Search Results

Overview

Uniprot IDP68104
Protein NameElongation factor 1-alpha 1
Gene NameEEF1A1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
146 LAYTLGVKQLIVGVN
165 TEPPYSQKRYEEIVK
172 KRYEEIVKEVSTYIK
179 KEVSTYIKKIGYNPD
180 EVSTYIKKIGYNPDT
20 IGHVDSGKSTTTGHL
219 KGWKVTRKDGNASGT
244 PPTRPTDKPLRLPLQ
255 LPLQDVYKIGGIGTV
273 RVETGVLKPGMVVTF
385 KIDRRSGKKLEDGPK
386 IDRRSGKKLEDGPKF
392 KKLEDGPKFLKSGDA
395 EDGPKFLKSGDAAIV
408 IVDMVPGKPMCVESF
41 IDKRTIEKFEKEAAE
439 TVAVGVIKAVDKKAA
44 RTIEKFEKEAAEMGK
450 KKAAGAGKVTKSAQK
453 AGAGKVTKSAQKAQK
457 KVTKSAQKAQKAK**
5 ***MGKEKTHINIVV
79 TIDISLWKFETSKYY

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 (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). 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 (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). 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 (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623). Also plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1 (PubMed:17177976). Also plays a role in cytoskeleton organization by promoting actin bundling (By similarity)

Protein Sequence

10 MGKEKTHINI 20 VVIGHVDSGK 30 STTTGHLIYK 40 CGGIDKRTIE 50 KFEKEAAEMG 60 KGSFKYAWVL 70 DKLKAERERG 80 ITIDISLWKF 90 ETSKYYVTII 100 DAPGHRDFIK 110 NMITGTSQAD 120 CAVLIVAAGV 130 GEFEAGISKN 140 GQTREHALLA 150 YTLGVKQLIV 160 GVNKMDSTEP 170 PYSQKRYEEI 180 VKEVSTYIKK 190 IGYNPDTVAF 200 VPISGWNGDN 210 MLEPSANMPW 220 FKGWKVTRKD 230 GNASGTTLLE 240 ALDCILPPTR 250 PTDKPLRLPL 260 QDVYKIGGIG 270 TVPVGRVETG 280 VLKPGMVVTF 290 APVNVTTEVK 300 SVEMHHEALS 310 EALPGDNVGF 320 NVKNVSVKDV 330 RRGNVAGDSK 340 NDPPMEAAGF 350 TAQVIILNHP 360 GQISAGYAPV 370 LDCHTAHIAC 380 KFAELKEKID 390 RRSGKKLEDG 400 PKFLKSGDAA 410 IVDMVPGKPM 420 CVESFSDYPP 430 LGRFAVRDMR 440 QTVAVGVIKA 450 VDKKAAGAGK 460 VTKSAQKAQK AK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0030864 cortical actin cytoskeleton
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0098574 cytoplasmic side of lysosomal membrane
Cellular Component GO:0005829 cytosol
Cellular Component GO:0022626 cytosolic ribosome
Cellular Component GO:0005853 eukaryotic translation elongation factor 1 complex
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0005615 extracellular space
Cellular Component GO:1904813 ficolin-1-rich granule lumen
Cellular Component GO:0016020 membrane
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0005840 ribosome
Cellular Component GO:0032587 ruffle membrane
Cellular Component GO:0034774 secretory granule lumen
Molecular Function GO:0005525 GTP binding
Molecular Function GO:0003924 GTPase activity
Molecular Function GO:0019209 kinase activator activity
Molecular Function GO:0019900 kinase binding
Molecular Function GO:0060090 molecular adaptor activity
Molecular Function GO:0019901 protein kinase binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003746 translation elongation factor activity
Molecular Function GO:0000049 tRNA binding
Biological Process GO:0071364 cellular response to epidermal growth factor stimulus
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0044829 host-mediated activation of viral genome replication
Biological Process GO:1904714 regulation of chaperone-mediated autophagy
Biological Process GO:0006412 translation
Biological Process GO:0006414 translational elongation

Reference

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[2] 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.

[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] 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] 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.

[7] 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.

[8] 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.

[9] 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.

[10] 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.

[11] 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.