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Gene Review

NEIL2  -  nei endonuclease VIII-like 2 (E. coli)

Homo sapiens

Synonyms: DNA glycosylase/AP lyase Neil2, DNA-(apurinic or apyrimidinic site) lyase Neil2, Endonuclease 8-like 2, Endonuclease VIII-like 2, FLJ31644, ...
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Disease relevance of NEIL2

  • The recently identified human NEIL2 (Nei-like-2) protein, a DNA glycosylase/AP lyase specific for oxidatively damaged bases, shares structural features and reaction mechanism with the Escherichia coli DNA glycosylases, Nei and Fpg [1].
  • Polymorphisms of the NEIL2 gene may be markers for risk and progression of SCCOOP, particularly in patients with oropharyngeal cancer [2].

High impact information on NEIL2

  • In human cells, oxidative pyrimidine lesions are restored by the base excision repair pathway initiated by homologues of Endo III (hNTH1) and Endo VIII (hNEIL1 and hNEIL2) [3].
  • We thereby conclude that the zinc finger motif in NEIL2 is essential for its structural integrity and enzyme activity [1].
  • Amino acid sequence analysis of NEIL2 suggested it to have a zinc finger-like Nei/Fpg [1].
  • However, the Cys-X2-His-X16-Cys-X2-Cys (CHCC) motif present near the C terminus of NEIL2 is distinct from the zinc finger motifs of Nei/Fpg, which are of the C4 type [1].
  • Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2 [4].

Biological context of NEIL2


Associations of NEIL2 with chemical compounds


Other interactions of NEIL2

  • However, NEIL2 shows a unique preference for excising lesions from a DNA bubble, whereas NTH1 and OGG1 are only active with duplex DNA [4].
  • CONCLUSION: We detected novel germline alterations in NEIL2, TDG and UNG patients with CRC [8].


  1. Identification of a zinc finger domain in the human NEIL2 (Nei-like-2) protein. Das, A., Rajagopalan, L., Mathura, V.S., Rigby, S.J., Mitra, S., Hazra, T.K. J. Biol. Chem. (2004) [Pubmed]
  2. Functional variants of the NEIL1 and NEIL2 genes and risk and progression of squamous cell carcinoma of the oral cavity and oropharynx. Zhai, X., Zhao, H., Liu, Z., Wang, L.E., El-Naggar, A.K., Sturgis, E.M., Wei, Q. Clin. Cancer Res. (2008) [Pubmed]
  3. Differential specificity of human and Escherichia coli endonuclease III and VIII homologues for oxidative base lesions. Katafuchi, A., Nakano, T., Masaoka, A., Terato, H., Iwai, S., Hanaoka, F., Ide, H. J. Biol. Chem. (2004) [Pubmed]
  4. Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2. Dou, H., Mitra, S., Hazra, T.K. J. Biol. Chem. (2003) [Pubmed]
  5. Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions. Hazra, T.K., Kow, Y.W., Hatahet, Z., Imhoff, B., Boldogh, I., Mokkapati, S.K., Mitra, S., Izumi, T. J. Biol. Chem. (2002) [Pubmed]
  6. NEIL2-initiated, APE-independent repair of oxidized bases in DNA: Evidence for a repair complex in human cells. Das, A., Wiederhold, L., Leppard, J.B., Kedar, P., Prasad, R., Wang, H., Boldogh, I., Karimi-Busheri, F., Weinfeld, M., Tomkinson, A.E., Wilson, S.H., Mitra, S., Hazra, T.K. DNA Repair (Amst.) (2006) [Pubmed]
  7. Acetylation of the human DNA glycosylase NEIL2 and inhibition of its activity. Bhakat, K.K., Hazra, T.K., Mitra, S. Nucleic Acids Res. (2004) [Pubmed]
  8. Evaluation of NTHL1, NEIL1, NEIL2, MPG, TDG, UNG and SMUG1 genes in familial colorectal cancer predisposition. Broderick, P., Bagratuni, T., Vijayakrishnan, J., Lubbe, S., Chandler, I., Houlston, R.S. BMC Cancer (2006) [Pubmed]
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