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Overview

Uniprot IDQ13541
Protein NameEukaryotic translation initiation factor 4E-binding protein 1
Gene NameEIF4EBP1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
69 CRNSPVTKTPPRDLP

Function

Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways

Protein Sequence

10 MSGGSSCSQT 20 PSRAIPATRR 30 VVLGDGVQLP 40 PGDYSTTPGG 50 TLFSTTPGGT 60 RIIYDRKFLM 70 ECRNSPVTKT 80 PPRDLPTIPG 90 VTSPSSDEPP 100 MEASQSHLRN 110 SPEDKRAGGE ESQFEMDI

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005654 nucleoplasm
Molecular Function GO:0008190 eukaryotic initiation factor 4E binding
Molecular Function GO:0031369 translation initiation factor binding
Molecular Function GO:0030371 translation repressor activity
Biological Process GO:0000082 G1/S transition of mitotic cell cycle
Biological Process GO:0017148 negative regulation of translation
Biological Process GO:0045947 negative regulation of translational initiation
Biological Process GO:0045931 positive regulation of mitotic cell cycle
Biological Process GO:0031929 TOR signaling

Reference

[1] 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.

[2] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[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.