Eef1a1
entrez
13627
canonical
uniprot
P10126
canonical
ensembl
ENSMUSG00000037742
resolver
ensp
ENSMUSP00000042457
resolver
enst
ENSMUST00000042235
resolver
genesymbol
Eef1a1
resolver
genesymbol_syn
Eef1a
resolver
uniprot
Q58E64
resolver
uniprot
Q61511
resolver
uniprot
Q6ZWN2
resolver
uniprot
Q8BMB8
resolver
uniprot
Q8BVS8
resolver
uniprot
Q99KU5
resolver
uniprot_entry
EF1A1_MOUSE
resolver
uniprot_entry
Q58E64_MOUSE
resolver
uniprot_sec
Q61511
resolver
uniprot_sec
Q6ZWN2
resolver
uniprot_sec
Q8BMB8
resolver
uniprot_sec
Q8BVS8
resolver
uniprot_sec
Q99KU5
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by plitidepsin, a chemical compound extracted from the ascidian Aplidium albicans. {ECO:0000250|UniProtKB:P68104}.
uniprot
proteins
amino_acid_sequence
MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGSASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK
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. 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. 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. 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 (By similarity). Also plays a role in cytoskeleton organization by promoting actin bundling. {ECO:0000250|UniProtKB:P68104, ECO:0000250|UniProtKB:P68105}.
uniprot
proteins
mass_dalton
50114
uniprot
proteins
post_translational_modification
PTM: ISGylated. {ECO:0000250|UniProtKB:P68104}.; PTM: Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency. Phosphorylated by ROCK2. Phosphorylation by TGFBR1 inhibits translation elongation. {ECO:0000250|UniProtKB:P68104}.; PTM: Trimethylated at Lys-79 by EEF1AKMT1. 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. Trimethylated at Lys-318 by EEF1AKMT2. 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. Trimethylated at Gly-2 by METTL13. Mono- and dimethylated at Lys-55 by METTL13; dimethylated form is predominant. {ECO:0000250|UniProtKB:P68104}.; 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:0000250|UniProtKB:P68104}.
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
15489334
uniprot
proteins
pubmed
16139798
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19856081
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
2569467
uniprot
proteins
pubmed
28108655
uniprot
proteins
pubmed
2911475
uniprot
proteins
pubmed
3215517
uniprot
proteins
pubmed
3481036
uniprot
proteins
pubmed
39349455
uniprot
proteins
pubmed
3960725
uniprot
proteins
sequence_length
462
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19856081}. Nucleus {ECO:0000250|UniProtKB:P68104}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P68104}. Cell membrane {ECO:0000250|UniProtKB:P68104}. Note=Colocalizes with DLC1 at actin-rich regions in the cell periphery. Translocates together with ZPR1 from the cytoplasm to the nucleus and nucleolus after treatment with mitogens. Localization at the cell membrane depends on EEF1A1 phosphorylation status and the presence of PPP1R16B. {ECO:0000250|UniProtKB:P68104}.
uniprot
proteins