RFA3_HUMAN
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 03-AUG-2022, entry version 196.
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=9; 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 SMR; P35244; -.
DR BioGRID; 112039; 471.
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; 72.
DR MINT; P35244; -.
DR STRING; 9606.ENSP00000223129; -.
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; P35244; -.
DR PeptideAtlas; P35244; -.
DR PRIDE; P35244; -.
DR ProteomicsDB; 55011; -.
DR TopDownProteomics; P35244; -.
DR Antibodypedia; 1308; 301 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 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; INRPVCF; -.
DR OrthoDB; 1594928at2759; -.
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; 807 hits in 1034 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 205 other tissues.
DR ExpressionAtlas; P35244; baseline and differential.
DR Genevisible; P35244; HS.
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 Gene3D; 2.40.50.140; -; 1.
DR IDEAL; IID00040; -.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013970; Rfa2.
DR Pfam; PF08661; Rep_fac-A_3; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
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
