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Entry version 227 (02 Jun 2021)
Sequence version 3 (05 Sep 2006)
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Protein

eIF-2-alpha kinase GCN2

Gene

GCN2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/SUI2) on 'Ser-52' in response to low amino acid, carbon, or purine availability (PubMed:1739968, PubMed:7623840, PubMed:8798780, PubMed:9528799, PubMed:10983975, PubMed:17202131, PubMed:8336737, PubMed:10733573).

Plays a role as an activator of the general amino acid control (GAAC) pathway required for adapatation to nutrient starvation. Converts phosphorylated eIF-2-alpha/SUI2 either to a competitive inhibitor of translation initiation factor eIF-2B, leading to a global protein synthesis repression, and thus to a reduced overall utilization of amino acids, or to a translational initiation activation of specific mRNAs, such as the transcriptional activator GCN4, and hence allowing GCN4-mediated reprogramming of transcription to alleviate nutrient depletion (PubMed:2660141, PubMed:2188100, PubMed:1739968, PubMed:7621831, PubMed:7623840, PubMed:8798780, PubMed:10801780, PubMed:11350982, PubMed:24333428, PubMed:10733573).

Binds uncharged tRNAs (PubMed:7623840, PubMed:10983975).

15 Publications

(orthologuous-specific) Binds to aminoacylated tRNA(Phe) less tightly than to deacylated tRNA(Phe) (PubMed:10983975).

Binds to double-stranded RNA (PubMed:9430731).

2 Publications

Miscellaneous

Present with 279 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The kinase activity is stimulated upon binding to uncharged tRNAs (PubMed:7623840).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei628ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei835Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi605 – 613ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, Kinase, RNA-binding, Serine/threonine-protein kinase, Transferase, tRNA-binding
Biological processProtein biosynthesis, Stress response, Translation regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.20, 984

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-SCE-381042, PERK regulates gene expression

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
eIF-2-alpha kinase GCN2By similarity (EC:2.7.11.15 Publications)
Alternative name(s):
General control non-derepressible protein 2Imported
Serine/threonine-protein kinase GCN2Curated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:GCN2Imported
Synonyms:AAS1Imported
Ordered Locus Names:YDR283C
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome IV

Organism-specific databases

Saccharomyces Genome Database

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SGDi
S000002691, GCN2

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
FungiDB:YDR283C

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Abolishes phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/SUI2) during amino acid, purine, and glucose starvation (PubMed:8336737, PubMed:10733573). Inhibits GCN4 derepression in glucose, amino acid, or purine-starved cells (PubMed:8336737, PubMed:10733573). Decreases vacuolar free amino acid levels during glucose starvation (PubMed:10733573). Sensitive to the purine analog 8-azaadenine (PubMed:8336737). Increases duration of lag phase on return to glucose-rich medium following glucose starvation (PubMed:10733573).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi74Y → A: Inhibits interaction with GCN1, eIF-2-alpha phosphorylation and fails to derepress GCN4 translation in amino acid-starved cells. 2 Publications1
Mutagenesisi582S → F: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi594R → D: Inhibits autophosphorylation, eIF-2-alpha kinase activity and derepression of GCN4 translation. Restores eIF-2-alpha kinase activity and derepression of GCN4, but not autophosphorylation; when associated with R-598. 1 Publication1
Mutagenesisi598D → R: Inhibits autophosphorylation, eIF-2-alpha kinase activity and derepression of GCN4 translation. Restores eIF-2-alpha kinase activity and derepression of GCN4, but not autophosphorylation; when associated with D-594. 1 Publication1
Mutagenesisi601E → K: Increases the constitutive kinase activity in absence of amino acid starvation. 1 Publication1
Mutagenesisi628K → V or R: Inhibits autophosphorylation, eIF-2-alpha kinase activity and derepression of GCN4 translation in amino acid-starved cells. 7 Publications1
Mutagenesisi629K → A: Does not abolish derepression of GCN4 translation and amino acid biosynthetic genes in amino acid-starved cells. 1 Publication1
Mutagenesisi716F → S: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi788M → V: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi794R → G: Constitutively active allele, bypass the tRNA binding-requirement for kinase activity. 1 Publication1
Mutagenesisi803E → V: Increases tRNA binding and the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 2 Publications1
Mutagenesisi821E → K: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 2 Publications1
Mutagenesisi835D → N: Loss of function. 1 Publication1
Mutagenesisi861H → Y: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi882T → A, E or D: Partially impairs kinase activity. 1 Publication1
Mutagenesisi882T → S: No effect. 1 Publication1
Mutagenesisi887T → A, E or D: Completely abolishes kinase activity. 1 Publication1
Mutagenesisi887T → S: Partially impairs kinase activity. 1 Publication1
Mutagenesisi1080V → A: Inhibits dimerization; when associated with A-1088 and A-1090. 1 Publication1
Mutagenesisi1088L → A: Inhibits dimerization; when associated with A-1080 and A-1090. 1 Publication1
Mutagenesisi1090L → A: Inhibits dimerization; when associated with A-1080 and A-1088. 1 Publication1
Mutagenesisi1119Y → L: Inhibits binding to uncharged tRNAs, decreases eIF-2-alpha kinase activity and derepression of GCN4 translation and amino acid biosynthetic genes in amino acid-starved cells; when associated with L-1120. 3 Publications1
Mutagenesisi1120R → L: Inhibits binding to uncharged tRNAs, decreases eIF-2-alpha kinase activity and derepression of GCN4 translation and amino acid biosynthetic genes in amino acid-starved cells; when associated with L-1119. 3 Publications1
Mutagenesisi1134F → L: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi1138D → N: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi1197A → G: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi1308H → Y: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi1338G → D: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi1552 – 1556KKANK → LLANI: Fails to derepress of GCN4 translation and amino acid biosynthetic genes in amino acid-starved cells and does not inhibit autophosphorylation. 1 Publication5
Mutagenesisi1552K → L: Reduces interaction with TIF11, Inhibits binding to uncharged tRNAs, reduces autophosphorylation, eIF-2-alpha kinase activity and ribosome association, but not dimerization; when associated with I-1553 and I-1556. 2 Publications1
Mutagenesisi1553K → I: Reduces interaction with TIF11, Inhibits binding to uncharged tRNAs, reduces autophosphorylation, eIF-2-alpha kinase activity and ribosome association, but not dimerization; when associated with L-1552 and I-1556. 2 Publications1
Mutagenesisi1556K → I: Reduces interaction with TIF11, Inhibits binding to uncharged tRNAs, reduces autophosphorylation, eIF-2-alpha kinase activity and ribosome association, but not dimerization; when associated with L-1552 and I-1553. 2 Publications1
Mutagenesisi1557R → K: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi1591E → K: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 1 Publication1
Mutagenesisi1606E → K: Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. 2 Publications1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000859631 – 1659eIF-2-alpha kinase GCN2Add BLAST1659

