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DNA repair protein XRCC1 (X-ray repair cross-complementing protein 1)

 XRCC1_HUMAN             Reviewed;         633 AA.
P18887; Q6IBS4; Q9HCB1;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
18-JUL-2018, entry version 199.
RecName: Full=DNA repair protein XRCC1;
AltName: Full=X-ray repair cross-complementing protein 1;
Name=XRCC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT TYR-576.
PubMed=2247054; DOI=10.1128/MCB.10.12.6160;
Thompson L.H., Brookman K.W., Jones N.J., Allen S.A., Carrano A.V.;
"Molecular cloning of the human XRCC1 gene, which corrects defective
DNA strand break repair and sister chromatid exchange.";
Mol. Cell. Biol. 10:6160-6171(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-72; LEU-161;
TRP-194; HIS-280; ALA-304; SER-309; GLN-399 AND SER-576.
NIEHS SNPs program;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLN-399 AND
TYR-576.
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-399.
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLN-399 AND
TYR-576.
TISSUE=Eye;
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]
INTERACTION.
PubMed=11163244; DOI=10.1016/S0092-8674(01)00195-7;
Whitehouse C.J., Taylor R.M., Thistlethwaite A., Zhang H.,
Karimi-Busheri F., Lasko D.D., Weinfeld M., Caldecott K.W.;
"XRCC1 stimulates human polynucleotide kinase activity at damaged DNA
termini and accelerates DNA single-strand break repair.";
Cell 104:107-117(2001).
[7]
INTERACTION WITH APTX.
PubMed=14755728; DOI=10.1002/ana.10808;
Sano Y., Date H., Igarashi S., Onodera O., Oyake M., Takahashi T.,
Hayashi S., Morimatsu M., Takahashi H., Makifuchi T., Fukuhara N.,
Tsuji S.;
"Aprataxin, the causative protein for EAOH is a nuclear protein with a
potential role as a DNA repair protein.";
Ann. Neurol. 55:241-249(2004).
[8]
PHOSPHORYLATION AT SER-485 AND THR-488, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=15066279; DOI=10.1016/S0092-8674(04)00206-5;
Loizou J.I., El-Khamisy S.F., Zlatanou A., Moore D.J., Chan D.W.,
Qin J., Sarno S., Meggio F., Pinna L.A., Caldecott K.W.;
"The protein kinase CK2 facilitates repair of chromosomal DNA single-
strand breaks.";
Cell 117:17-28(2004).
[9]
INTERACTION WITH APTX, AND PHOSPHORYLATION.
PubMed=15380105; DOI=10.1016/j.dnarep.2004.06.017;
Clements P.M., Breslin C., Deeks E.D., Byrd P.J., Ju L.,
Bieganowski P., Brenner C., Moreira M.-C., Taylor A.M.R.,
Caldecott K.W.;
"The ataxia-oculomotor apraxia 1 gene product has a role distinct from
ATM and interacts with the DNA strand break repair proteins XRCC1 and
XRCC4.";
DNA Repair 3:1493-1502(2004).
[10]
INTERACTION WITH APTX.
PubMed=15044383; DOI=10.1093/hmg/ddh122;
Gueven N., Becherel O.J., Kijas A.W., Chen P., Howe O., Rudolph J.H.,
Gatti R., Date H., Onodera O., Taucher-Scholz G., Lavin M.F.;
"Aprataxin, a novel protein that protects against genotoxic stress.";
Hum. Mol. Genet. 13:1081-1093(2004).
[11]
SUMOYLATION.
PubMed=15561718; DOI=10.1074/jbc.M411718200;
Gocke C.B., Yu H., Kang J.;
"Systematic identification and analysis of mammalian small ubiquitin-
like modifier substrates.";
J. Biol. Chem. 280:5004-5012(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[13]
SUBUNIT, AND PHOSPHORYLATION AT SER-371.
PubMed=16397295; DOI=10.1093/nar/gkj409;
Levy N., Martz A., Bresson A., Spenlehauer C., de Murcia G.,
Menissier-de Murcia J.;
"XRCC1 is phosphorylated by DNA-dependent protein kinase in response
to DNA damage.";
Nucleic Acids Res. 34:32-41(2006).
[14]
INTERACTION WITH APLF.
