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Replication protein A 32 kDa subunit (RP-A p32) (Replication factor A protein 2) (RF-A protein 2) (Replication protein A 34 kDa subunit) (RP-A p34)

 RFA2_HUMAN              Reviewed;         270 AA.
P15927; Q52II0; Q5TEI9; Q5TEJ5;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
10-OCT-2018, entry version 200.
RecName: Full=Replication protein A 32 kDa subunit;
Short=RP-A p32;
AltName: Full=Replication factor A protein 2;
Short=RF-A protein 2;
AltName: Full=Replication protein A 34 kDa subunit;
Short=RP-A p34;
Name=RPA2; Synonyms=REPA2, RPA32, RPA34;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE,
FUNCTION IN DNA REPLICATION, AND IDENTIFICATION IN RPA COMPLEX.
PubMed=2406247;
Erdile L.F., Wold M.S., Kelly T.J.;
"The primary structure of the 32-kDa subunit of human replication
protein A.";
J. Biol. Chem. 265:3177-3182(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-14; ARG-15 AND
SER-203.
NIEHS SNPs program;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney, Lung, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
CELL CYCLE-DEPENDENT PHOSPHORYLATION.
PubMed=2200738; DOI=10.1101/gad.4.6.968;
Din S., Brill S.J., Fairman M.P., Stillman B.;
"Cell-cycle-regulated phosphorylation of DNA replication factor A from
human and yeast cells.";
Genes Dev. 4:968-977(1990).
[7]
DNA DAMAGE-INDUCED PHOSPHORYLATION, AND PHOSPHORYLATION AT SER-23 AND
SER-29.
PubMed=1318195;
Dutta A., Stillman B.;
"cdc2 family kinases phosphorylate a human cell DNA replication
factor, RPA, and activate DNA replication.";
EMBO J. 11:2189-2199(1992).
[8]
PHOSPHORYLATION AT SER-23 AND SER-29.
PubMed=8246944; DOI=10.1128/MCB.13.12.7222;
Liu V.F., Weaver D.T.;
"The ionizing radiation-induced replication protein A phosphorylation
response differs between ataxia telangiectasia and normal human
cells.";
Mol. Cell. Biol. 13:7222-7231(1993).
[9]
FUNCTION IN NUCLEOTIDE EXCISION REPAIR.
PubMed=7697716; DOI=10.1016/0092-8674(95)90289-9;
Aboussekhra A., Biggerstaff M., Shivji M.K., Vilpo J.A., Moncollin V.,
Podust V.N., Protic M., Huebscher U., Egly J.M., Wood R.D.;
"Mammalian DNA nucleotide excision repair reconstituted with purified
protein components.";
Cell 80:859-868(1995).
[10]
FUNCTION IN NUCLEOTIDE EXCISION REPAIR, AND INTERACTION WITH XPA.
PubMed=7700386; DOI=10.1038/374566a0;
He Z., Henricksen L.A., Wold M.S., Ingles C.J.;
"RPA involvement in the damage-recognition and incision steps of
nucleotide excision repair.";
Nature 374:566-569(1995).
[11]
FUNCTION IN HOMOLOGOUS RECOMBINATION, AND INTERACTION WITH RAD52.
PubMed=8702565; DOI=10.1074/jbc.271.31.18996;
Park M.S., Ludwig D.L., Stigger E., Lee S.H.;
"Physical interaction between human RAD52 and RPA is required for
homologous recombination in mammalian cells.";
J. Biol. Chem. 271:18996-19000(1996).
[12]
ACETYLATION AT MET-1, PHOSPHORYLATION AT THR-21; SER-29 AND SER-33,
IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF SER-29.
PubMed=9139719; DOI=10.1074/jbc.272.19.12634;
Niu H., Erdjument-Bromage H., Pan Z.-Q., Lee S.-H., Tempst P.,
Hurwitz J.;
"Mapping of amino acid residues in the p34 subunit of human single-
stranded DNA-binding protein phosphorylated by DNA-dependent protein
kinase and Cdc2 kinase in vitro.";
J. Biol. Chem. 272:12634-12641(1997).
[13]
PHOSPHORYLATION AT THR-21; SER-23; SER-29 AND SER-33.
PubMed=9295339; DOI=10.1074/jbc.272.38.23896;
Zernik-Kobak M., Vasunia K., Connelly M., Anderson C.W., Dixon K.;
"Sites of UV-induced phosphorylation of the p34 subunit of replication
protein A from HeLa cells.";
J. Biol. Chem. 272:23896-23904(1997).
[14]
FUNCTION IN DNA REPLICATION, FUNCTION IN DNA MISMATCH REPAIR, AND
FUNCTION IN NUCLEOTIDE EXCISION REPAIR.
PubMed=9430682; DOI=10.1074/jbc.273.3.1453;
Lin Y.L., Shivji M.K., Chen C., Kolodner R., Wood R.D., Dutta A.;
"The evolutionarily conserved zinc finger motif in the largest subunit
of human replication protein A is required for DNA replication and
mismatch repair but not for nucleotide excision repair.";
J. Biol. Chem. 273:1453-1461(1998).
[15]
FUNCTION IN BASE EXCISION REPAIR.
PubMed=9765279; DOI=10.1074/jbc.273.42.27492;
DeMott M.S., Zigman S., Bambara R.A.;
"Replication protein A stimulates long patch DNA base excision
repair.";
J. Biol. Chem. 273:27492-27498(1998).
[16]
INTERACTION WITH SERTAD3, AND SUBCELLULAR LOCATION.
PubMed=10982866; DOI=10.1093/nar/28.18.3478;
Cho J.M., Song D.J., Bergeron J., Benlimame N., Wold M.S.,
Alaoui-Jamali M.A.;
"RBT1, a novel transcriptional co-activator, binds the second subunit
of replication protein A.";
Nucleic Acids Res. 28:3478-3485(2000).
