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Overview

Uniprot IDQ99613
Protein NameEukaryotic translation initiation factor 3 subunit C
Gene NameEIF3C
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
200 AATFLKKKSEAPSGE
320 EKPKMFAKGTEITHA
331 ITHAVVIKKLNEILQ
643 IQSSGRAKELLGQGL
712 ARRRMISKQFHHQLR
877 NERVFDHKQGTYGGY
894 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 (PubMed:17581632, 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 (PubMed:17581632). 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 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 EEEEDNEGGE 310 WERVRGGVPL 320 VKEKPKMFAK 330 GTEITHAVVI 340 KKLNEILQAR 350 GKKGTDRAAQ 360 IELLQLLVQI 370 AAENNLGEGV 380 IVKIKFNIIA 390 SLYDYNPNLA 400 TYMKPEMWGK 410 CLDCINELMD 420 ILFANPNIFV 430 GENILEESEN 440 LHNADQPLRV 450 RGCILTLVER 460 MDEEFTKIMQ 470 NTDPHSQEYV 480 EHLKDEAQVC 490 AIIERVQRYL 500 EEKGTTEEVC 510 RIYLLRILHT 520 YYKFDYKAHQ 530 RQLTPPEGSS 540 KSEQDQAENE 550 GEDSAVLMER 560 LCKYIYAKDR 570 TDRIRTCAIL 580 CHIYHHALHS 590 RWYQARDLML 600 MSHLQDNIQH 610 ADPPVQILYN 620 RTMVQLGICA 630 FRQGLTKDAH 640 NALLDIQSSG 650 RAKELLGQGL 660 LLRSLQERNQ 670 EQEKVERRRQ 680 VPFHLHINLE 690 LLECVYLVSA 700 MLLEIPYMAA 710 HESDARRRMI 720 SKQFHHQLRV 730 GERQPLLGPP 740 ESMREHVVAA 750 SKAMKMGDWK 760 TCHSFIINEK 770 MNGKVWDLFP 780 EADKVRTMLV 790 RKIQEESLRT 800 YLFTYSSVYD 810 SISMETLSDM 820 FELDLPTVHS 830 IISKMIINEE 840 LMASLDQPTQ 850 TVVMHRTEPT 860 AQQNLALQLA 870 EKLGSLVENN 880 ERVFDHKQGT 890 YGGYFRDQKD 900 GYRKNEGYMR 910 RGGYRQQQSQ TAY

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:0043022 ribosome binding
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:0045727 positive regulation of translation
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] 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] 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] 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.