ID XRCC1_HUMAN Reviewed; 633 AA. AC P18887; Q6IBS4; Q9HCB1; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 23-FEB-2022, sequence version 3. DT 27-MAR-2024, entry version 231. DE RecName: Full=DNA repair protein XRCC1 {ECO:0000305}; DE AltName: Full=X-ray repair cross-complementing protein 1; GN Name=XRCC1 {ECO:0000303|PubMed:2247054, ECO:0000312|HGNC:HGNC:12828}; 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 VARIANT ARG-399. RX PubMed=2247054; DOI=10.1128/mcb.10.12.6160-6171.1990; RA Thompson L.H., Brookman K.W., Jones N.J., Allen S.A., Carrano A.V.; RT "Molecular cloning of the human XRCC1 gene, which corrects defective DNA RT strand break repair and sister chromatid exchange."; RL Mol. Cell. Biol. 10:6160-6171(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-72; LEU-161; TRP-194; RP HIS-280; ALA-304; SER-309; ARG-399 AND SER-576. RG NIEHS SNPs program; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-576. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; 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. RX PubMed=11163244; DOI=10.1016/s0092-8674(01)00195-7; RA Whitehouse C.J., Taylor R.M., Thistlethwaite A., Zhang H., RA Karimi-Busheri F., Lasko D.D., Weinfeld M., Caldecott K.W.; RT "XRCC1 stimulates human polynucleotide kinase activity at damaged DNA RT termini and accelerates DNA single-strand break repair."; RL Cell 104:107-117(2001). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 360-LEU-ILE-361; TRP-385 RP AND CYS-389. RX PubMed=14500814; DOI=10.1093/nar/gkg761; RA El-Khamisy S.F., Masutani M., Suzuki H., Caldecott K.W.; RT "A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear RT foci at sites of oxidative DNA damage."; RL Nucleic Acids Res. 31:5526-5533(2003). RN [8] RP INTERACTION WITH APTX. RX PubMed=14755728; DOI=10.1002/ana.10808; RA Sano Y., Date H., Igarashi S., Onodera O., Oyake M., Takahashi T., RA Hayashi S., Morimatsu M., Takahashi H., Makifuchi T., Fukuhara N., RA Tsuji S.; RT "Aprataxin, the causative protein for EAOH is a nuclear protein with a RT potential role as a DNA repair protein."; RL Ann. Neurol. 55:241-249(2004). RN [9] RP PHOSPHORYLATION AT SER-485 AND THR-488, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=15066279; DOI=10.1016/s0092-8674(04)00206-5; RA Loizou J.I., El-Khamisy S.F., Zlatanou A., Moore D.J., Chan D.W., Qin J., RA Sarno S., Meggio F., Pinna L.A., Caldecott K.W.; RT "The protein kinase CK2 facilitates repair of chromosomal DNA single-strand RT breaks."; RL Cell 117:17-28(2004). RN [10] RP INTERACTION WITH APTX, AND PHOSPHORYLATION. RX PubMed=15380105; DOI=10.1016/j.dnarep.2004.06.017; RA Clements P.M., Breslin C., Deeks E.D., Byrd P.J., Ju L., Bieganowski P., RA Brenner C., Moreira M.-C., Taylor A.M.R., Caldecott K.W.; RT "The ataxia-oculomotor apraxia 1 gene product has a role distinct from ATM RT and interacts with the DNA strand break repair proteins XRCC1 and XRCC4."; RL DNA Repair 3:1493-1502(2004). RN [11] RP INTERACTION WITH APTX. RX PubMed=15044383; DOI=10.1093/hmg/ddh122; RA Gueven N., Becherel O.J., Kijas A.W., Chen P., Howe O., Rudolph J.H., RA Gatti R., Date H., Onodera O., Taucher-Scholz G., Lavin M.F.; RT "Aprataxin, a novel protein that protects against genotoxic stress."; RL Hum. Mol. Genet. 13:1081-1093(2004). RN [12] RP SUMOYLATION. RX PubMed=15561718; DOI=10.1074/jbc.m411718200; RA Gocke C.B., Yu H., Kang J.; RT "Systematic identification and analysis of mammalian small ubiquitin-like RT modifier substrates."; RL J. Biol. Chem. 280:5004-5012(2005). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [14] RP SUBUNIT, AND PHOSPHORYLATION AT SER-371. RX PubMed=16397295; DOI=10.1093/nar/gkj409; RA Levy N., Martz A., Bresson A., Spenlehauer C., de Murcia G., RA Menissier-de Murcia J.; RT "XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA RT damage."; RL Nucleic Acids Res. 34:32-41(2006). RN [15] RP INTERACTION WITH APLF. RX PubMed=17507382; DOI=10.1074/jbc.c700060200; RA Bekker-Jensen S., Fugger K., Danielsen J.R., Gromova I., Sehested M., RA Celis J., Bartek J., Lukas J., Mailand N.; RT "Human Xip1 (C2orf13) is a novel regulator of cellular responses to DNA RT strand breaks."; RL J. Biol. Chem. 282:19638-19643(2007). RN [16] RP INTERACTION WITH APLF, PHOSPHORYLATION, AND SUBCELLULAR LOCATION. RX PubMed=17353262; DOI=10.1128/mcb.02269-06; RA Iles N., Rulten S., El-Khamisy S.F., Caldecott K.W.; RT "APLF (C2orf13) is a novel human protein involved in the cellular response RT to chromosomal DNA strand breaks."; RL Mol. Cell. Biol. 27:3793-3803(2007). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-241; THR-257; RP SER-259; SER-408; SER-409; SER-410 AND THR-453, AND IDENTIFICATION BY MASS RP 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 [18] RP IDENTIFICATION BY MASS 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 [19] RP INTERACTION WITH POLB. RX PubMed=19336415; DOI=10.1093/nar/gkp201; RA Guo Z., Zheng L., Dai H., Zhou M., Xu H., Shen B.; RT "Human DNA polymerase beta polymorphism, Arg137Gln, impairs its polymerase RT activity and interaction with PCNA and the cellular base excision repair RT capacity."; RL Nucleic Acids Res. 37:3431-3441(2009). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-198; SER-199; SER-226; RP SER-241; THR-453; SER-461; SER-485 AND THR-488, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [21] RP INTERACTION WITH APEX1. RX PubMed=19934257; DOI=10.1093/nar/gkp1039; RA Yamamori T., DeRicco J., Naqvi A., Hoffman T.A., Mattagajasingh I., RA Kasuno K., Jung S.B., Kim C.S., Irani K.; RT "SIRT1 deacetylates APE1 and regulates cellular base excision repair."; RL Nucleic Acids Res. 38:832-845(2010). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; THR-202; SER-204; RP SER-241 AND THR-257, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; THR-453 AND THR-457, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-241; SER-266; RP THR-281; SER-447; THR-453 AND THR-457, AND IDENTIFICATION BY MASS RP 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 [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446; SER-447; THR-453; RP THR-457 AND SER-461, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [26] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-176, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [27] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-176, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [28] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-176, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [29] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-176, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [30] RP FUNCTION. RX PubMed=34102106; DOI=10.1016/j.molcel.2021.05.009; RA Demin A.A., Hirota K., Tsuda M., Adamowicz M., Hailstone R., Brazina J., RA Gittens W., Kalasova I., Shao Z., Zha S., Sasanuma H., Hanzlikova H., RA Takeda S., Caldecott K.W.; RT "XRCC1 prevents toxic PARP1 trapping during DNA base excision repair."; RL Mol. Cell 81:3018-3030(2021). RN [31] RP FUNCTION, INTERACTION WITH PARP1, AND MUTAGENESIS OF ARG-335 AND LYS-369. RX PubMed=34811483; DOI=10.1038/s41556-021-00792-w; RA Adamowicz M., Hailstone R., Demin A.A., Komulainen E., Hanzlikova H., RA Brazina J., Gautam A., Wells S.E., Caldecott K.W.; RT "XRCC1 protects transcription from toxic PARP1 activity during DNA base RT excision repair."; RL Nat. Cell Biol. 23:1287-1298(2021). RN [32] RP STRUCTURE BY NMR OF 306-422. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the first BRCT domain of DNA-repair protein XRCC1."; RL Submitted (JUN-2006) to the PDB data bank. RN [33] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 515-522 IN COMPLEX WITH PNKP, AND RP PHOSPHORYLATION AT SER-518; THR-519 AND THR-523. RX PubMed=19155274; DOI=10.1093/nar/gkn1086; RA Ali A.A., Jukes R.M., Pearl L.H., Oliver A.W.; RT "Specific recognition of a multiply phosphorylated motif in the DNA repair RT scaffold XRCC1 by the FHA domain of human PNK."; RL Nucleic Acids Res. 37:1701-1712(2009). RN [34] RP VARIANTS TRP-194; HIS-280 AND ARG-399. RX PubMed=9485007; RA Shen M.R., Jones I.M., Mohrenweiser H.; RT "Nonconservative amino acid substitution variants exist at polymorphic RT frequency in DNA repair genes in healthy humans."; RL Cancer Res. 58:604-608(1998). RN [35] RP VARIANT ARG-399. RX PubMed=10783319; DOI=10.1093/carcin/21.5.965; RA Duell E.J., Wiencke J.K., Cheng T.J., Varkonyi A., Zuo Z.F., Ashok T.D., RA Mark E.J., Wain J.C., Christiani D.C., Kelsey K.T.; RT "Polymorphisms in the DNA repair genes XRCC1 and ERCC2 and biomarkers of RT DNA damage in human blood mononuclear cells."; RL Carcinogenesis 21:965-971(2000). RN [36] RP VARIANT ARG-399. RX PubMed=11782372; RA Nelson H.H., Kelsey K.T., Mott L.A., Karagas M.R.; RT "The XRCC1 Arg399Gln polymorphism, sunburn, and non-melanoma skin cancer: RT evidence of gene-environment interaction."; RL Cancer Res. 62:152-155(2002). RN [37] RP VARIANT [LARGE SCALE ANALYSIS] TRP-350. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [38] RP INVOLVEMENT IN SCAR26, VARIANTS SCAR26 ASN-431 AND 465-GLN--ALA-633 DEL, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=28002403; DOI=10.1038/nature20790; RG Care4Rare Canada Consortium; RA Hoch N.C., Hanzlikova H., Rulten S.L., Tetreault M., Komulainen E., Ju L., RA Hornyak P., Zeng Z., Gittens W., Rey S.A., Staras K., Mancini G.M., RA McKinnon P.J., Wang Z.Q., Wagner J.D., Yoon G., Caldecott K.W.; RT "XRCC1 mutation is associated with PARP1 hyperactivation and cerebellar RT ataxia."; RL Nature 541:87-91(2017). RN [39] 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). CC -!- FUNCTION: Scaffold protein involved in DNA single-strand break repair CC by mediating the assembly of DNA break repair protein complexes CC (PubMed:11163244, PubMed:28002403). Negatively regulates ADP- CC ribosyltransferase activity of PARP1 during base-excision repair in CC order to prevent excessive PARP1 activity (PubMed:34102106, CC PubMed:34811483, PubMed:28002403). Recognizes and binds poly-ADP-ribose CC chains: specifically binds auto-poly-ADP-ribosylated PARP1, limiting CC its activity (PubMed:14500814, PubMed:34102106, PubMed:34811483). CC {ECO:0000269|PubMed:11163244, ECO:0000269|PubMed:14500814, CC ECO:0000269|PubMed:28002403, ECO:0000269|PubMed:34102106, CC ECO:0000269|PubMed:34811483}. CC -!