[17]
PHOSPHORYLATION BY ATR, AND SUBCELLULAR LOCATION.
PubMed=12814551; DOI=10.1016/S0960-9822(03)00376-2;
Barr S.M., Leung C.G., Chang E.E., Cimprich K.A.;
"ATR kinase activity regulates the intranuclear translocation of ATR
and RPA following ionizing radiation.";
Curr. Biol. 13:1047-1051(2003).
[18]
FUNCTION IN DNA REPLICATION.
PubMed=15205463; DOI=10.1074/jbc.M403825200;
Weisshart K., Pestryakov P., Smith R.W.P., Hartmann H., Kremmer E.,
Lavrik O., Nasheuer H.-P.;
"Coordinated regulation of replication protein A activities by its
subunits p14 and p32.";
J. Biol. Chem. 279:35368-35376(2004).
[19]
INTERACTION WITH TIMELESS AND TIPIN.
PubMed=17141802; DOI=10.1016/j.jmb.2006.10.097;
Gotter A.L., Suppa C., Emanuel B.S.;
"Mammalian TIMELESS and Tipin are evolutionarily conserved replication
fork-associated factors.";
J. Mol. Biol. 366:36-52(2007).
[20]
FUNCTION IN HOMOLOGOUS RECOMBINATION REPAIR, AND INTERACTION WITH
RAD52.
PubMed=17765923; DOI=10.1016/j.jmb.2007.07.068;
Sleeth K.M., Sorensen C.S., Issaeva N., Dziegielewski J., Bartek J.,
Helleday T.;
"RPA mediates recombination repair during replication stress and is
displaced from DNA by checkpoint signalling in human cells.";
J. Mol. Biol. 373:38-47(2007).
[21]
INTERACTION WITH TIPIN.
PubMed=17296725; DOI=10.1128/MCB.02190-06;
Uensal-Kacmaz K., Chastain P.D., Qu P.-P., Minoo P.,
Cordeiro-Stone M., Sancar A., Kaufmann W.K.;
"The human Tim/Tipin complex coordinates an Intra-S checkpoint
response to UV that slows replication fork displacement.";
Mol. Cell. Biol. 27:3131-3142(2007).
[22]
FUNCTION IN TELOMERE MAINTENANCE, AND SUBCELLULAR LOCATION.
PubMed=17959650; DOI=10.1093/nar/gkm738;
Grudic A., Jul-Larsen A., Haring S.J., Wold M.S., Loenning P.E.,
Bjerkvig R., Boee S.O.;
"Replication protein A prevents accumulation of single-stranded
telomeric DNA in cells that use alternative lengthening of
telomeres.";
Nucleic Acids Res. 35:7267-7278(2007).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[25]
INTERACTION WITH SMARCAL1.
PubMed=19793863; DOI=10.1101/gad.1831509;
Yusufzai T., Kong X., Yokomori K., Kadonaga J.T.;
"The annealing helicase HARP is recruited to DNA repair sites via an
interaction with RPA.";
Genes Dev. 23:2400-2404(2009).
[26]
INTERACTION WITH SMARCAL1.
PubMed=19793861; DOI=10.1101/gad.1839909;
Bansbach C.E., Betous R., Lovejoy C.A., Glick G.G., Cortez D.;
"The annealing helicase SMARCAL1 maintains genome integrity at stalled
replication forks.";
Genes Dev. 23:2405-2414(2009).
[27]
INTERACTION WITH SMARCAL1.
PubMed=19793862; DOI=10.1101/gad.1832309;
Ciccia A., Bredemeyer A.L., Sowa M.E., Terret M.E., Jallepalli P.V.,
Harper J.W., Elledge S.J.;
"The SIOD disorder protein SMARCAL1 is an RPA-interacting protein
involved in replication fork restart.";
Genes Dev. 23:2415-2425(2009).
[28]
FUNCTION AS PART OF THE RPA COMPLEX.
PubMed=19116208; DOI=10.1074/jbc.M808963200;
Mason A.C., Haring S.J., Pryor J.M., Staloch C.A., Gan T.F.,
Wold M.S.;
"An alternative form of replication protein a prevents viral
replication in vitro.";
J. Biol. Chem. 284:5324-5331(2009).
[29]
TISSUE SPECIFICITY.
PubMed=19996105; DOI=10.1074/jbc.M109.079418;
Kemp M.G., Mason A.C., Carreira A., Reardon J.T., Haring S.J.,
Borgstahl G.E., Kowalczykowski S.C., Sancar A., Wold M.S.;
"An alternative form of replication protein a expressed in normal
human tissues supports DNA repair.";
J. Biol. Chem. 285:4788-4797(2010).
[30]
FUNCTION IN DNA REPAIR, PHOSPHORYLATION, DEPHOSPHORYLATION BY PP4,
INTERACTION WITH PPP4C; PPP4R2 AND RAD51, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF SER-8; SER-23; SER-29 AND SER-33.
PubMed=20154705; DOI=10.1038/nsmb.1769;
Lee D.H., Pan Y., Kanner S., Sung P., Borowiec J.A., Chowdhury D.;
"A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA
repair via homologous recombination.";
Nat. Struct. Mol. Biol. 17:365-372(2010).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-23 AND SER-29, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[33]
FUNCTION IN REPLICATION CHECKPOINT, INTERACTION WITH RFWD3, AND
SUBCELLULAR LOCATION.
PubMed=21504906; DOI=10.1074/jbc.M111.222869;
Gong Z., Chen J.;
"E3 ligase RFWD3 participates in replication checkpoint control.";
J. Biol. Chem. 286:22308-22313(2011).
[34]
INTERACTION WITH RFWD3, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT
THR-21.