PubMed=17507382; DOI=10.1074/jbc.C700060200;
Bekker-Jensen S., Fugger K., Danielsen J.R., Gromova I., Sehested M.,
Celis J., Bartek J., Lukas J., Mailand N.;
"Human Xip1 (C2orf13) is a novel regulator of cellular responses to
DNA strand breaks.";
J. Biol. Chem. 282:19638-19643(2007).
[15]
INTERACTION WITH APLF, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=17353262; DOI=10.1128/MCB.02269-06;
Iles N., Rulten S., El-Khamisy S.F., Caldecott K.W.;
"APLF (C2orf13) is a novel human protein involved in the cellular
response to chromosomal DNA strand breaks.";
Mol. Cell. Biol. 27:3793-3803(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-241; THR-257;
SER-259; SER-408; SER-409; SER-410 AND THR-453, AND 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).
[17]
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-198; SER-199; SER-226;
SER-241; THR-453; SER-461; SER-485 AND THR-488, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
INTERACTION WITH APEX1.
PubMed=19934257; DOI=10.1093/nar/gkp1039;
Yamamori T., DeRicco J., Naqvi A., Hoffman T.A., Mattagajasingh I.,
Kasuno K., Jung S.B., Kim C.S., Irani K.;
"SIRT1 deacetylates APE1 and regulates cellular base excision
repair.";
Nucleic Acids Res. 38:832-845(2010).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; THR-202; SER-204;
SER-241 AND THR-257, 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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; THR-453 AND
THR-457, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-241; SER-266;
THR-281; SER-447; THR-453 AND THR-457, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446; SER-447; THR-453;
THR-457 AND SER-461, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-176, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-176, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-176, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-176, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[28]
STRUCTURE BY NMR OF 306-422.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the first BRCT domain of DNA-repair protein
XRCC1.";
Submitted (JUN-2006) to the PDB data bank.
[29]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 515-522 IN COMPLEX WITH
PNKP, AND PHOSPHORYLATION AT SER-518; THR-519 AND THR-523.
PubMed=19155274; DOI=10.1093/nar/gkn1086;
Ali A.A., Jukes R.M., Pearl L.H., Oliver A.W.;
"Specific recognition of a multiply phosphorylated motif in the DNA
repair scaffold XRCC1 by the FHA domain of human PNK.";
Nucleic Acids Res. 37:1701-1712(2009).
[30]
VARIANTS TRP-194; HIS-280 AND GLN-399.
PubMed=9485007;
Shen M.R., Jones I.M., Mohrenweiser H.;
"Nonconservative amino acid substitution variants exist at polymorphic
frequency in DNA repair genes in healthy humans.";
Cancer Res. 58:604-608(1998).
[31]
VARIANT GLN-399.
PubMed=10783319; DOI=10.1093/carcin/21.5.965;
Duell E.J., Wiencke J.K., Cheng T.J., Varkonyi A., Zuo Z.F.,
Ashok T.D., Mark E.J., Wain J.C., Christiani D.C., Kelsey K.T.;
"Polymorphisms in the DNA repair genes XRCC1 and ERCC2 and biomarkers
of DNA damage in human blood mononuclear cells.";
Carcinogenesis 21:965-971(2000).
[32]
VARIANT GLN-399.
PubMed=11782372;
Nelson H.H., Kelsey K.T., Mott L.A., Karagas M.R.;
"The XRCC1 Arg399Gln polymorphism, sunburn, and non-melanoma skin
cancer: evidence of gene-environment interaction.";
Cancer Res. 62:152-155(2002).
[33]
VARIANT [LARGE SCALE ANALYSIS] TRP-350.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[34]
INVOLVEMENT IN SCAR26, VARIANTS SCAR26 ASN-431 AND 465-GLN--ALA-633
DEL, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=28002403; DOI=10.1038/nature20790;
Care4Rare Canada Consortium;
Hoch N.C., Hanzlikova H., Rulten S.L., Tetreault M., Komulainen E.,
Ju L., Hornyak P., Zeng Z., Gittens W., Rey S.A., Staras K.,
Mancini G.M., McKinnon P.J., Wang Z.Q., Wagner J.D., Yoon G.,
Caldecott K.W.;
"XRCC1 mutation is associated with PARP1 hyperactivation and
cerebellar ataxia.";
Nature 541:87-91(2017).
