Search Results

Overview

Uniprot IDP15170
Protein NameEukaryotic peptide chain release factor GTP-binding subunit ERF3A
Gene NameGSPT1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
138 QEERDKGKTVEVGRA
151 RAYFETEKKHFTILD
152 AYFETEKKHFTILDA
196 EFETGFEKGGQTREH
253 KKVGFNPKKDIHFMP
309 IRLPIVDKYKDMGTV
490 GKTIAIGKVLKLVPE
71 VAPPGAPKKEHVNVV
72 APPGAPKKEHVNVVF

Function

GTPase component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons UAA, UAG and UGA (PubMed:15987998, PubMed:19417105, PubMed:2511002, PubMed:27863242). GSPT1/ERF3A mediates ETF1/ERF1 delivery to stop codons: The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site (PubMed:27863242). GTP hydrolysis by GSPT1/ERF3A induces a conformational change that leads to its dissociation, permitting ETF1/ERF1 to accommodate fully in the A-site (PubMed:16777602, PubMed:27863242). Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons (PubMed:24486019). Required for SHFL-mediated translation termination which inhibits programmed ribosomal frameshifting (-1PRF) of mRNA from viruses and cellular genes (PubMed:30682371)

Protein Sequence

10 MELSEPIVEN 20 GETEMSPEES 30 WEHKEEISEA 40 EPGGGSLGDG 50 RPPEESAHEM 60 MEEEEEIPKP 70 KSVVAPPGAP 80 KKEHVNVVFI 90 GHVDAGKSTI 100 GGQIMYLTGM 110 VDKRTLEKYE 120 REAKEKNRET 130 WYLSWALDTN 140 QEERDKGKTV 150 EVGRAYFETE 160 KKHFTILDAP 170 GHKSFVPNMI 180 GGASQADLAV 190 LVISARKGEF 200 ETGFEKGGQT 210 REHAMLAKTA 220 GVKHLIVLIN 230 KMDDPTVNWS 240 NERYEECKEK 250 LVPFLKKVGF 260 NPKKDIHFMP 270 CSGLTGANLK 280 EQSDFCPWYI 290 GLPFIPYLDN 300 LPNFNRSVDG 310 PIRLPIVDKY 320 KDMGTVVLGK 330 LESGSICKGQ 340 QLVMMPNKHN 350 VEVLGILSDD 360 VETDTVAPGE 370 NLKIRLKGIE 380 EEEILPGFIL 390 CDPNNLCHSG 400 RTFDAQIVII 410 EHKSIICPGY 420 NAVLHIHTCI 430 EEVEITALIC 440 LVDKKSGEKS 450 KTRPRFVKQD 460 QVCIARLRTA 470 GTICLETFKD 480 FPQMGRFTLR 490 DEGKTIAIGK VLKLVPEKD

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0022626 cytosolic ribosome
Cellular Component GO:0018444 translation release factor complex
Molecular Function GO:0005525 GTP binding
Molecular Function GO:0003924 GTPase activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003747 translation release factor activity
Biological Process GO:0000082 G1/S transition of mitotic cell cycle
Biological Process GO:0000184 nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
Biological Process GO:0006479 protein methylation
Biological Process GO:0006449 regulation of translational termination
Biological Process GO:0006412 translation
Biological Process GO:0006415 translational termination

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] 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.

[5] 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.