Etf1
entrez
307503
canonical
uniprot
Q5U2Q7
canonical
ensembl
ENSRNOG00000019450
resolver
ensembl
ENSRNOG00055023044
resolver
ensembl
ENSRNOG00060026180
resolver
ensembl
ENSRNOG00065012587
resolver
ensp
ENSRNOP00000026398
resolver
ensp
ENSRNOP00055032150
resolver
ensp
ENSRNOP00060037640
resolver
ensp
ENSRNOP00065015717
resolver
enst
ENSRNOT00000026398
resolver
enst
ENSRNOT00055039595
resolver
enst
ENSRNOT00060045334
resolver
enst
ENSRNOT00065020464
resolver
genesymbol
Etf1
resolver
uniprot_entry
ERF1_RAT
resolver
amino_acid_sequence
MADDPSAADRNVEIWKIKKLIKSLEAARGNGTSMISLIIPPKDQISRVAKMLADEFGTASNIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTIVTEEGKEKKVNIDFEPFKPINTSLYLCDNKFHTEALTALLSDDSKFGFIVIDGSGALFGTLQGNTREVLHKFTVDLPKKHGRGGQSALRFARLRMEKRHNYVRKVAETAVQLFISGDKVNVAGLVLAGSADFKTELSQSDMFDQRLQSKVLKLVDISYGGENGFNQAIELSTEVLSNVKFIQEKKLIGRYFDEISQDTGKYCFGVEDTLKALEMGAVEILIVYENLDIMRYVLHCQGTEEEKILYLTPEQEKDKSHFTDKETGQEHELIESMPLLEWFANNYKKFGATLEIVTDKSQEGSQFVKGFGGIGGILRYRVDFQGMEYQGGDDEFFDLDDY
uniprot
proteins
function
FUNCTION: Component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons. The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site. ETF1/ERF1 is responsible for stop codon recognition and inducing hydrolysis of peptidyl-tRNA. Following GTP hydrolysis, eRF3 (GSPT1/ERF3A or GSPT2/ERF3B) dissociates, permitting ETF1/eRF1 to accommodate fully in the A-site, followed by hydrolysis of peptidyl-tRNA. 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. {ECO:0000250|UniProtKB:P62495}.
uniprot
proteins
mass_dalton
49031
uniprot
proteins
post_translational_modification
PTM: Hydroxylation at Lys-63 by JMJD4 promotes its translational termination efficiency. {ECO:0000250|UniProtKB:P62495}.; PTM: Methylated at Gln-185 by N6AMT1. {ECO:0000250|UniProtKB:P62495}.; PTM: Ubiquitinated at Lys-279 via 'Lys-6'-linked polyubiquitin chains by RNF14 and RNF25 in response to ribosome collisions (ribosome stalling), leading to its degradation by the proteasome and rescue of stalled ribosomes. {ECO:0000250|UniProtKB:P62495}.
uniprot
proteins
protein_family
Eukaryotic release factor 1 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
sequence_length
437
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62495}.
uniprot
proteins