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Overview

Uniprot ID	Q9Y262
Protein Name	Eukaryotic translation initiation factor 3 subunit L
Gene Name	EIF3L
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
207	YRCKTAKKSEEEIDF
267	YGRHSLYKMLGYFSL
549	FFIRQIHKFEELNRT

Function

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)

Protein Sequence

10 MSYPADDYES 20 EAAYDPYAYP 30 SDYDMHTGDP 40 KQDLAYERQY 50 EQQTYQVIPE 60 VIKNFIQYFH 70 KTVSDLIDQK 80 VYELQASRVS 90 SDVIDQKVYE 100 IQDIYENSWT 110 KLTERFFKNT 120 PWPEAEAIAP 130 QVGNDAVFLI 140 LYKELYYRHI 150 YAKVSGGPSL 160 EQRFESYYNY 170 CNLFNYILNA 180 DGPAPLELPN 190 QWLWDIIDEF 200 IYQFQSFSQY 210 RCKTAKKSEE 220 EIDFLRSNPK 230 IWNVHSVLNV 240 LHSLVDKSNI 250 NRQLEVYTSG 260 GDPESVAGEY 270 GRHSLYKMLG 280 YFSLVGLLRL 290 HSLLGDYYQA 300 IKVLENIELN 310 KKSMYSRVPE 320 CQVTTYYYVG 330 FAYLMMRRYQ 340 DAIRVFANIL 350 LYIQRTKSMF 360 QRTTYKYEMI 370 NKQNEQMHAL 380 LAIALTMYPM 390 RIDESIHLQL 400 REKYGDKMLR 410 MQKGDPQVYE 420 ELFSYSCPKF 430 LSPVVPNYDN 440 VHPNYHKEPF 450 LQQLKVFSDE 460 VQQQAQLSTI 470 RSFLKLYTTM 480 PVAKLAGFLD 490 LTEQEFRIQL 500 LVFKHKMKNL 510 VWTSGISALD 520 GEFQSASEVD 530 FYIDKDMIHI 540 ADTKVARRYG 550 DFFIRQIHKF 560 EELNRTLKKM GQRP

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005829	cytosol
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
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:0001650	fibrillar center
Cellular Component	GO:0016020	membrane
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0045202	synapse

Reference

[1] 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.

[2] 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.

[3] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[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.