|
P02994
|
Elongation factor 1-alpha |
GTP-binding component of the eukaryotic elongation factor 1complex (eEF1). In its active GTP-bound form, binds to and deliversaminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.In the presence of a correct codon-anticodon match between theaminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, theribosome acts as a GTPase activator and the GTP is hydrolyzed. Theinactive GDP-bound form leaves the ribosome and must be recycled by itsguanine nucleotide exchange factor (GEF) (eEF1B subcomplex) beforebinding another molecule of aminoacyl-tRNA. Required for nuclear exportof aminoacyl-tRNAs. May also be involved in translational qualitycontrol by targeting cotranslationally damaged proteins to theproteasome. Also exhibits actin filament-binding and -bundlingactivities and is involved in cytoskeleton organization. Plays a roleas a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells(PubMed:21849502). |
YBR118W |
Saccharomyces cerevisiae |
RSY255 |
20559436
|
|
P02994
|
Elongation factor 1-alpha |
GTP-binding component of the eukaryotic elongation factor 1complex (eEF1). In its active GTP-bound form, binds to and deliversaminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.In the presence of a correct codon-anticodon match between theaminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, theribosome acts as a GTPase activator and the GTP is hydrolyzed. Theinactive GDP-bound form leaves the ribosome and must be recycled by itsguanine nucleotide exchange factor (GEF) (eEF1B subcomplex) beforebinding another molecule of aminoacyl-tRNA. Required for nuclear exportof aminoacyl-tRNAs. May also be involved in translational qualitycontrol by targeting cotranslationally damaged proteins to theproteasome. Also exhibits actin filament-binding and -bundlingactivities and is involved in cytoskeleton organization. Plays a roleas a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells(PubMed:21849502). |
YBR118W |
Saccharomyces cerevisiae |
RSY782 |
20559436
|
|
P02994
|
Elongation factor 1-alpha |
GTP-binding component of the eukaryotic elongation factor 1complex (eEF1). In its active GTP-bound form, binds to and deliversaminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.In the presence of a correct codon-anticodon match between theaminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, theribosome acts as a GTPase activator and the GTP is hydrolyzed. Theinactive GDP-bound form leaves the ribosome and must be recycled by itsguanine nucleotide exchange factor (GEF) (eEF1B subcomplex) beforebinding another molecule of aminoacyl-tRNA. Required for nuclear exportof aminoacyl-tRNAs. May also be involved in translational qualitycontrol by targeting cotranslationally damaged proteins to theproteasome. Also exhibits actin filament-binding and -bundlingactivities and is involved in cytoskeleton organization. Plays a roleas a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells(PubMed:21849502). |
YBR118W |
Saccharomyces cerevisiae |
RSY954 |
20559436
|
|
P02994
|
Elongation factor 1-alpha |
GTP-binding component of the eukaryotic elongation factor 1complex (eEF1). In its active GTP-bound form, binds to and deliversaminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.In the presence of a correct codon-anticodon match between theaminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, theribosome acts as a GTPase activator and the GTP is hydrolyzed. Theinactive GDP-bound form leaves the ribosome and must be recycled by itsguanine nucleotide exchange factor (GEF) (eEF1B subcomplex) beforebinding another molecule of aminoacyl-tRNA. Required for nuclear exportof aminoacyl-tRNAs. May also be involved in translational qualitycontrol by targeting cotranslationally damaged proteins to theproteasome. Also exhibits actin filament-binding and -bundlingactivities and is involved in cytoskeleton organization. Plays a roleas a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells(PubMed:21849502). |
YBR118W |
Saccharomyces cerevisiae |
SEY6210 |
20559436
|
|
P02994
|
Elongation factor 1-alpha |
GTP-binding component of the eukaryotic elongation factor 1complex (eEF1). In its active GTP-bound form, binds to and deliversaminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.In the presence of a correct codon-anticodon match between theaminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, theribosome acts as a GTPase activator and the GTP is hydrolyzed. Theinactive GDP-bound form leaves the ribosome and must be recycled by itsguanine nucleotide exchange factor (GEF) (eEF1B subcomplex) beforebinding another molecule of aminoacyl-tRNA. Required for nuclear exportof aminoacyl-tRNAs. May also be involved in translational qualitycontrol by targeting cotranslationally damaged proteins to theproteasome. Also exhibits actin filament-binding and -bundlingactivities and is involved in cytoskeleton organization. Plays a roleas a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells(PubMed:21849502). |
