| Gene Symbol | Apex1 |
|---|---|
| Entrez Gene | 79116 |
| Alt Symbol | APE, Apex, REF-1 |
| Species | Rat |
| Gene Type | protein-coding |
| Description | APEX nuclease (multifunctional DNA repair enzyme) 1 |
| Other Description | AP endonuclease 1|APEN|APEX nuclease 1|DNA-(apurinic or apyrimidinic site) lyase|apurinic-apyrimidinic endonuclease 1|apurinic/apyrimidinic endonuclease 1|redox factor-1 |
| Swissprots | P43138 Q548N9 |
| Accessions | BAA82124 EDL88426 EDL88427 P43138 AF309114 AAG40859 AF311054 AAG49922 BC078816 AAH78816 D44495 BAA07938 FQ220521 L27076 AAA21019 XM_006251913 XP_006251975 NM_024148 NP_077062 |
| Function | Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 in DNA repair and redox regulation of transcriptional factors. Functions as a 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. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' |
| Subcellular Location | Nucleus {ECO:0000255|PROSITE- ProRule:PRU00764, ECO:0000269|PubMed:11182545}. Nucleus, nucleolus {ECO:0000250}. Nucleus speckle {ECO:0000255|PROSITE- ProRule:PRU00764}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00764}. Note=Colocalized with SIRT1 in the nucleus. Colocalized with YBX1 in nuclear speckles after genotoxic stress. Together with OGG1 is recruited to nuclear speckles in UVA-irradiated cells. Colocalized with nucleolin and NPM1 in the nucleolus. Its nucleolar localization is cell cycle dependent and requires active rRNA transcription. Colocalized with calreticulin in the endoplasmic reticulum. Translocation from the nucleus to the cytoplasm is stimulated in presence of nitric oxide (NO) and function in a CRM1-dependent manner, possibly as a consequence of demasking a nuclear export signal (amino acid position 63-79). S-nitrosylation at Cys-92 and Cys-309 regulates its nuclear-cytosolic shuttling. Detected in the cytoplasm of B cells stimul |
| Top Pathways | Base excision repair |