XRCC1 je protein popravke DNK. On formira kompleks sa DNK ligazom III.

XRCC1
PDB prikaz baziran na 1cdz​.
Dostupne strukture
1CDZ​, 1XNA​, 1XNT​, 2D8M​, 2W3O​, 3K75​, 3K77​, 3LQC
Identifikatori
Simboli XRCC1; RCC
Vanjski ID OMIM194360 MGI99137 HomoloGene31368 GeneCards: XRCC1 Gene
Pregled RNK izražavanja
podaci
Ortolozi
Vrsta Čovek Miš
Entrez 7515 22594
Ensembl ENSG00000073050 ENSMUSG00000051768
UniProt P18887 Q60596
RefSeq (mRNA) NM_006297.2 NM_009532.4
RefSeq (protein) NP_006288.2 NP_033558.3
Lokacija (UCSC) Chr 19:
44.05 - 44.08 Mb
Chr 7:
25.33 - 25.36 Mb
PubMed pretraga [1] [2]

Ovaj protein učestvuje u popravci jednolančankih prekida DNK formiranih izlaganjem jonizujućoj radijaciji i alkilujućim agensima. Ovaj protein formira interakcije sa DNK ligazom III, polimerazom beta i poli ADP-riboznom polimerazom da bi učestvovao u putu popravke isecanjem baza. Moguće je da ima ulogu u DNK manipulacijama tokom mejoze i rekombinacije u ćelijama zametka. Retki mikrosatelitni polimorfizam ovog genu je vezan za pojavu pojedinih tipova kancera.[1]

Interakcije

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XRCC1 formira interakcije sa PARP2,[2] DNK polimerazom beta,[3][4][5][6] Aprataksinom,[7][8] Oksoguaninskom glikosilaza,[9] PCNA,[4] APEX1,[10] PNKP[11][12] i PARP1.[8][13]

Reference

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  1. ^ „Entrez Gene: XRCC1 X-ray repair complementing defective repair in Chinese hamster cells 1”. 
  2. ^ Schreiber, Valérie; et al. (2002). „Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1”. J. Biol. Chem. United States. 277 (25): 23028—36. ISSN 0021-9258. PMID 11948190. doi:10.1074/jbc.M202390200. 
  3. ^ Wang, Liming; et al. (2004). „A novel nuclear protein, MGC5306 interacts with DNA polymerase beta and has a potential role in cellular phenotype”. Cancer Res. United States. 64 (21): 7673—7. ISSN 0008-5472. PMID 15520167. doi:10.1158/0008-5472.CAN-04-2801. 
  4. ^ а б Fan, Jinshui; et al. (2004). „XRCC1 co-localizes and physically interacts with PCNA”. Nucleic Acids Res. England. 32 (7): 2193—201. PMC 407833 . PMID 15107487. doi:10.1093/nar/gkh556. 
  5. ^ Kubota, Y; et al. (1996). „Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein”. EMBO J. ENGLAND. 15 (23): 6662—70. ISSN 0261-4189. PMC 452490 . PMID 8978692. 
  6. ^ Bhattacharyya, N; S, Banerjee (2001). „A novel role of XRCC1 in the functions of a DNA polymerase beta variant”. Biochemistry. United States. 40 (30): 9005—13. ISSN 0006-2960. PMID 11467963. doi:10.1021/bi0028789. 
  7. ^ Date, Hidetoshi; et al. (2004). „The FHA domain of aprataxin interacts with the C-terminal region of XRCC1”. Biochem. Biophys. Res. Commun. United States. 325 (4): 1279—85. ISSN 0006-291X. PMID 15555565. doi:10.1016/j.bbrc.2004.10.162. 
  8. ^ а б Gueven, Nuri; et al. (2004). „Aprataxin, a novel protein that protects against genotoxic stress”. Hum. Mol. Genet. England. 13 (10): 1081—93. ISSN 0964-6906. PMID 15044383. doi:10.1093/hmg/ddh122. 
  9. ^ Marsin, Stéphanie; et al. (2003). „Role of XRCC1 in the coordination and stimulation of oxidative DNA damage repair initiated by the DNA glycosylase hOGG1”. J. Biol. Chem. United States. 278 (45): 44068—74. ISSN 0021-9258. PMID 12933815. doi:10.1074/jbc.M306160200. 
  10. ^ Vidal, A E; et al. (2001). „XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactions”. EMBO J. England. 20 (22): 6530—9. ISSN 0261-4189. PMC 125722 . PMID 11707423. doi:10.1093/emboj/20.22.6530. 
  11. ^ Whitehouse, C J; et al. (2001). „XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair”. Cell. United States. 104 (1): 107—17. ISSN 0092-8674. PMID 11163244. doi:10.1016/S0092-8674(01)00195-7. 
  12. ^ Ewing, Rob M; et al. (2007). „Large-scale mapping of human protein-protein interactions by mass spectrometry”. Mol. Syst. Biol. England. 3 (1): 89. PMC 1847948 . PMID 17353931. doi:10.1038/msb4100134. 
  13. ^ Masson, M; et al. (1998). „XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage”. Mol. Cell. Biol. UNITED STATES. 18 (6): 3563—71. ISSN 0270-7306. PMC 108937 . PMID 9584196. 

Literatura

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Spoljašnje veze

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