RFA1_HUMAN
ID RFA1_HUMAN Reviewed; 616 AA.
AC P27694; A8K0Y9; Q59ES9;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 226.
DE RecName: Full=Replication protein A 70 kDa DNA-binding subunit;
DE Short=RP-A p70;
DE AltName: Full=Replication factor A protein 1;
DE Short=RF-A protein 1;
DE AltName: Full=Single-stranded DNA-binding protein;
DE Contains:
DE RecName: Full=Replication protein A 70 kDa DNA-binding subunit, N-terminally processed;
GN Name=RPA1; Synonyms=REPA1, RPA70;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2050703; DOI=10.1016/s0021-9258(18)99069-1;
RA Erdile L.F., Heyer W.-D., Kolodner R., Kelly T.J.;
RT "Characterization of a cDNA encoding the 70-kDa single-stranded DNA-binding
RT subunit of human replication protein A and the role of the protein in DNA
RT replication.";
RL J. Biol. Chem. 266:12090-12098(1991).
RN [2]
RP SEQUENCE REVISION TO 217.
RX PubMed=8420996; DOI=10.1016/s0021-9258(18)53993-4;
RA Erdile L.F., Heyer W.-D., Kolodner R., Kelly T.J.;
RT "Type I human complement C2 deficiency. A 28-base pair gene deletion causes
RT skipping of exon 6 during RNA splicing.";
RL J. Biol. Chem. 268:2268-2268(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-351.
RC TISSUE=Aortic endothelium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-351.
RG NIEHS SNPs program;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [8]
RP PROTEIN SEQUENCE OF 2-41; 82-88; 93-103; 168-196; 221-259; 314-324;
RP 345-379; 390-410; 413-472; 490-499; 503-511; 552-568; 576-586 AND 589-600,
RP CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
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 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 [12]
RP INTERACTION WITH POLA1.
RX PubMed=9214288; DOI=10.1021/bi970473r;
RA Braun K.A., Lao Y., He Z., Ingles C.J., Wold M.S.;
RT "Role of protein-protein interactions in the function of replication
RT protein A (RPA): RPA modulates the activity of DNA polymerase alpha by
RT multiple mechanisms.";
RL Biochemistry 36:8443-8454(1997).
RN [13]
RP FUNCTION IN DNA REPLICATION, FUNCTION IN DNA MISMATCH REPAIR, FUNCTION IN
RP NUCLEOTIDE EXCISION REPAIR, AND MUTAGENESIS OF CYS-500 AND CYS-503.
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 [14]
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 [15]
RP INTERACTION WITH XPA.
RX PubMed=9699634; DOI=10.1038/1400;
RA Ikegami T., Kuraoka I., Saijo M., Kodo N., Kyogoku Y., Morikawa K.,
RA Tanaka K., Shirakawa M.;
RT "Solution structure of the DNA- and RPA-binding domain of the human repair
RT factor XPA.";
RL Nat. Struct. Biol. 5:701-706(1998).
RN [16]
RP INTERACTION WITH XPA.
RX PubMed=10563794; DOI=10.1021/bi991755p;
RA Buchko G.W., Daughdrill G.W., de Lorimier R., Sudha Rao B.K., Isern N.G.,
RA Lingbeck J.M., Taylor J.-S., Wold M.S., Gochin M., Spicer L.D., Lowry D.F.,
RA Kennedy M.A.;
RT "Interactions of human nucleotide excision repair protein XPA with DNA and
RT RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studies.";
RL Biochemistry 38:15116-15128(1999).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [18]
RP FUNCTION IN CHEK1 SIGNALING.
RX PubMed=12791985; DOI=10.1126/science.1083430;
RA Zou L., Elledge S.J.;
RT "Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes.";
RL Science 300:1542-1548(2003).
RN [19]
RP INTERACTION WITH RIPK1.
RX PubMed=16135809; DOI=10.1128/mcb.25.18.8202-8214.2005;
RA Park J., Seo T., Kim H., Choe J.;
RT "Sumoylation of the novel protein hRIPbeta is involved in replication
RT protein A deposition in PML nuclear bodies.";
RL Mol. Cell. Biol. 25:8202-8214(2005).
RN [20]
RP FUNCTION IN HOMOLOGOUS RECOMBINATION REPAIR.
