Search Results

Overview

Uniprot IDP63241
Protein NameEukaryotic translation initiation factor 5A-1
Gene NameEIF5A
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
121 LPEGDLGKEIEQKYD
126 LGKEIEQKYDCGEEI
34 KNGFVVLKGRPCKIV
39 VLKGRPCKIVEMSTS
47 IVEMSTSKTGKHGHA
67 GIDIFTGKKYEDICP
68 IDIFTGKKYEDICPS
85 NMDVPNIKRNDFQLI

Function

Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (PubMed:33547280). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome (By similarity). Acts as a ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step (By similarity). Also involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity (PubMed:16987817). With syntenin SDCBP, functions as a regulator of p53/TP53 and p53/TP53-dependent apoptosis (PubMed:15371445). Also regulates TNF-mediated apoptosis (PubMed:15452064, PubMed:17187778). Mediates effects of polyamines on neuronal process extension and survival (PubMed:17360499). Is required for autophagy by assisting the ribosome in translating the ATG3 protein at a specific amino acid sequence, the 'ASP-ASP-Gly' motif, leading to the increase of the efficiency of ATG3 translation and facilitation of LC3B lipidation and autophagosome formation (PubMed:29712776)

Protein Sequence

10 MADDLDFETG 20 DAGASATFPM 30 QCSALRKNGF 40 VVLKGRPCKI 50 VEMSTSKTGK 60 HGHAKVHLVG 70 IDIFTGKKYE 80 DICPSTHNMD 90 VPNIKRNDFQ 100 LIGIQDGYLS 110 LLQDSGEVRE 120 DLRLPEGDLG 130 KEIEQKYDCG 140 EEILITVLSA 150 MTEEAAVAIK AMAK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005642 annulate lamellae
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0016020 membrane
Cellular Component GO:0005643 nuclear pore
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0045202 synapse
Molecular Function GO:0043022 ribosome binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003746 translation elongation factor activity
Molecular Function GO:0017070 U6 snRNA binding
Biological Process GO:0098586 cellular response to virus
Biological Process GO:1902255 positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0045901 positive regulation of translational elongation
Biological Process GO:0006414 translational elongation
Biological Process GO:0033209 tumor necrosis factor-mediated signaling pathway

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] 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.

[5] 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.

[6] 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.