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X-ray repair complementing defective repair in Chinese hamster cells 1
Protein XRCC1 PDB 1cdz.png
PDB rendering based on 1cdz.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols XRCC1 ; RCC
External IDs OMIM194360 MGI99137 HomoloGene31368 GeneCards: XRCC1 Gene
RNA expression pattern
PBB GE XRCC1 203655 at tn.png
More reference expression data
Species Human Mouse
Entrez 7515 22594
Ensembl ENSG00000073050 ENSMUSG00000051768
UniProt P18887 Q60596
RefSeq (mRNA) NM_006297 NM_009532
RefSeq (protein) NP_006288 NP_033558
Location (UCSC) Chr 19:
44.05 – 44.08 Mb
Chr 7:
24.55 – 24.57 Mb
PubMed search [1] [2]

DNA repair protein XRCC1 also known as X-ray repair cross-complementing protein 1 is a protein that in humans is encoded by the XRCC1 gene. XRCC1 is involved in DNA repair where it complexes with DNA ligase III.


PDB 1xna EBI.jpg
nmr solution structure of the single-strand break repair protein xrcc1-n-terminal domain
Symbol XRCC1_N
Pfam PF01834
Pfam clan CL0202
InterPro IPR002706
SCOP 1xnt

XRCC1 is involved in the efficient repair of DNA single-strand breaks formed by exposure to ionizing radiation and alkylating agents. This protein interacts with DNA ligase III, polymerase beta and poly (ADP-ribose) polymerase to participate in the base excision repair pathway. It may play a role in DNA processing during meiogenesis and recombination in germ cells. A rare microsatellite polymorphism in this gene is associated with cancer in patients of varying radiosensitivity.[1]


The NMR solution structure of the Xrcc1 N-terminal domain (Xrcc1 NTD) shows that the structural core is a beta-sandwich with beta-strands connected by loops, three helices and two short two-stranded beta-sheets at each connection side. The Xrcc1 NTD specifically binds single-strand break DNA (gapped and nicked) and a gapped DNA-beta-Pol complex.[2]


XRCC1 has been shown to interact with:


  1. ^ "Entrez Gene: XRCC1 X-ray repair complementing defective repair in Chinese hamster cells 1". 
  2. ^ Marintchev A, Mullen MA, Maciejewski MW, Pan B, Gryk MR, Mullen GP (Sep 1999). "Solution structure of the single-strand break repair protein XRCC1 N-terminal domain". Nature Structural Biology 6 (9): 884–93. doi:10.1038/12347. PMID 10467102. 
  3. ^ Vidal AE, Boiteux S, Hickson ID, Radicella JP (Nov 2001). "XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactions". The EMBO Journal 20 (22): 6530–9. doi:10.1093/emboj/20.22.6530. PMC 125722. PMID 11707423. 
  4. ^ Date H, Igarashi S, Sano Y, Takahashi T, Takahashi T, Takano H et al. (Dec 2004). "The FHA domain of aprataxin interacts with the C-terminal region of XRCC1". Biochemical and Biophysical Research Communications 325 (4): 1279–85. doi:10.1016/j.bbrc.2004.10.162. PMID 15555565. 
  5. ^ a b Gueven N, Becherel OJ, Kijas AW, Chen P, Howe O, Rudolph JH et al. (May 2004). "Aprataxin, a novel protein that protects against genotoxic stress". Human Molecular Genetics 13 (10): 1081–93. doi:10.1093/hmg/ddh122. PMID 15044383. 
  6. ^ Marsin S, Vidal AE, Sossou M, Ménissier-de Murcia J, Le Page F, Boiteux S et al. (Nov 2003). "Role of XRCC1 in the coordination and stimulation of oxidative DNA damage repair initiated by the DNA glycosylase hOGG1". The Journal of Biological Chemistry 278 (45): 44068–74. doi:10.1074/jbc.M306160200. PMID 12933815.  Vancouver style error (help)
  7. ^ Schreiber V, Amé JC, Dollé P, Schultz I, Rinaldi B, Fraulob V et al. (Jun 2002). "Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1". The Journal of Biological Chemistry 277 (25): 23028–36. doi:10.1074/jbc.M202390200. PMID 11948190.  Vancouver style error (help)
  8. ^ a b Fan J, Otterlei M, Wong HK, Tomkinson AE, Wilson DM (2004). "XRCC1 co-localizes and physically interacts with PCNA". Nucleic Acids Research 32 (7): 2193–201. doi:10.1093/nar/gkh556. PMC 407833. PMID 15107487. 
  9. ^ Whitehouse CJ, Taylor RM, Thistlethwaite A, Zhang H, Karimi-Busheri F, Lasko DD et al. (Jan 2001). "XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair". Cell 104 (1): 107–17. doi:10.1016/S0092-8674(01)00195-7. PMID 11163244. 
  10. ^ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. 
  11. ^ Wang L, Bhattacharyya N, Chelsea DM, Escobar PF, Banerjee S (Nov 2004). "A novel nuclear protein, MGC5306 interacts with DNA polymerase beta and has a potential role in cellular phenotype". Cancer Research 64 (21): 7673–7. doi:10.1158/0008-5472.CAN-04-2801. PMID 15520167. 
  12. ^ Kubota Y, Nash RA, Klungland A, Schär P, Barnes DE, Lindahl T (Dec 1996). "Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein". The EMBO Journal 15 (23): 6662–70. PMC 452490. PMID 8978692.  Vancouver style error (help)
  13. ^ Bhattacharyya N, Banerjee S (Jul 2001). "A novel role of XRCC1 in the functions of a DNA polymerase beta variant". Biochemistry 40 (30): 9005–13. doi:10.1021/bi0028789. PMID 11467963. 
  14. ^ Masson M, Niedergang C, Schreiber V, Muller S, Menissier-de Murcia J, de Murcia G (Jun 1998). "XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage". Molecular and Cellular Biology 18 (6): 3563–71. PMC 108937. PMID 9584196. 

Further reading[edit]

External links[edit]

This article incorporates text from the public domain Pfam and InterPro IPR002706