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 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [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 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 [26]
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 [27]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-163; LYS-167 AND LYS-259, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [28]
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 [29]
RP SUMOYLATION AT LYS-449 AND LYS-577, DESUMOYLATION BY SENP6, MUTAGENESIS OF
RP LYS-449 AND LYS-577, AND INTERACTION WITH SENP6 AND RAD51.
RX PubMed=20705237; DOI=10.1016/j.molcel.2010.07.021;
RA Dou H., Huang C., Singh M., Carpenter P.B., Yeh E.T.;
RT "Regulation of DNA repair through desumoylation and sumoylation of
RT replication protein A complex.";
RL Mol. Cell 39:333-345(2010).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180; THR-191 AND SER-384, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [31]
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 [32]
RP INTERACTION WITH HELB, AND MUTAGENESIS OF ARG-41 AND ARG-43.
RX PubMed=22194613; DOI=10.1074/jbc.m111.324582;
RA Guler G.D., Liu H., Vaithiyalingam S., Arnett D.R., Kremmer E.,
RA Chazin W.J., Fanning E.;
RT "Human DNA helicase B (HDHB) binds to replication protein A and facilitates
RT cellular recovery from replication stress.";
RL J. Biol. Chem. 287:6469-6481(2012).
RN [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [34]
RP INTERACTION WITH PRIMPOL.
RX PubMed=24126761; DOI=10.1038/embor.2013.159;
RA Wan L., Lou J., Xia Y., Su B., Liu T., Cui J., Sun Y., Lou H., Huang J.;
RT "hPrimpol1/CCDC111 is a human DNA primase-polymerase required for the
RT maintenance of genome integrity.";
RL EMBO Rep. 14:1104-1112(2013).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-191 AND SER-384, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [36]
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 [37]
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 [38]
RP INTERACTION WITH PRIMPOL.
RX PubMed=25550423; DOI=10.1093/nar/gku1321;
RA Guilliam T.A., Jozwiakowski S.K., Ehlinger A., Barnes R.P., Rudd S.G.,
RA Bailey L.J., Skehel J.M., Eckert K.A., Chazin W.J., Doherty A.J.;
RT "Human PrimPol is a highly error-prone polymerase regulated by single-
RT stranded DNA binding proteins.";
RL Nucleic Acids Res. 43:1056-1068(2015).
RN [39]
RP INTERACTION WITH HELB.
RX PubMed=26774285; DOI=10.1016/j.molcel.2015.12.013;
RA Tkac J., Xu G., Adhikary H., Young J.T., Gallo D., Escribano-Diaz C.,
RA Krietsch J., Orthwein A., Munro M., Sol W., Al-Hakim A., Lin Z.Y.,
RA Jonkers J., Borst P., Brown G.W., Gingras A.C., Rottenberg S., Masson J.Y.,
RA Durocher D.;
RT "HELB is a feedback inhibitor of DNA end resection.";
RL Mol. Cell 61:405-418(2016).
RN [40]
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 [41]
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 [42]
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 [43]
RP UBIQUITINATION AT LYS-22; LYS-88; LYS-163; LYS-167; LYS-183; LYS-220;
RP LYS-244; LYS-259; LYS-267; LYS-331; LYS-410; LYS-431; LYS-458 AND LYS-553.
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 [44]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 183-420.
RX PubMed=8990123; DOI=10.1038/385176a0;
RA Bochkarev A., Pfuetzner R.A., Edwards A.M., Frappier L.;
RT "Structure of the single-stranded-DNA-binding domain of replication protein
RT A bound to DNA.";
RL Nature 385:176-181(1997).
RN [45] {ECO:0007744|PDB:5N85, ECO:0007744|PDB:5N8A}
RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) OF 1-120 IN COMPLEX WITH PRIMPOL,
RP AND INTERACTION WITH PRIMPOL.
RX PubMed=28534480; DOI=10.1038/ncomms15222;
RA Guilliam T.A., Brissett N.C., Ehlinger A., Keen B.A., Kolesar P.,
RA Taylor E.M., Bailey L.J., Lindsay H.D., Chazin W.J., Doherty A.J.;
RT "Molecular basis for PrimPol recruitment to replication forks by RPA.";
RL Nat. Commun. 8:15222-15222(2017).
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 (PubMed:27723720,
CC PubMed:27723717). Thereby, it plays an essential role both in DNA
CC replication and the cellular response to DNA damage (PubMed:9430682).