PubMed=21558276; DOI=10.1074/jbc.M111.222802;
Liu S., Chu J., Yucer N., Leng M., Wang S.Y., Chen B.P.,
Hittelman W.N., Wang Y.;
"RING finger and WD repeat domain 3 (RFWD3) associates with
replication protein A (RPA) and facilitates RPA-mediated DNA damage
response.";
J. Biol. Chem. 286:22314-22322(2011).
[35]
PHOSPHORYLATION AT SER-4 AND SER-8 BY PRKDC, AND MUTAGENESIS OF SER-4
AND SER-8.
PubMed=21731742; DOI=10.1371/journal.pone.0021424;
Liaw H., Lee D., Myung K.;
"DNA-PK-dependent RPA2 hyperphosphorylation facilitates DNA repair and
suppresses sister chromatid exchange.";
PLoS ONE 6:E21424-E21424(2011).
[36]
INDUCTION BY DNA DAMAGE.
PubMed=23393223; DOI=10.1093/carcin/bgt052;
Yin J.Y., Dong Z.Z., Liu R.Y., Chen J., Liu Z.Q., Zhang J.T.;
"Translational regulation of RPA2 via internal ribosomal entry site
and by eIF3a.";
Carcinogenesis 34:1224-1231(2013).
[37]
INTERACTION WITH FBH1.
PubMed=23319600; DOI=10.1083/jcb.201209002;
Jeong Y.T., Rossi M., Cermak L., Saraf A., Florens L., Washburn M.P.,
Sung P., Schildkraut C.L., Schildkraut C., Pagano M.;
"FBH1 promotes DNA double-strand breakage and apoptosis in response to
DNA replication stress.";
J. Cell Biol. 200:141-149(2013).
[38]
FUNCTION, INTERACTION WITH PRPF19, AND UBIQUITINATION BY PRPF19.
PubMed=24332808; DOI=10.1016/j.molcel.2013.11.002;
Marechal A., Li J.M., Ji X.Y., Wu C.S., Yazinski S.A., Nguyen H.D.,
Liu S., Jimenez A.E., Jin J., Zou L.;
"PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and
drives ATR activation via a ubiquitin-mediated circuitry.";
Mol. Cell 53:235-246(2014).
[39]
UBIQUITINATION AT LYS-37 AND LYS-38, PHOSPHORYLATION AT SER-4; SER-8;
THR-21 AND SER-33, AND MUTAGENESIS OF 37-LYS-LYS-38.
PubMed=26474068; DOI=10.1016/j.molcel.2015.09.011;
Elia A.E., Wang D.C., Willis N.A., Boardman A.P., Hajdu I.,
Adeyemi R.O., Lowry E., Gygi S.P., Scully R., Elledge S.J.;
"RFWD3-dependent ubiquitination of RPA regulates repair at stalled
replication forks.";
Mol. Cell 60:280-293(2015).
[40]
INTERACTION WITH ETAA1.
PubMed=27601467; DOI=10.1074/jbc.C116.747758;
Feng S., Zhao Y., Xu Y., Ning S., Huo W., Hou M., Gao G., Ji J.,
Guo R., Xu D.;
"Ewing Tumor-associated Antigen 1 interacts with replication protein A
to promote restart of stalled replication forks.";
J. Biol. Chem. 291:21956-21962(2016).
[41]
FUNCTION, AND INTERACTION WITH ETAA1.
PubMed=27723720; DOI=10.1038/ncb3415;
Bass T.E., Luzwick J.W., Kavanaugh G., Carroll C., Dungrawala H.,
Glick G.G., Feldkamp M.D., Putney R., Chazin W.J., Cortez D.;
"ETAA1 acts at stalled replication forks to maintain genome
integrity.";
Nat. Cell Biol. 18:1185-1195(2016).
[42]
FUNCTION, AND INTERACTION WITH ETAA1.
PubMed=27723717; DOI=10.1038/ncb3422;
Haahr P., Hoffmann S., Tollenaere M.A., Ho T., Toledo L.I., Mann M.,
Bekker-Jensen S., Raeschle M., Mailand N.;
"Activation of the ATR kinase by the RPA-binding protein ETAA1.";
Nat. Cell Biol. 18:1196-1207(2016).
[43]
INTERACTION WITH RFWD3, AND MUTAGENESIS OF PHE-248; GLU-252; GLY-253
AND HIS-254.
PubMed=28575657; DOI=10.1016/j.molcel.2017.04.021;
Feeney L., Munoz I.M., Lachaud C., Toth R., Appleton P.L.,
Schindler D., Rouse J.;
"RPA-mediated recruitment of the E3 ligase RFWD3 is vital for
interstrand crosslink repair and human health.";
Mol. Cell 66:610-621(2017).
[44]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 43-171 IN COMPLEX WITH RPA1
AND RPA3.
PubMed=10449415; DOI=10.1093/emboj/18.16.4498;
Bochkarev A., Bochkareva E., Frappier L., Edwards A.M.;
"The crystal structure of the complex of replication protein A
subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA
binding.";
EMBO J. 18:4498-4504(1999).
[45]
STRUCTURE BY NMR OF 172-270, INTERACTION WITH RAD52; UNG AND XPA, AND
REGION.
PubMed=11081631; DOI=10.1016/S0092-8674(00)00136-7;
Mer G., Bochkarev A., Gupta R., Bochkareva E., Frappier L.,
Ingles C.J., Edwards A.M., Chazin W.J.;
"Structural basis for the recognition of DNA repair proteins UNG2,
XPA, and RAD52 by replication factor RPA.";
Cell 103:449-456(2000).
[46]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 44-171.