- SUBUNIT: Homodimer (PubMed:16397295). Interacts with polynucleotide CC kinase (PNK), DNA polymerase-beta (POLB) and DNA ligase III (LIG3) CC (PubMed:19336415, PubMed:19155274). Interacts with APTX and APLF CC (PubMed:14755728, PubMed:15044383, PubMed:15380105, PubMed:17507382, CC PubMed:17353262). Interacts with APEX1; the interaction is induced by CC SIRT1 and increases with the acetylated form of APEX1 CC (PubMed:19934257). Interacts with (poly-ADP-ribosylated) PARP1 CC (PubMed:34811483). {ECO:0000269|PubMed:14755728, CC ECO:0000269|PubMed:15044383, ECO:0000269|PubMed:15380105, CC ECO:0000269|PubMed:16397295, ECO:0000269|PubMed:17353262, CC ECO:0000269|PubMed:17507382, ECO:0000269|PubMed:19155274, CC ECO:0000269|PubMed:19336415, ECO:0000269|PubMed:19934257, CC ECO:0000269|PubMed:34811483}. CC -!- INTERACTION: CC P18887; Q8IW19: APLF; NbExp=11; IntAct=EBI-947466, EBI-1256044; CC P18887; Q7Z2E3: APTX; NbExp=11; IntAct=EBI-947466, EBI-847814; CC P18887; O96017: CHEK2; NbExp=8; IntAct=EBI-947466, EBI-1180783; CC P18887; P61244: MAX; NbExp=2; IntAct=EBI-947466, EBI-751711; CC P18887; P09874: PARP1; NbExp=6; IntAct=EBI-947466, EBI-355676; CC P18887; Q96T60: PNKP; NbExp=6; IntAct=EBI-947466, EBI-1045072; CC P18887; P06746: POLB; NbExp=3; IntAct=EBI-947466, EBI-713836; CC P18887; Q9UNA4: POLI; NbExp=2; IntAct=EBI-947466, EBI-741774; CC P18887; Q9NUW8: TDP1; NbExp=2; IntAct=EBI-947466, EBI-2902553; CC P18887; P06766: Polb; Xeno; NbExp=4; IntAct=EBI-947466, EBI-15845002; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17353262, CC ECO:0000269|PubMed:28002403}. Chromosome {ECO:0000269|PubMed:14500814}. CC Note=Moves from the nucleoli to the global nuclear chromatin upon DNA CC damage (PubMed:28002403). Recruited to DNA damage sites fowwing CC interaction with poly-ADP-ribose chains (PubMed:14500814). CC {ECO:0000269|PubMed:14500814, ECO:0000269|PubMed:28002403}. CC -!- TISSUE SPECIFICITY: Expressed in fibroblasts, retinal pigmented CC epithelial cells and lymphoblastoid cells (at protein level). CC {ECO:0000269|PubMed:28002403}. CC -!- PTM: Phosphorylation of Ser-371 causes dimer dissociation. CC Phosphorylation by CK2 promotes interaction with APTX and APLF. CC {ECO:0000269|PubMed:15066279, ECO:0000269|PubMed:15380105, CC ECO:0000269|PubMed:16397295, ECO:0000269|PubMed:17353262, CC ECO:0000269|PubMed:19155274}. CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}. CC -!- POLYMORPHISM: Carriers of the polymorphic Gln-399 allele may be at CC greater risk for tobacco- and age-related DNA damage. CC -!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 26 (SCAR26) CC [MIM:617633]: A form of spinocerebellar ataxia, a clinically and CC genetically heterogeneous group of cerebellar disorders due to CC degeneration of the cerebellum with variable involvement of the CC brainstem and spinal cord. SCAR26 is a progressive disease CC characterized by gait and limb ataxia, loss of independent ambulation, CC oculomotor apraxia, and peripheral neuropathy with distal muscle CC weakness and areflexia. {ECO:0000269|PubMed:28002403}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/xrcc1/"; 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; M36089; AAA63270.1; -; mRNA. DR EMBL; AF512504; AAM34791.1; -; Genomic_DNA. DR EMBL; CR456728; CAG33009.1; -; mRNA. DR EMBL; AC018758; AAG09061.1; -; Genomic_DNA. DR EMBL; KC877750; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L34079; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC023593; AAH23593.1; -; mRNA. DR CCDS; CCDS12624.1; -. DR PIR; A36353; A36353. DR RefSeq; NP_006288.2; NM_006297.2. DR PDB; 1CDZ; X-ray; 3.20 A; A=538-633. DR PDB; 1XNA; NMR; -; A=1-183. DR PDB; 