[35]
VARIANT [LARGE SCALE ANALYSIS] TYR-576, AND 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).
-!- FUNCTION: Involved in DNA single-strand break repair by mediating
the assembly of DNA break repair protein complexes. Probably
during DNA repair, negatively regulates ADP-ribose levels by
modulating ADP-ribosyltransferase PARP1 activity.
{ECO:0000269|PubMed:28002403}.
-!- SUBUNIT: Homodimer. Interacts with polynucleotide kinase (PNK),
DNA polymerase-beta (POLB) and DNA ligase III (LIG3). Interacts
with APTX and APLF. Interacts with APEX1; the interaction is
induced by SIRT1 and increases with the acetylated form of APEX1.
{ECO:0000269|PubMed:11163244, ECO:0000269|PubMed:14755728,
ECO:0000269|PubMed:15044383, ECO:0000269|PubMed:15380105,
ECO:0000269|PubMed:16397295, ECO:0000269|PubMed:17353262,
ECO:0000269|PubMed:17507382, ECO:0000269|PubMed:19155274,
ECO:0000269|PubMed:19934257}.
-!- INTERACTION:
Q8IW19:APLF; NbExp=10; IntAct=EBI-947466, EBI-1256044;
Q7Z2E3:APTX; NbExp=16; IntAct=EBI-947466, EBI-847814;
O96017:CHEK2; NbExp=8; IntAct=EBI-947466, EBI-1180783;
P03126:E6 (xeno); NbExp=3; IntAct=EBI-947466, EBI-1177242;
P06428:E6 (xeno); NbExp=2; IntAct=EBI-947466, EBI-7463243;
P06929:E6 (xeno); NbExp=2; IntAct=EBI-947466, EBI-7463272;
P49916:LIG3; NbExp=2; IntAct=EBI-947466, EBI-1753381;
P61244:MAX; NbExp=2; IntAct=EBI-947466, EBI-751711;
P09874:PARP1; NbExp=6; IntAct=EBI-947466, EBI-355676;
Q96T60:PNKP; NbExp=8; IntAct=EBI-947466, EBI-1045072;
P06766:Polb (xeno); NbExp=4; IntAct=EBI-947466, EBI-15845002;
Q9UNA4:POLI; NbExp=2; IntAct=EBI-947466, EBI-741774;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17353262,
ECO:0000269|PubMed:28002403}. Note=Moves from the nucleoli to the
global nuclear chromatin upon DNA damage.
{ECO:0000269|PubMed:28002403}.
-!- TISSUE SPECIFICITY: Expressed in fibroblasts, retinal pigmented
epithelial cells and lymphoblastoid cells (at protein level).
{ECO:0000269|PubMed:28002403}.
-!- PTM: Phosphorylation of Ser-371 causes dimer dissociation.
Phosphorylation by CK2 promotes interaction with APTX and APLF.
{ECO:0000269|PubMed:15066279, ECO:0000269|PubMed:15380105,
ECO:0000269|PubMed:16397295, ECO:0000269|PubMed:17353262,
ECO:0000269|PubMed:19155274}.
-!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.
-!- POLYMORPHISM: Carriers of the polymorphic Gln-399 allele may be at
greater risk for tobacco- and age-related DNA damage.
-!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 26 (SCAR26)
[MIM:617633]: A form of spinocerebellar ataxia, a clinically and
genetically heterogeneous group of cerebellar disorders due to
degeneration of the cerebellum with variable involvement of the
brainstem and spinal cord. SCAR26 is a progressive disease
characterized by gait and limb ataxia, loss of independent
ambulation, oculomotor apraxia, and peripheral neuropathy with
distal muscle weakness and areflexia.
{ECO:0000269|PubMed:28002403}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/xrcc1/";
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EMBL; M36089; AAA63270.1; -; mRNA.
EMBL; AF512504; AAM34791.1; -; Genomic_DNA.
EMBL; CR456728; CAG33009.1; -; mRNA.
EMBL; AC018758; AAG09061.1; -; Genomic_DNA.
EMBL; L34079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC023593; AAH23593.1; -; mRNA.
CCDS; CCDS12624.1; -.
PIR; A36353; A36353.
RefSeq; NP_006288.2; NM_006297.2.
UniGene; Hs.98493; -.
PDB; 1CDZ; X-ray; 3.20 A; A=538-633.