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei761PhosphoserineCombined sources1
Modified residuei882Phosphothreonine; by autocatalysis1 Publication1
Modified residuei887Phosphothreonine; by autocatalysis1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylated, autophosphorylation on Thr-882 and Thr-887 increases kinase activity.6 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

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MaxQBi
P15442

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P15442

PRoteomics IDEntifications database

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PRIDEi
P15442

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P15442

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; homodimerization is important for kinase activation by uncharged tRNAs (PubMed:9566889, PubMed:10983975, PubMed:11250908, PubMed:17202131, PubMed:15964839).

Interacts (via N-terminal RWD domain) with GCN1 (via N- and C-terminus); this interaction stimulates GCN2 kinase activity in a GCN20-dependent manner in response to amino acid starvation (PubMed:10775272, PubMed:11101534, PubMed:10801780, PubMed:11350982, PubMed:21849502).

Interacts (via N-terminus) with the GCN1-GCN20 complex on translating ribosomes in amino acid-starved cells; GCN1 may bind near the ribosomal A-site and promotes the transfer of uncharged tRNAs from the A-site to the tRNA-binding domain in GCN2 for its subsequent kinase activation, and hence allowing GCN4 translational activation and derepression of amino acid biosynthetic genes (PubMed:10775272, PubMed:11101534).

Interacts (via C-terminus) with TIF11; 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 but not GCN2 autophosphorylation and is lost in amino acid-starved cells and by uncharged tRNAs (PubMed:21849502). Associates (via C-terminus) with ribosomes (PubMed:2038314, PubMed:9430731, PubMed:10983975, PubMed:22888004).

13 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
32336, 239 interactors

Database of interacting proteins

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DIPi
DIP-2346N

Protein interaction database and analysis system

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IntActi
P15442, 27 interactors

Molecular INTeraction database

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MINTi
P15442

STRING: functional protein association networks

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STRINGi
4932.YDR283C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P15442, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11659
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P15442

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P15442

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini17 – 128RWDPROSITE-ProRule annotationAdd BLAST112
Domaini256 – 527Protein kinase 1PROSITE-ProRule annotationAdd BLAST272
Domaini599 – 981Protein kinase 2PROSITE-ProRule annotationAdd BLAST383

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni149 – 171DisorderedSequence analysisAdd BLAST23
Regioni671 – 691DisorderedSequence analysisAdd BLAST21
Regioni727 – 768DisorderedSequence analysisAdd BLAST42
Regioni999 – 1519Histidyl-tRNA synthetase-likeAdd BLAST521

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi728 – 744Basic and acidic residuesSequence analysisAdd BLAST17