PubMed=11927569; DOI=10.1093/emboj/21.7.1855;
Bochkareva E., Korolev S., Lees-Miller S.P., Bochkarev A.;
"Structure of the RPA trimerization core and its role in the multistep
DNA-binding mechanism of RPA.";
EMBO J. 21:1855-1863(2002).
-!- FUNCTION: As part of the heterotrimeric replication protein A
complex (RPA/RP-A), binds and stabilizes single-stranded DNA
intermediates, that form during DNA replication or upon DNA
stress. It prevents their reannealing and in parallel, recruits
and activates different proteins and complexes involved in DNA
metabolism. Thereby, it plays an essential role both in DNA
replication and the cellular response to DNA damage. In the
cellular response to DNA damage, the RPA complex controls DNA
repair and DNA damage checkpoint activation. Through recruitment
of ATRIP activates the ATR kinase a master regulator of the DNA
damage response. It is required for the recruitment of the DNA
double-strand break repair factors RAD51 and RAD52 to chromatin in
response to DNA damage. Also recruits to sites of DNA damage
proteins like XPA and XPG that are involved in nucleotide excision
repair and is required for this mechanism of DNA repair. Plays
also a role in base excision repair (BER) probably through
interaction with UNG. Also recruits SMARCAL1/HARP, which is
involved in replication fork restart, to sites of DNA damage. May
also play a role in telomere maintenance.
{ECO:0000269|PubMed:15205463, ECO:0000269|PubMed:17765923,
ECO:0000269|PubMed:17959650, ECO:0000269|PubMed:19116208,
ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:21504906,
ECO:0000269|PubMed:2406247, ECO:0000269|PubMed:24332808,
ECO:0000269|PubMed:7697716, ECO:0000269|PubMed:7700386,
ECO:0000269|PubMed:8702565, ECO:0000269|PubMed:9430682,
ECO:0000269|PubMed:9765279}.
-!- SUBUNIT: Component of the replication protein A complex (RPA/RP-
A), a heterotrimeric complex composed of RPA1, RPA2 and RPA3
(PubMed:2406247, PubMed:19116208, PubMed:10449415). Interacts with
PRPF19; the PRP19-CDC5L complex is recruited to the sites of DNA
repair where it ubiquitinates the replication protein A complex
(RPA) (PubMed:24332808). Interacts with SERTAD3 (PubMed:10982866).
Interacts with TIPIN (PubMed:17141802, PubMed:17296725). Interacts
with TIMELESS (PubMed:17141802). Interacts with PPP4R2; the
interaction is direct, DNA damage-dependent and mediates the
recruitment of the PP4 catalytic subunit PPP4C (PubMed:20154705).
Interacts (hyperphosphorylated) with RAD51 (PubMed:20154705).
Interacts with SMARCAL1; the interaction is direct and mediates
the recruitment to the RPA complex of SMARCAL1 (PubMed:19793861,
PubMed:19793862, PubMed:19793863). Interacts with RAD52 and XPA;
those interactions are direct and associate RAD52 and XPA to the
RPA complex (PubMed:7700386, PubMed:8702565, PubMed:17765923,
PubMed:11081631). Interacts with FBH1 (PubMed:23319600). Interacts
with ETAA1; the interaction is direct and promotes ETAA1
recruitment at stalled replication forks (PubMed:27601467,
PubMed:27723720, PubMed:27723717). Interacts with RFWD3
(PubMed:21504906, PubMed:21558276, PubMed:26474068,
PubMed:28575657). {ECO:0000269|PubMed:10449415,
ECO:0000269|PubMed:10982866, ECO:0000269|PubMed:11081631,
ECO:0000269|PubMed:17141802, ECO:0000269|PubMed:17296725,
ECO:0000269|PubMed:17765923, ECO:0000269|PubMed:19793861,
ECO:0000269|PubMed:19793862, ECO:0000269|PubMed:19793863,
ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:21504906,
ECO:0000269|PubMed:21558276, ECO:0000269|PubMed:23319600,
ECO:0000269|PubMed:2406247, ECO:0000269|PubMed:24332808,
ECO:0000269|PubMed:26474068, ECO:0000269|PubMed:27601467,
ECO:0000269|PubMed:27723717, ECO:0000269|PubMed:27723720,
ECO:0000269|PubMed:28575657, ECO:0000269|PubMed:7700386,
ECO:0000269|PubMed:8702565}.
-!- INTERACTION:
O75419:CDC45; NbExp=4; IntAct=EBI-621404, EBI-374969;
O60516:EIF4EBP3; NbExp=3; IntAct=EBI-621404, EBI-746950;
P04406:GAPDH; NbExp=2; IntAct=EBI-621404, EBI-354056;
P49643-1:PRIM2; NbExp=3; IntAct=EBI-621404, EBI-15866483;
P27694:RPA1; NbExp=11; IntAct=EBI-621404, EBI-621389;
P35244:RPA3; NbExp=8; IntAct=EBI-621404, EBI-621428;
Q9UJW9:SERTAD3; NbExp=5; IntAct=EBI-621404, EBI-748621;
Q9NZC9:SMARCAL1; NbExp=13; IntAct=EBI-621404, EBI-5457961;
Q9BVW5:TIPIN; NbExp=4; IntAct=EBI-621404, EBI-2515360;
P13051:UNG; NbExp=6; IntAct=EBI-621404, EBI-1025947;
P23025:XPA; NbExp=7; IntAct=EBI-621404, EBI-295222;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10982866,
ECO:0000269|PubMed:12814551, ECO:0000269|PubMed:20154705,
ECO:0000269|PubMed:21504906}. Nucleus, PML body
{ECO:0000269|PubMed:12814551}. Note=Redistributes to discrete
nuclear foci upon DNA damage in an ATR-dependent manner.