PDB; 1XNA; NMR; -; A=1-183.
PDB; 1XNT; NMR; -; A=1-183.
PDB; 2D8M; NMR; -; A=305-420.
PDB; 2W3O; X-ray; 1.85 A; C/D=515-522.
PDB; 3K75; X-ray; 2.95 A; B/C=1-183.
PDB; 3K77; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-155.
PDB; 3LQC; X-ray; 2.35 A; A=1-183.
PDB; 5E6Q; X-ray; 2.31 A; A=241-276.
PDB; 5W7X; X-ray; 2.00 A; E/F/G/H=514-522.
PDB; 5W7Y; X-ray; 2.10 A; C/D=514-521.
PDBsum; 1CDZ; -.
PDBsum; 1XNA; -.
PDBsum; 1XNT; -.
PDBsum; 2D8M; -.
PDBsum; 2W3O; -.
PDBsum; 3K75; -.
PDBsum; 3K77; -.
PDBsum; 3LQC; -.
PDBsum; 5E6Q; -.
PDBsum; 5W7X; -.
PDBsum; 5W7Y; -.
ProteinModelPortal; P18887; -.
SMR; P18887; -.
BioGrid; 113349; 78.
CORUM; P18887; -.
DIP; DIP-39067N; -.
IntAct; P18887; 52.
MINT; P18887; -.
STRING; 9606.ENSP00000262887; -.
iPTMnet; P18887; -.
PhosphoSitePlus; P18887; -.
BioMuta; XRCC1; -.
DMDM; 317373290; -.
EPD; P18887; -.
MaxQB; P18887; -.
PaxDb; P18887; -.
PeptideAtlas; P18887; -.
PRIDE; P18887; -.
ProteomicsDB; 53619; -.
Ensembl; ENST00000262887; ENSP00000262887; ENSG00000073050.
GeneID; 7515; -.
KEGG; hsa:7515; -.
UCSC; uc002owt.3; human.
CTD; 7515; -.
DisGeNET; 7515; -.
EuPathDB; HostDB:ENSG00000073050.11; -.
GeneCards; XRCC1; -.
H-InvDB; HIX0040090; -.
HGNC; HGNC:12828; XRCC1.
HPA; CAB005427; -.
HPA; HPA006717; -.
MalaCards; XRCC1; -.
MIM; 194360; gene.
MIM; 617633; phenotype.
neXtProt; NX_P18887; -.
PharmGKB; PA369; -.
eggNOG; KOG3226; Eukaryota.
eggNOG; ENOG410ZE1H; LUCA.
HOVERGEN; HBG052992; -.
InParanoid; P18887; -.
KO; K10803; -.
OrthoDB; EOG091G0KP0; -.
PhylomeDB; P18887; -.
TreeFam; TF101201; -.
Reactome; R-HSA-110381; Resolution of AP sites via the single-nucleotide replacement pathway.
Reactome; R-HSA-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
Reactome; R-HSA-5685939; HDR through MMEJ (alt-NHEJ).
Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
SignaLink; P18887; -.
SIGNOR; P18887; -.
ChiTaRS; XRCC1; human.
EvolutionaryTrace; P18887; -.
GeneWiki; XRCC1; -.
GenomeRNAi; 7515; -.
PRO; PR:P18887; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000073050; -.
CleanEx; HS_XRCC1; -.
ExpressionAtlas; P18887; baseline and differential.
Genevisible; P18887; HS.
GO; GO:0070522; C:ERCC4-ERCC1 complex; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:1990599; F:3' overhang single-stranded DNA endodeoxyribonuclease activity; IEA:Ensembl.
GO; GO:0003909; F:DNA ligase activity; TAS:Reactome.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0032356; F:oxidized DNA binding; IMP:UniProtKB.
GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
GO; GO:0006288; P:base-excision repair, DNA ligation; TAS:Reactome.
GO; GO:0021587; P:cerebellum morphogenesis; IEA:Ensembl.
GO; GO:0000724; P:double-strand break repair via homologous recombination; TAS:Reactome.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:Ensembl.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:1905765; P:negative regulation of protection from non-homologous end joining at telomere; IEA:Ensembl.
GO; GO:0010836; P:negative regulation of protein ADP-ribosylation; IMP:UniProtKB.
GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; TAS:Reactome.
