Search Results

Overview

Uniprot IDP20042
Protein NameEukaryotic translation initiation factor 2 subunit 2
Gene NameEIF2S2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
132 KKKKKNVKFPDEDEI
20 SKKKKKKKKPFMLDE
293 SPDTILQKDTRLYFL
324 GFQAVTGKRAQLRAK
79 DLNFFNQKKKKKKTK
87 KKKKKTKKIFDIDEA

Function

Component of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (PubMed:31836389). This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form the 43S pre-initiation complex (43S PIC). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF2B (By similarity)

Protein Sequence

10 MSGDEMIFDP 20 TMSKKKKKKK 30 KPFMLDEEGD 40 TQTEETQPSE 50 TKEVEPEPTE 60 DKDLEADEED 70 TRKKDASDDL 80 DDLNFFNQKK 90 KKKKTKKIFD 100 IDEAEEGVKD 110 LKIESDVQEP 120 TEPEDDLDIM 130 LGNKKKKKKN 140 VKFPDEDEIL 150 EKDEALEDED 160 NKKDDGISFS 170 NQTGPAWAGS 180 ERDYTYEELL 190 NRVFNIMREK 200 NPDMVAGEKR 210 KFVMKPPQVV 220 RVGTKKTSFV 230 NFTDICKLLH 240 RQPKHLLAFL 250 LAELGTSGSI 260 DGNNQLVIKG 270 RFQQKQIENV 280 LRRYIKEYVT 290 CHTCRSPDTI 300 LQKDTRLYFL 310 QCETCHSRCS 320 VASIKTGFQA 330 VTGKRAQLRA KAN

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005850 eukaryotic translation initiation factor 2 complex
Cellular Component GO:0045202 synapse
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0008135 translation factor activity, RNA binding
Molecular Function GO:0003743 translation initiation factor activity
Molecular Function GO:0031369 translation initiation factor binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0002183 cytoplasmic translational initiation
Biological Process GO:0001731 formation of translation preinitiation complex
Biological Process GO:0006446 regulation of translational initiation
Biological Process GO:0006413 translational initiation

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 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.

[6] 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.

[7] 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.

[8] 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.