Search Results

Overview

Uniprot IDQ86VM9
Protein NameZinc finger CCCH domain-containing protein 18
Gene NameZC3H18
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
168 GTPREEGKAGVQSVG
499 SRQAEPPKKEAATTG
500 RQAEPPKKEAATTGP
510 ATTGPQVKRADEWKD
528 RSKSPKKKLGVSVSP
622 HRPSIRTKGEPAPPP
631 EPAPPPGKAGEKSVK
780 DSSTQPPKSAKPPAG
814 QGTFVAHKEIKLTLL
817 FVAHKEIKLTLLNKA
823 IKLTLLNKAADKGSR
880 RQRGQNSKAPAAPAD
901 PQSKSSSKVTSVPGK
908 KVTSVPGKASDPGAA
918 DPGAASTKSGKASTL
921 AASTKSGKASTLSRR
936 EELLKQLKAVEDAIA

Function

No function data available.

Protein Sequence

10 MDVAESPERD 20 PHSPEDEEQP 30 QGLSDDDILR 40 DSGSDQDLDG 50 AGVRASDLED 60 EESAARGPSQ 70 EEEDNHSDEE 80 DRASEPKSQD 90 QDSEVNELSR 100 GPTSSPCEEE 110 GDEGEEDRTS 120 DLRDEASSVT 130 RELDEHELDY 140 DEEVPEEPAP 150 AVQEDEAEKA 160 GAEDDEEKGE 170 GTPREEGKAG 180 VQSVGEKESL 190 EAAKEKKKED 200 DDGEIDDGEI 210 DDDDLEEGEV 220 KDPSDRKVRP 230 RPTCRFFMKG 240 NCTWGMNCRF 250 IHPGVNDKGN 260 YSLITKADPF 270 PPNGAPPLGP 280 HPLMPANPWG 290 GPVVDEILPP 300 PPPEPPTESA 310 WERGLRHAKE 320 VLKKATIRKE 330 QEPDFEEKRF 340 TVTIGEDERE 350 FDKENEVFRD 360 WNSRIPRDVR 370 DTVLEPYADP 380 YYDYEIERFW 390 RGGQYENFRV 400 QYTETEPYHN 410 YRERERERER 420 ENRQRERERE 430 RERDRERERR 440 QRERERERER 450 ERDKERQRRK 460 EEWERERAKR 470 DEKDRQHRDR 480 DREKEREKEK 490 GKPKPRSPQP 500 PSRQAEPPKK 510 EAATTGPQVK 520 RADEWKDPWR 530 RSKSPKKKLG 540 VSVSPSRARR 550 RRKTSASSAS 560 ASNSSRSSSR 570 SSSYSGSGSS 580 RSRSRSSSYS 590 SYSSRSSRHS 600 SFSGSRSRSR 610 SFSSSPSPSP 620 TPSPHRPSIR 630 TKGEPAPPPG 640 KAGEKSVKKP 650 APPPAPPQAT 660 KTTAPVPEPT 670 KPGDPREARR 680 KERPARTPPR 690 RRTLSGSGSG 700 SGSSYSGSSS 710 RSRSLSVSSV 720 SSVSSATSSS 730 SSAHSVDSED 740 MYADLASPVS 750 SASSRSPAPA 760 QTRKEKGKSK 770 KEDGVKEEKR 780 KRDSSTQPPK 790 SAKPPAGGKS 800 SQQPSTPQQA 810 PPGQPQQGTF 820 VAHKEIKLTL 830 LNKAADKGSR 840 KRYEPSDKDR 850 QSPPPAKRPN 860 TSPDRGSRDR 870 KSGGRLGSPK 880 PERQRGQNSK 890 APAAPADRKR 900 QLSPQSKSSS 910 KVTSVPGKAS 920 DPGAASTKSG 930 KASTLSRREE 940 LLKQLKAVED 950 AIARKRAKIP GKA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:1990904 ribonucleoprotein complex
Molecular Function GO:0140262 mRNA cap binding complex binding
Molecular Function GO:0030674 protein-macromolecule adaptor activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0050779 RNA destabilization

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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] 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.

[4] 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.

[5] 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.

[6] 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.

[7] 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.