Search Results

Overview

Uniprot IDP49005
Protein NameDNA polymerase delta subunit 2
Gene NamePOLD2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
267 KAKYLTKKTQAASVE

Function

Accessory component of both the DNA polymerase delta complex and the DNA polymerase zeta complex (PubMed:17317665, PubMed:22801543, PubMed:24449906). As a component of the trimeric and tetrameric DNA polymerase delta complexes (Pol-delta3 and Pol-delta4, respectively), plays a role in high fidelity genome replication, including in lagging strand synthesis, and repair (PubMed:12403614, PubMed:16510448, PubMed:19074196, PubMed:20334433, PubMed:24035200). Pol-delta3 and Pol-delta4 are characterized by the absence or the presence of POLD4. They exhibit differences in catalytic activity. Most notably, Pol-delta3 shows higher proofreading activity than Pol-delta4 (PubMed:19074196, PubMed:20334433). Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may also be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated (PubMed:24035200). Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation (PubMed:20227374). Under conditions of DNA replication stress, required for the repair of broken replication forks through break-induced replication (BIR) (PubMed:24310611). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine or abasic sites performed by Pol-delta4, independently of DNA polymerase zeta (REV3L) or eta (POLH). Facilitates abasic site bypass by DNA polymerase delta by promoting extension from the nucleotide inserted opposite the lesion. Also involved in TLS as a component of the DNA polymerase zeta complex (PubMed:24449906). Along with POLD3, dramatically increases the efficiency and processivity of DNA synthesis of the DNA polymerase zeta complex compared to the minimal zeta complex, consisting of only REV3L and REV7 (PubMed:24449906)

Protein Sequence

10 MFSEQAAQRA 20 HTLLSPPSAN 30 NATFARVPVA 40 TYTNSSQPFR 50 LGERSFSRQY 60 AHIYATRLIQ 70 MRPFLENRAQ 80 QHWGSGVGVK 90 KLCELQPEEK 100 CCVVGTLFKA 110 MPLQPSILRE 120 VSEEHNLLPQ 130 PPRSKYIHPD 140 DELVLEDELQ 150 RIKLKGTIDV 160 SKLVTGTVLA 170 VFGSVRDDGK 180 FLVEDYCFAD 190 LAPQKPAPPL 200 DTDRFVLLVS 210 GLGLGGGGGE 220 SLLGTQLLVD 230 VVTGQLGDEG 240 EQCSAAHVSR 250 VILAGNLLSH 260 STQSRDSINK 270 AKYLTKKTQA 280 ASVEAVKMLD 290 EILLQLSASV 300 PVDVMPGEFD 310 PTNYTLPQQP 320 LHPCMFPLAT 330 AYSTLQLVTN 340 PYQATIDGVR 350 FLGTSGQNVS 360 DIFRYSSMED 370 HLEILEWTLR 380 VRHISPTAPD 390 TLGCYPFYKT 400 DPFIFPECPH 410 VYFCGNTPSF 420 GSKIIRGPED 430 QTVLLVTVPD 440 FSATQTACLV 450 NLRSLACQPI 460 SFSGFGAEDD DLGGLGLGP

Gene Ontology

Classification GO ID Description
Cellular Component GO:0043625 delta DNA polymerase complex
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0016035 zeta DNA polymerase complex
Molecular Function GO:0003677 DNA binding
Biological Process GO:0071897 DNA biosynthetic process
Biological Process GO:0006281 DNA repair
Biological Process GO:0006260 DNA replication
Biological Process GO:0006271 DNA strand elongation involved in DNA replication
Biological Process GO:0006261 DNA-templated DNA replication
Biological Process GO:0042276 error-prone translesion synthesis

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] 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.