Moncollin V., RA Podust V.N., Protic M., Huebscher U., Egly J.M., Wood R.D.; RT "Mammalian DNA nucleotide excision repair reconstituted with purified RT protein components."; RL Cell 80:859-868(1995). RN [10] RP FUNCTION IN NUCLEOTIDE EXCISION REPAIR, AND INTERACTION WITH XPA. RX PubMed=7700386; DOI=10.1038/374566a0; RA He Z., Henricksen L.A., Wold M.S., Ingles C.J.; RT "RPA involvement in the damage-recognition and incision steps of nucleotide RT excision repair."; RL Nature 374:566-569(1995). RN [11] RP FUNCTION IN HOMOLOGOUS RECOMBINATION, AND INTERACTION WITH RAD52. 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 [12] RP ACETYLATION AT MET-1, PHOSPHORYLATION AT THR-21; SER-29 AND SER-33, RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF SER-29. RX PubMed=9139719; DOI=10.1074/jbc.272.19.12634; RA Niu H., Erdjument-Bromage H., Pan Z.-Q., Lee S.-H., Tempst P., Hurwitz J.; RT "Mapping of amino acid residues in the p34 subunit of human single-stranded RT DNA-binding protein phosphorylated by DNA-dependent protein kinase and Cdc2 RT kinase in vitro."; RL J. Biol. Chem. 272:12634-12641(1997). RN [13] RP PHOSPHORYLATION AT THR-21; SER-23; SER-29 AND SER-33. RX PubMed=9295339; DOI=10.1074/jbc.272.38.23896; RA Zernik-Kobak M., Vasunia K., Connelly M., Anderson C.W., Dixon K.; RT "Sites of UV-induced phosphorylation of the p34 subunit of replication RT protein A from HeLa cells."; RL J. Biol. Chem. 272:23896-23904(1997). RN [14] RP FUNCTION IN DNA REPLICATION, FUNCTION IN DNA MISMATCH REPAIR, AND FUNCTION RP IN NUCLEOTIDE EXCISION REPAIR. RX PubMed=9430682; DOI=10.1074/jbc.273.3.1453; RA Lin Y.L., Shivji M.K., Chen C., Kolodner R., Wood R.D., Dutta A.; RT "The evolutionarily conserved zinc finger motif in the largest subunit of RT human replication protein A is required for DNA replication and mismatch RT repair but not for nucleotide excision repair."; RL J. Biol. Chem. 273:1453-1461(1998). RN [15] RP FUNCTION IN BASE EXCISION REPAIR. RX PubMed=9765279; DOI=10.1074/jbc.273.42.27492; RA DeMott M.S., Zigman S., Bambara R.A.; RT "Replication protein A stimulates long patch DNA base excision repair."; RL J. Biol. Chem. 273:27492-27498(1998). RN [16] RP INTERACTION WITH SERTAD3, AND SUBCELLULAR LOCATION. RX PubMed=10982866; DOI=10.1093/nar/28.18.3478; RA Cho J.M., Song D.J., Bergeron J., Benlimame N., Wold M.S., RA Alaoui-Jamali M.A.; RT "RBT1, a novel transcriptional co-activator, binds the second subunit of RT replication protein A."; RL Nucleic Acids Res. 28:3478-3485(2000). RN [17] RP PHOSPHORYLATION BY ATR, AND SUBCELLULAR LOCATION. RX PubMed=12814551; DOI=10.1016/s0960-9822(03)00376-2; RA Barr S.M., Leung C.G., Chang E.E., Cimprich K.A.; RT "ATR kinase activity regulates the intranuclear translocation of ATR and RT RPA following ionizing radiation."; RL Curr. Biol. 13:1047-1051(2003). RN [18] RP FUNCTION IN DNA REPLICATION. RX PubMed=15205463; DOI=10.1074/jbc.m403825200; RA Weisshart K., Pestryakov P., Smith R.W.P., Hartmann H., Kremmer E., RA Lavrik O., Nasheuer H.-P.; RT "Coordinated regulation of replication protein A activities by its subunits RT p14 and p32."; RL J. Biol. Chem. 279:35368-35376(2004). RN [19] RP INTERACTION WITH TIMELESS AND TIPIN. RX PubMed=17141802; DOI=10.1016/j.jmb.2006.10.097; RA Gotter A.L., Suppa C., Emanuel B.S.; RT "Mammalian TIMELESS and Tipin are evolutionarily conserved replication RT fork-associated factors."; RL J. Mol. Biol. 366:36-52(2007). RN [20] RP FUNCTION IN HOMOLOGOUS RECOMBINATION REPAIR, AND INTERACTION WITH RAD52. RX PubMed=17765923; DOI=10.1016/j.jmb.2007.07.068; RA Sleeth K.M., Sorensen C.S., Issaeva N., Dziegielewski J., Bartek J., RA Helleday T.; RT "RPA mediates recombination repair during replication stress and is RT displaced from DNA by checkpoint signalling in human cells."; RL J. Mol. Biol. 373:38-47(2007). RN [21] RP INTERACTION WITH TIPIN. RX PubMed=17296725; DOI=10.1128/mcb.02190-06; RA Uensal-Kacmaz K., Chastain P.D., Qu P.