P02994 · EF1A_YEAST
- ProteinElongation factor 1-alpha
- GeneTEF1; TEF2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids458 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
GTP-binding component of the eukaryotic elongation factor 1 complex (eEF1). In its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be recycled by its guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) before binding another molecule of aminoacyl-tRNA. Required for nuclear export of aminoacyl-tRNAs. May also be involved in translational quality control by targeting cotranslationally damaged proteins to the proteasome. Also exhibits actin filament-binding and -bundling activities and is involved in cytoskeleton organization. Plays a role as a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells (PubMed:21849502).
Miscellaneous
Present with 827 molecules/cell in log phase SD medium.
There are two genes for eEF1A in yeast.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.14 mM | GTP |
Pathway
Protein biosynthesis; polypeptide chain elongation.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 21 | GTP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 22 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 153 | GTP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 154 | GTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 156 | GTP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 192 | GTP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 193 | GTP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 194 | GTP (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Site | 298 | Not modified | ||||
Sequence: E | ||||||
Site | 372 | Not modified | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytoskeleton | |
Cellular Component | cytosol | |
Cellular Component | eukaryotic translation elongation factor 1 complex | |
Cellular Component | fungal-type vacuole membrane | |
Cellular Component | mitochondrion | |
Cellular Component | ribosome | |
Molecular Function | actin filament binding | |
Molecular Function | GDP binding | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Molecular Function | melatonin binding | |
Molecular Function | protein kinase binding | |
Molecular Function | ribosome binding | |
Molecular Function | translation elongation factor activity | |
Biological Process | actin filament bundle assembly | |
Biological Process | cellular response to amino acid starvation | |
Biological Process | negative regulation of protein kinase activity | |
Biological Process | negative regulation of protein phosphorylation | |
Biological Process | translation | |
Biological Process | translational elongation | |
Biological Process | tRNA export from nucleus |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameElongation factor 1-alpha
- Short namesEF-1-alpha
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP02994
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 122 | Reduces interaction with YEF3. | ||||
Sequence: E → K | ||||||
Mutagenesis | 153 | Increases KM for GTP to 2.7 mM. | ||||
Sequence: N → D | ||||||
Mutagenesis | 153 | Increases KM for GTP to 6.0 mM and reduces translation fidelity. Increases Km for GTP to 10.3 mM and reduces translation fidelity; when associated with E-156. | ||||
Sequence: N → T | ||||||
Mutagenesis | 156 | Increases KM for GTP to 10.3 mM and reduces translation fidelity; when associated with T-152. | ||||
Sequence: D → E | ||||||
Mutagenesis | 156 | Increases KM for GTP to 13.1 mM and reduces translation fidelity. Confers hyperresistance to canavanine. | ||||
Sequence: D → N | ||||||
Mutagenesis | 156 | Increases KM for GTP to 4.2 mM. Preferres XTP over GTP as substrate. | ||||
Sequence: D → W | ||||||
Mutagenesis | 286 | In TEF2-1; strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation. | ||||
Sequence: E → K | ||||||
Mutagenesis | 317 | In TEF2-2; strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation. | ||||
Sequence: E → K |
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; by EFM7 | ||||
Sequence: G | ||||||
Chain | PRO_0000090973 | 2-458 | Elongation factor 1-alpha | |||
Sequence: GKEKSHINVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYQVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGVGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDSVKWDESRFQEIVKETSNFIKKVGYNPKTVPFVPISGWNGDNMIEATTNAPWYKGWEKETKAGVVKGKTLLEAIDAIEQPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFAPAGVTTEVKSVEMHHEQLEQGVPGDNVGFNVKNVSVKEIRRGNVCGDAKNDPPKGCASFNATVIVLNHPGQISAGYSPVLDCHTAHIACRFDELLEKNDRRSGKKLEDHPKFLKSGDAALVKFVPSKPMCVEAFSEYPPLGRFAVRDMRQTVAVGVIKSVDKTEKAAKVTKAAQKAAKK | ||||||
Modified residue | 3 | N6,N6-dimethyllysine; by EFM7; alternate | ||||
Sequence: K | ||||||
Modified residue | 3 | N6-methyllysine; by EFM7; alternate | ||||
Sequence: K | ||||||
Modified residue | 18 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 30 | N6-methyllysine; by EFM1 | ||||
Sequence: K | ||||||
Modified residue | 72 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 79 | N6,N6,N6-trimethyllysine; by EFM5 | ||||
Sequence: K | ||||||
Modified residue | 82 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 163 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 224 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 242 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 253 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 259 | Phosphothreonine | ||||
Sequence: T | ||||||
Cross-link | 271 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 289 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 316 | N6,N6-dimethyllysine; by EFM4; alternate | ||||
Sequence: K | ||||||
Modified residue | 316 | N6-methyllysine; by EFM4; alternate | ||||
Sequence: K | ||||||
Modified residue | 390 | N6-methyllysine; by EFM6 | ||||
Sequence: K | ||||||
Cross-link | 393 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 414 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 430 | Phosphothreonine | ||||
Sequence: T | ||||||
Cross-link | 437 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 458 | Lysine methyl ester | ||||
Sequence: K |
Post-translational modification
S-thiolated in response to oxidative stress, probably inhibiting the protein and causing a reduction in protein synthesis.