{ECO:0000269|PubMed:12814551}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P15927-1; Sequence=Displayed;
Name=2;
IsoId=P15927-2; Sequence=VSP_017201;
Note=No experimental confirmation available.;
Name=3;
IsoId=P15927-3; Sequence=VSP_017202;
Note=No experimental confirmation available.;
-!- INDUCTION: Translationally up-regulated in response to DNA damage
(at protein level). {ECO:0000269|PubMed:23393223}.
-!- PTM: Differentially phosphorylated throughout the cell cycle,
becoming phosphorylated at the G1-S transition and
dephosphorylated in late mitosis. Mainly phosphorylated at Ser-23
and Ser-29, by cyclin A-CDK2 and cyclin B-CDK1, respectively
during DNA replication and mitosis. Dephosphorylation may require
the serine/threonine-protein phosphatase 4. Phosphorylation at
Ser-23 and Ser-29 is a prerequisite for further phosphorylation.
Becomes hyperphosphorylated on additional residues including Ser-
4, Ser-8, Thr-21 and Ser-33 in response to DNA damage.
Hyperphosphorylation is mediated by ATM, ATR and PRKDC. Primarily
recruited to DNA repair nuclear foci as a hypophosphorylated form
it undergoes subsequent hyperphosphorylation, catalyzed by ATR.
Hyperphosphorylation is required for RAD51 recruitment to
chromatin and efficient DNA repair. Phosphorylation at Thr-21
depends upon RFWD3 presence. {ECO:0000269|PubMed:12814551,
ECO:0000269|PubMed:1318195, ECO:0000269|PubMed:20154705,
ECO:0000269|PubMed:21558276, ECO:0000269|PubMed:21731742,
ECO:0000269|PubMed:26474068, ECO:0000269|PubMed:8246944,
ECO:0000269|PubMed:9139719, ECO:0000269|PubMed:9295339}.
-!- PTM: DNA damage-induced 'Lys-63'-linked polyubiquitination by
PRPF19 mediates ATRIP recruitment to the RPA complex at sites of
DNA damage and activation of ATR (PubMed:24332808). Ubiquitinated
by RFWD3 at stalled replication forks in response to DNA damage:
ubiquitination by RFWD3 does not lead to degradation by the
proteasome and promotes removal of the RPA complex from stalled
replication forks, promoting homologous recombination
(PubMed:26474068). {ECO:0000269|PubMed:24332808,
ECO:0000269|PubMed:26474068}.
-!- SIMILARITY: Belongs to the replication factor A protein 2 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/rpa2/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RPA2ID42146ch1p35.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; J05249; AAA36560.1; -; mRNA.
EMBL; CR450348; CAG29344.1; -; mRNA.
EMBL; DQ001128; AAX84514.1; -; Genomic_DNA.
EMBL; AL109927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001630; AAH01630.1; -; mRNA.
EMBL; BC012157; AAH12157.1; -; mRNA.
EMBL; BC021257; AAH21257.1; -; mRNA.
CCDS; CCDS314.1; -. [P15927-1]
CCDS; CCDS72740.1; -. [P15927-2]
PIR; A43711; A43711.
RefSeq; NP_001273005.1; NM_001286076.1.
RefSeq; NP_001284487.1; NM_001297558.1. [P15927-2]
RefSeq; NP_002937.1; NM_002946.4. [P15927-1]
UniGene; Hs.79411; -.
PDB; 1DPU; NMR; -; A=172-270.
PDB; 1L1O; X-ray; 2.80 A; B/E=44-171.
PDB; 1QUQ; X-ray; 2.50 A; A/C=43-171.
PDB; 1Z1D; NMR; -; A=172-270.
PDB; 2PI2; X-ray; 2.00 A; A/B/C/D=1-270.
PDB; 2PQA; X-ray; 2.50 A; A/C=42-172.
PDB; 2Z6K; X-ray; 3.00 A; A/B=1-270.
PDB; 3KDF; X-ray; 1.98 A; B/D=41-172.
PDB; 4MQV; X-ray; 1.95 A; A/C=202-270.
PDB; 4OU0; X-ray; 1.40 A; A=202-270.
PDBsum; 1DPU; -.
PDBsum; 1L1O; -.
PDBsum; 1QUQ; -.
PDBsum; 1Z1D; -.
PDBsum; 2PI2; -.
PDBsum; 2PQA; -.
PDBsum; 2Z6K; -.
PDBsum; 3KDF; -.
PDBsum; 4MQV; -.
PDBsum; 4OU0; -.
ProteinModelPortal; P15927; -.
SMR; P15927; -.
BioGrid; 112038; 462.
CORUM; P15927; -.
DIP; DIP-24187N; -.
IntAct; P15927; 89.
MINT; P15927; -.
STRING; 9606.ENSP00000363021; -.
iPTMnet; P15927; -.
PhosphoSitePlus; P15927; -.
SwissPalm; P15927; -.
BioMuta; RPA2; -.
DMDM; 132474; -.
EPD; P15927; -.
MaxQB; P15927; -.
PaxDb; P15927; -.
PeptideAtlas; P15927; -.
PRIDE; P15927; -.
ProteomicsDB; 53246; -.
ProteomicsDB; 53247; -. [P15927-2]
ProteomicsDB; 53248; -. [P15927-3]
DNASU; 6118; -.
Ensembl; ENST00000313433; ENSP00000363015; ENSG00000117748. [P15927-3]
Ensembl; ENST00000373909; ENSP00000363017; ENSG00000117748. [P15927-2]
Ensembl; ENST00000373912; ENSP00000363021; ENSG00000117748. [P15927-1]
GeneID; 6118; -.
KEGG; hsa:6118; -.
