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Overview

Uniprot IDP60228
Protein NameEukaryotic translation initiation factor 3 subunit E
Gene NameEIF3E
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
172 ALSSLWGKLASEILM
387 LDAKIDSKLGHVVMG
407 PYQQVIEKTKSLSFR
409 QQVIEKTKSLSFRSQ
425 LAMNIEKKLNQNSRS

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). Required for nonsense-mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway (PubMed:17468741). May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins (PubMed:17310990, PubMed:17324924)

Protein Sequence

10 MAEYDLTTRI 20 AHFLDRHLVF 30 PLLEFLSVKE 40 IYNEKELLQG 50 KLDLLSDTNM 60 VDFAMDVYKN 70 LYSDDIPHAL 80 REKRTTVVAQ 90 LKQLQAETEP 100 IVKMFEDPET 110 TRQMQSTRDG 120 RMLFDYLADK 130 HGFRQEYLDT 140 LYRYAKFQYE 150 CGNYSGAAEY 160 LYFFRVLVPA 170 TDRNALSSLW 180 GKLASEILMQ 190 NWDAAMEDLT 200 RLKETIDNNS 210 VSSPLQSLQQ 220 RTWLIHWSLF 230 VFFNHPKGRD 240 NIIDLFLYQP 250 QYLNAIQTMC 260 PHILRYLTTA 270 VITNKDVRKR 280 RQVLKDLVKV 290 IQQESYTYKD 300 PITEFVECLY 310 VNFDFDGAQK 320 KLRECESVLV 330 NDFFLVACLE 340 DFIENARLFI 350 FETFCRIHQC 360 ISINMLADKL 370 NMTPEEAERW 380 IVNLIRNARL 390 DAKIDSKLGH 400 VVMGNNAVSP 410 YQQVIEKTKS 420 LSFRSQMLAM 430 NIEKKLNQNS 440 RSEAPNWATQ DSGFY

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
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:0071540 eukaryotic translation initiation factor 3 complex, eIF3e
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0016605 PML body
Cellular Component GO:0014069 postsynaptic density
Molecular Function GO:0045296 cadherin binding
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:0045947 negative regulation of translational initiation
Biological Process GO:0000184 nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
Biological Process GO:0045727 positive regulation of translation
Biological Process GO:0006446 regulation of translational initiation
Biological Process GO:0006413 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] 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] 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.