YBR118W |
Saccharomyces cerevisiae |
SF264-1D |
20559436
|
|
P02994
|
Elongation factor 1-alpha |
GTP-binding component of the eukaryotic elongation factor 1complex (eEF1). In its active GTP-bound form, binds to and deliversaminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.In the presence of a correct codon-anticodon match between theaminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, theribosome acts as a GTPase activator and the GTP is hydrolyzed. Theinactive GDP-bound form leaves the ribosome and must be recycled by itsguanine nucleotide exchange factor (GEF) (eEF1B subcomplex) beforebinding another molecule of aminoacyl-tRNA. Required for nuclear exportof aminoacyl-tRNAs. May also be involved in translational qualitycontrol by targeting cotranslationally damaged proteins to theproteasome. Also exhibits actin filament-binding and -bundlingactivities and is involved in cytoskeleton organization. Plays a roleas a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells(PubMed:21849502). |
YBR118W |
Saccharomyces cerevisiae |
Snf7 |
20559436
|
|
P02994
|
Elongation factor 1-alpha |
GTP-binding component of the eukaryotic elongation factor 1complex (eEF1). In its active GTP-bound form, binds to and deliversaminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.In the presence of a correct codon-anticodon match between theaminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, theribosome acts as a GTPase activator and the GTP is hydrolyzed. Theinactive GDP-bound form leaves the ribosome and must be recycled by itsguanine nucleotide exchange factor (GEF) (eEF1B subcomplex) beforebinding another molecule of aminoacyl-tRNA. Required for nuclear exportof aminoacyl-tRNAs. May also be involved in translational qualitycontrol by targeting cotranslationally damaged proteins to theproteasome. Also exhibits actin filament-binding and -bundlingactivities and is involved in cytoskeleton organization. Plays a roleas a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells(PubMed:21849502). |
YBR118W |
Saccharomyces cerevisiae |
VPS23 |
20559436
|
|
P02994
|
Elongation factor 1-alpha |
GTP-binding component of the eukaryotic elongation factor 1complex (eEF1). In its active GTP-bound form, binds to and deliversaminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.In the presence of a correct codon-anticodon match between theaminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, theribosome acts as a GTPase activator and the GTP is hydrolyzed. Theinactive GDP-bound form leaves the ribosome and must be recycled by itsguanine nucleotide exchange factor (GEF) (eEF1B subcomplex) beforebinding another molecule of aminoacyl-tRNA. Required for nuclear exportof aminoacyl-tRNAs. May also be involved in translational qualitycontrol by targeting cotranslationally damaged proteins to theproteasome. Also exhibits actin filament-binding and -bundlingactivities and is involved in cytoskeleton organization. Plays a roleas a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells(PubMed:21849502). |
YPR080W |
Saccharomyces cerevisiae |
RSY255 |
20559436
|
|
P02994
|
Elongation factor 1-alpha |
GTP-binding component of the eukaryotic elongation factor 1complex (eEF1). In its active GTP-bound form, binds to and deliversaminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.In the presence of a correct codon-anticodon match between theaminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, theribosome acts as a GTPase activator and the GTP is hydrolyzed. Theinactive GDP-bound form leaves the ribosome and must be recycled by itsguanine nucleotide exchange factor (GEF) (eEF1B subcomplex) beforebinding another molecule of aminoacyl-tRNA. Required for nuclear exportof aminoacyl-tRNAs. May also be involved in translational qualitycontrol by targeting cotranslationally damaged proteins to theproteasome. Also exhibits actin filament-binding and -bundlingactivities and is involved in cytoskeleton organization. Plays a roleas a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells(PubMed:21849502). |
YPR080W |
Saccharomyces cerevisiae |
RSY782 |
20559436
|
|
P02994
|
Elongation factor 1-alpha |