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C-terminal domain negatively regulates kinase activity via an autoinhibitory association with the protein kinase and histidyl-tRNA synthetase-like domains in amino acid-repleted cells, that is counteracted by uncharged tRNAs in amino acid-starved cells (PubMed:7623840, PubMed:8798780, PubMed:10983975, PubMed:11250908). The C-terminal, histidyl-tRNA synthetase-like region and protein kinase domains are necessary for homodimer formation (PubMed:9566889, PubMed:10983975, PubMed:11250908). The C-terminal and protein kinase domains are necessary for ribosome association (PubMed:9566889, PubMed:10983975). The C-terminal and histidyl-tRNA synthetase-like regions are required for uncharged tRNAs binding in amino acid-starved cells (PubMed:7623840, PubMed:8798780, PubMed:9430731, PubMed:10983975).6 Publications

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1035, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000158121

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_001222_2_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P15442

Identification of Orthologs from Complete Genome Data

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OMAi
GSEMIYE

Family and domain databases

Conserved Domains Database

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CDDi
cd00773, HisRS-like_core, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.10.110.10, 1 hit
3.40.50.800, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR036621, Anticodon-bd_dom_sf
IPR016255, Gcn2
IPR041715, HisRS-like_core
IPR024435, HisRS-related_dom
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR006575, RWD-domain
IPR008271, Ser/Thr_kinase_AS
IPR016135, UBQ-conjugating_enzyme/RWD

Pfam protein domain database

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Pfami
View protein in Pfam
PF12745, HGTP_anticodon2, 1 hit
PF00069, Pkinase, 3 hits
PF05773, RWD, 1 hit
PF13393, tRNA-synt_His, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF000660, Ser/Thr_PK_GCN2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00591, RWD, 1 hit
SM00220, S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54495, SSF54495, 1 hit
SSF56112, SSF56112, 2 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00107, PROTEIN_KINASE_ATP, 1 hit
PS50011, PROTEIN_KINASE_DOM, 2 hits
PS00108, PROTEIN_KINASE_ST, 1 hit
PS50908, RWD, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P15442-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLSHLTLDQ YYEIQCNELE AIRSIYMDDF TDLTKRKSSW DKQPQIIFEI
60 70 80 90 100
TLRSVDKEPV ESSITLHFAM TPMYPYTAPE IEFKNVQNVM DSQLQMLKSE
110 120 130 140 150
FKKIHNTSRG QEIIFEITSF TQEKLDEFQN VVNTQSLEDD RLQRIKETKE
160 170 180 190 200
QLEKEEREKQ QETIKKRSDE QRRIDEIVQR ELEKRQDDDD DLLFNRTTQL
210 220 230 240 250
DLQPPSEWVA SGEAIVFSKT IKAKLPNNSM FKFKAVVNPK PIKLTSDIFS
260 270 280 290 300
FSKQFLVKPY IPPESPLADF LMSSEMMENF YYLLSEIELD NSYFNTSNGK
310 320 330 340 350
KEIANLEKEL ETVLKAKHDN VNRLFGYTVE RMGRNNATFV WKIRLLTEYC
360 370 380 390 400
NYYPLGDLIQ SVGFVNLATA RIWMIRLLEG LEAIHKLGIV HKCINLETVI
410 420 430 440 450
LVKDADFGST IPKLVHSTYG YTVLNMLSRY PNKNGSSVEL SPSTWIAPEL
460 470 480 490 500
LKFNNAKPQR LTDIWQLGVL FIQIISGSDI VMNFETPQEF LDSTSMDETL
510 520 530 540 550
YDLLSKMLNN DPKKRLGTLE LLPMKFLRTN IDSTINRFNL VSESVNSNSL
560 570 580 590 600
ELTPGDTITV RGNGGRTLSQ SSIRRRSFNV GSRFSSINPA TRSRYASDFE
610 620 630 640 650
EIAVLGQGAF GQVVKARNAL DSRYYAIKKI RHTEEKLSTI LSEVMLLASL
660 670 680 690 700
NHQYVVRYYA AWLEEDSMDE NVFESTDEES DLSESSSDFE ENDLLDQSSI
710 720 730 740 750
FKNRTNHDLD NSNWDFISGS GYPDIVFENS SRDDENEDLD HDTSSTSSSE
760 770 780 790 800
SQDDTDKESK SIQNVPRRRN FVKPMTAVKK KSTLFIQMEY CENRTLYDLI
810 820 830 840 850
HSENLNQQRD EYWRLFRQIL EALSYIHSQG IIHRDLKPMN IFIDESRNVK
860 870 880 890 900
IGDFGLAKNV HRSLDILKLD SQNLPGSSDN LTSAIGTAMY VATEVLDGTG
910 920 930 940 950
HYNEKIDMYS LGIIFFEMIY PFSTGMERVN ILKKLRSVSI EFPPDFDDNK
960 970 980 990 1000
MKVEKKIIRL LIDHDPNKRP GARTLLNSGW LPVKHQDEVI KEALKSLSNP
1010 1020 1030 1040 1050
SSPWQQQVRE SLFNQSYSLT NDILFDNSVP TSTPFANILR SQMTEEVVKI
1060 1070 1080 1090 1100
FRKHGGIENN APPRIFPKAP IYGTQNVYEV LDKGGTVLQL QYDLTYPMAR
1110 1120 1130 1140 1150
YLSKNPSLIS KQYRMQHVYR PPDHSRSSLE PRKFGEIDFD IISKSSSESG
1160 1170 1180 1190 1200
FYDAESLKII DEILTVFPVF EKTNTFFILN HADILESVFN FTNIDKAQRP
1210 1220 1230 1240 1250
LVSRMLSQVG FARSFKEVKN ELKAQLNISS TALNDLELFD FRLDFEAAKK
1260 1270 1280 1290 1300
RLYKLMIDSP HLKKIEDSLS HISKVLSYLK PLEVARNVVI SPLSNYNSAF
1310 1320 1330 1340 1350
YKGGIMFHAV YDDGSSRNMI AAGGRYDTLI SFFARPSGKK SSNTRKAVGF
1360 1370 1380 1390 1400
NLAWETIFGI AQNYFKLASG NRIKKRNRFL KDTAVDWKPS RCDVLISSFS
1410 1420 1430 1440 1450
NSLLDTIGVT ILNTLWKQNI KADMLRDCSS VDDVVTGAQQ DGIDWILLIK
1460 1470 1480 1490 1500
QQAYPLTNHK RKYKPLKIKK LSTNVDIDLD LDEFLTLYQQ ETGNKSLIND
1510 1520 1530 1540 1550
SLTLGDKADE FKRWDENSSA GSSQEGDIDD VVAGSTNNQK VIYVPNMATR
1560 1570 1580 1590 1600
SKKANKREKW VYEDAARNSS NMILHNLSNA PIITVDALRD ETLEIISITS
1610 1620 1630 1640 1650
LAQKEEWLRK VFGSGNNSTP RSFATSIYNN LSKEAHKGNR WAILYCHKTG

