UniProt functional annotation for P02994



	UniProt functional annotation for P02994

UniProt code: P02994.

Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).

Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.

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). {ECO:0000269|PubMed:10766739, ECO:0000269|PubMed:15601860, ECO:0000269|PubMed:21849502, ECO:0000269|PubMed:3066688}.

Biophysicochemical properties: Kinetic parameters: KM=0.14 mM for GTP {ECO:0000269|PubMed:9786872};

Pathway: Protein biosynthesis; polypeptide chain elongation.

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. eEF1A interacts directly with eEF1Balpha. Interacts with elongation factor 3 (YEF3 or HEF3), BNI1, SRV2 and ZPR1. Binds to actin and forms a ternary complex with BNI1 and profilin. Interacts with the proteasome, probably via RPT1. Interacts with CEX1 and NAP1. 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). Associates with ribosomes (PubMed:21849502). {ECO:0000269|PubMed:11106763, ECO:0000269|PubMed:11290701, ECO:0000269|PubMed:11373622, ECO:0000269|PubMed:15601860, ECO:0000269|PubMed:17203074, ECO:0000269|PubMed:18086883, ECO:0000269|PubMed:21849502, ECO:0000269|PubMed:9125210, ECO:0000269|PubMed:9591785, ECO:0000269|PubMed:9852145, ECO:0000269|PubMed:9990316}.

Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14562095}.

Ptm: S-thiolated in response to oxidative stress, probably inhibiting the protein and causing a reduction in protein synthesis. {ECO:0000269|PubMed:12755685}.

Miscellaneous: Present with 827 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.

Miscellaneous: There are two genes for eEF1A in yeast.

Similarity: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Taxonomy:		Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.



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). {ECO:0000269\|PubMed:10766739, ECO:0000269\|PubMed:15601860, ECO:0000269\|PubMed:21849502, ECO:0000269\|PubMed:3066688}.


Biophysicochemical properties:		Kinetic parameters: KM=0.14 mM for GTP {ECO:0000269\|PubMed:9786872};
Pathway:		Protein biosynthesis; polypeptide chain elongation.
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. eEF1A interacts directly with eEF1Balpha. Interacts with elongation factor 3 (YEF3 or HEF3), BNI1, SRV2 and ZPR1. Binds to actin and forms a ternary complex with BNI1 and profilin. Interacts with the proteasome, probably via RPT1. Interacts with CEX1 and NAP1. 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). Associates with ribosomes (PubMed:21849502). {ECO:0000269\|PubMed:11106763, ECO:0000269\|PubMed:11290701, ECO:0000269\|PubMed:11373622, ECO:0000269\|PubMed:15601860, ECO:0000269\|PubMed:17203074, ECO:0000269\|PubMed:18086883, ECO:0000269\|PubMed:21849502, ECO:0000269\|PubMed:9125210, ECO:0000269\|PubMed:9591785, ECO:0000269\|PubMed:9852145, ECO:0000269\|PubMed:9990316}.
Subcellular location:		Cytoplasm {ECO:0000269\|PubMed:14562095}. Cytoplasm, cytoskeleton {ECO:0000269\|PubMed:14562095}.
Ptm:		S-thiolated in response to oxidative stress, probably inhibiting the protein and causing a reduction in protein synthesis. {ECO:0000269\|PubMed:12755685}.
Miscellaneous:		Present with 827 molecules/cell in log phase SD medium. {ECO:0000269\|PubMed:14562106}.
Miscellaneous:		There are two genes for eEF1A in yeast.
Similarity:		Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily. {ECO:0000305}.