ID RFA3_HUMAN Reviewed; 121 AA. AC P35244; Q549U6; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 27-MAR-2024, entry version 205. DE RecName: Full=Replication protein A 14 kDa subunit; DE Short=RP-A p14; DE AltName: Full=Replication factor A protein 3; DE Short=RF-A protein 3; GN Name=RPA3; Synonyms=REPA3, RPA14; 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]. RX PubMed=8454588; DOI=10.1016/s0021-9258(18)53229-4; RA Umbricht C.B., Kelly T.J.; RT "Cloning, overexpression, and genomic mapping of the 14-kDa subunit of RT human replication protein A."; RL J. Biol. Chem. 268:6131-6138(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney, and Lung; 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 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 [7] RP INTERACTION WITH RPA4. RX PubMed=7760808; DOI=10.1128/mcb.15.6.3119; RA Keshav K.F., Chen C., Dutta A.; RT "Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A RT complex."; RL Mol. Cell. Biol. 15:3119-3128(1995). RN [8] RP FUNCTION IN DNA REPLICATION, SUBCELLULAR LOCATION, FUNCTION IN DNA MISMATCH RP REPAIR, AND FUNCTION 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 [9] 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 [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [11] RP IDENTIFICATION IN THE ARPA COMPLEX, AND FUNCTION OF THE ARPA 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 [12] RP SINGLE-STRANDED DNA-BINDING. RX PubMed=19010961; DOI=10.1093/nar/gkn895; RA Salas T.R., Petruseva I., Lavrik O., Saintome C.; RT "Evidence for direct contact between the RPA3 subunit of the human RT replication protein A and single-stranded DNA."; RL Nucleic Acids Res. 37:38-46(2009). RN [13] RP FUNCTION OF THE ARPA COMPLEX. 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 [14] 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 [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP FUNCTION. 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 [19] RP UBIQUITINATION AT LYS-23; LYS-39 AND LYS-88. 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 [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH RPA1 AND RPA2. 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 that CC 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 (PubMed:9430682). In the cellular response to DNA damage, the CC RPA complex controls DNA repair and DNA damage checkpoint activation. CC Through recruitment of ATRIP activates the ATR kinase a master CC regulator of the DNA damage response (PubMed:24332808). It is required CC for the recruitment of the DNA double-strand break repair factors RAD51 CC and RAD52 to chromatin, in response to DNA damage. Also recruits to CC sites of DNA damage proteins like XPA and XPG that are involved in CC nucleotide excision repair and is required for this mechanism of DNA CC repair (PubMed:7697716). Also plays a role in base excision repair CC (BER), probably through interaction with UNG (PubMed:9765279). 