Post Translational Modifications | Ubiquitinated by the CUL9-RBX1 complex. |
Function | Functions as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Also displays double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially. Also exhibits 3'-5' exonuclease activity on a single nucleotide gap containing heteroduplex DNA and on blunt-ended substrates. Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents. In the nucleus functions in the PCNA-dependent BER pathway. Plays a role in reversing blocked 3' DNA ends, problematic lesions that preclude DNA synthesis. Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes. Required for proper cell cycle progression during proliferation of peripheral lymphocytes. |
Protein Name | Dna-(Apurinic Or Apyrimidinic Site Endonuclease 2Ap Endonuclease Xth2Apex Nuclease 2Apex Nuclease-Like 2Apurinic-Apyrimidinic Endonuclease 2Ap Endonuclease 2 |
Cellular Localisation | NucleusCytoplasmMitochondrionTogether With PcnaIs Redistributed In Discrete Nuclear Foci In Presence Of Oxidative Dna Damaging Agents |
Alternative Antibody Names | Anti-Dna-(Apurinic Or Apyrimidinic Site Endonuclease 2 antibodyAnti-Ap Endonuclease Xth2 antibodyAnti-Apex Nuclease 2 antibodyAnti-Apex Nuclease-Like 2 antibodyAnti-Apurinic-Apyrimidinic Endonuclease 2 antibodyAnti-Ap Endonuclease 2 antibodyAnti-APEX2 antibodyAnti-APE2 antibodyAnti-APEXL2 antibodyAnti-XTH2 antibody |
Information sourced from Uniprot.org