CC In the cellular response to DNA damage, the RPA complex controls DNA
CC repair and DNA damage checkpoint activation. Through recruitment of
CC ATRIP activates the ATR kinase a master regulator of the DNA damage
CC response (PubMed:24332808). It is required for the recruitment of the
CC DNA double-strand break repair factors RAD51 and RAD52 to chromatin in
CC response to DNA damage (PubMed:17765923). Also recruits to sites of DNA
CC damage proteins like XPA and XPG that are involved in nucleotide
CC excision repair and is required for this mechanism of DNA repair
CC (PubMed:7697716). Also plays a role in base excision repair (BER)
CC probably through interaction with UNG (PubMed:9765279). Also recruits
CC SMARCAL1/HARP, which is involved in replication fork restart, to sites
CC of DNA damage. May also play a role in telomere maintenance
CC (PubMed:17959650). 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:12791985, ECO:0000269|PubMed:17765923,
CC ECO:0000269|PubMed:17959650, ECO:0000269|PubMed:19116208,
CC ECO:0000269|PubMed:19996105, ECO:0000269|PubMed:24332808,
CC ECO:0000269|PubMed:27723717, ECO:0000269|PubMed:27723720,
CC ECO:0000269|PubMed:7697716, ECO:0000269|PubMed:7700386,
CC ECO:0000269|PubMed:9430682, ECO:0000269|PubMed:9765279}.
CC -!- SUBUNIT: Component of the canonical replication protein A complex
CC (RPA), a heterotrimer composed of RPA1, RPA2 and RPA3 (PubMed:27723720,
CC PubMed:27723717). Also a component of the aRPA, the alternative
CC replication protein A complex, a trimeric complex similar to the
CC replication protein A complex/RPA but where RPA1 and RPA3 are
CC associated with RPA4 instead of RPA2 (PubMed:7760808, PubMed:19116208).
CC The DNA-binding activity may reside exclusively on the RPA1 subunit.
CC Interacts with PRPF19; the PRP19-CDC5L complex is recruited to the
CC sites of DNA repair where it ubiquitinates the replication protein A
CC complex (RPA) (PubMed:24332808). Interacts with RIPK1
CC (PubMed:16135809). Interacts with the polymerase alpha subunit
CC POLA1/p180; this interaction stabilizes the replicative complex and
CC reduces the misincorporation rate of DNA polymerase alpha by acting as
CC a fidelity clamp (PubMed:9214288). Interacts with RAD51 and SENP6 to
CC regulate DNA repair (PubMed:20705237). Interacts with HELB; this
CC interaction promotes HELB recruitment to chromatin following DNA damage
CC (PubMed:22194613, PubMed:26774285). Interacts with PRIMPOL; leading to
CC recruit PRIMPOL on chromatin and stimulate its DNA primase activity
CC (PubMed:24126761, PubMed:25550423, PubMed:28534480). Interacts with
CC XPA; the interaction is direct and associates XPA with the RPA complex
CC (PubMed:7700386, PubMed:9699634, PubMed:10563794). Interacts with
CC ETAA1; the interaction is direct and promotes ETAA1 recruitment at
CC stalled replication forks (PubMed:27601467, PubMed:27723720,
CC PubMed:27723717). Interacts with RPA1; this interaction associates HROB
CC with the RPA complex (By similarity). {ECO:0000250|UniProtKB:Q8VEE4,
CC ECO:0000269|PubMed:10563794, ECO:0000269|PubMed:16135809,
CC ECO:0000269|PubMed:19116208, ECO:0000269|PubMed:20705237,
CC ECO:0000269|PubMed:22194613, ECO:0000269|PubMed:24126761,
CC ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:25550423,
CC ECO:0000269|PubMed:26774285, ECO:0000269|PubMed:27601467,
CC ECO:0000269|PubMed:27723717, ECO:0000269|PubMed:27723720,
CC ECO:0000269|PubMed:28534480, ECO:0000269|PubMed:7700386,
CC ECO:0000269|PubMed:7760808, ECO:0000269|PubMed:9214288,
CC ECO:0000269|PubMed:9699634}.
