EEF1A1
entrez
1915
canonical
uniprot
P68104
canonical
ensembl
ENSG00000156508
resolver
ensp
ENSP00000330054
resolver
ensp
ENSP00000339053
resolver
ensp
ENSP00000339063
resolver
ensp
ENSP00000348651
resolver
ensp
ENSP00000392366
resolver
ensp
ENSP00000479055
resolver
ensp
ENSP00000503192
resolver
ensp
ENSP00000503249
resolver
ensp
ENSP00000503823
resolver
ensp
ENSP00000504335
resolver
ensp
ENSP00000545873
resolver
ensp
ENSP00000545875
resolver
ensp
ENSP00000545876
resolver
ensp
ENSP00000603336
resolver
ensp
ENSP00000637495
resolver
enst
ENST00000309268
resolver
enst
ENST00000316292
resolver
enst
ENST00000331523
resolver
enst
ENST00000356303
resolver
enst
ENST00000455918
resolver
enst
ENST00000615060
resolver
enst
ENST00000676710
resolver
enst
ENST00000677236
resolver
enst
ENST00000678508
resolver
enst
ENST00000678702
resolver
enst
ENST00000875814
resolver
enst
ENST00000875816
resolver
enst
ENST00000875817
resolver
enst
ENST00000933277
resolver
enst
ENST00000967436
resolver
genesymbol
EEF1A1
resolver
genesymbol_syn
EEF1A
resolver
genesymbol_syn
EF1A
resolver
genesymbol_syn
LENG7
resolver
hgnc
HGNC:3189
resolver
uniprot
P04719
resolver
uniprot
P04720
resolver
uniprot
Q6IPS9
resolver
uniprot
Q6IQ15
resolver
uniprot_entry
EF1A1_HUMAN
resolver
uniprot_entry
Q6IPS9_HUMAN
resolver
uniprot_sec
P04719
resolver
uniprot_sec
P04720
resolver
uniprot_sec
Q6IQ15
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by plitidepsin, a chemical compound extracted from the ascidian Aplidium albicans (PubMed:33495306). Specifically inhibited by didemnin B, a natural product that triggers ribosome stalling by preventing aminoacyl-tRNA (aa-tRNA) release from EEF1A1 on the ribosome (PubMed:26651998, PubMed:36264623). Specifically inhibited by ternatin-4, a small-molecule inhibitor that triggers ribosome stalling by traping EEF1A1 on the ribosome and preventing aminoacyl-tRNA (aa-tRNA) accommodation (PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). Ribosome stalling by ternatin-4 causes ubiquitination and degradation of EEF1A1 (PubMed:36638793). Specifically inhibited by ternatin SR-A3, which differs from ternatin-4 by the addition of a single oxygen atom into the side chain of N-Me-Leu (PubMed:36123449). Inhibition by ternatin-4 can be reversed, while it is not the case for didemnin B (PubMed:36264623). {ECO:0000269|PubMed:26651998, ECO:0000269|PubMed:33495306, ECO:0000269|PubMed:36123449, ECO:0000269|PubMed:36264623, ECO:0000269|PubMed:36638793}.
uniprot
proteins
amino_acid_sequence
MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
FUNCTION: Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond formation (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623). Also plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1 (PubMed:17177976). Also plays a role in cytoskeleton organization by promoting actin bundling (By similarity). {ECO:0000250|UniProtKB:P68105, ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:26593721, ECO:0000269|PubMed:26651998, ECO:0000269|PubMed:36123449, ECO:0000269|PubMed:36264623, ECO:0000269|PubMed:36638793}.; FUNCTION: (Microbial infection) Required for the translation of viral proteins and viral replication during human coronavirus SARS-CoV-2 infection. {ECO:0000269|PubMed:33495306}.