-P., Minoo P., Cordeiro-Stone M., RA Sancar A., Kaufmann W.K.; RT "The human Tim/Tipin complex coordinates an Intra-S checkpoint response to RT UV that slows replication fork displacement."; RL Mol. Cell. Biol. 27:3131-3142(2007). RN [22] RP FUNCTION IN TELOMERE MAINTENANCE, AND SUBCELLULAR LOCATION. RX PubMed=17959650; DOI=10.1093/nar/gkm738; RA Grudic A., Jul-Larsen A., Haring S.J., Wold M.S., Loenning P.E., RA Bjerkvig R., Boee S.O.; RT "Replication protein A prevents accumulation of single-stranded telomeric RT DNA in cells that use alternative lengthening of telomeres."; RL Nucleic Acids Res. 35:7267-7278(2007). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [25] RP INTERACTION WITH SMARCAL1. RX PubMed=19793863; DOI=10.1101/gad.1831509; RA Yusufzai T., Kong X., Yokomori K., Kadonaga J.T.; RT "The annealing helicase HARP is recruited to DNA repair sites via an RT interaction with RPA."; RL Genes Dev. 23:2400-2404(2009). RN [26] RP INTERACTION WITH SMARCAL1. RX PubMed=19793861; DOI=10.1101/gad.1839909; RA Bansbach C.E., Betous R., Lovejoy C.A., Glick G.G., Cortez D.; RT "The annealing helicase SMARCAL1 maintains genome integrity at stalled RT replication forks."; RL Genes Dev. 23:2405-2414(2009). RN [27] RP INTERACTION WITH SMARCAL1. RX PubMed=19793862; DOI=10.1101/gad.1832309; RA Ciccia A., Bredemeyer A.L., Sowa M.E., Terret M.E., Jallepalli P.V., RA Harper J.W., Elledge S.J.; RT "The SIOD disorder protein SMARCAL1 is an RPA-interacting protein involved RT in replication fork restart."; RL Genes Dev. 23:2415-2425(2009). RN [28] RP FUNCTION AS PART OF THE RPA COMPLEX. RX PubMed=19116208; DOI=10.1074/jbc.m808963200; RA Mason A.C., Haring S.J., Pryor J.M., Staloch C.A., Gan T.F., Wold M.S.; RT "An alternative form of replication protein a prevents viral replication in RT vitro."; RL J. Biol. Chem. 284:5324-5331(2009). RN [29] RP TISSUE SPECIFICITY. RX PubMed=19996105; DOI=10.1074/jbc.m109.079418; RA Kemp M.G., Mason A.C., Carreira A., Reardon J.T., Haring S.J., RA Borgstahl G.E., Kowalczykowski S.C., Sancar A., Wold M.S.; RT "An alternative form of replication protein a expressed in normal human RT tissues supports DNA repair."; RL J. Biol. Chem. 285:4788-4797(2010). RN [30] RP FUNCTION IN DNA REPAIR, PHOSPHORYLATION, DEPHOSPHORYLATION BY PP4, RP INTERACTION WITH PPP4C; PPP4R2 AND RAD51, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF SER-8; SER-23; SER-29 AND SER-33. RX PubMed=20154705; DOI=10.1038/nsmb.1769; RA Lee D.H., Pan Y., Kanner S., Sung P., Borowiec J.A., Chowdhury D.; RT "A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair RT via homologous recombination."; RL Nat. Struct. Mol. Biol. 17:365-372(2010). RN [31] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-23 AND SER-29, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [32] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [33] RP FUNCTION IN REPLICATION CHECKPOINT, INTERACTION WITH RFWD3, AND SUBCELLULAR RP LOCATION. RX PubMed=21504906; DOI=10.1074/jbc.m111.222869; RA Gong Z., Chen J.; RT "E3 ligase RFWD3 participates in replication checkpoint control."; RL J. Biol. Chem. 286:22308-22313(2011). RN [34] RP INTERACTION WITH RFWD3, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT RP THR-21. RX PubMed=21558276; DOI=10.1074/jbc.m111.222802; RA Liu S., Chu J., Yucer N., Leng M., Wang S.Y., Chen B.P., Hittelman W.N., RA Wang Y.; RT "RING finger and WD repeat domain 3 (RFWD3) associates with replication RT protein A (RPA) and facilitates RPA-mediated DNA damage response."; RL J. Biol. Chem. 286:22314-22322(2011). RN [35] RP PHOSPHORYLATION AT SER-4 AND SER-8 BY PRKDC, AND MUTAGENESIS OF SER-4 AND RP SER-8. RX PubMed=21731742; DOI=10.1371/journal.pone.0021424; RA Liaw H., Lee D., Myung K.; RT "DNA-PK-dependent RPA2 hyperphosphorylation facilitates DNA repair and RT suppresses sister chromatid exchange."; RL PLoS ONE 6:E21424-E21424(2011). RN [36] RP INTERACTION WITH EIF4EBP3. RX PubMed=22684010; DOI=10.1016/j.febslet.2012.05.059; RA Chen C.C., Lee J.C., Chang M.C.; RT "4E-BP3 regulates eIF4E-mediated nuclear mRNA export and interacts with RT replication protein A2."; RL FEBS Lett. 586:2260-2266(2012). RN [37] RP INDUCTION BY DNA DAMAGE. RX PubMed=23393223; DOI=10.1093/carcin/bgt052; RA Yin J.Y., Dong Z.Z., Liu R.Y., Chen J., Liu Z.Q., Zhang J.T.; RT "Translational regulation of RPA2 via internal ribosomal entry site and by RT eIF3a."; RL Carcinogenesis 34:1224-1231(2013). RN [38] RP INTERACTION WITH FBH1. RX PubMed=23319600; DOI=10.1083/jcb.201209002; RA Jeong Y.T., Rossi M., Cermak L., Saraf