Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) Binds 2 magnesium ions per subunit. Interacts with APEX1, HUWE1/ARF-BP1, STUB1/CHIP and USP47 (By similarity). Monomer. Interacts with FAM168A (By similarity). Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage (By similarity). Residues 239-252 form a flexible loop which appears to affect the polymerase fidelity. Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity. Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by HUWE1/ARF-BP1. Monoubiquitinated protein is then the target of STUB1/CHIP, which catalyzes polyubiquitination from monoubiquitin, leading to degradation by the proteasome. USP47 mediates the deubiquitination of monoubiquitinated protein, preventing polyubiquitination by STUB1/CHIP and its subsequent degradation (By similarity). Belongs to the DNA polymerase type-X family.