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 RPA3 has its own single-stranded DNA-binding activity and may be CC responsible for polarity of the binding of the complex to DNA CC (PubMed:19010961). As part of the alternative replication protein A CC complex, aRPA, binds single-stranded DNA and probably plays a role in CC DNA repair. Compared to the RPA2-containing, canonical RPA complex, may CC not support chromosomal DNA replication and cell cycle progression CC through S-phase. The aRPA may not promote efficient priming by DNA CC polymerase alpha but could support DNA synthesis by polymerase delta in CC presence of PCNA and replication factor C (RFC), the dual CC incision/excision reaction of nucleotide excision repair and RAD51- CC dependent strand exchange (PubMed:19996105). CC {ECO:0000269|PubMed:19010961, ECO:0000269|PubMed:19116208, CC ECO:0000269|PubMed:19996105, ECO:0000269|PubMed:7697716, CC ECO:0000269|PubMed:9430682, ECO:0000269|PubMed:9765279, CC ECO:0000303|PubMed:24332808}. CC -!- SUBUNIT: Component of the canonical replication protein A complex CC (RPA), a heterotrimer composed of RPA1, RPA2 and RPA3. Also a component CC of the aRPA, the alternative replication protein A complex, a trimeric CC complex similar to the replication protein A complex/RPA but where RPA1 CC and RPA3 are associated with RPA4 instead of RPA2. CC {ECO:0000269|PubMed:11927569, ECO:0000269|PubMed:19116208}. CC -!- INTERACTION: CC P35244; P43351: RAD52; NbExp=3; IntAct=EBI-621428, EBI-706448; CC P35244; P27694: RPA1; NbExp=11; IntAct=EBI-621428, EBI-621389; CC P35244; P15927: RPA2; NbExp=12; IntAct=EBI-621428, EBI-621404; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9430682}. CC -!- PTM: Ubiquitinated by RFWD3 at stalled replication forks in response to CC DNA damage: ubiquitination by RFWD3 does not lead to degradation by the CC proteasome and promotes removal of the RPA complex from stalled CC replication forks, promoting homologous recombination CC (PubMed:26474068). {ECO:0000269|PubMed:26474068}. CC -!- SIMILARITY: Belongs to the replication factor A protein 3 family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/rpa3/"; 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; L07493; AAA58350.1; -; mRNA. DR EMBL; BT007320; AAP35984.1; -; mRNA. DR EMBL; DQ003136; AAX84517.1; -; Genomic_DNA. DR EMBL; AC004948; AAQ96878.1; -; Genomic_DNA. DR EMBL; BC005264; AAH05264.1; -; mRNA. DR EMBL; BC009868; AAH09868.1; -; mRNA. DR CCDS; CCDS5356.1; -. DR PIR; A46008; A46008. DR RefSeq; NP_002938.1; NM_002947.4. DR PDB; 1L1O; X-ray; 2.80 A; A/D=1-121. DR PDB; 1QUQ; X-ray; 2.50 A; B/D=1-121. DR PDB; 2PI2; X-ray; 2.00 A; E/F/G/H=1-121. DR PDB; 2PQA; X-ray; 2.50 A; B/D=1-121. DR PDB; 2Z6K; X-ray; 3.00 A; C/D=1-121. DR PDB; 3KDF; X-ray; 1.98 A; A/C=1-121. DR PDBsum; 1L1O; -. DR PDBsum; 1QUQ; -. DR PDBsum; 2PI2; -. DR PDBsum; 2PQA; -. DR PDBsum; 2Z6K; -. DR PDBsum; 3KDF; -. DR AlphaFoldDB; P35244; -. DR SASBDB; P35244; -. DR SMR; P35244; -. DR BioGRID; 112039; 511. DR ComplexPortal; CPX-1878; Replication protein A complex, RPA2 variant. DR ComplexPortal; CPX-1879; Replication protein A complex, RPA4 variant. DR CORUM; P35244; -. DR DIP; DIP-24190N; -. DR IntAct; P35244; 75. DR MINT; P35244; -. DR STRING; 9606.ENSP00000223129; -. DR GlyGen; P35244; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P35244; -. DR MetOSite; P35244; -. DR PhosphoSitePlus; P35244; -. DR BioMuta; RPA3; -. DR DMDM; 464608; -. DR EPD; P35244; -. DR jPOST; P35244; -. DR MassIVE; P35244; -. DR MaxQB; P35244; -. DR PaxDb; 9606-ENSP00000223129; -. DR PeptideAtlas; P35244; -. DR ProteomicsDB; 55011; -. DR Pumba; P35244; -. DR TopDownProteomics; P35244; -. DR Antibodypedia; 1308; 326 antibodies from 31 providers. DR DNASU; 6119; -. DR Ensembl; ENST00000223129.8; ENSP00000223129.4; ENSG00000106399.11. DR Ensembl; ENST00000396682.6; ENSP00000379914.2; ENSG00000106399.11. DR GeneID; 6119; -. DR KEGG; hsa:6119; -. DR