ETF1

Termination of protein biosynthesis and release of the nascent polypeptide chain are signaled by the presence of an in-frame stop codon at the aminoacyl site of the ribosome. The process of translation termination is universal and is mediated by protein release factors (RFs) and GTP. A class 1 RF recognizes the stop codon and promotes the hydrolysis of the ester bond linking the polypeptide chain with the peptidyl site tRNA, a reaction catalyzed at the peptidyl transferase center of the ribosome. Class 2 RFs, which are not codon specific and do not recognize codons, stimulate class 1 RF activity and confer GTP dependency upon the process. In prokaryotes, both class 1 RFs, RF1 and RF2, recognize UAA; however, UAG and UGA are decoded specifically by RF1 and RF2, respectively. In eukaryotes, eRF1, or ETF1, the functional counterpart of RF1 and RF2, functions as an omnipotent RF, decoding all 3 stop codons (Frolova et al., 1994 [PubMed 7990965]).[supplied by OMIM

eukaryotic translation termination factor 1

Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA (PubMed:7990965, PubMed:24486019).

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. Required for SHFL-mediated translation termination which inhibits programmed ribosomal frameshifting (-1PRF) of mRNA from viruses and cellular genes (PubMed:30682371).

Cytoplasmic translational termination Source: GO_Central
Nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB-KW
Protein methylation Source: MGI
Regulation of translational termination Source: UniProtKB
Translational termination Source: MGI

Cytoplasm

Methylated at Gln-185 by N6AMT1.
Hydroxylation at Lys-63 by JMJD4 promotes its translational termination efficiency.