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Overview

Uniprot IDQ96T60
Protein NameBifunctional polynucleotide phosphatase/kinase
Gene NamePNKP
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
142 LPKKRMRKSNPGWEN
226 QMSIGRGKLPAEEFK

Function

Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways (PubMed:10446192, PubMed:10446193, PubMed:15385968, PubMed:20852255, PubMed:28453785). Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone (PubMed:10446192, PubMed:10446193)

Protein Sequence

10 MGEVEAPGRL 20 WLESPPGGAP 30 PIFLPSDGQA 40 LVLGRGPLTQ 50 VTDRKCSRTQ 60 VELVADPETR 70 TVAVKQLGVN 80 PSTTGTQELK 90 PGLEGSLGVG 100 DTLYLVNGLH 110 PLTLRWEETR 120 TPESQPDTPP 130 GTPLVSQDEK 140 RDAELPKKRM 150 RKSNPGWENL 160 EKLLVFTAAG 170 VKPQGKVAGF 180 DLDGTLITTR 190 SGKVFPTGPS 200 DWRILYPEIP 210 RKLRELEAEG 220 YKLVIFTNQM 230 SIGRGKLPAE 240 EFKAKVEAVV 250 EKLGVPFQVL 260 VATHAGLYRK 270 PVTGMWDHLQ 280 EQANDGTPIS 290 IGDSIFVGDA 300 AGRPANWAPG 310 RKKKDFSCAD 320 RLFALNLGLP 330 FATPEEFFLK 340 WPAAGFELPA 350 FDPRTVSRSG 360 PLCLPESRAL 370 LSASPEVVVA 380 VGFPGAGKST 390 FLKKHLVSAG 400 YVHVNRDTLG 410 SWQRCVTTCE 420 TALKQGKRVA 430 IDNTNPDAAS 440 RARYVQCARA 450 AGVPCRCFLF 460 TATLEQARHN 470 NRFREMTDSS 480 HIPVSDMVMY 490 GYRKQFEAPT 500 LAEGFSAILE 510 IPFRLWVEPR 520 LGRLYCQFSE G

Gene Ontology

Classification GO ID Description
Cellular Component GO:0016020 membrane
Biological Process GO:0006289 nucleotide-excision repair
Biological Process GO:2001034 positive regulation of double-strand break repair via nonhomologous end joining
Biological Process GO:0032206 positive regulation of telomere maintenance
Biological Process GO:0006282 regulation of DNA repair
Biological Process GO:0006979 response to oxidative stress
Biological Process GO:0009314 response to radiation
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0090734 site of DNA damage
Cellular Component GO:0035861 site of double-strand break
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0046404 ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity
Molecular Function GO:0003684 damaged DNA binding
Molecular Function GO:0003690 double-stranded DNA binding
Molecular Function GO:0004519 endonuclease activity
Molecular Function GO:0046403 polynucleotide 3'-phosphatase activity
Molecular Function GO:0017076 purine nucleotide binding
Biological Process GO:0006287 base-excision repair, gap-filling
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

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[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] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[5] 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.