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XRCC1

Protein FULL name:

DNA repair protein XRCC1, X-ray repair cross-complementing protein 1


Protein SHORT name:

XRCC-1


XRCC1 (Homo sapiens) is product of expression of XRCC1 gene.


XRCC1 is involved in:

BER in Homo sapiens




FUNCTION: Corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents.

SUBUNIT: Homodimer. Interacts with polynucleotide kinase (PNK), DNA polymerase-beta (POLB) and DNA ligase III (LIG3). Interacts with APTX and APLF.

INTERACTION: Q8IW19:APLF; NbExp=4; IntAct=EBI-947466, EBI-1256044; P06241:FYN; NbExp=1; IntAct=EBI-947466, EBI-515315; P49916:LIG3; NbExp=1; IntAct=EBI-947466, EBI-1753381; Q96T60:PNKP; NbExp=1; IntAct=EBI-947466, EBI-1045072;

SUBCELLULAR LOCATION: Nucleus. Note=Accumulates at sites of DNA damage.

PTM: Phosphorylation of Ser-371 causes dimer dissociation. Phosphorylation by CK2 promotes interaction with APTX and APLF.

PTM: Sumoylated.

POLYMORPHISM: Carriers of the polymorphic Gln-399 allele may be at greater risk for tobacco- and age-related DNA damage.

SIMILARITY: Contains 2 BRCT domains.

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


NCBI GenPept GI number(s): 190684675
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P18887 P18887
PFAM: - P18887 (Link - using uniprot id)
InterPro: - P18887 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MPEIRLRHVVSCSSQDSTHCAENLLKADTYRKWRAAKAGEKTISVVLQLE
KEEQIHSVDIGNDGSAFVEVLVGSSAGGAGEQDYEVLLVTSSFMSPSESR
SGSNPNRVRMFGPDKLVRAAAEKRWDRVKIVCSQPYSKDSPFGLSFVRFH
SPPDKDEAEAPSQKVTVTKLGQFRVKEEDESANSLRPGALFFSRINKTSP
VTASDPAGPSYAAATLQASSAASSASPVSRAIGSTSKPQESPKGKRKLDL
NQEEKKTPSKPPAQLSPSVPKRPKLPAPTRTPATAPVPARAQGAVTGKPR
GEGTEPRRPRAGPEELGKILQGVVVVLSGFQNPFRSELRDKALELGAKYR
PDWTRDSTHLICAFANTPKYSQVLGLGGRIVRKEWVLDCHRMRRRLPSQR
YLMAGPGSSSEEDEASHSGGSGDEAPKLPQKQPQTKTKPTQAAGPSSPQK
PPTPEETKAASPVLQEDIDIEGVQSEGQDNGAEDSGDTEDELRRVAEQKE
HRLPPGQEENGEDPYAGSTDENTDSEEHQEPPDLPVPELPDFFQGKHFFL
YGEFPGDERRKLIRYVTAFNGELEDYMSDRVQFVITAQEWDPSFEEALMD
NPSLAFVRPRWIYSCNEKQKLLPHQLYGVVPQA

XRCC1 (Homo sapiens) is able to recognize following damages:
XRCC1 (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
Molecular cloning of the human XRCC1 gene, which corrects defective DNA strand break repair and sister chromatid exchange. Thompson LH, Brookman KW, Jones NJ, Allen SA, Carrano AV Mol Cell Biol Dec. 1, 1990
Nonconservative amino acid substitution variants exist at polymorphic frequency in DNA repair genes in healthy humans. Shen MR, Jones IM, Mohrenweiser H Cancer Res Jan. 15, 1998
Polymorphisms in the DNA repair genes XRCC1 and ERCC2 and biomarkers of DNA damage in human blood mononuclear cells. Duell EJ, Wiencke JK, Cheng TJ, Varkonyi A, Zuo ZF, Ashok TD, Mark EJ, Wain JC, Christiani DC, Kelsey KT Carcinogenesis May 1, 2000
XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair. Whitehouse CJ, Taylor RM, Thistlethwaite A, Zhang H, Karimi-Busheri F, Lasko DD, Weinfeld M, Caldecott KW Cell Feb. 12, 2001
The XRCC1 Arg399Gln polymorphism, sunburn, and non-melanoma skin cancer: evidence of gene-environment interaction. Nelson HH, Kelsey KT, Mott LA, Karagas MR Cancer Res Feb. 1, 2002
Aprataxin, the causative protein for EAOH is a nuclear protein with a potential role as a DNA repair protein. Sano Y, Date H, Igarashi S, Onodera O, Oyake M, Takahashi T, Hayashi S, Morimatsu M, Takahashi H, Makifuchi T, Fukuhara N, Tsuji S Ann Neurol Jan. 1, 2004
The DNA sequence and biology of human chromosome 19. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, 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, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, 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 SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, 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 TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM Nature April 1, 2004
Aprataxin, a novel protein that protects against genotoxic stress. Gueven N, Becherel OJ, Kijas AW, Chen P, Howe O, Rudolph JH, Gatti R, Date H, Onodera O, Taucher-Scholz G, Lavin MF Hum Mol Genet May 15, 2004
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J Genome Res Oct. 1, 2004
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. Clements PM, Breslin C, Deeks ED, Byrd PJ, Ju L, Bieganowski P, Brenner C, Moreira MC, Taylor AM, Caldecott KW DNA Repair (Amst) Nov. 2, 2004
Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates. Gocke CB, Yu H, Kang J J Biol Chem Jan. 11, 2005
XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage. Levy N, Martz A, Bresson A, Spenlehauer C, de Murcia G, Menissier-de Murcia J Nucleic Acids Res Jan. 1, 2006
The consensus coding sequences of human breast and colorectal cancers. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE Science Oct. 13, 2006
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M Cell Nov. 3, 2006
Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A Proc Natl Acad Sci U S A Jan. 13, 2007
APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal DNA strand breaks. Iles N, Rulten S, El-Khamisy SF, Caldecott KW Mol Cell Biol May 1, 2007
Human Xip1 (C2orf13) is a novel regulator of cellular responses to DNA strand breaks. Bekker-Jensen S, Fugger K, Danielsen JR, Gromova I, Sehested M, Celis J, Bartek J, Lukas J, Mailand N J Biol Chem July 6, 2007
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A Aug. 5, 2008
Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Wang B, Malik R, Nigg EA, Korner R Anal Chem Dec. 15, 2008
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal Jan. 1, 2009
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S Anal Chem June 1, 2009


Last modification of this entry: Oct. 6, 2010.

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