CC -!- INTERACTION:
CC P27694; P54132: BLM; NbExp=4; IntAct=EBI-621389, EBI-621372;
CC P27694; P17066: HSPA6; NbExp=3; IntAct=EBI-621389, EBI-355106;
CC P27694; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-621389, EBI-742948;
CC P27694; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-621389, EBI-11522433;
CC P27694; P09884: POLA1; NbExp=2; IntAct=EBI-621389, EBI-850026;
CC P27694; Q96LW4: PRIMPOL; NbExp=7; IntAct=EBI-621389, EBI-10044038;
CC P27694; P15927: RPA2; NbExp=15; IntAct=EBI-621389, EBI-621404;
CC P27694; P35244: RPA3; NbExp=11; IntAct=EBI-621389, EBI-621428;
CC P27694; Q13156: RPA4; NbExp=6; IntAct=EBI-621389, EBI-2856301;
CC P27694; Q14191: WRN; NbExp=9; IntAct=EBI-621389, EBI-368417;
CC P27694; P03070; Xeno; NbExp=3; IntAct=EBI-621389, EBI-617698;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17959650}. Nucleus,
CC PML body {ECO:0000269|PubMed:17959650}. Note=Enriched in PML bodies in
CC cells displaying alternative lengthening of their telomeres.
CC {ECO:0000269|PubMed:17959650}.
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 -!- PTM: Sumoylated on lysine residues Lys-449 and Lys-577, with Lys-449
CC being the major site. Sumoylation promotes recruitment of RAD51 to the
CC DNA damage foci to initiate DNA repair through homologous
CC recombination. Desumoylated by SENP6. {ECO:0000269|PubMed:20705237}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92969.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rpa1/";
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DR EMBL; M63488; AAA36584.1; -; mRNA.
DR EMBL; AK289704; BAF82393.1; -; mRNA.
DR EMBL; AB209732; BAD92969.1; ALT_INIT; mRNA.
DR EMBL; AY599563; AAS94324.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90574.1; -; Genomic_DNA.
DR EMBL; BC018126; AAH18126.1; -; mRNA.
DR CCDS; CCDS11014.1; -.
DR PIR; A40457; A40457.
DR RefSeq; NP_002936.1; NM_002945.3.
DR PDB; 1EWI; NMR; -; A=1-114.
DR PDB; 1FGU; X-ray; 2.50 A; A/B=182-432.
DR PDB; 1JMC; X-ray; 2.40 A; A=181-422.
DR PDB; 1L1O; X-ray; 2.80 A; C/F=436-616.
DR PDB; 2B29; X-ray; 1.60 A; A=1-120.
DR PDB; 2B3G; X-ray; 1.60 A; A=1-120.
DR PDB; 4IJH; X-ray; 1.50 A; A=1-120.
DR PDB; 4IJL; X-ray; 1.70 A; A=1-120.
DR PDB; 4IPC; X-ray; 1.22 A; A=1-120.
DR PDB; 4IPD; X-ray; 1.51 A; A=1-120.
DR PDB; 4IPG; X-ray; 1.58 A; A=1-120.
DR PDB; 4IPH; X-ray; 1.94 A; A=1-120.
DR PDB; 4LUO; X-ray; 1.54 A; A=1-120.
DR PDB; 4LUV; X-ray; 1.40 A; A=1-120.
DR PDB; 4LUZ; X-ray; 1.90 A; A=1-120.
DR PDB; 4LW1; X-ray; 1.63 A; A=1-120.
DR PDB; 4LWC; X-ray; 1.61 A; A=1-120.
DR PDB; 4NB3; X-ray; 1.35 A; A/B=1-120.
DR PDB; 4O0A; X-ray; 1.20 A; A=1-120.
DR PDB; 4R4C; X-ray; 1.40 A; A=1-120.
DR PDB; 4R4I; X-ray; 1.40 A; A=1-120.
DR PDB; 4R4O; X-ray; 1.33 A; A=1-120.
DR PDB; 4R4Q; X-ray; 1.35 A; A=1-120.
DR PDB; 4R4T; X-ray; 1.28 A; A=1-120.
DR PDB; 5E7N; X-ray; 1.21 A; A=1-120.
DR PDB; 5EAY; X-ray; 1.55 A; A/B/C/D=3-120.
DR PDB; 5N85; X-ray; 2.00 A; A=1-120.
DR PDB; 5N8A; X-ray; 1.28 A; A=1-120.
DR PDBsum; 1EWI; -.
