Search Results

Overview

Uniprot IDP55010
Protein NameEukaryotic translation initiation factor 5
Gene NameEIF5
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
114 TDLHVNPKKQTIGNS
115 DLHVNPKKQTIGNSC
28 LIAKVEGKGNGIKTV
33 EGKGNGIKTVIVNMV
413 SKAASVPKVETVKSD

Function

Component of the 43S pre-initiation complex (43S PIC), which binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated region, and locates the initiation codon (PubMed:11166181, PubMed:22813744, PubMed:24319994). In this complex, acts as a GTPase-activating protein, by promoting GTP hydrolysis by eIF2G (EIF2S3) (PubMed:11166181). During scanning, interacts with both EIF1 (via its C-terminal domain (CTD)) and EIF1A (via its NTD) (PubMed:22813744). This interaction with EIF1A contributes to the maintenance of EIF1 within the open 43S PIC (PubMed:24319994). When start codon is recognized, EIF5, via its NTD, induces eIF2G (EIF2S3) to hydrolyze the GTP (PubMed:11166181). Start codon recognition also induces a conformational change of the PIC to a closed state (PubMed:22813744). This change increases the affinity of EIF5-CTD for EIF2-beta (EIF2S2), which allows the release, by an indirect mechanism, of EIF1 from the PIC (PubMed:22813744). Finally, EIF5 stabilizes the PIC in its closed conformation (PubMed:22813744)

Protein Sequence

10 MSVNVNRSVS 20 DQFYRYKMPR 30 LIAKVEGKGN 40 GIKTVIVNMV 50 DVAKALNRPP 60 TYPTKYFGCE 70 LGAQTQFDVK 80 NDRYIVNGSH 90 EANKLQDMLD 100 GFIKKFVLCP 110 ECENPETDLH 120 VNPKKQTIGN 130 SCKACGYRGM 140 LDTHHKLCTF 150 ILKNPPENSD 160 SGTGKKEKEK 170 KNRKGKDKEN 180 GSVSSSETPP 190 PPPPPNEINP 200 PPHTMEEEED 210 DDWGEDTTEE 220 AQRRRMDEIS 230 DHAKVLTLSD 240 DLERTIEERV 250 NILFDFVKKK 260 KEEGVIDSSD 270 KEIVAEAERL 280 DVKAMGPLVL 290 TEVLFNEKIR 300 EQIKKYRRHF 310 LRFCHNNKKA 320 QRYLLHGLEC 330 VVAMHQAQLI 340 SKIPHILKEM 350 YDADLLEEEV 360 IISWSEKASK 370 KYVSKELAKE 380 IRVKAEPFIK 390 WLKEAEEESS 400 GGEEEDEDEN 410 IEVVYSKAAS 420 VPKVETVKSD 430 NKDDDIDIDA I

Gene Ontology

Classification GO ID Description
Biological Process GO:0006446 regulation of translational initiation
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0045202 synapse
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0071074 eukaryotic initiation factor eIF2 binding
Molecular Function GO:0005092 GDP-dissociation inhibitor activity
Molecular Function GO:0005525 GTP binding
Molecular Function GO:0005096 GTPase activator activity
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:0042255 ribosome assembly

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] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[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.