GO; GO:1904877; P:positive regulation of DNA ligase activity; IMP:UniProtKB.
GO; GO:1903518; P:positive regulation of single strand break repair; IMP:UniProtKB.
GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP:UniProtKB.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0033194; P:response to hydroperoxide; IDA:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0010033; P:response to organic substance; IEA:Ensembl.
GO; GO:0000012; P:single strand break repair; IEA:InterPro.
GO; GO:0061819; P:telomeric DNA-containing double minutes formation; IEA:Ensembl.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
GO; GO:0050882; P:voluntary musculoskeletal movement; IMP:UniProtKB.
CDD; cd00027; BRCT; 2.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 3.40.50.10190; -; 2.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR036420; BRCT_dom_sf.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR002706; Xrcc1_N.
Pfam; PF00533; BRCT; 1.
Pfam; PF16589; BRCT_2; 1.
Pfam; PF01834; XRCC1_N; 1.
SMART; SM00292; BRCT; 2.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF52113; SSF52113; 2.
PROSITE; PS50172; BRCT; 2.
1: Evidence at protein level;
3D-structure; Complete proteome; DNA damage; DNA repair;
Isopeptide bond; Neurodegeneration; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Ubl conjugation.
CHAIN 1 633 DNA repair protein XRCC1.
/FTId=PRO_0000066044.
DOMAIN 315 403 BRCT 1. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 538 629 BRCT 2. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 198 198 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 202 202 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 204 204 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 257 257 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 259 259 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 266 266 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 281 281 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 371 371 Phosphoserine; by PRKDC.
{ECO:0000269|PubMed:16397295}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 410 410 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 421 421 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 446 446 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 453 453 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 457 457 Phosphothreonine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 461 461 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 485 485 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:15066279}.
MOD_RES 488 488 Phosphothreonine.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:15066279}.
MOD_RES 518 518 Phosphoserine.
{ECO:0000269|PubMed:19155274}.
MOD_RES 519 519 Phosphothreonine.
{ECO:0000269|PubMed:19155274}.
MOD_RES 523 523 Phosphothreonine.
{ECO:0000269|PubMed:19155274}.
CROSSLNK 176 176 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 176 176 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
VARIANT 7 7 R -> L (in dbSNP:rs2307186).
/FTId=VAR_014773.
VARIANT 10 10 V -> M (in dbSNP:rs2307171).
/FTId=VAR_014774.
VARIANT 72 72 V -> A (in dbSNP:rs25496).
{ECO:0000269|Ref.2}.
/FTId=VAR_016168.
VARIANT 107 107 R -> H (in dbSNP:rs2228487).
/FTId=VAR_029228.
VARIANT 157 157 E -> K (in dbSNP:rs2307180).
/FTId=VAR_014775.
VARIANT 161 161 P -> L (in dbSNP:rs2307191).
{ECO:0000269|Ref.2}.
/FTId=VAR_014776.
VARIANT 194 194 R -> W (in dbSNP:rs1799782).
{ECO:0000269|PubMed:9485007,
ECO:0000269|Ref.2}.
/FTId=VAR_013400.
VARIANT 280 280 R -> H (in dbSNP:rs25489).
{ECO:0000269|PubMed:9485007,
ECO:0000269|Ref.2}.
/FTId=VAR_013401.
VARIANT 298 298 K -> N (in dbSNP:rs2307188).
/FTId=VAR_014777.
VARIANT 304 304 T -> A (in dbSNP:rs25490).
{ECO:0000269|Ref.2}.
/FTId=VAR_018775.
VARIANT 309 309 P -> S (in dbSNP:rs25491).
{ECO:0000269|Ref.2}.
/FTId=VAR_014778.
VARIANT 350 350 R -> W (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036277.
VARIANT 399 399 R -> Q (in dbSNP:rs25487).
{ECO:0000269|PubMed:10783319,
ECO:0000269|PubMed:11782372,
ECO:0000269|PubMed:15057824,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9485007,
ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
/FTId=VAR_011487.
VARIANT 431 431 K -> N (in SCAR26; may result in aberrant
splicing; dbSNP:rs761564262).
{ECO:0000269|PubMed:28002403}.
/FTId=VAR_079140.
VARIANT 465 633 Missing (in SCAR26).
{ECO:0000269|PubMed:28002403}.
