Search Results

Overview

Uniprot IDQ6IN85
Protein NameSerine/threonine-protein phosphatase 4 regulatory subunit 3A
Gene NamePPP4R3A
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
655 RERQDNPKLDSMRSI
715 DIMDPISKFMERKKL
733 EEKEVLLKTNLSGRQ
745 GRQSPSFKLSLSSGT
9 TDTRRRVKVYTLNED

Function

Regulatory subunit of serine/threonine-protein phosphatase 4. May regulate the activity of PPP4C at centrosomal microtubule organizing centers. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AX phosphorylated on 'Ser-140' (gamma-H2AX) generated during DNA replication and required for DNA DSB repair

Protein Sequence

10 MTDTRRRVKV 20 YTLNEDRQWD 30 DRGTGHVSSG 40 YVERLKGMSL 50 LVRAESDGSL 60 LLESKINPNT 70 AYQKQQDTLI 80 VWSEAENYDL 90 ALSFQEKAGC 100 DEIWEKICQV 110 QGKDPSVDIT 120 QDLVDESEEE 130 RFDDMSSPGL 140 ELPSCELSRL 150 EEIAELVASS 160 LPSPLRREKL 170 ALALENEGYI 180 KKLLELFHVC 190 EDLENIEGLH 200 HLYEIIKGIF 210 LLNRTALFEV 220 MFSEECIMDV 230 IGCLEYDPAL 240 SQPRKHREFL 250 TKTAKFKEVI 260 PISDPELKQK 270 IHQTYRVQYI 280 QDMVLPTPSV 290 FEENMLSTLH 300 SFIFFNKVEI 310 VGMLQEDEKF 320 LTDLFAQLTD 330 EATDEEKRQE 340 LVNFLKEFCA 350 FSQTLQPQNR 360 DAFFKTLSNM 370 GILPALEVIL 380 GMDDTQVRSA 390 ATDIFSYLVE 400 YNPSMVREFV 410 MQEAQQNDDV 420 SKKLTEQKIT 430 SKDILLINLI 440 IEHMICDTDP 450 ELGGAVQLMG 460 LLRTLVDPEN 470 MLATANKTEK 480 TEFLGFFYKH 490 CMHVLTAPLL 500 ANTTEDKPSK 510 DDFQTAQLLA 520 LVLELLTFCV 530 EHHTYHIKNY 540 IINKDILRRV 550 LVLMASKHAF 560 LALCALRFKR 570 KIIGLKDEFY 580 NRYIMKSFLF 590 EPVVKAFLNN 600 GSRYNLMNSA 610 IIEMFEFIRV 620 EDIKSLTAHV 630 IENYWKALED 640 VDYVQTFKGL 650 KLRFEQQRER 660 QDNPKLDSMR 670 SILRNHRYRR 680 DARTLEDEEE 690 MWFNTDEDDM 700 EDGEAVVSPS 710 DKTKNDDDIM 720 DPISKFMERK 730 KLKESEEKEV 740 LLKTNLSGRQ 750 SPSFKLSLSS 760 GTKTNLTSQS 770 STTNLPGSPG 780 SPGSPGSPGS 790 PGSVPKNTSQ 800 TAAITTKGGL 810 VGLVDYPDDD 820 EDDDEDEDKE 830 DTLPLSKKAK FDS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005813 centrosome
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0030289 protein phosphatase 4 complex
Molecular Function GO:0072542 protein phosphatase activator activity
Biological Process GO:0006974 DNA damage response
Biological Process GO:2000779 regulation of double-strand break repair

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] 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.

[3] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[4] 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.

[5] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[6] 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.

[7] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[8] 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.