Search Results

Overview

Uniprot IDP23588
Protein NameEukaryotic translation initiation factor 4B
Gene NameEIF4B
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
13 KKKNKKGKTISLTDF
177 VADQAQDKDRDDRSF
194 DRNRDSDKTDTDWRA
223 GDDSFGDKYRDRYDS
333 RGPPQRPKLNLKPRS
343 LKPRSTPKEDDSSAS
365 ASIFGGAKPVDTAAR
395 QRQLDEPKLERRPRE
480 VMPAPPPKENAWVKR
486 PKENAWVKRSSNPPA
511 SPTSGGGKVAPAQPS
537 VDGMNAPKGQTGNSS
577 SRSAPEPKKPEENPA
586 PEENPASKFSSASKY

Function

Required for the binding of mRNA to ribosomes. Functions in close association with EIF4-F and EIF4-A. Binds near the 5'-terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F

Protein Sequence

10 MAASAKKKNK 20 KGKTISLTDF 30 LAEDGGTGGG 40 STYVSKPVSW 50 ADETDDLEGD 60 VSTTWHSNDD 70 DVYRAPPIDR 80 SILPTAPRAA 90 REPNIDRSRL 100 PKSPPYTAFL 110 GNLPYDVTEE 120 SIKEFFRGLN 130 ISAVRLPREP 140 SNPERLKGFG 150 YAEFEDLDSL 160 LSALSLNEES 170 LGNRRIRVDV 180 ADQAQDKDRD 190 DRSFGRDRNR 200 DSDKTDTDWR 210 ARPATDSFDD 220 YPPRRGDDSF 230 GDKYRDRYDS 240 DRYRDGYRDG 250 YRDGPRRDMD 260 RYGGRDRYDD 270 RGSRDYDRGY 280 DSRIGSGRRA 290 FGSGYRRDDD 300 YRGGGDRYED 310 RYDRRDDRSW 320 SSRDDYSRDD 330 YRRDDRGPPQ 340 RPKLNLKPRS 350 TPKEDDSSAS 360 TSQSTRAASI 370 FGGAKPVDTA 380 AREREVEERL 390 QKEQEKLQRQ 400 LDEPKLERRP 410 RERHPSWRSE 420 ETQERERSRT 430 GSESSQTGTS 440 TTSSRNARRR 450 ESEKSLENET 460 LNKEEDCHSP 470 TSKPPKPDQP 480 LKVMPAPPPK 490 ENAWVKRSSN 500 PPARSQSSDT 510 EQQSPTSGGG 520 KVAPAQPSEE 530 GPGRKDENKV 540 DGMNAPKGQT 550 GNSSRGPGDG 560 GNRDHWKESD 570 RKDGKKDQDS 580 RSAPEPKKPE 590 ENPASKFSSA 600 SKYAALSVDG 610 EDENEGEDYA E

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016281 eukaryotic translation initiation factor 4F complex
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003743 translation initiation factor activity
Biological Process GO:0006446 regulation of translational initiation

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] 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.

[4] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[5] 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.

[6] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[7] 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.

[8] 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.

[9] 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.

[10] 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.