DR PDBsum; 1FGU; -.
DR PDBsum; 1JMC; -.
DR PDBsum; 1L1O; -.
DR PDBsum; 2B29; -.
DR PDBsum; 2B3G; -.
DR PDBsum; 4IJH; -.
DR PDBsum; 4IJL; -.
DR PDBsum; 4IPC; -.
DR PDBsum; 4IPD; -.
DR PDBsum; 4IPG; -.
DR PDBsum; 4IPH; -.
DR PDBsum; 4LUO; -.
DR PDBsum; 4LUV; -.
DR PDBsum; 4LUZ; -.
DR PDBsum; 4LW1; -.
DR PDBsum; 4LWC; -.
DR PDBsum; 4NB3; -.
DR PDBsum; 4O0A; -.
DR PDBsum; 4R4C; -.
DR PDBsum; 4R4I; -.
DR PDBsum; 4R4O; -.
DR PDBsum; 4R4Q; -.
DR PDBsum; 4R4T; -.
DR PDBsum; 5E7N; -.
DR PDBsum; 5EAY; -.
DR PDBsum; 5N85; -.
DR PDBsum; 5N8A; -.
DR AlphaFoldDB; P27694; -.
DR BMRB; P27694; -.
DR SASBDB; P27694; -.
DR SMR; P27694; -.
DR BioGRID; 112037; 587.
DR ComplexPortal; CPX-1878; Replication protein A complex, RPA2 variant.
DR ComplexPortal; CPX-1879; Replication protein A complex, RPA4 variant.
DR CORUM; P27694; -.
DR DIP; DIP-24189N; -.
DR IntAct; P27694; 103.
DR MINT; P27694; -.
DR STRING; 9606.ENSP00000254719; -.
DR BindingDB; P27694; -.
DR ChEMBL; CHEMBL1764940; -.
DR GlyGen; P27694; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P27694; -.
DR MetOSite; P27694; -.
DR PhosphoSitePlus; P27694; -.
DR SwissPalm; P27694; -.
DR BioMuta; RPA1; -.
DR DMDM; 1350579; -.
DR EPD; P27694; -.
DR jPOST; P27694; -.
DR MassIVE; P27694; -.
DR MaxQB; P27694; -.
DR PaxDb; P27694; -.
DR PeptideAtlas; P27694; -.
DR PRIDE; P27694; -.
DR ProteomicsDB; 54405; -.
DR Antibodypedia; 1868; 491 antibodies from 41 providers.
DR CPTC; P27694; 1 antibody.
DR DNASU; 6117; -.
DR Ensembl; ENST00000254719.10; ENSP00000254719.4; ENSG00000132383.12.
DR GeneID; 6117; -.
DR KEGG; hsa:6117; -.
DR MANE-Select; ENST00000254719.10; ENSP00000254719.4; NM_002945.5; NP_002936.1.
DR UCSC; uc002fto.3; human.
DR CTD; 6117; -.
DR DisGeNET; 6117; -.
DR GeneCards; RPA1; -.
DR GeneReviews; RPA1; -.
DR HGNC; HGNC:10289; RPA1.
DR HPA; ENSG00000132383; Low tissue specificity.
DR MIM; 179835; gene.
DR neXtProt; NX_P27694; -.
DR OpenTargets; ENSG00000132383; -.
DR PharmGKB; PA34651; -.
DR VEuPathDB; HostDB:ENSG00000132383; -.
DR eggNOG; KOG0851; Eukaryota.
DR GeneTree; ENSGT00390000012403; -.
DR HOGENOM; CLU_012393_2_1_1; -.
DR InParanoid; P27694; -.
DR OMA; VRVTIWG; -.
DR OrthoDB; 1189265at2759; -.
DR PhylomeDB; P27694; -.
DR TreeFam; TF105241; -.
DR PathwayCommons; P27694; -.
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-3108214; SUMOylation of DNA damage response and repair proteins.
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; P27694; -.
DR SIGNOR; P27694; -.
DR BioGRID-ORCS; 6117; 806 hits in 1085 CRISPR screens.
DR ChiTaRS; RPA1; human.
DR EvolutionaryTrace; P27694; -.
DR GeneWiki; Replication_protein_A1; -.
DR GenomeRNAi; 6117; -.
DR Pharos; P27694; Tchem.
DR PRO; PR:P27694; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P27694; protein.