A., Florens L., Washburn M.P., RA Sung P., Schildkraut C.L., Schildkraut C., Pagano M.; RT "FBH1 promotes DNA double-strand breakage and apoptosis in response to DNA RT replication stress."; RL J. Cell Biol. 200:141-149(2013). RN [39] RP FUNCTION, INTERACTION WITH PRPF19, AND UBIQUITINATION BY PRPF19. RX PubMed=24332808; DOI=10.1016/j.molcel.2013.11.002; RA Marechal A., Li J.M., Ji X.Y., Wu C.S., Yazinski S.A., Nguyen H.D., Liu S., RA Jimenez A.E., Jin J., Zou L.; RT "PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives RT ATR activation via a ubiquitin-mediated circuitry."; RL Mol. Cell 53:235-246(2014). RN [40] RP UBIQUITINATION AT LYS-37 AND LYS-38, PHOSPHORYLATION AT SER-4; SER-8; RP THR-21 AND SER-33, AND MUTAGENESIS OF 37-LYS-LYS-38. RX PubMed=26474068; DOI=10.1016/j.molcel.2015.09.011; RA Elia A.E., Wang D.C., Willis N.A., Boardman A.P., Hajdu I., Adeyemi R.O., RA Lowry E., Gygi S.P., Scully R., Elledge S.J.; RT "RFWD3-dependent ubiquitination of RPA regulates repair at stalled RT replication forks."; RL Mol. Cell 60:280-293(2015). RN [41] RP INTERACTION WITH ETAA1. RX PubMed=27601467; DOI=10.1074/jbc.c116.747758; RA Feng S., Zhao Y., Xu Y., Ning S., Huo W., Hou M., Gao G., Ji J., Guo R., RA Xu D.; RT "Ewing Tumor-associated Antigen 1 interacts with replication protein A to RT promote restart of stalled replication forks."; RL J. Biol. Chem. 291:21956-21962(2016). RN [42] RP FUNCTION, AND INTERACTION WITH ETAA1. RX PubMed=27723720; DOI=10.1038/ncb3415; RA Bass T.E., Luzwick J.W., Kavanaugh G., Carroll C., Dungrawala H., RA Glick G.G., Feldkamp M.D., Putney R., Chazin W.J., Cortez D.; RT "ETAA1 acts at stalled replication forks to maintain genome integrity."; RL Nat. Cell Biol. 18:1185-1195(2016). RN [43] RP FUNCTION, AND INTERACTION WITH ETAA1. RX PubMed=27723717; DOI=10.1038/ncb3422; RA Haahr P., Hoffmann S., Tollenaere M.A., Ho T., Toledo L.I., Mann M., RA Bekker-Jensen S., Raeschle M., Mailand N.; RT "Activation of the ATR kinase by the RPA-binding protein ETAA1."; RL Nat. Cell Biol. 18:1196-1207(2016). RN [44] RP INTERACTION WITH RFWD3, AND MUTAGENESIS OF PHE-248; GLU-252; GLY-253 AND RP HIS-254. RX PubMed=28575657; DOI=10.1016/j.molcel.2017.04.021; RA Feeney L., Munoz I.M., Lachaud C., Toth R., Appleton P.L., Schindler D., RA Rouse J.; RT "RPA-mediated recruitment of the E3 ligase RFWD3 is vital for interstrand RT crosslink repair and human health."; RL Mol. Cell 66:610-621(2017). RN [45] RP INTERACTION WITH DDI2. RX PubMed=29290612; DOI=10.1016/j.molcel.2017.11.035; RA Kottemann M.C., Conti B.A., Lach F.P., Smogorzewska A.; RT "Removal of RTF2 from Stalled Replisomes Promotes Maintenance of Genome RT Integrity."; RL Mol. Cell 69:24-35.E5(2018). RN [46] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 43-171 IN COMPLEX WITH RPA1 AND RP RPA3. RX PubMed=10449415; DOI=10.1093/emboj/18.16.4498; RA Bochkarev A., Bochkareva E., Frappier L., Edwards A.M.; RT "The crystal structure of the complex of replication protein A subunits RT RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding."; RL EMBO J. 18:4498-4504(1999). RN [47] RP STRUCTURE BY NMR OF 172-270, INTERACTION WITH RAD52; UNG AND XPA, AND RP REGION. RX PubMed=11081631; DOI=10.1016/s0092-8674(00)00136-7; RA Mer G., Bochkarev A., Gupta R., Bochkareva E., Frappier L., Ingles C.J., RA Edwards A.M., Chazin W.J.; RT "Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RT RAD52 by replication factor RPA."; RL Cell 103:449-456(2000). RN [48] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 44-171. RX PubMed=11927569; DOI=10.1093/emboj/21.7.1855; RA Bochkareva E., Korolev S., Lees-Miller S.P., Bochkarev A.; RT "Structure of the RPA trimerization core and its role in the multistep DNA- RT binding mechanism of RPA."; RL EMBO J. 21:1855-1863(2002). CC -!