/FTId=VAR_079141.
VARIANT 485 485 S -> Y (in dbSNP:rs2307184).
/FTId=VAR_014779.
VARIANT 514 514 P -> L (in dbSNP:rs25474).
/FTId=VAR_016169.
VARIANT 559 559 R -> Q (in dbSNP:rs2307167).
/FTId=VAR_014780.
VARIANT 560 560 R -> W (in dbSNP:rs2307166).
/FTId=VAR_014781.
VARIANT 576 576 N -> S (in dbSNP:rs2307177).
{ECO:0000269|Ref.2}.
/FTId=VAR_014782.
VARIANT 576 576 N -> Y (in dbSNP:rs2682557).
{ECO:0000244|PubMed:21269460,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2247054,
ECO:0000269|Ref.3}.
/FTId=VAR_061727.
HELIX 4 6 {ECO:0000244|PDB:3LQC}.
STRAND 7 12 {ECO:0000244|PDB:3LQC}.
HELIX 17 25 {ECO:0000244|PDB:3LQC}.
HELIX 28 36 {ECO:0000244|PDB:3LQC}.
TURN 37 39 {ECO:0000244|PDB:3LQC}.
STRAND 41 53 {ECO:0000244|PDB:3LQC}.
STRAND 57 64 {ECO:0000244|PDB:3LQC}.
STRAND 66 73 {ECO:0000244|PDB:3LQC}.
STRAND 75 77 {ECO:0000244|PDB:1XNA}.
HELIX 81 83 {ECO:0000244|PDB:3LQC}.
STRAND 85 93 {ECO:0000244|PDB:3LQC}.
HELIX 96 101 {ECO:0000244|PDB:3LQC}.
STRAND 108 111 {ECO:0000244|PDB:3LQC}.
HELIX 113 115 {ECO:0000244|PDB:3LQC}.
HELIX 118 121 {ECO:0000244|PDB:3LQC}.
STRAND 125 133 {ECO:0000244|PDB:3LQC}.
STRAND 138 140 {ECO:0000244|PDB:3K75}.
STRAND 143 150 {ECO:0000244|PDB:3LQC}.
HELIX 313 316 {ECO:0000244|PDB:2D8M}.
TURN 317 319 {ECO:0000244|PDB:2D8M}.
STRAND 323 329 {ECO:0000244|PDB:2D8M}.
HELIX 334 344 {ECO:0000244|PDB:2D8M}.
STRAND 347 352 {ECO:0000244|PDB:2D8M}.
STRAND 359 366 {ECO:0000244|PDB:2D8M}.
HELIX 368 376 {ECO:0000244|PDB:2D8M}.
STRAND 379 382 {ECO:0000244|PDB:2D8M}.
HELIX 384 391 {ECO:0000244|PDB:2D8M}.
HELIX 398 401 {ECO:0000244|PDB:2D8M}.
STRAND 404 407 {ECO:0000244|PDB:2D8M}.
TURN 542 545 {ECO:0000244|PDB:1CDZ}.
STRAND 547 550 {ECO:0000244|PDB:1CDZ}.
HELIX 557 568 {ECO:0000244|PDB:1CDZ}.
STRAND 582 585 {ECO:0000244|PDB:1CDZ}.
HELIX 592 598 {ECO:0000244|PDB:1CDZ}.
STRAND 605 607 {ECO:0000244|PDB:1CDZ}.
HELIX 610 616 {ECO:0000244|PDB:1CDZ}.
TURN 617 619 {ECO:0000244|PDB:1CDZ}.
HELIX 624 627 {ECO:0000244|PDB:1CDZ}.
SEQUENCE 633 AA; 69477 MW; 30DB3321234DBFC2 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 RMRRRLPSRR YLMAGPGSSS EEDEASHSGG
SGDEAPKLPQ KQPQTKTKPT QAAGPSSPQK PPTPEETKAA SPVLQEDIDI EGVQSEGQDN
GAEDSGDTED ELRRVAEQKE HRLPPGQEEN GEDPYAGSTD ENTDSEEHQE PPDLPVPELP
DFFQGKHFFL YGEFPGDERR KLIRYVTAFN GELEDNMSDR VQFVITAQEW DPSFEEALMD
NPSLAFVRPR WIYSCNEKQK LLPHQLYGVV PQA


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