GTP-binding component of the eukaryotic elongation factor 1complex (eEF1). In its active GTP-bound form, binds to and deliversaminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.In the presence of a correct codon-anticodon match between theaminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, theribosome acts as a GTPase activator and the GTP is hydrolyzed. Theinactive GDP-bound form leaves the ribosome and must be recycled by itsguanine nucleotide exchange factor (GEF) (eEF1B subcomplex) beforebinding another molecule of aminoacyl-tRNA. Required for nuclear exportof aminoacyl-tRNAs. May also be involved in translational qualitycontrol by targeting cotranslationally damaged proteins to theproteasome. Also exhibits actin filament-binding and -bundlingactivities and is involved in cytoskeleton organization. Plays a roleas a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells(PubMed:21849502). |
YPR080W |
Saccharomyces cerevisiae |
RSY954 |
20559436
|
|
P02994
|
Elongation factor 1-alpha |
GTP-binding component of the eukaryotic elongation factor 1complex (eEF1). In its active GTP-bound form, binds to and deliversaminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.In the presence of a correct codon-anticodon match between theaminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, theribosome acts as a GTPase activator and the GTP is hydrolyzed. Theinactive GDP-bound form leaves the ribosome and must be recycled by itsguanine nucleotide exchange factor (GEF) (eEF1B subcomplex) beforebinding another molecule of aminoacyl-tRNA. Required for nuclear exportof aminoacyl-tRNAs. May also be involved in translational qualitycontrol by targeting cotranslationally damaged proteins to theproteasome. Also exhibits actin filament-binding and -bundlingactivities and is involved in cytoskeleton organization. Plays a roleas a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells(PubMed:21849502). |
YPR080W |
Saccharomyces cerevisiae |
SEY6210 |
20559436
|
|
P02994
|
Elongation factor 1-alpha |
GTP-binding component of the eukaryotic elongation factor 1complex (eEF1). In its active GTP-bound form, binds to and deliversaminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.In the presence of a correct codon-anticodon match between theaminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, theribosome acts as a GTPase activator and the GTP is hydrolyzed. Theinactive GDP-bound form leaves the ribosome and must be recycled by itsguanine nucleotide exchange factor (GEF) (eEF1B subcomplex) beforebinding another molecule of aminoacyl-tRNA. Required for nuclear exportof aminoacyl-tRNAs. May also be involved in translational qualitycontrol by targeting cotranslationally damaged proteins to theproteasome. Also exhibits actin filament-binding and -bundlingactivities and is involved in cytoskeleton organization. Plays a roleas a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells(PubMed:21849502). |
YPR080W |
Saccharomyces cerevisiae |
SF264-1D |
20559436
|
|
P02994
|
Elongation factor 1-alpha |
GTP-binding component of the eukaryotic elongation factor 1complex (eEF1). In its active GTP-bound form, binds to and deliversaminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.In the presence of a correct codon-anticodon match between theaminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, theribosome acts as a GTPase activator and the GTP is hydrolyzed. Theinactive GDP-bound form leaves the ribosome and must be recycled by itsguanine nucleotide exchange factor (GEF) (eEF1B subcomplex) beforebinding another molecule of aminoacyl-tRNA. Required for nuclear exportof aminoacyl-tRNAs. May also be involved in translational qualitycontrol by targeting cotranslationally damaged proteins to theproteasome. Also exhibits actin filament-binding and -bundlingactivities and is involved in cytoskeleton organization. Plays a roleas a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells(PubMed:21849502). |
YPR080W |
Saccharomyces cerevisiae |
Snf7 |
20559436
|
|
P02994
|
Elongation factor 1-alpha |
GTP-binding component of the eukaryotic elongation factor 1complex (eEF1). In its active GTP-bound form, binds to and deliversaminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.In the presence of a correct codon-anticodon match between theaminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, theribosome acts as a GTPase activator and the GTP is hydrolyzed. Theinactive GDP-bound form leaves the ribosome and must be recycled by itsguanine nucleotide exchange factor (GEF) (eEF1B subcomplex) beforebinding another molecule of aminoacyl-tRNA. Required for nuclear exportof aminoacyl-tRNAs. May also be involved in translational qualitycontrol by targeting cotranslationally damaged proteins to theproteasome. Also exhibits actin filament-binding and -bundlingactivities and is involved in cytoskeleton organization. Plays a roleas a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells(PubMed:21849502). |
YPR080W |
Saccharomyces cerevisiae |
VPS23 |
20559436
|