- FUNCTION: As part of the heterotrimeric replication protein A complex CC (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, CC that form during DNA replication or upon DNA stress. It prevents their CC reannealing and in parallel, recruits and activates different proteins CC and complexes involved in DNA metabolism. Thereby, it plays an CC essential role both in DNA replication and the cellular response to DNA CC damage. In the cellular response to DNA damage, the RPA complex CC controls DNA repair and DNA damage checkpoint activation. Through CC recruitment of ATRIP activates the ATR kinase a master regulator of the CC DNA damage response. It is required for the recruitment of the DNA CC double-strand break repair factors RAD51 and RAD52 to chromatin in CC response to DNA damage. Also recruits to sites of DNA damage proteins CC like XPA and XPG that are involved in nucleotide excision repair and is CC required for this mechanism of DNA repair. Also plays a role in base CC excision repair (BER) probably through interaction with UNG. Also CC recruits SMARCAL1/HARP, which is involved in replication fork restart, CC to sites of DNA damage. May also play a role in telomere maintenance. CC {ECO:0000269|PubMed:15205463, ECO:0000269|PubMed:17765923, CC ECO:0000269|PubMed:17959650, ECO:0000269|PubMed:19116208, CC ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:21504906, CC ECO:0000269|PubMed:2406247, ECO:0000269|PubMed:24332808, CC ECO:0000269|PubMed:7697716, ECO:0000269|PubMed:7700386, CC ECO:0000269|PubMed:8702565, ECO:0000269|PubMed:9430682, CC ECO:0000269|PubMed:9765279}. CC -!- SUBUNIT: Component of the replication protein A complex (RPA/RP-A), a CC heterotrimeric complex composed of RPA1, RPA2 and RPA3 (PubMed:2406247, CC PubMed:19116208, PubMed:10449415). Interacts with PRPF19; the PRP19- CC CDC5L complex is recruited to the sites of DNA repair where it CC ubiquitinates the replication protein A complex (RPA) CC (PubMed:24332808). Interacts with SERTAD3 (PubMed:10982866). Interacts CC with TIPIN (PubMed:17141802, PubMed:17296725). Interacts with TIMELESS CC (PubMed:17141802). Interacts with PPP4R2; the interaction is direct, CC DNA damage-dependent and mediates the recruitment of the PP4 catalytic CC subunit PPP4C (PubMed:20154705). Interacts (hyperphosphorylated) with CC RAD51 (PubMed:20154705). Interacts with SMARCAL1; the interaction is CC direct and mediates the recruitment to the RPA complex of SMARCAL1 CC (PubMed:19793861, PubMed:19793862, PubMed:19793863). Interacts with CC RAD52 and XPA; those interactions are direct and associate RAD52 and CC XPA to the RPA complex (PubMed:7700386, PubMed:8702565, CC PubMed:17765923, PubMed:11081631). Interacts with FBH1 CC (PubMed:23319600). Interacts with ETAA1; the interaction is direct and CC promotes ETAA1 recruitment at stalled replication forks CC (PubMed:27601467, PubMed:27723720, PubMed:27723717). Interacts with CC RFWD3 (PubMed:21504906, PubMed:21558276, PubMed:26474068, CC PubMed:28575657). Interacts with DDI2 (PubMed:29290612). Interacts (in CC unphosphorylated form via N-terminus) with EIF4EBP3; the interaction CC enhances EIF4EBP3-mediated inhibition of EIF4E-mediated mRNA nuclear CC export (PubMed:22684010). {ECO:0000269|PubMed:10449415, CC ECO:0000269|PubMed:10982866, ECO:0000269|PubMed:11081631, CC ECO:0000269|PubMed:17141802, ECO:0000269|PubMed:17296725, CC ECO:0000269|PubMed:17765923, ECO:0000269|PubMed:19793861, CC ECO:0000269|PubMed:19793862, ECO:0000269|PubMed:19793863, CC ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:21504906, CC ECO:0000269|PubMed:21558276, ECO:0000269|PubMed:22684010, CC ECO:0000269|PubMed:23319600, ECO:0000269|PubMed:2406247, CC ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:26474068, CC ECO:0000269|PubMed:27601467, ECO:0000269|PubMed:27723717, CC ECO:0000269|PubMed:27723720, ECO:0000269|PubMed:28575657, CC ECO:0000269|PubMed:29290612, ECO:0000269|PubMed:7700386, CC ECO:0000269|PubMed:8702565}. CC -!- INTERACTION: CC P15927; P24863: CCNC; NbExp=3; IntAct=EBI-621404, EBI-395261; CC P15927; O75419: CDC45; NbExp=4; IntAct=EBI-621404, EBI-374969; CC P15927; O60516: EIF4EBP3; NbExp=3; IntAct=EBI-621404, EBI-746950; CC P15927; P04406: GAPDH; NbExp=2; IntAct=EBI-621404, EBI-354056; CC P15927; P49643-1: PRIM2; NbExp=3; IntAct=EBI-621404, EBI-15866483; CC P15927; Q6PCD5: RFWD3; NbExp=3; IntAct=EBI-621404, EBI-2129159; CC P15927; P27694: RPA1; NbExp=18; IntAct=EBI-621404, EBI-621389; CC P15927; P35244: RPA3; NbExp=12; IntAct=EBI-621404, EBI-621428; CC P15927; Q9UJW9: SERTAD3; NbExp=5; IntAct=EBI-621404, EBI-748621; CC P15927; Q9NZC9: SMARCAL1; NbExp=14; IntAct=EBI-621404, EBI-5457961; CC P15927; Q9BVW5: TIPIN; NbExp=4; IntAct=EBI-621404, EBI-2515360; CC