Glutaminylated at Glu-45. An L-glutamine is linked to Glu-45 via the alpha amino group. This glutaminylation is yeast-specific and not essential for the normal functions of eEF1A. However, eEF1A glutaminylation slightly reduced growth under antibiotic-induced translational stress conditions.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
The eukaryotic elongation factor 1 complex (eEF1) is probably a heterohexamer. Two trimeric complexes, each composed of eEF1A (TEF1 or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or TEF4), are probably dimerized via the eF1Bgamma subunits (PubMed:11106763, PubMed:11373622).
Interacts with eEF1Balpha; the interaction is direct (PubMed:11106763, PubMed:11373622).
Interacts with GCN2 (via C-terminus); this interaction is direct, occurs in amino acid-repleted cells, may be stabilzed in a ribosome-dependent manner, reduces GCN2-mediated eIF-2-alpha phosphorylation and is lost in amino acid-starved cells and by uncharged tRNAs (PubMed:21849502).
Interacts with CEX1 (PubMed:17203074).
Interacts with elongation factor 3 (YEF3 or HEF3) (PubMed:9990316).
Interacts with NAP1 (PubMed:18086883).
Interacts with SRV2 (PubMed:9125210).
Interacts with chaperone ZPR1; the interaction is required for its proper folding (PubMed:36630955, PubMed:9852145).
Binds to actin and forms a ternary complex with BNI1 and profilin (PubMed:11290701, PubMed:9591785).
Interacts with the proteasome, probably via RPT1 (PubMed:15601860).
Associates with ribosomes (PubMed:21849502).
Interacts with eEF1Balpha; the interaction is direct (PubMed:11106763, PubMed:11373622).
Interacts with GCN2 (via C-terminus); this interaction is direct, occurs in amino acid-repleted cells, may be stabilzed in a ribosome-dependent manner, reduces GCN2-mediated eIF-2-alpha phosphorylation and is lost in amino acid-starved cells and by uncharged tRNAs (PubMed:21849502).
Interacts with CEX1 (PubMed:17203074).
Interacts with elongation factor 3 (YEF3 or HEF3) (PubMed:9990316).
Interacts with NAP1 (PubMed:18086883).
Interacts with SRV2 (PubMed:9125210).
Interacts with chaperone ZPR1; the interaction is required for its proper folding (PubMed:36630955, PubMed:9852145).
Binds to actin and forms a ternary complex with BNI1 and profilin (PubMed:11290701, PubMed:9591785).
Interacts with the proteasome, probably via RPT1 (PubMed:15601860).
Associates with ribosomes (PubMed:21849502).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P02994 | BUD27 P43573 | 2 | EBI-6314, EBI-22787 | |
BINARY | P02994 | EFB1 P32471 | 4 | EBI-6314, EBI-6319 | |
BINARY | P02994 | FAR8 Q05040 | 2 | EBI-6314, EBI-28053 | |
BINARY | P02994 | SRV2 P17555 | 3 | EBI-6314, EBI-4024 | |
XENO | P02994 | Zpr1 Q62384 | 2 | EBI-6314, EBI-11566629 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-240 | tr-type G | ||||
Sequence: KSHINVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYQVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGVGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDSVKWDESRFQEIVKETSNFIKKVGYNPKTVPFVPISGWNGDNMIEATTNAPWYKGWEKETKAGVVKGKTLLEAIDAIEQPSRPT | ||||||
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 | 192-194 | 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
- Length458
- Mass (Da)50,033
- Last updated1986-07-21 v1
- Checksum411C66D830716576
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 86 | in Ref. 14; AA sequence | ||||
Sequence: Q → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X00779 EMBL· GenBank· DDBJ | CAA25356.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X01638 EMBL· GenBank· DDBJ | CAA25798.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M10992 EMBL· GenBank· DDBJ | AAA34585.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M15666 EMBL· GenBank· DDBJ | AAA34584.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M15667 EMBL· GenBank· DDBJ | AAA34586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X78993 EMBL· GenBank· DDBJ | CAA55620.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35987 EMBL· GenBank· DDBJ | CAA85075.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U51033 EMBL· GenBank· DDBJ | AAB68129.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY692927 EMBL· GenBank· DDBJ | AAT92946.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X73532 EMBL· GenBank· DDBJ | CAA51936.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF402004 EMBL· GenBank· DDBJ | AAP86465.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY130810 EMBL· GenBank· DDBJ | AAM83111.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY130811 EMBL· GenBank· DDBJ | AAM83112.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY130812 EMBL· GenBank· DDBJ | AAM83113.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY130813 EMBL· GenBank· DDBJ | AAM83114.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006936 EMBL· GenBank· DDBJ | DAA07236.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006949 EMBL· GenBank· DDBJ | DAA11498.1 EMBL· GenBank· DDBJ | Genomic DNA |