Search Results

Overview

Uniprot ID	Q15397
Protein Name	Pumilio homolog 3
Gene Name	PUM3
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
12	GKKQFTGKSTKTAQE
33	NSDSGSSKTFPTRKV
59	NFEKSITKLGKKGVK
81	GDKSPKNKFQPANKF
93	NKFNKKRKFQPDGRS

Function

Inhibits the poly(ADP-ribosyl)ation activity of PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress (PubMed:21266351). Binds to double-stranded RNA or DNA without sequence specificity (PubMed:25512524). Involved in development of the eye and of primordial germ cells (By similarity)

Protein Sequence

10 MEVKGKKQFT 20 GKSTKTAQEK 30 NRFHKNSDSG 40 SSKTFPTRKV 50 AKEGGPKVTS 60 RNFEKSITKL 70 GKKGVKQFKN 80 KQQGDKSPKN 90 KFQPANKFNK 100 KRKFQPDGRS 110 DESAAKKPKW 120 DDFKKKKKEL 130 KQSRQLSDKT 140 NYDIVVRAKQ 150 MWEILRRKDC 160 DKEKRVKLMS 170 DLQKLIQGKI 180 KTIAFAHDST 190 RVIQCYIQYG 200 NEEQRKQAFE 210 ELRDDLVELS 220 KAKYSRNIVK 230 KFLMYGSKPQ 240 IAEIIRSFKG 250 HVRKMLRHAE 260 ASAIVEYAYN 270 DKAILEQRNM 280 LTEELYGNTF 290 QLYKSADHRT 300 LDKVLEVQPE 310 KLELIMDEMK 320 QILTPMAQKE 330 AVIKHSLVHK 340 VFLDFFTYAP 350 PKLRSEMIEA 360 IREAVVYLAH 370 THDGARVAMH 380 CLWHGTPKDR 390 KVIVKTMKTY 400 VEKVANGQYS 410 HLVLLAAFDC 420 IDDTKLVKQI 430 IISEIISSLP 440 SIVNDKYGRK 450 VLLYLLSPRD 460 PAHTVREIIE 470 VLQKGDGNAH 480 SKKDTEVRRR 490 ELLESISPAL 500 LSYLQEHAQE 510 VVLDKSACVL 520 VSDILGSATG 530 DVQPTMNAIA 540 SLAATGLHPG 550 GKDGELHIAE 560 HPAGHLVLKW 570 LIEQDKKMKE 580 NGREGCFAKT 590 LVEHVGMKNL 600 KSWASVNRGA 610 IILSSLLQSC 620 DLEVANKVKA 630 ALKSLIPTLE 640 KTKSTSKGIE ILLEKLST

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005694	chromosome
Cellular Component	GO:0005783	endoplasmic reticulum
Cellular Component	GO:0005730	nucleolus
Cellular Component	GO:0005654	nucleoplasm
Molecular Function	GO:0003677	DNA binding
Molecular Function	GO:0003729	mRNA binding
Molecular Function	GO:0003723	RNA binding
Biological Process	GO:0010835	regulation of protein ADP-ribosylation
Biological Process	GO:0006417	regulation of translation

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] 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.

[3] 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.

[4] 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.