Search Results

Overview

Uniprot IDP29692
Protein NameElongation factor 1-delta
Gene NameEEF1D
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
10 TNFLAHEKIWFDKFK
117 ARLNVLEKSSPGHRA
143 RQVEPPAKKPATPAE
17 KIWFDKFKYDDAERR
188 QYAEKKAKKPALVAK
189 YAEKKAKKPALVAKS
242 PVGYGIRKLQIQCVV
59 RARENIQKSLAGSSG

Function

EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome

Protein Sequence

10 MATNFLAHEK 20 IWFDKFKYDD 30 AERRFYEQMN 40 GPVAGASRQE 50 NGASVILRDI 60 ARARENIQKS 70 LAGSSGPGAS 80 SGTSGDHGEL 90 VVRIASLEVE 100 NQSLRGVVQE 110 LQQAISKLEA 120 RLNVLEKSSP 130 GHRATAPQTQ 140 HVSPMRQVEP 150 PAKKPATPAE 160 DDEDDDIDLF 170 GSDNEEEDKE 180 AAQLREERLR 190 QYAEKKAKKP 200 ALVAKSSILL 210 DVKPWDDETD 220 MAQLEACVRS 230 IQLDGLVWGA 240 SKLVPVGYGI 250 RKLQIQCVVE 260 DDKVGTDLLE 270 EEITKFEEHV 280 QSVDIAAFNK I

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005853 eukaryotic translation elongation factor 1 complex
Cellular Component GO:0001650 fibrillar center
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0140297 DNA-binding transcription factor binding
Molecular Function GO:0005085 guanyl-nucleotide exchange factor activity
Molecular Function GO:0031072 heat shock protein binding
Molecular Function GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Function GO:0003746 translation elongation factor activity
Molecular Function GO:0008135 translation factor activity, RNA binding
Biological Process GO:0034605 cellular response to heat
Biological Process GO:0071479 cellular response to ionizing radiation
Biological Process GO:0002182 cytoplasmic translational elongation
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
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] 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.

[4] 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.

[5] 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.

[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.