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Overview

Uniprot IDO75822
Protein NameEukaryotic translation initiation factor 3 subunit J
Gene NameEIF3J
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
117 PEEQLADKLRLKKLQ
122 ADKLRLKKLQEESDL
166 FGKLLKDKITQYEKS
224 SKAKKKKKGVVPGGG
233 VVPGGGLKATMKDDL

Function

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:25849773, PubMed:27462815). 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. 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 MAAAAAAAGD 20 SDSWDADAFS 30 VEDPVRKVGG 40 GGTAGGDRWE 50 GEDEDEDVKD 60 NWDDDDDEKK 70 EEAEVKPEVK 80 ISEKKKIAEK 90 IKEKERQQKK 100 RQEEIKKRLE 110 EPEEPKVLTP 120 EEQLADKLRL 130 KKLQEESDLE 140 LAKETFGVNN 150 AVYGIDAMNP 160 SSRDDFTEFG 170 KLLKDKITQY 180 EKSLYYASFL 190 EVLVRDVCIS 200 LEIDDLKKIT 210 NSLTVLCSEK 220 QKQEKQSKAK 230 KKKKGVVPGG 240 GLKATMKDDL 250 ADYGGYDGGY VQDYEDFM

Gene Ontology

Classification GO ID Description
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
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0003743 translation initiation factor activity
Biological Process GO:0001732 formation of cytoplasmic translation initiation complex
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] 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.