P15927; P13051: UNG; NbExp=6; IntAct=EBI-621404, EBI-1025947; CC P15927; P23025: XPA; NbExp=8; IntAct=EBI-621404, EBI-295222; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10982866, CC ECO:0000269|PubMed:12814551, ECO:0000269|PubMed:20154705, CC ECO:0000269|PubMed:21504906}. Nucleus, PML body CC {ECO:0000269|PubMed:12814551}. Note=Redistributes to discrete nuclear CC foci upon DNA damage in an ATR-dependent manner. CC {ECO:0000269|PubMed:12814551}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P15927-1; Sequence=Displayed; CC Name=2; CC IsoId=P15927-2; Sequence=VSP_017201; CC Name=3; CC IsoId=P15927-3; Sequence=VSP_017202; CC -!- INDUCTION: Translationally up-regulated in response to DNA damage (at CC protein level). {ECO:0000269|PubMed:23393223}. CC -!- PTM: Differentially phosphorylated throughout the cell cycle, becoming CC phosphorylated at the G1-S transition and dephosphorylated in late CC mitosis. Mainly phosphorylated at Ser-23 and Ser-29, by cyclin A-CDK2 CC and cyclin B-CDK1, respectively during DNA replication and mitosis. CC Dephosphorylation may require the serine/threonine-protein phosphatase CC 4. Phosphorylation at Ser-23 and Ser-29 is a prerequisite for further CC phosphorylation. Becomes hyperphosphorylated on additional residues CC including Ser-4, Ser-8, Thr-21 and Ser-33 in response to DNA damage. CC Hyperphosphorylation is mediated by ATM, ATR and PRKDC. Primarily CC recruited to DNA repair nuclear foci as a hypophosphorylated form it CC undergoes subsequent hyperphosphorylation, catalyzed by ATR. CC Hyperphosphorylation is required for RAD51 recruitment to chromatin and CC efficient DNA repair. Phosphorylation at Thr-21 depends upon RFWD3 CC presence. {ECO:0000269|PubMed:12814551, ECO:0000269|PubMed:1318195, CC ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:21558276, CC ECO:0000269|PubMed:21731742, ECO:0000269|PubMed:26474068, CC ECO:0000269|PubMed:8246944, ECO:0000269|PubMed:9139719, CC ECO:0000269|PubMed:9295339}. CC -!- PTM: DNA damage-induced 'Lys-63'-linked polyubiquitination by PRPF19 CC mediates ATRIP recruitment to the RPA complex at sites of DNA damage CC and activation of ATR (PubMed:24332808). Ubiquitinated by RFWD3 at CC stalled replication forks in response to DNA damage: ubiquitination by CC RFWD3 does not lead to degradation by the proteasome and promotes CC removal of the RPA complex from stalled replication forks, promoting CC homologous recombination (PubMed:26474068). CC {ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:26474068}. CC -!- SIMILARITY: Belongs to the replication factor A protein 2 family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/rpa2/"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42146/RPA2"; 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; J05249; AAA36560.1; -; mRNA. DR EMBL; CR450348; CAG29344.1; -; mRNA. DR EMBL; DQ001128; AAX84514.1; -; Genomic_DNA. DR EMBL; AL109927; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001630; AAH01630.1; -; mRNA. DR EMBL; BC012157; AAH12157.1; -; mRNA. DR EMBL; BC021257; AAH21257.1; -; mRNA. DR CCDS; CCDS314.1; -. [P15927-1] DR CCDS; CCDS72740.1; -. [P15927-2] DR PIR; A43711; A43711. DR RefSeq; NP_001273005.1; NM_001286076.1. DR RefSeq; NP_001284487.1; NM_001297558.1. [P15927-2] DR RefSeq; NP_002937.1; NM_002946.4. [P15927-1] DR PDB; 1DPU; NMR; -; A=172-270. DR PDB; 1L1O; X-ray; 2.80 A; B/E=44-171. DR PDB; 1QUQ; X-ray; 2.50 A; A/C=43-171. DR PDB; 1Z1D; NMR; -; A=172-270. DR PDB; 2PI2; X-ray; 2.00 A; A/B/C/D=1-270. DR PDB; 2PQA; X-ray; 2.50 A; A/C=42-172. DR PDB; 2Z6K; X-ray; 3.00 A; A/B=1-270. DR PDB; 3KDF; X-ray; 1.98 A; B/D=41-172. DR PDB; 4MQV; X-ray; 1.95 A; A/C=202-270. DR PDB; 4OU0; X-ray; 1.40 A; A=202-270. DR PDBsum; 1DPU; -. DR PDBsum; 1L1O; -. DR PDBsum; 1QUQ; -. DR PDBsum; 1Z1D; -. DR PDBsum; 2PI2; -. DR PDBsum; 2PQA; -. DR PDBsum; 2Z6K; -. DR PDBsum; 3KDF; -. DR PDBsum; 4MQV; -. DR PDBsum; 4OU0; -. DR AlphaFoldDB; P15927; -. DR BMRB; P15927; -. DR SASBDB; P15927; -. DR SMR; P15927; -. DR BioGRID; 112038; 620. DR ComplexPortal; CPX-1878; Replication protein A complex, RPA2 variant. DR CORUM; P15927; -. DR DIP; DIP-24187N; -. DR IntAct; P15927; 117. DR MINT; P15927; -. DR STRING; 9606.ENSP00000363017; -. DR