uniprot
proteins
mass_dalton
50141
uniprot
proteins
mutagenesis
MUTAGEN 36; /note="K->R: No effect on methylation by EEF1AKMT2. Abolishes EEF1AKMT4-mediated methylation."; /evidence="ECO:0000269|PubMed:25144183, ECO:0000269|PubMed:28520920"; MUTAGEN 55; /note="K->R: No effect on methylation by EEF1AKMT2. Abolishes methylation by METTL13."; /evidence="ECO:0000269|PubMed:25144183, ECO:0000269|PubMed:30143613, ECO:0000269|PubMed:30612740"; MUTAGEN 79; /note="K->R: No effect on methylation by EEF1AKMT2."; /evidence="ECO:0000269|PubMed:25144183"; MUTAGEN 165; /note="K->A: Abolishes methylation by EEF1AKMT3."; /evidence="ECO:0000269|PubMed:28108655"; MUTAGEN 165; /note="K->R: No effect on methylation by EEF1AKMT2."; /evidence="ECO:0000269|PubMed:25144183"; MUTAGEN 318; /note="K->R: Abolishes methylation by EEF1AKMT2."; /evidence="ECO:0000269|PubMed:25144183"; MUTAGEN 385; /note="K->R: Impaired ubiquitination in response to ribosome stalling caused by ternatin-4."; /evidence="ECO:0000269|PubMed:36638793"; MUTAGEN 399; /note="A->V: Resistant to inhibition by plitidepsin and ternatin-4. No effect on SARS-CoV-2 proteins translation."; /evidence="ECO:0000269|PubMed:26651998, ECO:0000269|PubMed:33495306, ECO:0000269|PubMed:36264623"; MUTAGEN 432; /note="T->A: Abolishes phosphorylation by PASK."; /evidence="ECO:0000269|PubMed:17595531
uniprot
proteins
post_translational_modification
PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Phosphorylated by TXK (PubMed:17177976). Phosphorylation by PASK increases translation efficiency (PubMed:17595531). Phosphorylated by ROCK2 (PubMed:26497934). Phosphorylation by TGFBR1 inhibits translation elongation (PubMed:20832312). {ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:17595531, ECO:0000269|PubMed:20832312, ECO:0000269|PubMed:26497934}.; PTM: Trimethylated at Lys-79 by EEF1AKMT1 (PubMed:26545399). Methylated at Lys-165 by EEF1AKMT3, methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stress, and plays a regulatory role on mRNA translation (PubMed:28108655). Trimethylated at Lys-318 by EEF1AKMT2 (PubMed:25144183). Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of translation rates for a subset of tRNAs (PubMed:28520920). Trimethylated at Gly-2 by METTL13 (PubMed:30143613). Mono- and dimethylated at Lys-55 by METTL13; dimethylated form is predominant (PubMed:30143613, PubMed:30612740). {ECO:0000269|PubMed:25144183, ECO:0000269|PubMed:26545399, ECO:0000269|PubMed:28108655, ECO:0000269|PubMed:28520920, ECO:0000269|PubMed:30143613, ECO:0000269|PubMed:30612740}.; PTM: Ubiquitinated at Lys-385 by RNF14 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
Classic translation factor GTPase family
uniprot
proteins
protein_family
EF-Tu/EF-1A subfamily
uniprot
proteins
protein_family
TRAFAC class translation factor GTPase superfamily
uniprot
proteins
pubmed
12426392
uniprot
proteins
pubmed
12426393
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16139798
uniprot
proteins
pubmed
17177976
uniprot
proteins
pubmed
17595531
uniprot
proteins
pubmed
17980171
uniprot
proteins
pubmed
18029264
uniprot
proteins
pubmed
18263879
uniprot
proteins
pubmed
19158340
uniprot
proteins
pubmed
20832312
uniprot
proteins
pubmed
2183196
uniprot
proteins
pubmed
25144183
uniprot
proteins
pubmed
2564392
uniprot
proteins
pubmed
2569467
uniprot
proteins
pubmed
26497934
uniprot
proteins
pubmed
26545399
uniprot
proteins
pubmed
26593721
uniprot
proteins
pubmed
26651998
uniprot
proteins
pubmed
28108655
uniprot
proteins
pubmed
28520920
uniprot
proteins
pubmed
30143613
uniprot
proteins
pubmed
30612740
uniprot
proteins
pubmed
3346208
uniprot
proteins
pubmed
33495306
uniprot
proteins
pubmed
3512269
uniprot
proteins
pubmed
36123449
uniprot
proteins
pubmed
36264623
uniprot
proteins
pubmed
36638793
uniprot
proteins
pubmed
39349455
uniprot
proteins
pubmed
3960725
uniprot
proteins
pubmed
8650580
uniprot
proteins
pubmed
9677419
uniprot
proteins
sequence_length
462
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19158340, ECO:0000269|PubMed:8650580}. Nucleus {ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:8650580}. Nucleus, nucleolus {ECO:0000269|PubMed:8650580}. Cell membrane {ECO:0000269|PubMed:26497934}. Note=Colocalizes with DLC1 at actin-rich regions in the cell periphery (PubMed:19158340). Translocates together with ZPR1 from the cytoplasm to the nucleus and nucleolus after treatment with mitogens (PubMed:8650580). Localization at the cell membrane depends on EEF1A1 phosphorylation status and the presence of PPP1R16B (PubMed:26497934). {ECO:0000269|PubMed:19158340, ECO:0000269|PubMed:26497934, ECO:0000269|PubMed:8650580}.
uniprot
proteins