REPAIRtoire - a database of DNA repair pathways

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Protein FULL name:

DNA-(apurinic or apyrimidinic site) lyase, Apurinic-apyrimidinic endonuclease 1, APEX nuclease, Protein REF-1.,

Protein SHORT name:

AP endonuclease 1 APEN

APEX1 (Homo sapiens) is product of expression of APEX1 gene.

APEX1 is involved in:

BER in Homo sapiens


FUNCTION: Repairs oxidative DNA damages in vitro. May have a role in protection against cell lethality and suppression of mutations. Removes the blocking groups from the 3'-termini of the DNA strand breaks generated by ionizing radiations and bleomycin.

CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.

SUBUNIT: Monomer. Component of the SET complex, which also contains SET, ANP32A, HMGB2 and NME1.


SIMILARITY: Belongs to the DNA repair enzymes AP/exoA family.


NCBI GenPept GI number(s): 113984
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P27695 P27695
PFAM: PF03372
InterPro: IPR000097
CATH: - -
SCOP: - -
PDB: - -

Protein sequence:

APEX1 (Homo sapiens) is able to recognize following damages:
APEX1 (Homo sapiens) belongs to following protein families:

Title Authors Journal
Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III) mutants. Robson CN, Hickson ID Nucleic Acids Res Oct. 25, 1991
Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA repair enzymes. Demple B, Herman T, Chen DS Proc Natl Acad Sci U S A Dec. 15, 1991
Nucleotide sequence of a cDNA for an apurinic/apyrimidinic endonuclease from HeLa cells. Cheng XB, Bunville J, Patterson TA Nucleic Acids Res Feb. 25, 1992
cDNA cloning, sequencing, expression and possible domain structure of human APEX nuclease homologous to Escherichia coli exonuclease III. Seki S, Hatsushika M, Watanabe S, Akiyama K, Nagao K, Tsutsui K Biochim Biophys Acta July 15, 1992
The human gene for apurinic/apyrimidinic endonuclease (HAP1): sequence and localization to chromosome 14 band q12. Zhao B, Grandy DK, Hagerup JM, Magenis RE, Smith L, Chauhan BC, Henner WD Nucleic Acids Res Aug. 11, 1992
Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. Xanthoudakis S, Miao G, Wang F, Pan YC, Curran T EMBO J Sept. 1, 1992
Structure of the human DNA repair gene HAP1 and its localisation to chromosome 14q 11.2-12. Robson CN, Hochhauser D, Craig R, Rack K, Buckle VJ, Hickson ID Nucleic Acids Res Sept. 11, 1992
Human apurinic endonuclease gene (APE): structure and genomic mapping (chromosome 14q11.2-12). Harrison L, Ascione G, Menninger JC, Ward DC, Demple B Hum Mol Genet Dec. 1, 1992
Structure, promoter analysis and chromosomal assignment of the human APEX gene. Akiyama K, Seki S, Oshida T, Yoshida MC Biochim Biophys Acta Sept. 13, 1994
Asparagine 212 is essential for abasic site recognition by the human DNA repair endonuclease HAP1. Rothwell DG, Hickson ID Nucleic Acids Res Nov. 1, 1996
Large-scale concatenation cDNA sequencing. Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA Genome Res April 1, 1997
The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites. Gorman MA, Morera S, Rothwell DG, de La Fortelle E, Mol CD, Tainer JA, Hickson ID, Freemont PS EMBO J Nov. 3, 1997
DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination [corrected] Mol CD, Izumi T, Mitra S, Tainer JA Nature Feb. 27, 2000
Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: implications for the catalytic mechanism. Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B J Mol Biol April 6, 2001
Cleaving the oxidative repair protein Ape1 enhances cell death mediated by granzyme A. Fan Z, Beresford PJ, Zhang D, Xu Z, Novina CD, Yoshida A, Pommier Y, Lieberman J Nat Immunol Jan. 1, 2003
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
Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ Nat Biotechnol Feb. 1, 2005
Lysine acetylation targets protein complexes and co-regulates major cellular functions. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M Science Aug. 14, 2009

Last modification of this entry: Oct. 16, 2010.

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