1XNT; NMR; -; A=1-183. DR PDB; 2D8M; NMR; -; A=305-420. DR PDB; 2W3O; X-ray; 1.85 A; C/D=515-522. DR PDB; 3K75; X-ray; 2.95 A; B/C=1-183. DR PDB; 3K77; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-155. DR PDB; 3LQC; X-ray; 2.35 A; A=1-183. DR PDB; 5E6Q; X-ray; 2.31 A; A=241-276. DR PDB; 5W7X; X-ray; 2.00 A; E/F/G/H=514-522. DR PDB; 5W7Y; X-ray; 2.10 A; C/D=514-521. DR PDB; 6WH1; X-ray; 2.40 A; A=538-633. DR PDB; 6WH2; X-ray; 2.41 A; A/B=538-633. DR PDBsum; 1CDZ; -. DR PDBsum; 1XNA; -. DR PDBsum; 1XNT; -. DR PDBsum; 2D8M; -. DR PDBsum; 2W3O; -. DR PDBsum; 3K75; -. DR PDBsum; 3K77; -. DR PDBsum; 3LQC; -. DR PDBsum; 5E6Q; -. DR PDBsum; 5W7X; -. DR PDBsum; 5W7Y; -. DR PDBsum; 6WH1; -. DR PDBsum; 6WH2; -. DR AlphaFoldDB; P18887; -. DR BMRB; P18887; -. DR SASBDB; P18887; -. DR SMR; P18887; -. DR BioGRID; 113349; 210. DR ComplexPortal; CPX-793; XRCC1 DNA repair complex. DR CORUM; P18887; -. DR DIP; DIP-39067N; -. DR IntAct; P18887; 73. DR MINT; P18887; -. DR STRING; 9606.ENSP00000262887; -. DR GlyGen; P18887; 6 sites, 2 O-linked glycans (6 sites). DR iPTMnet; P18887; -. DR PhosphoSitePlus; P18887; -. DR BioMuta; XRCC1; -. DR DMDM; 317373290; -. DR EPD; P18887; -. DR jPOST; P18887; -. DR MassIVE; P18887; -. DR MaxQB; P18887; -. DR PaxDb; 9606-ENSP00000262887; -. DR PeptideAtlas; P18887; -. DR ProteomicsDB; 53619; -. DR Pumba; P18887; -. DR Antibodypedia; 1863; 669 antibodies from 44 providers. DR DNASU; 7515; -. DR Ensembl; ENST00000262887.10; ENSP00000262887.5; ENSG00000073050.12. DR GeneID; 7515; -. DR KEGG; hsa:7515; -. DR MANE-Select; ENST00000262887.10; ENSP00000262887.5; NM_006297.3; NP_006288.2. DR UCSC; uc002owt.3; human. DR AGR; HGNC:12828; -. DR CTD; 7515; -. DR DisGeNET; 7515; -. DR GeneCards; XRCC1; -. DR HGNC; HGNC:12828; XRCC1. DR HPA; ENSG00000073050; Low tissue specificity. DR MalaCards; XRCC1; -. DR MIM; 194360; gene. DR MIM; 617633; phenotype. DR neXtProt; NX_P18887; -. DR OpenTargets; ENSG00000073050; -. DR PharmGKB; PA369; -. DR VEuPathDB; HostDB:ENSG00000073050; -. DR eggNOG; KOG3226; Eukaryota. DR GeneTree; ENSGT00390000004140; -. DR HOGENOM; CLU_030026_0_0_1; -. DR InParanoid; P18887; -. DR OMA; PEWIYAI; -. DR OrthoDB; 1334125at2759; -. DR PhylomeDB; P18887; -. DR TreeFam; TF101201; -. DR PathwayCommons; P18887; -. DR Reactome; R-HSA-110381; Resolution of AP sites via the single-nucleotide replacement pathway. DR Reactome; R-HSA-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway. DR Reactome; R-HSA-5685939; HDR through MMEJ (alt-NHEJ). DR Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER. DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER. DR SignaLink; P18887; -. DR SIGNOR; P18887; -. DR BioGRID-ORCS; 7515; 128 hits in 1163 CRISPR screens. DR ChiTaRS; XRCC1; human. DR EvolutionaryTrace; P18887; -. DR GeneWiki; XRCC1; -. DR GenomeRNAi; 7515; -. DR Pharos; P18887; Tbio. DR PRO; PR:P18887; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P18887; Protein. DR Bgee; ENSG00000073050; Expressed in ventricular zone and 204 other cell types or tissues. DR ExpressionAtlas; P18887; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl. DR GO; GO:0070522; C:ERCC4-ERCC1 complex; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0090734; C:site of DNA damage; IDA:UniProtKB. DR GO; GO:1990599; F:3' overhang single-stranded DNA endodeoxyribonuclease activity; IEA:Ensembl. DR GO; GO:0160002; F:ADP-D-ribose modification-dependent protein binding; IDA:UniProt. DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL. DR