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Overview

Uniprot IDB5ME19
Protein NameEukaryotic translation initiation factor 3 subunit C-like protein
Gene NameEIF3CL
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
321 EKPKMFAKGTEITHA
333 THAVVIKKLNEILQA
644 IQSSGRAKELLGQGL
713 ARRRMISKQFHHQLR
783 VRTMLVRKIQEESLR
895 DQKDGYRKNEGYMRR
99 KAKSIVDKEGVPRFY

Function

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. 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

Protein Sequence

10 MSRFFTTGSD 20 SESESSLSGE 30 ELVTKPVGGN 40 YGKQPLLLSE 50 DEEDTKRVVR 60 SAKDKRFEEL 70 TNLIRTIRNA 80 MKIRDVTKCL 90 EEFELLGKAY 100 GKAKSIVDKE 110 GVPRFYIRIL 120 ADLEDYLNEL 130 WEDKEGKKKM 140 NKNNAKALST 150 LRQKIRKYNR 160 DFESHITSYK 170 QNPEQSADED 180 AEKNEEDSEG 190 SSDEDEDEDG 200 VSAATFLKKK 210 SEAPSGESRK 220 FLKKMDDEDE 230 DSEDSEDDED 240 WDTGSTSSDS 250 DSEEEEGKQT 260 ALASRFLKKA 270 PTTDEDKKAA 280 EKKREDKAKK 290 KHDRKSKRLD 300 EEEEEDNEGG 310 EWERVRGGVP 320 LVKEKPKMFA 330 KGTEITHAVV 340 IKKLNEILQA 350 RGKKGTDRAA 360 QIELLQLLVQ 370 IAAENNLGEG 380 VIVKIKFNII 390 ASLYDYNPNL 400 ATYMKPEMWG 410 KCLDCINELM 420 DILFANPNIF 430 VGENILEESE 440 NLHNADQPLR 450 VRGCILTLVE 460 RMDEEFTKIM 470 QNTDPHSQEY 480 VEHLKDEAQV 490 CAIIERVQRY 500 LEEKGTTEEV 510 CRIYLLRILH 520 TYYKFDYKAH 530 QRQLTPPEGS 540 SKSEQDQAEN 550 EGEDSAVLME 560 RLCKYIYAKD 570 RTDRIRTCAI 580 LCHIYHHALH 590 SRWYQARDLM 600 LMSHLQDNIQ 610 HADPPVQILY 620 NRTMVQLGIC 630 AFRQGLTKDA 640 HNALLDIQSS 650 GRAKELLGQG 660 LLLRSLQERN 670 QEQEKVERRR 680 QVPFHLHINL 690 ELLECVYLVS 700 AMLLEIPYMA 710 AHESDARRRM 720 ISKQFHHQLR 730 VGERQPLLGP 740 PESMREHVVA 750 ASKAMKMGDW 760 KTCHSFIINE 770 KMNGKVWDLF 780 PEADKVRTML 790 VRKIQEESLR 800 TYLFTYSSVY 810 DSISMETLSD 820 MFELDLPTVH 830 SIISKMIINE 840 ELMASLDQPT 850 QTVVMHRTEP 860 TAQQNLALQL 870 AEKLGSLVEN 880 NERVFDHKQG 890 TYGGYFRDQK 900 DGYRKNEGYM 910 RRGGYRQQQS QTAY

Gene Ontology

Classification GO ID Description
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: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:0006413 translational initiation

Reference

[1] 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.

[2] 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.

[3] 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.