P62629 · EF1A1_CRIGR
- ProteinElongation factor 1-alpha 1
- GeneEEF1A1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids462 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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.
Catalytic activity
- GTP + H2O = GDP + H+ + phosphateThis reaction proceeds in the forward direction.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleolus | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Molecular Function | calmodulin binding | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Molecular Function | translation elongation factor activity | |
Biological Process | cellular response to epidermal growth factor stimulus | |
Biological Process | regulation of D-erythro-sphingosine kinase activity | |
Biological Process | translational elongation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameElongation factor 1-alpha 1
- EC number
- Short namesEF-1-alpha-1
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Cricetidae > Cricetinae > Cricetulus
Accessions
- Primary accessionP62629
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N,N,N-trimethylglycine | ||||
Sequence: G | ||||||
Chain | PRO_0000090883 | 2-462 | Elongation factor 1-alpha 1 | |||
Sequence: GKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGSASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK | ||||||
Modified residue | 36 | N6,N6,N6-trimethyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 36 | N6,N6-dimethyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 36 | N6-methyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 55 | N6,N6-dimethyllysine | ||||
Sequence: K | ||||||
Modified residue | 79 | N6,N6,N6-trimethyllysine; by EEF1AKMT1 | ||||
Sequence: K | ||||||
Modified residue | 165 | N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT3 | ||||
Sequence: K | ||||||
Modified residue | 165 | N6,N6-dimethyllysine; alternate; by EEF1AKMT3 | ||||
Sequence: K | ||||||
Modified residue | 165 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 165 | N6-methyllysine; alternate; by EEF1AKMT3 | ||||
Sequence: K | ||||||
Modified residue | 172 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 273 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 300 | Phosphoserine; by TGFBR1 | ||||
Sequence: S | ||||||
Modified residue | 301 | 5-glutamyl glycerylphosphorylethanolamine | ||||
Sequence: E | ||||||
Modified residue | 318 | N6,N6,N6-trimethyllysine; by EEF1AKMT2 | ||||
Sequence: K | ||||||
Modified residue | 374 | 5-glutamyl glycerylphosphorylethanolamine | ||||
Sequence: E | ||||||
Cross-link | 385 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 392 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 392 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 432 | Phosphothreonine; by PASK | ||||
Sequence: T | ||||||
Modified residue | 439 | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
ISGylated.
Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency. Phosphorylated by ROCK2. Phosphorylation by TGFBR1 inhibits translation elongation.
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.
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.
Keywords
- PTM
Proteomic databases
Interaction
Subunit
Found in a nuclear export complex with XPO5, EEF1A1, Ran and aminoacylated tRNA. Interacts with PARP1 and TXK. Interacts with KARS1. May interact with ERGIC2. Interacts with IFIT1 (via TPR repeats 4-7) (By similarity).
May interact with ERGIC2. Interacts with IFIT1 (via TPR repeats 4-7) (By similarity).
Interacts with DLC1, facilitating distribution to the membrane periphery and ruffles upon growth factor stimulation. Interacts with ZPR1; the interaction occurs in a epidermal growth factor (EGF)-dependent manner (By similarity).
Interacts with PPP1R16B (By similarity).
Interacts with SPHK1 and SPHK2; both interactions increase SPHK1 and SPHK2 kinase activity (By similarity).
May interact with ERGIC2. Interacts with IFIT1 (via TPR repeats 4-7) (By similarity).
Interacts with DLC1, facilitating distribution to the membrane periphery and ruffles upon growth factor stimulation. Interacts with ZPR1; the interaction occurs in a epidermal growth factor (EGF)-dependent manner (By similarity).
Interacts with PPP1R16B (By similarity).
Interacts with SPHK1 and SPHK2; both interactions increase SPHK1 and SPHK2 kinase activity (By similarity).
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-242 | tr-type G | ||||
Sequence: KTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGSASGTTLLEALDCILPPTRPT | ||||||
Region | 14-21 | G1 | ||||
Sequence: GHVDSGKS | ||||||
Region | 70-74 | G2 | ||||
Sequence: GITID | ||||||
Region | 91-94 | G3 | ||||
Sequence: DAPG | ||||||
Region | 153-156 | G4 | ||||
Sequence: NKMD | ||||||
Region | 194-196 | G5 | ||||
Sequence: SGW |
Sequence similarities
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length462
- Mass (Da)50,114
- Last updated2004-07-19 v1
- Checksum71072871DE7405DC
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D00522 EMBL· GenBank· DDBJ | BAA00409.1 EMBL· GenBank· DDBJ | mRNA |