GO; GO:0032356; F:oxidized DNA binding; IMP:UniProtKB. DR GO; GO:0072572; F:poly-ADP-D-ribose binding; IDA:UniProtKB. DR GO; GO:0006284; P:base-excision repair; IDA:UniProtKB. DR GO; GO:0021587; P:cerebellum morphogenesis; IEA:Ensembl. DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:Ensembl. DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl. DR GO; GO:1905765; P:negative regulation of protection from non-homologous end joining at telomere; IEA:Ensembl. DR GO; GO:0010836; P:negative regulation of protein ADP-ribosylation; IDA:UniProtKB. DR GO; GO:1904877; P:positive regulation of DNA ligase activity; IMP:UniProtKB. DR GO; GO:1903518; P:positive regulation of single strand break repair; IMP:UniProtKB. DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP:UniProtKB. DR GO; GO:0033194; P:response to hydroperoxide; IDA:UniProtKB. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0010033; P:response to organic substance; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0000012; P:single strand break repair; IEA:InterPro. DR GO; GO:0061819; P:telomeric DNA-containing double minutes formation; IEA:Ensembl. DR GO; GO:0050882; P:voluntary musculoskeletal movement; IMP:UniProtKB. DR CDD; cd17725; BRCT_XRCC1_rpt1; 1. DR CDD; cd17707; BRCT_XRCC1_rpt2; 1. DR Gene3D; 3.40.50.10190; BRCT domain; 2. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR036420; BRCT_dom_sf. DR InterPro; IPR045080; BRCT_XRCC1_rpt1. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR002706; Xrcc1_N. DR PANTHER; PTHR11370:SF6; DNA REPAIR PROTEIN XRCC1; 1. DR PANTHER; PTHR11370; DNA-REPAIR PROTEIN XRCC1; 1. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF16589; BRCT_2; 1. DR Pfam; PF01834; XRCC1_N; 1. DR SMART; SM00292; BRCT; 2. DR SUPFAM; SSF52113; BRCT domain; 2. DR SUPFAM; SSF49785; Galactose-binding domain-like; 1. DR PROSITE; PS50172; BRCT; 2. DR Genevisible; P18887; HS. PE 1: Evidence at protein level; KW 3D-structure; Chromosome; DNA damage; DNA repair; Isopeptide bond; KW Neurodegeneration; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Ubl conjugation. FT CHAIN 1..633 FT /note="DNA repair protein XRCC1" FT /id="PRO_0000066044" FT DOMAIN 315..403 FT /note="BRCT 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT DOMAIN 538..629 FT /note="BRCT 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT REGION 221..313 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 400..462 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 471..490 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 498..536 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 221..239 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 240..256 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 263..283 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 428..444 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 140 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 198 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 199 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 202 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 204 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 226 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 241 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 257 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 259 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 266 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 281 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 