UCSC; uc001bpe.3; human. [P15927-1]
CTD; 6118; -.
DisGeNET; 6118; -.
EuPathDB; HostDB:ENSG00000117748.9; -.
GeneCards; RPA2; -.
HGNC; HGNC:10290; RPA2.
HPA; CAB016538; -.
HPA; HPA026306; -.
HPA; HPA026309; -.
MIM; 179836; gene.
neXtProt; NX_P15927; -.
OpenTargets; ENSG00000117748; -.
PharmGKB; PA34652; -.
eggNOG; KOG3108; Eukaryota.
eggNOG; COG5235; LUCA.
GeneTree; ENSGT00390000010045; -.
HOGENOM; HOG000216562; -.
HOVERGEN; HBG000086; -.
InParanoid; P15927; -.
KO; K10739; -.
OMA; SNPGMGE; -.
OrthoDB; EOG091G0L35; -.
PhylomeDB; P15927; -.
TreeFam; TF105242; -.
Reactome; R-HSA-110312; Translesion synthesis by REV1.
Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
Reactome; R-HSA-110320; Translesion Synthesis by POLH.
Reactome; R-HSA-174437; Removal of the Flap Intermediate from the C-strand.
Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-3371511; HSF1 activation.
Reactome; R-HSA-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
Reactome; R-HSA-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
Reactome; R-HSA-5655862; Translesion synthesis by POLK.
Reactome; R-HSA-5656121; Translesion synthesis by POLI.
Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
Reactome; R-HSA-5696400; Dual Incision in GG-NER.
Reactome; R-HSA-6782135; Dual incision in TC-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-68962; Activation of the pre-replicative complex.
Reactome; R-HSA-69166; Removal of the Flap Intermediate.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
Reactome; R-HSA-912446; Meiotic recombination.
SIGNOR; P15927; -.
ChiTaRS; RPA2; human.
EvolutionaryTrace; P15927; -.
GeneWiki; RPA2; -.
GenomeRNAi; 6118; -.
PRO; PR:P15927; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117748; Expressed in 227 organ(s), highest expression level in leukocyte.
CleanEx; HS_RPA2; -.
ExpressionAtlas; P15927; baseline and differential.
Genevisible; P15927; HS.
GO; GO:0000785; C:chromatin; IDA:CACAO.
GO; GO:0005662; C:DNA replication factor A complex; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0000784; C:nuclear chromosome, telomeric region; HDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IDA:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0098505; F:G-rich strand telomeric DNA binding; IDA:BHF-UCL.
GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0006284; P:base-excision repair; IDA:UniProtKB.
GO; GO:0042769; P:DNA damage response, detection of DNA damage; TAS:Reactome.
GO; GO:0006260; P:DNA replication; IDA:UniProtKB.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
GO; GO:0070987; P:error-free translesion synthesis; TAS:Reactome.
GO; GO:0042276; P:error-prone translesion synthesis; TAS:Reactome.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0036297; P:interstrand cross-link repair; TAS:Reactome.
GO; GO:0006298; P:mismatch repair; IMP:UniProtKB.
GO; GO:0031571; P:mitotic G1 DNA damage checkpoint; IMP:UniProtKB.
GO; GO:0006289; P:nucleotide-excision repair; IMP:UniProtKB.
GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; TAS:Reactome.
GO; GO:0033683; P:nucleotide-excision repair, DNA incision; TAS:Reactome.
GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; TAS:Reactome.
GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; TAS:Reactome.
GO; GO:0006293; P:nucleotide-excision repair, preincision complex stabilization; TAS:Reactome.
GO; GO:0034502; P:protein localization to chromosome; IDA:UniProtKB.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:2000001; P:regulation of DNA damage checkpoint; IMP:UniProtKB.
GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:UniProtKB.
GO; GO:0000723; P:telomere maintenance; IMP:UniProtKB.
GO; GO:0032201; P:telomere maintenance via semi-conservative replication; TAS:Reactome.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
GO; GO:0019985; P:translesion synthesis; TAS:Reactome.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR014646; Rfa2/RPA32.
InterPro; IPR014892; RPA_C.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF08784; RPA_C; 1.
PIRSF; PIRSF036949; RPA32; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF50249; SSF50249; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; DNA damage; DNA recombination; DNA repair;
DNA replication; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
CHAIN 1 270 Replication protein A 32 kDa subunit.
/FTId=PRO_0000097270.
DNA_BIND 74 148 OB.
REGION 187 270 Interaction with RAD52, TIPIN, UNG and
XPA. {ECO:0000269|PubMed:11081631}.
COMPBIAS 1 29 Gly/Ser-rich.
COMPBIAS 37 45 Arg/Lys-rich (basic).
COMPBIAS 95 123 Asp/Glu-rich (acidic).
COMPBIAS 127 145 Arg/Lys-rich (basic).
COMPBIAS 247 270 Asp/Glu-rich (acidic).
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:9139719}.
MOD_RES 4 4 Phosphoserine; by PRKDC.
{ECO:0000269|PubMed:21731742,
ECO:0000269|PubMed:26474068}.
MOD_RES 8 8 Phosphoserine; by PRKDC.
{ECO:0000269|PubMed:21731742,
ECO:0000269|PubMed:26474068}.
MOD_RES 21 21 Phosphothreonine; by PRKDC.
{ECO:0000269|PubMed:21558276,
ECO:0000269|PubMed:26474068,
ECO:0000269|PubMed:9139719,
ECO:0000269|PubMed:9295339}.
MOD_RES 23 23 Phosphoserine; by CDK2.
{ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:1318195,
ECO:0000269|PubMed:8246944,
ECO:0000269|PubMed:9295339}.
MOD_RES 29 29 Phosphoserine; by CDK1.
{ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:1318195,
ECO:0000269|PubMed:8246944,
ECO:0000269|PubMed:9139719,
ECO:0000269|PubMed:9295339}.
MOD_RES 33 33 Phosphoserine; by PRKDC.
{ECO:0000269|PubMed:26474068,
ECO:0000269|PubMed:9139719,
ECO:0000269|PubMed:9295339}.
CROSSLNK 37 37 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305|PubMed:26474068}.
CROSSLNK 38 38 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305|PubMed:26474068}.
VAR_SEQ 1 4 MWNS -> MGRGDRNKRSIR (in isoform 2).
{ECO:0000305}.
/FTId=VSP_017201.
VAR_SEQ 1 4 MWNS -> MWNSNDGGAGWRRKRIAGGFSKRASLGSERRVV
AGEEGRERSWGVWGSPAGRRRGRLGRLGQCLKGRSLREPAG
FSEAWDVAQALILLFKTG (in isoform 3).
{ECO:0000305}.
/FTId=VSP_017202.
VARIANT 14 14 Y -> S (in dbSNP:rs28988896).
{ECO:0000269|Ref.3}.
/FTId=VAR_023300.
VARIANT 15 15 G -> R (in dbSNP:rs28988897).
{ECO:0000269|Ref.3}.
/FTId=VAR_023301.
VARIANT 203 203 N -> S (in dbSNP:rs28904899).
{ECO:0000269|Ref.3}.
/FTId=VAR_023302.
MUTAGEN 4 4 S->A: Increased RAD51 foci formation and
homologous recombination efficiency at
DNA double-strand breaks; when associated
with A-8. {ECO:0000269|PubMed:21731742}.
MUTAGEN 8 8 S->A: Increased RAD51 foci formation and
homologous recombination efficiency at
DNA double-strand breaks; when associated
with A-4. {ECO:0000269|PubMed:20154705,
ECO:0000269|PubMed:21731742}.
MUTAGEN 8 8 S->D: Lower homologous recombination
efficiency following DNA double strand
break. Impaired DNA synthesis following
DNA damage; when associated with D-33. No
effect on cell-cycle progression, nor DNA
synthesis in undamaged cells; when
associated with D-23; D-29 and D-33.
Impaired DNA double strand breaks repair;
when associated with D-23; D-29 and D-33.
Extended DNA damage-induced G2-M
checkpoint; when associated with D-23; D-
29 and D-33. Preferentially interacts
with RAD51; when associated with D-23; D-
29 and D-33.
{ECO:0000269|PubMed:20154705,
ECO:0000269|PubMed:21731742}.
MUTAGEN 23 23 S->D: No effect on DNA synthesis
following DNA damage; when associated
with D-29. No effect on cell-cycle
progression, nor DNA synthesis in
undamaged cells; when associated with D-
8; D-29 and D-33. Impaired DNA double
strand breaks repair; when associated
with D-8; D-29 and D-33. Extended DNA
damage-induced G2-M checkpoint; when
associated with D-8; D-29 and D-33.
Preferentially interacts with RAD51; when
associated with D-8; D-29 and D-33.
{ECO:0000269|PubMed:20154705}.
MUTAGEN 29 29 S->A: Reduces phosphorylation by CDK1.
{ECO:0000269|PubMed:20154705,
ECO:0000269|PubMed:9139719}.
MUTAGEN 29 29 S->D: No effect on DNA synthesis
following DNA damage; when associated
with D-23. No effect on cell-cycle
progression, nor DNA synthesis in
undamaged cells; when associated with D-
8; D-23 and D-33. Impaired DNA double
strand breaks repair; when associated
with D-8; D-23 and D-33. Extended DNA
damage-induced G2-M checkpoint; when
associated with D-8; D-23 and D-33.
Preferentially interacts with RAD51; when
associated with D-8; D-23 and D-33.
{ECO:0000269|PubMed:20154705,
ECO:0000269|PubMed:9139719}.
MUTAGEN 33 33 S->D: Lower homologous recombination
efficiency following DNA double strand
break. Impaired DNA synthesis following
DNA damage; when associated with D-8. No
effect on cell-cycle progression, nor DNA
synthesis in undamaged cells; when
associated with D-8; D-23 and D-29.
Impaired DNA double strand breaks repair;
when associated with D-8; D-23 and D-29.
Extended DNA damage-induced G2-M
checkpoint; when associated with D-8; D-
23 and D-29. Preferentially interacts
with RAD51; when associated with D-8; D-
23 and D-29.
{ECO:0000269|PubMed:20154705}.
MUTAGEN 37 38 KK->RR: Impaired ubiquitination without
affecting homologous recombination.
{ECO:0000269|PubMed:26474068}.
MUTAGEN 248 248 F->A: Abolishes interaction with RFWD3,
leading to impair DNA interstrand cross-
links (ICL) repair.
{ECO:0000269|PubMed:28575657}.
MUTAGEN 252 252 E->A: Abolishes interaction with RFWD3,
leading to impair DNA interstrand cross-
links (ICL) repair.
{ECO:0000269|PubMed:28575657}.
MUTAGEN 253 253 G->A: Does not affect interaction with
RFWD3. {ECO:0000269|PubMed:28575657}.
MUTAGEN 254 254 H->A: Abolishes interaction with RFWD3,
leading to impair DNA interstrand cross-
links (ICL) repair.
{ECO:0000269|PubMed:28575657}.
STRAND 46 48 {ECO:0000244|PDB:1L1O}.
HELIX 51 55 {ECO:0000244|PDB:3KDF}.
STRAND 58 62 {ECO:0000244|PDB:3KDF}.
STRAND 64 66 {ECO:0000244|PDB:3KDF}.
STRAND 69 71 {ECO:0000244|PDB:1QUQ}.
