Search Results

Overview

Uniprot IDO15371
Protein NameEukaryotic translation initiation factor 3 subunit D
Gene NameEIF3D
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
142 RLQKKFQKQFGVRQK
35 MPYQPFSKGDRLGKV
41 SKGDRLGKVADWTGA
53 TGATYQDKRYTNKYS
90 VDTARTQKTAYQRNR

Function

mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs (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:18599441, PubMed:25849773). 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). In the eIF-3 complex, EIF3D specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs (PubMed:27462815)

Protein Sequence

10 MAKFMTPVIQ 20 DNPSGWGPCA 30 VPEQFRDMPY 40 QPFSKGDRLG 50 KVADWTGATY 60 QDKRYTNKYS 70 SQFGGGSQYA 80 YFHEEDESSF 90 QLVDTARTQK 100 TAYQRNRMRF 110 AQRNLRRDKD 120 RRNMLQFNLQ 130 ILPKSAKQKE 140 RERIRLQKKF 150 QKQFGVRQKW 160 DQKSQKPRDS 170 SVEVRSDWEV 180 KEEMDFPQLM 190 KMRYLEVSEP 200 QDIECCGALE 210 YYDKAFDRIT 220 TRSEKPLRSI 230 KRIFHTVTTT 240 DDPVIRKLAK 250 TQGNVFATDA 260 ILATLMSCTR 270 SVYSWDIVVQ 280 RVGSKLFFDK 290 RDNSDFDLLT 300 VSETANEPPQ 310 DEGNSFNSPR 320 NLAMEATYIN 330 HNFSQQCLRM 340 GKERYNFPNP 350 NPFVEDDMDK 360 NEIASVAYRY 370 RRWKLGDDID 380 LIVRCEHDGV 390 MTGANGEVSF 400 INIKTLNEWD 410 SRHCNGVDWR 420 QKLDSQRGAV 430 IATELKNNSY 440 KLARWTCCAL 450 LAGSEYLKLG 460 YVSRYHVKDS 470 SRHVILGTQQ 480 FKPNEFASQI 490 NLSVENAWGI 500 LRCVIDICMK 510 LEEGKYLILK 520 DPNKQVIRVY 530 SLPDGTFSSD 540 EDEEEEEEEE EEEEEEET

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
Cellular Component GO:0071541 eukaryotic translation initiation factor 3 complex, eIF3m
Cellular Component GO:0016020 membrane
Cellular Component GO:0045202 synapse
Molecular Function GO:0098808 mRNA cap binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003743 translation initiation factor activity
Biological Process GO:0002191 cap-dependent translational initiation
Biological Process GO:0001732 formation of cytoplasmic translation initiation complex
Biological Process GO:0075522 IRES-dependent viral translational initiation
Biological Process GO:0006413 translational initiation
Biological Process GO:0075525 viral translational termination-reinitiation

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] 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.

[4] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[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.