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Overview

Uniprot IDP55884
Protein NameEukaryotic translation initiation factor 3 subunit B
Gene NameEIF3B
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
257 ADGYKLDKQHTFRVN
535 VKVDRTPKGTQGVVT
729 KDLKKYSKIFEQKDR
744 LSQSKASKELVERRR

Function

RNA-binding 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, PubMed:9388245). 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, PubMed:9388245). 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)

Protein Sequence

10 MQDAENVAVP 20 EAAEERAEPG 30 QQQPAAEPPP 40 AEGLLRPAGP 50 GAPEAAGTEA 60 SSEEVGIAEA 70 GPESEVRTEP 80 AAEAEAASGP 90 SESPSPPAAE 100 ELPGSHAEPP 110 VPAQGEAPGE 120 QARDERSDSR 130 AQAVSEDAGG 140 NEGRAAEAEP 150 RALENGDADE 160 PSFSDPEDFV 170 DDVSEEELLG 180 DVLKDRPQEA 190 DGIDSVIVVD 200 NVPQVGPDRL 210 EKLKNVIHKI 220 FSKFGKITND 230 FYPEEDGKTK 240 GYIFLEYASP 250 AHAVDAVKNA 260 DGYKLDKQHT 270 FRVNLFTDFD 280 KYMTISDEWD 290 IPEKQPFKDL 300 GNLRYWLEEA 310 ECRDQYSVIF 320 ESGDRTSIFW 330 NDVKDPVSIE 340 ERARWTETYV 350 RWSPKGTYLA 360 TFHQRGIALW 370 GGEKFKQIQR 380 FSHQGVQLID 390 FSPCERYLVT 400 FSPLMDTQDD 410 PQAIIIWDIL 420 TGHKKRGFHC 430 ESSAHWPIFK 440 WSHDGKFFAR 450 MTLDTLSIYE 460 TPSMGLLDKK 470 SLKISGIKDF 480 SWSPGGNIIA 490 FWVPEDKDIP 500 ARVTLMQLPT 510 RQEIRVRNLF 520 NVVDCKLHWQ 530 KNGDYLCVKV 540 DRTPKGTQGV 550 VTNFEIFRMR 560 EKQVPVDVVE 570 MKETIIAFAW 580 EPNGSKFAVL 590 HGEAPRISVS 600 FYHVKNNGKI 610 ELIKMFDKQQ 620 ANTIFWSPQG 630 QFVVLAGLRS 640 MNGALAFVDT 650 SDCTVMNIAE 660 HYMASDVEWD 670 PTGRYVVTSV 680 SWWSHKVDNA 690 YWLWTFQGRL 700 LQKNNKDRFC 710 QLLWRPRPPT 720 LLSQEQIKQI 730 KKDLKKYSKI 740 FEQKDRLSQS 750 KASKELVERR 760 RTMMEDFRKY 770 RKMAQELYME 780 QKNERLELRG 790 GVDTDELDSN 800 VDDWEEETIE 810 FFVTEEIIPL GNQE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0010494 cytoplasmic stress granule
Biological Process GO:0006413 translational initiation
Biological Process GO:0075525 viral translational termination-reinitiation
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:0071541 eukaryotic translation initiation factor 3 complex, eIF3m
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0045202 synapse
Molecular Function GO:0060090 molecular adaptor activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003743 translation initiation factor activity
Molecular Function GO:0031369 translation initiation factor binding
Biological Process GO:0001732 formation of cytoplasmic translation initiation complex
Biological Process GO:0075522 IRES-dependent viral translational initiation
Biological Process GO:0006446 regulation of 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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[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.