371 FT /note="Phosphoserine; by PRKDC" FT /evidence="ECO:0000269|PubMed:16397295" FT MOD_RES 408 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 409 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 410 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 421 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 446 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 447 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 453 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 457 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 461 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:24275569" FT MOD_RES 485 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15066279, FT ECO:0007744|PubMed:19690332" FT MOD_RES 488 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:15066279, FT ECO:0007744|PubMed:19690332" FT MOD_RES 518 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19155274" FT MOD_RES 519 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:19155274" FT MOD_RES 523 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:19155274" FT CROSSLNK 176 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 176 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT VARIANT 7 FT /note="R -> L (in dbSNP:rs2307186)" FT /id="VAR_014773" FT VARIANT 10 FT /note="V -> M (in dbSNP:rs2307171)" FT /id="VAR_014774" FT VARIANT 72 FT /note="V -> A (in dbSNP:rs25496)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_016168" FT VARIANT 107 FT /note="R -> H (in dbSNP:rs2228487)" FT /id="VAR_029228" FT VARIANT 157 FT /note="E -> K (in dbSNP:rs2307180)" FT /id="VAR_014775" FT VARIANT 161 FT /note="P -> L (in dbSNP:rs2307191)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_014776" FT VARIANT 194 FT /note="R -> W (in dbSNP:rs1799782)" FT /evidence="ECO:0000269|PubMed:9485007, ECO:0000269|Ref.2" FT /id="VAR_013400" FT VARIANT 280 FT /note="R -> H (in dbSNP:rs25489)" FT /evidence="ECO:0000269|PubMed:9485007, ECO:0000269|Ref.2" FT /id="VAR_013401" FT VARIANT 298 FT /note="K -> N (in dbSNP:rs2307188)" FT /id="VAR_014777" FT VARIANT 304 FT /note="T -> A (in dbSNP:rs25490)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_018775" FT VARIANT 309 FT /note="P -> S (in dbSNP:rs25491)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_014778" FT VARIANT 350 FT /note="R -> W (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs754041352)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036277" FT VARIANT 399 FT /note="Q -> R (in dbSNP:rs25487)" FT /evidence="ECO:0000269|PubMed:10783319, FT ECO:0000269|PubMed:11782372, ECO:0000269|PubMed:2247054, FT ECO:0000269|PubMed:9485007, ECO:0000269|Ref.2" FT /id="VAR_011487" FT VARIANT 431 FT /note="K -> N (in SCAR26; may result in aberrant splicing; FT dbSNP:rs761564262)" FT /evidence="ECO:0000269|PubMed:28002403" FT /id="VAR_079140" FT VARIANT 465..633 FT /note="Missing (in SCAR26)" FT /evidence="ECO:0000269|PubMed:28002403" FT /id="VAR_079141" FT VARIANT 485 FT /note="S -> Y (in dbSNP:rs2307184)" FT /id="VAR_014779" FT VARIANT 514 FT /note="P -> L (in dbSNP:rs25474)" FT /id="VAR_016169" FT VARIANT 559 FT /note="R -> Q (in dbSNP:rs2307167)" FT /id="VAR_014780" FT VARIANT 560 FT /note="R -> W (in dbSNP:rs2307166)" FT /id="VAR_014781" FT VARIANT 576 FT /note="Y -> N (in dbSNP:rs2682557)" FT /evidence="ECO:0000269|PubMed:15057824" FT /id="VAR_061727" FT VARIANT 576 FT /note="Y -> S (in dbSNP:rs2307177)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_014782" FT MUTAGEN 335 FT /note="R->A: Abolished binding to poly-ADP-ribose and FT ability to inhibit PARP1 activity; when associated with FT A-369." FT /evidence="ECO:0000269|PubMed:34811483" FT MUTAGEN 360..361 FT /note="LI->DD: Reduced binding to poly-ADP-ribose nuclear FT foci." FT /evidence="ECO:0000269|PubMed:14500814" FT MUTAGEN 369 FT /note="K->A: Abolished binding to poly-ADP-ribose and FT ability to inhibit PARP1 activity; when associated with FT A-335." FT /evidence="ECO:0000269|PubMed:34811483" FT MUTAGEN 385 FT /note="W->D: Strongly reduced binding to poly-ADP-ribose FT nuclear foci." FT /evidence="ECO:0000269|PubMed:14500814" FT MUTAGEN 389 FT /note="C->A: Reduced binding to poly-ADP-ribose nuclear FT foci." FT /evidence="ECO:0000269|PubMed:14500814" FT HELIX 4..6 FT /evidence="ECO:0007829|PDB:3LQC" FT STRAND 7..12 FT /evidence="ECO:0007829|PDB:3LQC" FT HELIX 17..25 FT /evidence="ECO:0007829|PDB:3LQC" FT HELIX 28..36 FT /evidence="ECO:0007829|PDB:3LQC" FT TURN 37..39 FT /evidence="ECO:0007829|PDB:3LQC" FT STRAND 41..53 FT /evidence="ECO:0007829|PDB:3LQC" FT STRAND 57..64 FT /evidence="ECO:0007829|PDB:3LQC" FT STRAND 66..73 FT /evidence="ECO:0007829|PDB:3LQC" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:1XNA" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:3LQC" FT STRAND 85..93 FT /evidence="ECO:0007829|PDB:3LQC" FT HELIX 96..101 FT /evidence="ECO:0007829|PDB:3LQC" FT STRAND 108..111 FT /evidence="ECO:0007829|PDB:3LQC" FT HELIX 113..115 FT /evidence="ECO:0007829|PDB:3LQC" FT HELIX 118..121 FT /evidence="ECO:0007829|PDB:3LQC" FT STRAND 125..133 FT /evidence="ECO:0007829|PDB:3LQC" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:3K75" FT STRAND 143..150 FT /evidence="ECO:0007829|PDB:3LQC" FT HELIX 313..316 FT /evidence="ECO:0007829|PDB:2D8M" FT TURN 317..319 FT /evidence="ECO:0007829|PDB:2D8M" FT STRAND 323..329 FT /evidence="ECO:0007829|PDB:2D8M" FT HELIX 334..344 FT /evidence="ECO:0007829|PDB:2D8M" FT STRAND 347..352 FT /evidence="ECO:0007829|PDB:2D8M" FT STRAND 359..366 FT /evidence="ECO:0007829|PDB:2D8M" FT HELIX 368..376 FT /evidence="ECO:0007829|PDB:2D8M" FT STRAND 379..382 FT /evidence="ECO:0007829|PDB:2D8M" FT HELIX 384..391 FT /evidence="ECO:0007829|PDB:2D8M" FT HELIX 398..401 FT /evidence="ECO:0007829|PDB:2D8M" FT STRAND 404..407 FT /evidence="ECO:0007829|PDB:2D8M" FT TURN 542..545 FT /evidence="ECO:0007829|PDB:6WH1" FT STRAND 547..550 FT /evidence="ECO:0007829|PDB:6WH1" FT HELIX 558..568 FT /evidence="ECO:0007829|PDB:6WH1" FT STRAND 583..585 FT /evidence="ECO:0007829|PDB:6WH1" FT HELIX 592..600 FT /evidence="ECO:0007829|PDB:6WH1" FT STRAND 605..607 FT /evidence="ECO:0007829|PDB:6WH1" FT HELIX 609..618 FT /evidence="ECO:0007829|PDB:6WH1" FT HELIX 624..627 FT /evidence="ECO:0007829|PDB:6WH1" SQ SEQUENCE 633 AA; 69498 MW; 76174967D034F89F CRC64; MPEIRLRHVV SCSSQDSTHC AENLLKADTY RKWRAAKAGE KTISVVLQLE KEEQIHSVDI GNDGSAFVEV LVGSSAGGAG EQDYEVLLVT SSFMSPSESR SGSNPNRVRM FGPDKLVRAA AEKRWDRVKI VCSQPYSKDS PFGLSFVRFH SPPDKDEAEA PSQKVTVTKL GQFRVKEEDE SANSLRPGAL FFSRINKTSP VTASDPAGPS YAAATLQASS AASSASPVSR AIGSTSKPQE SPKGKRKLDL NQEEKKTPSK PPAQLSPSVP KRPKLPAPTR TPATAPVPAR AQGAVTGKPR GEGTEPRRPR AGPEELGKIL QGVVVVLSGF QNPFRSELRD KALELGAKYR PDWTRDSTHL ICAFANTPKY SQVLGLGGRI VRKEWVLDCH RMRRRLPSQR YLMAGPGSSS EEDEASHSGG SGDEAPKLPQ KQPQTKTKPT QAAGPSSPQK PPTPEETKAA SPVLQEDIDI EGVQSEGQDN GAEDSGDTED ELRRVAEQKE HRLPPGQEEN GEDPYAGSTD ENTDSEEHQE PPDLPVPELP DFFQGKHFFL YGEFPGDERR KLIRYVTAFN GELEDYMSDR VQFVITAQEW DPSFEEALMD NPSLAFVRPR WIYSCNEKQK LLPHQLYGVV PQA //