Search Results

Overview

Uniprot IDP13639
Protein NameElongation factor 2
Gene NameEEF2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
152 QAIAERIKPVLMMNK
16 IRAIMDKKANIRNMS
239 YVAKFAAKGEGQLGP
272 YFDPANGKFSKSATS
275 PANGKFSKSATSPEG
283 SATSPEGKKLPRTFC
308 FDAIMNFKKEETAKL
309 DAIMNFKKEETAKLI
318 ETAKLIEKLDIKLDS
32 IAHVDHGKSTLTDSL
322 LIEKLDIKLDSEDKD
330 LDSEDKDKEGKPLLK
337 KEGKPLLKAVMRRWL
42 LTDSLVCKAGIIASA
426 GLVSTGLKVRIMGPN
438 GPNYTPGKKEDLYLK
439 PNYTPGKKEDLYLKP
445 KKEDLYLKPIQRTIL
498 AHNMRVMKFSVSPVV
512 VRVAVEAKNPADLPK
571 DHACIPIKKSDPVVS
572 HACIPIKKSDPVVSY
594 SNVLCLSKSPNKHNR
638 RARYLAEKYEWDVAE
648 WDVAEARKIWCFGPD

Function

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation (PubMed:26593721). During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively (PubMed:26593721). Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (PubMed:26593721)

Protein Sequence

10 MVNFTVDQIR 20 AIMDKKANIR 30 NMSVIAHVDH 40 GKSTLTDSLV 50 CKAGIIASAR 60 AGETRFTDTR 70 KDEQERCITI 80 KSTAISLFYE 90 LSENDLNFIK 100 QSKDGAGFLI 110 NLIDSPGHVD 120 FSSEVTAALR 130 VTDGALVVVD 140 CVSGVCVQTE 150 TVLRQAIAER 160 IKPVLMMNKM 170 DRALLELQLE 180 PEELYQTFQR 190 IVENVNVIIS 200 TYGEGESGPM 210 GNIMIDPVLG 220 TVGFGSGLHG 230 WAFTLKQFAE 240 MYVAKFAAKG 250 EGQLGPAERA 260 KKVEDMMKKL 270 WGDRYFDPAN 280 GKFSKSATSP 290 EGKKLPRTFC 300 QLILDPIFKV 310 FDAIMNFKKE 320 ETAKLIEKLD 330 IKLDSEDKDK 340 EGKPLLKAVM 350 RRWLPAGDAL 360 LQMITIHLPS 370 PVTAQKYRCE 380 LLYEGPPDDE 390 AAMGIKSCDP 400 KGPLMMYISK 410 MVPTSDKGRF 420 YAFGRVFSGL 430 VSTGLKVRIM 440 GPNYTPGKKE 450 DLYLKPIQRT 460 ILMMGRYVEP 470 IEDVPCGNIV 480 GLVGVDQFLV 490 KTGTITTFEH 500 AHNMRVMKFS 510 VSPVVRVAVE 520 AKNPADLPKL 530 VEGLKRLAKS 540 DPMVQCIIEE 550 SGEHIIAGAG 560 ELHLEICLKD 570 LEEDHACIPI 580 KKSDPVVSYR 590 ETVSEESNVL 600 CLSKSPNKHN 610 RLYMKARPFP 620 DGLAEDIDKG 630 EVSARQELKQ 640 RARYLAEKYE 650 WDVAEARKIW 660 CFGPDGTGPN 670 ILTDITKGVQ 680 YLNEIKDSVV 690 AGFQWATKEG 700 ALCEENMRGV 710 RFDVHDVTLH 720 ADAIHRGGGQ 730 IIPTARRCLY 740 ASVLTAQPRL 750 MEPIYLVEIQ 760 CPEQVVGGIY 770 GVLNRKRGHV 780 FEESQVAGTP 790 MFVVKAYLPV 800 NESFGFTADL 810 RSNTGGQAFP 820 QCVFDHWQIL 830 PGDPFDNSSR 840 PSQVVAETRK 850 RKGLKEGIPA LDNFLDKL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:1904813 ficolin-1-rich granule lumen
Cellular Component GO:0098978 glutamatergic synapse
Cellular Component GO:0016020 membrane
Cellular Component GO:0005634 nucleus
Cellular Component GO:0098794 postsynapse
Cellular Component GO:1990904 ribonucleoprotein complex
Cellular Component GO:0005840 ribosome
Cellular Component GO:0034774 secretory granule lumen
Molecular Function GO:0008097 5S rRNA binding
Molecular Function GO:0051015 actin filament binding
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0005525 GTP binding
Molecular Function GO:0003924 GTPase activity
Molecular Function GO:0106222 lncRNA binding
Molecular Function GO:0002039 p53 binding
Molecular Function GO:0019901 protein kinase binding
Molecular Function GO:0043022 ribosome binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003746 translation elongation factor activity
Biological Process GO:1990416 cellular response to brain-derived neurotrophic factor stimulus
Biological Process GO:0014009 glial cell proliferation
Biological Process GO:2000767 positive regulation of cytoplasmic translation
Biological Process GO:0045727 positive regulation of translation
Biological Process GO:0034976 response to endoplasmic reticulum stress
Biological Process GO:0032355 response to estradiol
Biological Process GO:0045471 response to ethanol
Biological Process GO:0051593 response to folic acid
Biological Process GO:0042542 response to hydrogen peroxide
Biological Process GO:0002931 response to ischemia
Biological Process GO:0009410 response to xenobiotic stimulus
Biological Process GO:0035914 skeletal muscle cell differentiation
Biological Process GO:0003009 skeletal muscle contraction
Biological Process GO:0140242 translation at postsynapse
Biological Process GO:0006414 translational elongation

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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[5] 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.

[6] 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.

[7] 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.

[8] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[9] 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.

[10] 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.

[11] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[12] 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.