ETF1
entrez
2107
canonical
uniprot
P62495
canonical
ensembl
ENSG00000120705
resolver
ensp
ENSP00000353741
resolver
ensp
ENSP00000421288
resolver
ensp
ENSP00000422203
resolver
ensp
ENSP00000536252
resolver
enst
ENST00000503014
resolver
genesymbol
ETF1
resolver
genesymbol_syn
ERF1
resolver
genesymbol_syn
RF1
resolver
genesymbol_syn
SUP45L1
resolver
hgnc
HGNC:3477
resolver
uniprot
B2R6B4
resolver
uniprot
B7Z7P8
resolver
uniprot
D3DQC1
resolver
uniprot
F6RN53
resolver
uniprot
P46055
resolver
uniprot
Q5M7Z7
resolver
uniprot
Q96CG1
resolver
uniprot_entry
B7Z7P8_HUMAN
resolver
uniprot_entry
ERF1_HUMAN
resolver
uniprot_entry
F6RN53_HUMAN
resolver
uniprot_sec
B2R6B4
resolver
uniprot_sec
D3DQC1
resolver
uniprot_sec
P46055
resolver
uniprot_sec
Q5M7Z7
resolver
uniprot_sec
Q96CG1
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 (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). {ECO:0000269|PubMed:10676813, ECO:0000269|PubMed:16777602, ECO:0000269|PubMed:19417104, ECO:0000269|PubMed:24486019, ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:30682371, ECO:0000269|PubMed:36638793, ECO:0000269|PubMed:7990965}.
uniprot
proteins
mass_dalton
49031
uniprot
proteins
mutagenesis
MUTAGEN 63; /note="K->A,R: Loss of hydroxylation."; /evidence="ECO:0000269|PubMed:24486019"; MUTAGEN 183..184; /note="GG->AA: In AAQ mutant; abolished ability to mediate translation termination. Can recognize stop codons in ribosomal A-site, but is unable to catalyze peptidyl-tRNA hydrolysis, promoting ribosome collisions."; /evidence="ECO:0000269|PubMed:10445876, ECO:0000269|PubMed:16777602, ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:36638793"; MUTAGEN 185; /note="Q->R,I,N: Abolishes methylation by N6AMT1."; /evidence="ECO:0000269|PubMed:20606008, ECO:0000269|PubMed:26797129
uniprot
proteins
post_translational_modification
PTM: Methylated at Gln-185 by N6AMT1. {ECO:0000269|PubMed:18539146, ECO:0000269|PubMed:20606008, ECO:0000269|PubMed:26797129}.; PTM: Hydroxylation at Lys-63 by JMJD4 promotes its translational termination efficiency. {ECO:0000269|PubMed:24486019}.; 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:0000269|PubMed:36638793}.
uniprot
proteins
protein_family
Eukaryotic release factor 1 family
uniprot
proteins
pubmed
10413110
uniprot
proteins
pubmed
10445876
uniprot
proteins
pubmed
10676813
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
1537561
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16777602
uniprot
proteins
pubmed
17651434
uniprot
proteins
pubmed
18539146
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19417104
uniprot
proteins
pubmed
19417105
uniprot
proteins
pubmed
20606008
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24486019
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26245381
uniprot
proteins
pubmed
26797129
uniprot
proteins
pubmed
27863242
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
30682371
uniprot
proteins
pubmed
36638793
uniprot
proteins
pubmed
37651229
uniprot
proteins
pubmed
7990965
uniprot
proteins
pubmed
9003791
uniprot
proteins
sequence_length
437
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24486019}.
uniprot
proteins