Search Results
Overview
| Uniprot ID | P62495 |
|---|---|
| Protein Name | Eukaryotic peptide chain release factor subunit 1 |
| Gene Name | ETF1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 178 | KFTVDLPKKHGRGGQ |
| 179 | FTVDLPKKHGRGGQS |
| 249 | FDQRLQSKVLKLVDI |
Function
Component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons (PubMed:10676813, PubMed:16777602, PubMed:24486019, PubMed:26245381, PubMed:27863242, PubMed:36638793, PubMed:7990965). The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site (PubMed:26245381, PubMed:27863242, PubMed:36638793). ETF1/ERF1 is responsible for stop codon recognition and inducing hydrolysis of peptidyl-tRNA (PubMed:26245381, PubMed:27863242, PubMed:36638793). Following GTP hydrolysis, eRF3 (GSPT1/ERF3A or GSPT2/ERF3B) dissociates, permitting ETF1/eRF1 to accommodate fully in the A-site and mediate hydrolysis of peptidyl-tRNA (PubMed:10676813, PubMed:16777602, PubMed:26245381, 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:19417104). Required for SHFL-mediated translation termination which inhibits programmed ribosomal frameshifting (-1PRF) of mRNA from viruses and cellular genes (PubMed:30682371)
Protein Sequence
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:0004045 | peptidyl-tRNA hydrolase activity |
| Molecular Function | GO:0043022 | ribosome binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:1990825 | sequence-specific mRNA binding |
| Molecular Function | GO:0003747 | translation release factor activity |
| Molecular Function | GO:0016149 | translation release factor activity, codon specific |
| Molecular Function | GO:0008079 | translation termination factor activity |
| Biological Process | GO:0002184 | cytoplasmic translational termination |
| 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: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] 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.