DR Bgee; ENSG00000132383; Expressed in secondary oocyte and 204 other tissues.
DR ExpressionAtlas; P27694; baseline and differential.
DR Genevisible; P27694; HS.
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:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:MGI.
DR GO; GO:0090734; C:site of DNA damage; IMP:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0006284; P:base-excision repair; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; TAS:ProtInc.
DR GO; GO:0006281; P:DNA repair; IDA:ComplexPortal.
DR GO; GO:0006260; P:DNA replication; IMP:UniProtKB.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; TAS:ProtInc.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; 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:0000723; P:telomere maintenance; IMP:UniProtKB.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
DR CDD; cd04476; RPA1_DBD_C; 1.
DR CDD; cd04477; RPA1N; 1.
DR Gene3D; 2.40.50.140; -; 4.
DR IDEAL; IID00036; -.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR013955; Rep_factor-A_C.
DR InterPro; IPR007199; Rep_factor-A_N.
DR InterPro; IPR031657; REPA_OB_2.
DR InterPro; IPR004591; Rfa1.
DR PANTHER; PTHR23273; PTHR23273; 1.
DR Pfam; PF04057; Rep-A_N; 1.
DR Pfam; PF08646; Rep_fac-A_C; 1.
DR Pfam; PF16900; REPA_OB_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SUPFAM; SSF50249; SSF50249; 4.
DR TIGRFAMs; TIGR00617; rpa1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; DNA damage;
KW DNA recombination; DNA repair; DNA replication; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..616
FT /note="Replication protein A 70 kDa DNA-binding subunit"
FT /id="PRO_0000423231"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|Ref.8"
FT CHAIN 2..616
FT /note="Replication protein A 70 kDa DNA-binding subunit, N-
FT terminally processed"
FT /id="PRO_0000097260"
FT DNA_BIND 197..281
FT /note="OB"
FT ZN_FING 481..503
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 121..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 163
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 167
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 191
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 259
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 22
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 CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:26474068"
FT CROSSLNK 167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:26474068"
FT CROSSLNK 183
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26474068"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26474068"
FT CROSSLNK 244
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26474068"
FT CROSSLNK 259
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:26474068"
FT CROSSLNK 267
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26474068"
FT CROSSLNK 331
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26474068"
FT CROSSLNK 410
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26474068"
FT CROSSLNK 431
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26474068"
FT CROSSLNK 449
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:20705237"
FT CROSSLNK 458
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26474068"
FT CROSSLNK 553
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26474068"
FT CROSSLNK 577
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:20705237"
FT VARIANT 351
FT /note="T -> A (in dbSNP:rs5030755)"
FT /evidence="ECO:0000269|Ref.4, ECO:0000269|Ref.5"
FT /id="VAR_019236"
FT MUTAGEN 41
FT /note="R->E: Loss of HELB-binding; when associated with E-
FT 43."
FT /evidence="ECO:0000269|PubMed:22194613"
FT MUTAGEN 43
FT /note="R->E: Loss of HELB-binding; when associated with E-
FT 41."
FT /evidence="ECO:0000269|PubMed:22194613"
FT MUTAGEN 449
FT /note="K->R: Significant reduction of sumoylation. Loss of
FT sumoylation; when associated with R-577."
FT /evidence="ECO:0000269|PubMed:20705237"
FT MUTAGEN 500
FT /note="C->S: Loss of function in DNA replication and
FT mismatch repair without effect on DNA-binding activity;
FT when associated with S-503."
FT /evidence="ECO:0000269|PubMed:9430682"
FT MUTAGEN 503
FT /note="C->S: Loss of function in DNA replication and
FT mismatch repair without effect on DNA-binding activity;
FT when associated with S-500."
FT /evidence="ECO:0000269|PubMed:9430682"
FT MUTAGEN 577
FT /note="K->R: Slight sumoylation decrease. Loss of
FT sumoylation; when associated with R-449."