GlyGen; P15927; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P15927; -. DR MetOSite; P15927; -. DR PhosphoSitePlus; P15927; -. DR SwissPalm; P15927; -. DR BioMuta; RPA2; -. DR DMDM; 132474; -. DR EPD; P15927; -. DR jPOST; P15927; -. DR MassIVE; P15927; -. DR MaxQB; P15927; -. DR PaxDb; 9606-ENSP00000363017; -. DR PeptideAtlas; P15927; -. DR ProteomicsDB; 53246; -. [P15927-1] DR ProteomicsDB; 53247; -. [P15927-2] DR ProteomicsDB; 53248; -. [P15927-3] DR Pumba; P15927; -. DR Antibodypedia; 4296; 1058 antibodies from 43 providers. DR DNASU; 6118; -. DR Ensembl; ENST00000313433.11; ENSP00000363015.3; ENSG00000117748.10. [P15927-3] DR Ensembl; ENST00000373909.7; ENSP00000363017.3; ENSG00000117748.10. [P15927-2] DR Ensembl; ENST00000373912.8; ENSP00000363021.3; ENSG00000117748.10. [P15927-1] DR GeneID; 6118; -. DR KEGG; hsa:6118; -. DR MANE-Select; ENST00000373912.8; ENSP00000363021.3; NM_002946.5; NP_002937.1. DR UCSC; uc001bpe.3; human. [P15927-1] DR AGR; HGNC:10290; -. DR CTD; 6118; -. DR DisGeNET; 6118; -. DR GeneCards; RPA2; -. DR HGNC; HGNC:10290; RPA2. DR HPA; ENSG00000117748; Low tissue specificity. DR MIM; 179836; gene. DR neXtProt; NX_P15927; -. DR OpenTargets; ENSG00000117748; -. DR PharmGKB; PA34652; -. DR VEuPathDB; HostDB:ENSG00000117748; -. DR eggNOG; KOG3108; Eukaryota. DR GeneTree; ENSGT00390000010045; -. DR HOGENOM; CLU_051033_1_0_1; -. DR InParanoid; P15927; -. DR OMA; SFGNKRY; -. DR OrthoDB; 72010at2759; -. DR PhylomeDB; P15927; -. DR TreeFam; TF105242; -. DR PathwayCommons; P15927; -. DR Reactome; R-HSA-110312; Translesion synthesis by REV1. DR Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex. DR Reactome; R-HSA-110320; Translesion Synthesis by POLH. DR Reactome; R-HSA-174437; Removal of the Flap Intermediate from the C-strand. DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress. DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response. DR Reactome; R-HSA-3371511; HSF1 activation. DR Reactome; R-HSA-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha). DR Reactome; R-HSA-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta). DR Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair. DR Reactome; R-HSA-5655862; Translesion synthesis by POLK. DR Reactome; R-HSA-5656121; Translesion synthesis by POLI. DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis. DR Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA). DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR). DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends. DR Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange. DR Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER. DR Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER. DR Reactome; R-HSA-5696400; Dual Incision in GG-NER. DR Reactome; R-HSA-6782135; Dual incision in TC-NER. DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER. DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway. DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation. DR Reactome; R-HSA-68962; Activation of the pre-replicative complex. DR Reactome; R-HSA-69166; Removal of the Flap Intermediate. DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint. DR Reactome; R-HSA-912446; Meiotic recombination. DR Reactome; R-HSA-9709570; Impaired BRCA2 binding to RAD51. DR SignaLink; P15927; -. DR SIGNOR; P15927; -. DR BioGRID-ORCS; 6118; 817 hits in 1171 CRISPR screens. DR ChiTaRS; RPA2; human. DR EvolutionaryTrace; P15927; -. DR GeneWiki; RPA2; -. DR GenomeRNAi; 6118; -. DR Pharos; P15927; Tbio. DR PRO; PR:P15927; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P15927; Protein. DR Bgee; ENSG00000117748; Expressed in ventricular zone and 204 other cell types or tissues. DR ExpressionAtlas; P15927; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:CACAO. DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL. DR GO; GO:0005662; C:DNA replication factor A complex; IDA:UniProtKB. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0016605; C:PML body; IDA:UniProtKB. DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; IDA:BHF-UCL. DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB. DR GO; GO:0006284; P:base-excision repair; IDA:UniProtKB. DR GO; GO:0006260; P:DNA replication; IDA:UniProtKB. