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Overview

Uniprot IDP06746
Protein NameDNA polymerase beta
Gene NamePOLB
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
35 NVSQAIHKYNAYRKA
48 KAASVIAKYPHKIKS
52 VIAKYPHKIKSGAEA
81 DEFLATGKLRKLEKI

Function

Repair polymerase that plays a key role in base-excision repair (PubMed:10556592, PubMed:9207062, PubMed:9572863). During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap (PubMed:10556592, PubMed:17526740, PubMed:8841119, PubMed:9556598, PubMed:9572863, PubMed:9614142). Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as an AP lyase (PubMed:9614142)

Protein Sequence

10 MSKRKAPQET 20 LNGGITDMLT 30 ELANFEKNVS 40 QAIHKYNAYR 50 KAASVIAKYP 60 HKIKSGAEAK 70 KLPGVGTKIA 80 EKIDEFLATG 90 KLRKLEKIRQ 100 DDTSSSINFL 110 TRVSGIGPSA 120 ARKFVDEGIK 130 TLEDLRKNED 140 KLNHHQRIGL 150 KYFGDFEKRI 160 PREEMLQMQD 170 IVLNEVKKVD 180 SEYIATVCGS 190 FRRGAESSGD 200 MDVLLTHPSF 210 TSESTKQPKL 220 LHQVVEQLQK 230 VHFITDTLSK 240 GETKFMGVCQ 250 LPSKNDEKEY 260 PHRRIDIRLI 270 PKDQYYCGVL 280 YFTGSDIFNK 290 NMRAHALEKG 300 FTINEYTIRP 310 LGVTGVAGEP 320 LPVDSEKDIF 330 DYIQWKYREP KDRSE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005874 microtubule
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0090734 site of DNA damage
Cellular Component GO:0005876 spindle microtubule
Molecular Function GO:0051575 5'-deoxyribose-5-phosphate lyase activity
Molecular Function GO:0140078 class I DNA-(apurinic or apyrimidinic site) endonuclease activity
Molecular Function GO:0003684 damaged DNA binding
Molecular Function GO:0003906 DNA-(apurinic or apyrimidinic site) endonuclease activity
Molecular Function GO:0003887 DNA-directed DNA polymerase activity
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0016829 lyase activity
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0008017 microtubule binding
Biological Process GO:0006284 base-excision repair
Biological Process GO:0006287 base-excision repair, gap-filling
Biological Process GO:0006974 DNA damage response
Biological Process GO:0006281 DNA repair
Biological Process GO:0006261 DNA-templated DNA replication
Biological Process GO:0006303 double-strand break repair via nonhomologous end joining
Biological Process GO:0006290 pyrimidine dimer repair
Biological Process GO:0006282 regulation of DNA repair
Biological Process GO:0045471 response to ethanol
Biological Process GO:0010332 response to gamma radiation
Biological Process GO:0055093 response to hyperoxia

Reference

[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.