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Overview

Uniprot IDQ05639
Protein NameElongation factor 1-alpha 2
Gene NameEEF1A2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
146 LAYTLGVKQLIVGVN
179 KEVSAYIKKIGYNPA
180 EVSAYIKKIGYNPAT
219 KGWKVERKEGNASGV
244 PPTRPTDKPLRLPLQ
255 LPLQDVYKIGGIGTV
30 TTGHLIYKCGGIDKR
386 IDRRSGKKLEDNPKS
392 KKLEDNPKSLKSGDA
408 IVEMVPGKPMCVESF
41 IDKRTIEKFEKEAAE
439 TVAVGVIKNVEKKSG
44 RTIEKFEKEAAEMGK
450 KKSGGAGKVTKSAQK
453 GGAGKVTKSAQKAQK
79 TIDISLWKFETTKYY

Function

Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis. Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome (By similarity). The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond formation (By similarity)

Protein Sequence

10 MGKEKTHINI 20 VVIGHVDSGK 30 STTTGHLIYK 40 CGGIDKRTIE 50 KFEKEAAEMG 60 KGSFKYAWVL 70 DKLKAERERG 80 ITIDISLWKF 90 ETTKYYITII 100 DAPGHRDFIK 110 NMITGTSQAD 120 CAVLIVAAGV 130 GEFEAGISKN 140 GQTREHALLA 150 YTLGVKQLIV 160 GVNKMDSTEP 170 AYSEKRYDEI 180 VKEVSAYIKK 190 IGYNPATVPF 200 VPISGWHGDN 210 MLEPSPNMPW 220 FKGWKVERKE 230 GNASGVSLLE 240 ALDTILPPTR 250 PTDKPLRLPL 260 QDVYKIGGIG 270 TVPVGRVETG 280 ILRPGMVVTF 290 APVNITTEVK 300 SVEMHHEALS 310 EALPGDNVGF 320 NVKNVSVKDI 330 RRGNVCGDSK 340 SDPPQEAAQF 350 TSQVIILNHP 360 GQISAGYSPV 370 IDCHTAHIAC 380 KFAELKEKID 390 RRSGKKLEDN 400 PKSLKSGDAA 410 IVEMVPGKPM 420 CVESFSQYPP 430 LGRFAVRDMR 440 QTVAVGVIKN 450 VEKKSGGAGK 460 VTKSAQKAQK AGK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0098574 cytoplasmic side of lysosomal membrane
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0005853 eukaryotic translation elongation factor 1 complex
Cellular Component GO:0045202 synapse
Molecular Function GO:0005525 GTP binding
Molecular Function GO:0003924 GTPase activity
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0019901 protein kinase binding
Molecular Function GO:0003746 translation elongation factor activity
Molecular Function GO:0008135 translation factor activity, RNA binding
Biological Process GO:0090218 positive regulation of lipid kinase activity
Biological Process GO:1904714 regulation of chaperone-mediated autophagy
Biological Process GO:0006412 translation
Biological Process GO:0006414 translational elongation

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] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[5] 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.

[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.