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB. DR GO; GO:0006298; P:mismatch repair; IMP:UniProtKB. DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IMP:UniProtKB. DR GO; GO:0006289; P:nucleotide-excision repair; IMP:UniProtKB. DR GO; GO:0034502; P:protein localization to chromosome; IDA:UniProtKB. DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IMP:UniProtKB. DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:UniProtKB. DR GO; GO:0000723; P:telomere maintenance; IMP:UniProtKB. DR CDD; cd04478; RPA2_DBD_D; 1. DR DisProt; DP01361; -. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR IDEAL; IID00026; -. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR040260; RFA2-like. DR InterPro; IPR014646; Rfa2/RPA32. DR InterPro; IPR014892; RPA_C. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR13989:SF16; REPLICATION PROTEIN A 32 KDA SUBUNIT; 1. DR PANTHER; PTHR13989; REPLICATION PROTEIN A-RELATED; 1. DR Pfam; PF08784; RPA_C; 1. DR PIRSF; PIRSF036949; RPA32; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR Genevisible; P15927; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; KW DNA damage; DNA recombination; DNA repair; DNA replication; DNA-binding; KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT CHAIN 1..270 FT /note="Replication protein A 32 kDa subunit" FT /id="PRO_0000097270" FT DNA_BIND 74..148 FT /note="OB" FT REGION 21..41 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 187..270 FT /note="Interaction with RAD52, TIPIN, UNG and XPA" FT /evidence="ECO:0000269|PubMed:11081631" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|PubMed:9139719, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231" FT MOD_RES 4 FT /note="Phosphoserine; by PRKDC" FT /evidence="ECO:0000269|PubMed:21731742, FT ECO:0000269|PubMed:26474068" FT MOD_RES 8 FT /note="Phosphoserine; by PRKDC" FT /evidence="ECO:0000269|PubMed:21731742, FT ECO:0000269|PubMed:26474068" FT MOD_RES 21 FT /note="Phosphothreonine; by PRKDC" FT /evidence="ECO:0000269|PubMed:21558276, FT ECO:0000269|PubMed:26474068, ECO:0000269|PubMed:9139719, FT ECO:0000269|PubMed:9295339" FT MOD_RES 23 FT /note="Phosphoserine; by CDK2" FT /evidence="ECO:0000269|PubMed:1318195, FT ECO:0000269|PubMed:8246944, ECO:0000269|PubMed:9295339, FT ECO:0007744|PubMed:20068231" FT MOD_RES 29 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:1318195, FT ECO:0000269|PubMed:8246944, ECO:0000269|PubMed:9139719, FT ECO:0000269|PubMed:9295339, ECO:0007744|PubMed:20068231" FT MOD_RES 33 FT /note="Phosphoserine; by PRKDC" FT /evidence="ECO:0000269|PubMed:26474068, FT ECO:0000269|PubMed:9139719, ECO:0000269|PubMed:9295339" FT CROSSLNK 37 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000305|PubMed:26474068" FT CROSSLNK 38 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000305|PubMed:26474068" FT VAR_SEQ 1..4 FT /note="MWNS -> MGRGDRNKRSIR (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_017201" FT VAR_SEQ 1..4 FT /note="MWNS -> MWNSNDGGAGWRRKRIAGGFSKRASLGSERRVVAGEEGRERSWG FT VWGSPAGRRRGRLGRLGQCLKGRSLREPAGFSEAWDVAQALILLFKTG (in FT isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_017202" FT VARIANT 14 FT /note="Y -> S (in dbSNP:rs28988896)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_023300" FT VARIANT 15 FT /note="G -> R (in dbSNP:rs28988897)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_023301" FT VARIANT 203 FT /note="N -> S (in dbSNP:rs28904899)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_023302" FT MUTAGEN 4 FT /note="S->A: Increased RAD51 foci formation and homologous FT recombination efficiency at DNA double-strand breaks; when FT associated with A-8." FT /evidence="ECO:0000269|PubMed:21731742" FT MUTAGEN 8 FT /note="S->A: Increased RAD51 foci formation and homologous FT recombination efficiency at DNA double-strand breaks; when FT associated with A-4." FT /evidence="ECO:0000269|PubMed:20154705, FT ECO:0000269|PubMed:21731742" FT MUTAGEN 8 FT /note="S->D: Lower homologous recombination efficiency FT following DNA double strand break. Impaired DNA synthesis FT following DNA damage; when associated with D-33. No effect FT on cell-cycle progression, nor DNA synthesis in undamaged FT cells; when associated with D-23; D-29 and D-33. Impaired FT DNA double strand breaks repair; when associated