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Overview

Uniprot ID	O75821
Protein Name	Eukaryotic translation initiation factor 3 subunit G
Gene Name	EIF3G
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
148	EEEDPMNKLKGQKIV
153	MNKLKGQKIVSCRIC
193	LGLSTGEKEKLPGEL
195	LSTGEKEKLPGELEP
209	PVQATQNKTGKYVPP
212	ATQNKTGKYVPPSLR
24	EEEGEDDKCVTSELL

Function

RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). This subunit can bind 18S rRNA

Protein Sequence

10 MPTGDFDSKP 20 SWADQVEEEG 30 EDDKCVTSEL 40 LKGIPLATGD 50 TSPEPELLPG 60 APLPPPKEVI 70 NGNIKTVTEY 80 KIDEDGKKFK 90 IVRTFRIETR 100 KASKAVARRK 110 NWKKFGNSEF 120 DPPGPNVATT 130 TVSDDVSMTF 140 ITSKEDLNCQ 150 EEEDPMNKLK 160 GQKIVSCRIC 170 KGDHWTTRCP 180 YKDTLGPMQK 190 ELAEQLGLST 200 GEKEKLPGEL 210 EPVQATQNKT 220 GKYVPPSLRD 230 GASRRGESMQ 240 PNRRADDNAT 250 IRVTNLSEDT 260 RETDLQELFR 270 PFGSISRIYL 280 AKDKTTGQSK 290 GFAFISFHRR 300 EDAARAIAGV 310 SGFGYDHLIL 320 NVEWAKPSTN

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0016282	eukaryotic 43S preinitiation complex
Cellular Component	GO:0033290	eukaryotic 48S preinitiation complex
Cellular Component	GO:0005852	eukaryotic translation initiation factor 3 complex
Cellular Component	GO:0048471	perinuclear region of cytoplasm
Molecular Function	GO:0003723	RNA binding
Molecular Function	GO:0003743	translation initiation factor activity
Biological Process	GO:0001732	formation of cytoplasmic translation initiation complex
Biological Process	GO:0006413	translational initiation
Biological Process	GO:0075525	viral translational termination-reinitiation

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] 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.