Search Results

Overview

Uniprot IDP60842
Protein NameEukaryotic initiation factor 4A-I
Gene NameEIF4A1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
146 NVRAEVQKLQMEAPH
174 NRRYLSPKYIKMFVL
193 EMLSRGFKDQIYDIF
238 PIRILVKKEELTLEG
284 IFINTRRKVDWLTEK
291 KVDWLTEKMHARDFT
309 MHGDMDQKERDVIMR
54 IYAYGFEKPSAIQQR

Function

ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome (PubMed:20156963). In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon. As a result, promotes cell proliferation and growth (PubMed:20156963)

Protein Sequence

10 MSASQDSRSR 20 DNGPDGMEPE 30 GVIESNWNEI 40 VDSFDDMNLS 50 ESLLRGIYAY 60 GFEKPSAIQQ 70 RAILPCIKGY 80 DVIAQAQSGT 90 GKTATFAISI 100 LQQIELDLKA 110 TQALVLAPTR 120 ELAQQIQKVV 130 MALGDYMGAS 140 CHACIGGTNV 150 RAEVQKLQME 160 APHIIVGTPG 170 RVFDMLNRRY 180 LSPKYIKMFV 190 LDEADEMLSR 200 GFKDQIYDIF 210 QKLNSNTQVV 220 LLSATMPSDV 230 LEVTKKFMRD 240 PIRILVKKEE 250 LTLEGIRQFY 260 INVEREEWKL 270 DTLCDLYETL 280 TITQAVIFIN 290 TRRKVDWLTE 300 KMHARDFTVS 310 AMHGDMDQKE 320 RDVIMREFRS 330 GSSRVLITTD 340 LLARGIDVQQ 350 VSLVINYDLP 360 TNRENYIHRI 370 GRGGRFGRKG 380 VAINMVTEED 390 KRTLRDIETF 400 YNTSIEEMPL NVADLI

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0010494 cytoplasmic stress granule
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016281 eukaryotic translation initiation factor 4F complex
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0097165 nuclear stress granule
Cellular Component GO:0048471 perinuclear region of cytoplasm
Cellular Component GO:0005886 plasma membrane
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0003725 double-stranded RNA binding
Molecular Function GO:0004386 helicase activity
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0000339 RNA cap binding
Molecular Function GO:0003724 RNA helicase activity
Molecular Function GO:0008135 translation factor activity, RNA binding
Molecular Function GO:0003743 translation initiation factor activity
Biological Process GO:0002183 cytoplasmic translational initiation
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
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] 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.