P43535 · GCN20_YEAST
- ProteinProtein GCN20
- GeneGCN20
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids752 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as a positive activator of the GCN2 protein kinase activity in response to in response to low amino acid, carbon, or purine availability (PubMed:10733573, PubMed:7621831).
Component of the GCN1-GCN20 complex that forms a complex with GCN2 on translating ribosomes; during this process, GCN20 helps GCN1 to act as a chaperone to facilitate delivery of uncharged tRNAs that enter the A site of ribosomes to the tRNA-binding domain of GCN2, and hence stimulating GCN2 kinase activity (PubMed:10775272, PubMed:15722345, PubMed:7621831, PubMed:9234705).
Participates in gene-specific mRNA translation activation, such as the transcriptional activator GCN4, by promoting the GCN2-mediated phosphorylation of eukaryotic translation initiation factor 2 (eIF-2-alpha/SUI2) on 'Ser-52', and hence allowing GCN4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:15722345).
Component of the GCN1-GCN20 complex that forms a complex with GCN2 on translating ribosomes; during this process, GCN20 helps GCN1 to act as a chaperone to facilitate delivery of uncharged tRNAs that enter the A site of ribosomes to the tRNA-binding domain of GCN2, and hence stimulating GCN2 kinase activity (PubMed:10775272, PubMed:15722345, PubMed:7621831, PubMed:9234705).
Participates in gene-specific mRNA translation activation, such as the transcriptional activator GCN4, by promoting the GCN2-mediated phosphorylation of eukaryotic translation initiation factor 2 (eIF-2-alpha/SUI2) on 'Ser-52', and hence allowing GCN4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:15722345).
Miscellaneous
Present with 14600 molecules/cell in log phase SD medium.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosolic ribosome | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ribosome binding | |
Molecular Function | translation initiation factor binding | |
Biological Process | cellular response to histidine | |
Biological Process | positive regulation of phosphorylation | |
Biological Process | positive regulation of translational initiation in response to starvation | |
Biological Process | protein unfolding | |
Biological Process | regulation of translational elongation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein GCN20
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP43535
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
Inhibits GCN4 derepression in amino acid or purine-starved cells (PubMed:10733573).
Attenuates GCN4 derepression in glucose-starved cells (PubMed:10733573).
Attenuates GCN4 derepression in glucose-starved cells (PubMed:10733573).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000093461 | 2-752 | Protein GCN20 | |||
Sequence: ASIGSQVRKAASSIDPIVTDYAVGYFNHLSGITFDAVQSKQVDLSTEVQFVSDLLIDAGASKAKVKELSESILKQLTTQLKENEAKLELTGDTSKRLLDINVLKSHNSKSDINVSLSMLGVNGDIEHTGRKMETRVDLKKLAKAEQKIAKKVAKRNNKFVKYEASKLINDQKEEDYDSFFLQINPLEFGSSAGKSKDIHIDTFDLYVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELNVPKHVSILHVEQELRGDDTKALQSVLDADVWRKQLLSEEAKINERLKEMDVLRQEFEEDSLEVKKLDNEREDLDNHLIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSHDRAFLNEVATDIIYQHNERLDYYRGQDFDTFYTTKEERRKNAQREYDNQMVYRKHLQEFIDKYRYNAAKSQEAQSRIKKLEKLPVLEPPEQDKTIDFKFPECDKLSPPIIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRLRIGYFTQHHVDSMDLTTSAVDWMSKSFPGKTDEEYRRHLGSFGITGTLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVKRFEGTIYDYRDYILQSADAAGVVKKH |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts (via N-terminus) with GCN1 (via C-terminus); this interaction stimulates GCN2 kinase activity in response to amino acid starvation (PubMed:11101534, PubMed:15722345, PubMed:7621831, PubMed:9234705).
The GCN1-GCN20 complex interacts with GCN2 on translating ribosomes in amino acid-starved cells; this association stimulates GCN2 kinase activation by uncharged tRNAs, and hence allowing GCN4 translational activation and derepression of amino acid biosynthetic genes (PubMed:10775272, PubMed:11101534, PubMed:7621831, PubMed:9234705).
Associates with ribosomes (PubMed:15722345, PubMed:7621831, PubMed:9234705).
The GCN1-GCN20 complex interacts with GCN2 on translating ribosomes in amino acid-starved cells; this association stimulates GCN2 kinase activation by uncharged tRNAs, and hence allowing GCN4 translational activation and derepression of amino acid biosynthetic genes (PubMed:10775272, PubMed:11101534, PubMed:7621831, PubMed:9234705).
Associates with ribosomes (PubMed:15722345, PubMed:7621831, PubMed:9234705).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P43535 | GCN1 P33892 | 4 | EBI-7423, EBI-7442 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 199-464 | ABC transporter 1 | ||||
Sequence: IHIDTFDLYVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELNVPKHVSILHVEQELRGDDTKALQSVLDADVWRKQLLSEEAKINERLKEMDVLRQEFEEDSLEVKKLDNEREDLDNHLIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSHDRAFLNEVATDIIYQHNERLDYYRGQDFDTFYTTKEERRKNA | ||||||
Domain | 532-748 | ABC transporter 2 | ||||
Sequence: IQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRLRIGYFTQHHVDSMDLTTSAVDWMSKSFPGKTDEEYRRHLGSFGITGTLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVKRFEGTIYDYRDYILQSADAAGV |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length752
- Mass (Da)85,027
- Last updated1995-11-01 v1
- Checksum486FED10305A572E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U19971 EMBL· GenBank· DDBJ | AAA75444.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D50617 EMBL· GenBank· DDBJ | BAA09248.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY723804 EMBL· GenBank· DDBJ | AAU09721.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006940 EMBL· GenBank· DDBJ | DAA12449.1 EMBL· GenBank· DDBJ | Genomic DNA |