with D-23; FT D-29 and D-33. Extended DNA damage-induced G2-M checkpoint; FT when associated with D-23; D-29 and D-33. Preferentially FT interacts with RAD51; when associated with D-23; D-29 and FT D-33." FT /evidence="ECO:0000269|PubMed:20154705, FT ECO:0000269|PubMed:21731742" FT MUTAGEN 23 FT /note="S->D: No effect on DNA synthesis following DNA FT damage; when associated with D-29. No effect on cell-cycle FT progression, nor DNA synthesis in undamaged cells; when FT associated with D-8; D-29 and D-33. Impaired DNA double FT strand breaks repair; when associated with D-8; D-29 and FT D-33. Extended DNA damage-induced G2-M checkpoint; when FT associated with D-8; D-29 and D-33. Preferentially FT interacts with RAD51; when associated with D-8; D-29 and FT D-33." FT /evidence="ECO:0000269|PubMed:20154705" FT MUTAGEN 29 FT /note="S->A: Reduces phosphorylation by CDK1." FT /evidence="ECO:0000269|PubMed:20154705, FT ECO:0000269|PubMed:9139719" FT MUTAGEN 29 FT /note="S->D: No effect on DNA synthesis following DNA FT damage; when associated with D-23. No effect on cell-cycle FT progression, nor DNA synthesis in undamaged cells; when FT associated with D-8; D-23 and D-33. Impaired DNA double FT strand breaks repair; when associated with D-8; D-23 and FT D-33. Extended DNA damage-induced G2-M checkpoint; when FT associated with D-8; D-23 and D-33. Preferentially FT interacts with RAD51; when associated with D-8; D-23 and FT D-33." FT /evidence="ECO:0000269|PubMed:20154705, FT ECO:0000269|PubMed:9139719" FT MUTAGEN 33 FT /note="S->D: Lower homologous recombination efficiency FT following DNA double strand break. Impaired DNA synthesis FT following DNA damage; when associated with D-8. No effect FT on cell-cycle progression, nor DNA synthesis in undamaged FT cells; when associated with D-8; D-23 and D-29. Impaired FT DNA double strand breaks repair; when associated with D-8; FT D-23 and D-29. Extended DNA damage-induced G2-M checkpoint; FT when associated with D-8; D-23 and D-29. Preferentially FT interacts with RAD51; when associated with D-8; D-23 and FT D-29." FT /evidence="ECO:0000269|PubMed:20154705" FT MUTAGEN 37..38 FT /note="KK->RR: Impaired ubiquitination without affecting FT homologous recombination." FT /evidence="ECO:0000269|PubMed:26474068" FT MUTAGEN 248 FT /note="F->A: Abolishes interaction with RFWD3, leading to FT impair DNA interstrand cross-links (ICL) repair." FT /evidence="ECO:0000269|PubMed:28575657" FT MUTAGEN 252 FT /note="E->A: Abolishes interaction with RFWD3, leading to FT impair DNA interstrand cross-links (ICL) repair." FT /evidence="ECO:0000269|PubMed:28575657" FT MUTAGEN 253 FT /note="G->A: Does not affect interaction with RFWD3." FT /evidence="ECO:0000269|PubMed:28575657" FT MUTAGEN 254 FT /note="H->A: Abolishes interaction with RFWD3, leading to FT impair DNA interstrand cross-links (ICL) repair." FT /evidence="ECO:0000269|PubMed:28575657" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:1L1O" FT HELIX 51..55 FT /evidence="ECO:0007829|PDB:3KDF" FT STRAND 58..62 FT /evidence="ECO:0007829|PDB:3KDF" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:3KDF" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:1QUQ" FT STRAND 73..85 FT /evidence="ECO:0007829|PDB:3KDF" FT STRAND 87..95 FT /evidence="ECO:0007829|PDB:3KDF" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:3KDF" FT STRAND 102..107 FT /evidence="ECO:0007829|PDB:3KDF" FT STRAND 125..135 FT /evidence="ECO:0007829|PDB:3KDF" FT STRAND 138..148 FT /evidence="ECO:0007829|PDB:3KDF" FT HELIX 153..171 FT /evidence="ECO:0007829|PDB:3KDF" FT HELIX 207..218 FT /evidence="ECO:0007829|PDB:4OU0" FT TURN 222..224 FT /evidence="ECO:0007829|PDB:1DPU" FT HELIX 227..233 FT /evidence="ECO:0007829|PDB:4OU0" FT HELIX 239..252 FT /evidence="ECO:0007829|PDB:4OU0" FT STRAND 254..257 FT /evidence="ECO:0007829|PDB:4OU0" FT STRAND 263..266 FT /evidence="ECO:0007829|PDB:4OU0" SQ SEQUENCE 270 AA; 29247 MW; 61A563EA7B34A9B1 CRC64; MWNSGFESYG SSSYGGAGGY TQSPGGFGSP APSQAEKKSR ARAQHIVPCT ISQLLSATLV DEVFRIGNVE ISQVTIVGII RHAEKAPTNI VYKIDDMTAA PMDVRQWVDT DDTSSENTVV PPETYVKVAG HLRSFQNKKS LVAFKIMPLE DMNEFTTHIL EVINAHMVLS KANSQPSAGR APISNPGMSE AGNFGGNSFM PANGLTVAQN QVLNLIKACP RPEGLNFQDL KNQLKHMSVS SIKQAVDFLS NEGHIYSTVD DDHFKSTDAE //