Search Results

Overview

Uniprot IDO60841
Protein NameEukaryotic translation initiation factor 5B
Gene NameEIF5B
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
275 KQKESQRKFEEETVK
284 EEETVKSKVTVDTGV
342 GPSKATVKAMQEALA
424 ARAEATLKLLQAQGV
436 QGVEVPSKDSLPKKR
453 YEDKKRKKIPQQLES
50 KKKKEKKKQDFDEDD

Function

Plays a role in translation initiation (PubMed:10659855, PubMed:35732735). Ribosome-dependent GTPase that promotes the joining of the 60S ribosomal subunit to the pre-initiation complex to form the 80S initiation complex with the initiator methionine-tRNA in the P-site base paired to the start codon (PubMed:10659855, PubMed:35732735). Together with eIF1A (EIF1AX), actively orients the initiator methionine-tRNA in a conformation that allows 60S ribosomal subunit joining to form the 80S initiation complex (PubMed:12569173, PubMed:35732735). Is released after formation of the 80S initiation complex (PubMed:35732735). Its GTPase activity is not essential for ribosomal subunits joining, but GTP hydrolysis is needed for eIF1A (EIF1AX) ejection quickly followed by EIF5B release to form elongation-competent ribosomes (PubMed:10659855, PubMed:35732735). In contrast to its procaryotic homolog, does not promote recruitment of Met-rRNA to the small ribosomal subunit (PubMed:10659855)

Protein Sequence

10 MGKKQKNKSE 20 DSTKDDIDLD 30 ALAAEIEGAG 40 AAKEQEPQKS 50 KGKKKKEKKK 60 QDFDEDDILK 70 ELEELSLEAQ 80 GIKADRETVA 90 VKPTENNEEE 100 FTSKDKKKKG 110 QKGKKQSFDD 120 NDSEELEDKD 130 SKSKKTAKPK 140 VEMYSGSDDD 150 DDFNKLPKKA 160 KGKAQKSNKK 170 WDGSEEDEDN 180 SKKIKERSRI 190 NSSGESGDES 200 DEFLQSRKGQ 210 KKNQKNKPGP 220 NIESGNEDDD 230 ASFKIKTVAQ 240 KKAEKKERER 250 KKRDEEKAKL 260 RKLKEKEELE 270 TGKKDQSKQK 280 ESQRKFEEET 290 VKSKVTVDTG 300 VIPASEEKAE 310 TPTAAEDDNE 320 GDKKKKDKKK 330 KKGEKEEKEK 340 EKKKGPSKAT 350 VKAMQEALAK 360 LKEEEERQKR 370 EEEERIKRLE 380 ELEAKRKEEE 390 RLEQEKRERK 400 KQKEKERKER 410 LKKEGKLLTK 420 SQREARARAE 430 ATLKLLQAQG 440 VEVPSKDSLP 450 KKRPIYEDKK 460 RKKIPQQLES 470 KEVSESMELC 480 AAVEVMEQGV 490 PEKEETPPPV 500 EPEEEEDTED 510 AGLDDWEAMA 520 SDEETEKVEG 530 NKVHIEVKEN 540 PEEEEEEEEE 550 EEEDEESEEE 560 EEEEGESEGS 570 EGDEEDEKVS 580 DEKDSGKTLD 590 KKPSKEMSSD 600 SEYDSDDDRT 610 KEERAYDKAK 620 RRIEKRRLEH 630 SKNVNTEKLR 640 APIICVLGHV 650 DTGKTKILDK 660 LRHTHVQDGE 670 AGGITQQIGA 680 TNVPLEAINE 690 QTKMIKNFDR 700 ENVRIPGMLI 710 IDTPGHESFS 720 NLRNRGSSLC 730 DIAILVVDIM 740 HGLEPQTIES 750 INLLKSKKCP 760 FIVALNKIDR 770 LYDWKKSPDS 780 DVAATLKKQK 790 KNTKDEFEER 800 AKAIIVEFAQ 810 QGLNAALFYE 820 NKDPRTFVSL 830 VPTSAHTGDG 840 MGSLIYLLVE 850 LTQTMLSKRL 860 AHCEELRAQV 870 MEVKALPGMG 880 TTIDVILING 890 RLKEGDTIIV 900 PGVEGPIVTQ 910 IRGLLLPPPM 920 KELRVKNQYE 930 KHKEVEAAQG 940 VKILGKDLEK 950 TLAGLPLLVA 960 YKEDEIPVLK 970 DELIHELKQT 980 LNAIKLEEKG 990 VYVQASTLGS 1000 LEALLEFLKT 1010 SEVPYAGINI 1020 GPVHKKDVMK 1030 ASVMLEHDPQ 1040 YAVILAFDVR 1050 IERDAQEMAD 1060 SLGVRIFSAE 1070 IIYHLFDAFT 1080 KYRQDYKKQK 1090 QEEFKHIAVF 1100 PCKIKILPQY 1110 IFNSRDPIVM 1120 GVTVEAGQVK 1130 QGTPMCVPSK 1140 NFVDIGIVTS 1150 IEINHKQVDV 1160 AKKGQEVCVK 1170 IEPIPGESPK 1180 MFGRHFEATD 1190 ILVSKISRQS 1200 IDALKDWFRD 1210 EMQKSDWQLI 1220 VELKKVFEII

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0045202 synapse
Molecular Function GO:0005525 GTP binding
Molecular Function GO:0003924 GTPase activity
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003743 translation initiation factor activity
Molecular Function GO:0000049 tRNA binding
Biological Process GO:0006446 regulation of translational initiation
Biological Process GO:0042255 ribosome assembly
Biological Process GO:0006413 translational initiation

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 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.

[3] 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.

[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.