MANE-Select; ENST00000223129.8; ENSP00000223129.4; NM_002947.5; NP_002938.1. DR UCSC; uc003sri.4; human. DR AGR; HGNC:10291; -. DR CTD; 6119; -. DR DisGeNET; 6119; -. DR GeneCards; RPA3; -. DR HGNC; HGNC:10291; RPA3. DR HPA; ENSG00000106399; Low tissue specificity. DR MIM; 179837; gene. DR neXtProt; NX_P35244; -. DR OpenTargets; ENSG00000106399; -. DR PharmGKB; PA34653; -. DR VEuPathDB; HostDB:ENSG00000106399; -. DR eggNOG; ENOG502S203; Eukaryota. DR GeneTree; ENSGT00390000008029; -. DR InParanoid; P35244; -. DR OMA; IGKPVCF; -. DR OrthoDB; 2901821at2759; -. DR PhylomeDB; P35244; -. DR TreeFam; TF105243; -. DR PathwayCommons; P35244; -. 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; P35244; -. DR SIGNOR; P35244; -. DR BioGRID-ORCS; 6119; 838 hits in 1112 CRISPR screens. DR ChiTaRS; RPA3; human. DR EvolutionaryTrace; P35244; -. DR GeneWiki; RPA3; -. DR GenomeRNAi; 6119; -. DR Pharos; P35244; Tbio. DR PRO; PR:P35244; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P35244; Protein. DR Bgee; ENSG00000106399; Expressed in bronchial epithelial cell and 207 other cell types or tissues. DR ExpressionAtlas; P35244; baseline and differential. DR GO; GO:0005662; C:DNA replication factor A complex; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central. DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0006284; P:base-excision repair; IDA:UniProtKB. DR GO; GO:0006281; P:DNA repair; IDA:ComplexPortal. DR GO; GO:0006260; P:DNA replication; IMP: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:0006289; P:nucleotide-excision repair; IMP:UniProtKB. DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IEA:Ensembl. DR GO; GO:0000723; P:telomere maintenance; TAS:BHF-UCL. DR CDD; cd04479; RPA3; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR IDEAL; IID00040; -. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR013970; Rfa2. DR PANTHER; PTHR15114:SF1; REPLICATION PROTEIN A 14 KDA SUBUNIT; 1. DR PANTHER; PTHR15114; REPLICATION PROTEIN A3; 1. DR Pfam; PF08661; Rep_fac-A_3; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR Genevisible; P35244; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; DNA damage; DNA recombination; DNA repair; KW DNA replication; Isopeptide bond; Nucleus; Reference proteome; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..121 FT /note="Replication protein A 14 kDa subunit" FT /id="PRO_0000097276" FT MOD_RES 2 FT /note="N-acetylvaline" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CROSSLNK 23 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:26474068" FT CROSSLNK 39 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:26474068" FT CROSSLNK 88 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:26474068" FT HELIX 4..6 FT /evidence="ECO:0007829|PDB:3KDF" FT STRAND 10..12 FT /evidence="ECO:0007829|PDB:3KDF" FT HELIX 14..20 FT /evidence="ECO:0007829|PDB:3KDF" FT STRAND 24..34 FT /evidence="ECO:0007829|PDB:3KDF" FT STRAND 38..44 FT /evidence="ECO:0007829|PDB:3KDF" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:3KDF" FT STRAND 65..73 FT /evidence="ECO:0007829|PDB:3KDF" FT STRAND 79..86 FT /evidence="ECO:0007829|PDB:3KDF" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:3KDF" FT HELIX 96..108 FT /evidence="ECO:0007829|PDB:3KDF" FT HELIX 110..112 FT /evidence="ECO:0007829|PDB:3KDF" SQ SEQUENCE 121 AA; 13569 MW; 3FD99851959FB498 CRC64; MVDMMDLPRS RINAGMLAQF IDKPVCFVGR LEKIHPTGKM FILSDGEGKN GTIELMEPLD EEISGIVEVV GRVTAKATIL CTSYVQFKED SHPFDLGLYN EAVKIIHDFP QFYPLGIVQH D //