FT /evidence="ECO:0000269|PubMed:20705237"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:4O0A"
FT HELIX 9..14
FT /evidence="ECO:0007829|PDB:4O0A"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:1EWI"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1EWI"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:4O0A"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:4O0A"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:4O0A"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:4O0A"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4O0A"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:4O0A"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:1EWI"
FT STRAND 76..86
FT /evidence="ECO:0007829|PDB:4O0A"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2B29"
FT STRAND 92..103
FT /evidence="ECO:0007829|PDB:4O0A"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:4O0A"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1JMC"
FT STRAND 198..206
FT /evidence="ECO:0007829|PDB:1JMC"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:1JMC"
FT STRAND 218..227
FT /evidence="ECO:0007829|PDB:1JMC"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:1JMC"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:1JMC"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:1JMC"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:1JMC"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:1JMC"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:1JMC"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:1JMC"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:1JMC"
FT HELIX 305..310
FT /evidence="ECO:0007829|PDB:1JMC"
FT STRAND 316..326
FT /evidence="ECO:0007829|PDB:1JMC"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:1JMC"
FT TURN 335..338
FT /evidence="ECO:0007829|PDB:1JMC"
FT STRAND 339..349
FT /evidence="ECO:0007829|PDB:1JMC"
FT STRAND 355..361
FT /evidence="ECO:0007829|PDB:1JMC"
FT HELIX 362..367
FT /evidence="ECO:0007829|PDB:1JMC"
FT STRAND 375..384
FT /evidence="ECO:0007829|PDB:1JMC"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:1JMC"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:1JMC"
FT HELIX 406..416
FT /evidence="ECO:0007829|PDB:1JMC"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:1JMC"
FT HELIX 445..451
FT /evidence="ECO:0007829|PDB:1L1O"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:1L1O"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:1L1O"
FT STRAND 460..471
FT /evidence="ECO:0007829|PDB:1L1O"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:1L1O"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:1L1O"
FT TURN 494..496
FT /evidence="ECO:0007829|PDB:1L1O"
FT STRAND 497..500
FT /evidence="ECO:0007829|PDB:1L1O"
FT TURN 501..504
FT /evidence="ECO:0007829|PDB:1L1O"
FT STRAND 505..509
FT /evidence="ECO:0007829|PDB:1L1O"
FT STRAND 512..521
FT /evidence="ECO:0007829|PDB:1L1O"
FT STRAND 526..532
FT /evidence="ECO:0007829|PDB:1L1O"
FT HELIX 533..540
FT /evidence="ECO:0007829|PDB:1L1O"
FT HELIX 544..550
FT /evidence="ECO:0007829|PDB:1L1O"
FT HELIX 555..564
FT /evidence="ECO:0007829|PDB:1L1O"
FT TURN 565..567
FT /evidence="ECO:0007829|PDB:1L1O"
FT STRAND 569..577
FT /evidence="ECO:0007829|PDB:1L1O"
FT STRAND 588..596
FT /evidence="ECO:0007829|PDB:1L1O"
FT HELIX 599..615
FT /evidence="ECO:0007829|PDB:1L1O"
SQ SEQUENCE 616 AA; 68138 MW; FE038F40F5886CD1 CRC64;
MVGQLSEGAI AAIMQKGDTN IKPILQVINI RPITTGNSPP RYRLLMSDGL NTLSSFMLAT
QLNPLVEEEQ LSSNCVCQIH RFIVNTLKDG RRVVILMELE VLKSAEAVGV KIGNPVPYNE
GLGQPQVAPP APAASPAASS RPQPQNGSSG MGSTVSKAYG ASKTFGKAAG PSLSHTSGGT
QSKVVPIASL TPYQSKWTIC ARVTNKSQIR TWSNSRGEGK LFSLELVDES GEIRATAFNE
QVDKFFPLIE VNKVYYFSKG TLKIANKQFT AVKNDYEMTF NNETSVMPCE DDHHLPTVQF
DFTGIDDLEN KSKDSLVDII GICKSYEDAT KITVRSNNRE VAKRNIYLMD TSGKVVTATL
WGEDADKFDG SRQPVLAIKG ARVSDFGGRS LSVLSSSTII ANPDIPEAYK LRGWFDAEGQ
ALDGVSISDL KSGGVGGSNT NWKTLYEVKS ENLGQGDKPD YFSSVATVVY LRKENCMYQA
CPTQDCNKKV IDQQNGLYRC EKCDTEFPNF KYRMILSVNI ADFQENQWVT CFQESAEAIL
GQNAAYLGEL KDKNEQAFEE VFQNANFRSF IFRVRVKVET YNDESRIKAT VMDVKPVDYR
EYGRRLVMSI RRSALM