STRAND 73 85 {ECO:0000244|PDB:3KDF}.
STRAND 87 95 {ECO:0000244|PDB:3KDF}.
STRAND 97 100 {ECO:0000244|PDB:3KDF}.
STRAND 102 107 {ECO:0000244|PDB:3KDF}.
STRAND 125 135 {ECO:0000244|PDB:3KDF}.
STRAND 138 148 {ECO:0000244|PDB:3KDF}.
HELIX 153 171 {ECO:0000244|PDB:3KDF}.
HELIX 207 218 {ECO:0000244|PDB:4OU0}.
TURN 222 224 {ECO:0000244|PDB:1DPU}.
HELIX 227 233 {ECO:0000244|PDB:4OU0}.
HELIX 239 252 {ECO:0000244|PDB:4OU0}.
STRAND 254 257 {ECO:0000244|PDB:4OU0}.
STRAND 263 266 {ECO:0000244|PDB:4OU0}.
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


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EIAAB34350 Homo sapiens,Human,Replication factor A protein 4,Replication protein A 30 kDa subunit,RF-A protein 4,RP-A p30,RPA4
EIAAB34343 Mouse,Mus musculus,Replication factor A protein 1,Replication protein A 70 kDa DNA-binding subunit,RF-A protein 1,RP-A p70,Rpa1
EIAAB34349 Mouse,Mus musculus,Replication factor A protein 3,Replication protein A 14 kDa subunit,RF-A protein 3,RP-A p14,Rpa3
EIAAB34347 Rat,Rattus norvegicus,Replication factor A protein 2,Replication protein A 32 kDa subunit,RF-A protein 2,RP-A p32,Rpa2
EIAAB34342 Homo sapiens,Human,REPA1,Replication factor A protein 1,Replication protein A 70 kDa DNA-binding subunit,RF-A protein 1,RP-A p70,RPA1,RPA70,Single-stranded DNA-binding protein
15-288-22278F Replication protein A 14 kDa subunit - RP-A; RF-A; Replication factor-A protein 3; p14 Polyclonal 0.05 mg
15-288-22278F Replication protein A 14 kDa subunit - RP-A; RF-A; Replication factor-A protein 3; p14 Polyclonal 0.1 mg
EIAAB34344 Chicken,Gallus gallus,RCJMB04_17l6,Replication factor A protein 1,Replication protein A 70 kDa DNA-binding subunit,RF-A protein 1,RP-A p70,RPA1
EIAAB34352 A1 140 kDa subunit,Activator 1 140 kDa subunit,Activator 1 large subunit,Activator 1 subunit 1,DNA-binding protein PO-GA,Homo sapiens,Human,Replication factor C 140 kDa subunit,Replication factor C la
10-288-22181F Replication protein A 32 kDa subunit - RP-A; RF-A; Replication factor-A protein 2; p32; p34 0.05 mg
10-288-22278F Replication protein A 14 kDa subunit - RP-A; RF-A; Replication factor-A protein 3; p14 0.05 mg
10-288-22278F Replication protein A 14 kDa subunit - RP-A; RF-A; Replication factor-A protein 3; p14 0.1 mg
10-288-22181F Replication protein A 32 kDa subunit - RP-A; RF-A; Replication factor-A protein 2; p32; p34 0.1 mg
EIAAB34361 A1 37 kDa subunit,Activator 1 37 kDa subunit,Activator 1 subunit 4,Homo sapiens,Human,Replication factor C 37 kDa subunit,Replication factor C subunit 4,RF-C 37 kDa subunit,RFC37,RFC4
EIAAB34363 A1 36 kDa subunit,Activator 1 36 kDa subunit,Activator 1 subunit 5,Homo sapiens,Human,Replication factor C 36 kDa subunit,Replication factor C subunit 5,RF-C 36 kDa subunit,RFC36,RFC5
EIAAB34355 A1 40 kDa subunit,Activator 1 40 kDa subunit,Activator 1 subunit 2,Homo sapiens,Human,Replication factor C 40 kDa subunit,Replication factor C subunit 2,RF-C 40 kDa subunit,RFC2,RFC40
EIAAB34360 A1 38 kDa subunit,Activator 1 38 kDa subunit,Activator 1 subunit 3,Homo sapiens,Human,Replication factor C 38 kDa subunit,Replication factor C subunit 3,RF-C 38 kDa subunit,RFC3,RFC38
EIAAB34364 A1 36 kDa subunit,Activator 1 36 kDa subunit,Activator 1 subunit 5,Mouse,Mus musculus,Replication factor C 36 kDa subunit,Replication factor C subunit 5,RF-C 36 kDa subunit,RFC36,Rfc5
EIAAB34359 A1 38 kDa subunit,Activator 1 38 kDa subunit,Activator 1 subunit 3,Mouse,Mus musculus,Replication factor C 38 kDa subunit,Replication factor C subunit 3,RF-C 38 kDa subunit,Rfc3,RFC38
EIAAB34358 A1 38 kDa subunit,Activator 1 38 kDa subunit,Activator 1 subunit 3,Bos taurus,Bovine,Replication factor C 38 kDa subunit,Replication factor C subunit 3,RF-C 38 kDa subunit,RFC3,RFC38
EIAAB34354 A1 40 kDa subunit,Activator 1 40 kDa subunit,Activator 1 subunit 2,Mouse,Mus musculus,Replication factor C 40 kDa subunit,Replication factor C subunit 2,RF-C 40 kDa subunit,Rfc2,RFC40
15-288-21946F Replication factor C subunit 3 - Replication factor C 38 kDa subunit; RFC38; Activator 1 38 kDa subunit; A1 38 kDa subunit; RF-C 38 kDa subunit Polyclonal 0.05 mg


 

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