KSSVIDLQR
Length:1,659
Mass (Da):190,193
Last modified:September 5, 2006 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i1F56E4B046D52325
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA34636 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAA34881 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti70M → I in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti220 – 226TIKAKLP → NYKGKIA in AAA34881 (PubMed:3290651).Curated7
Sequence conflicti271 – 279LMSSEMMEN → YVFSNHGKS in AAA34881 (PubMed:3290651).Curated9
Sequence conflicti374M → I in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti392K → Q in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti395N → S in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti407F → C in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti411 – 413IPK → MPE in AAA34881 (PubMed:3290651).Curated3
Sequence conflicti475I → M in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti589P → A in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti604 – 605VL → FS in AAA34881 (PubMed:3290651).Curated2
Sequence conflicti622S → T in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti640 – 641IL → MI in AAA34881 (PubMed:3290651).Curated2
Sequence conflicti727F → C in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti839M → K in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti954E → Q in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti1144K → E in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti1328 – 1331TLIS → RFHT in AAA34881 (PubMed:3290651).Curated4
Sequence conflicti1348V → A in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti1356T → I in AAA34881 (PubMed:3290651).Curated1
Sequence conflicti1434V → I in AAA34881 (PubMed:3290651).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M27082 Genomic DNA Translation: AAA34636.1 Different initiation.
U51030 Genomic DNA Translation: AAB64461.1
M20487 Genomic DNA Translation: AAA34881.1 Sequence problems.
BK006938 Genomic DNA Translation: DAA12123.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S70139, OKBYN2

NCBI Reference Sequences

More...
RefSeqi
NP_010569.3, NM_001180591.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YDR283C_mRNA; YDR283C; YDR283C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851877

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YDR283C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27082 Genomic DNA Translation: AAA34636.1 Different initiation.
U51030 Genomic DNA Translation: AAB64461.1
M20487 Genomic DNA Translation: AAA34881.1 Sequence problems.
BK006938 Genomic DNA Translation: DAA12123.1
PIRiS70139, OKBYN2
RefSeqiNP_010569.3, NM_001180591.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZXEX-ray2.60A/B/C/D/E/F594-997[»]
1ZY4X-ray1.95A/B594-997[»]
1ZY5X-ray2.00A/B594-997[»]
1ZYCX-ray3.00A/B/C/D594-997[»]
1ZYDX-ray2.75A/B594-997[»]
2YZ0NMR-A1-138[»]
4OTMX-ray1.95A/B1519-1659[»]
SMRiP15442
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi32336, 239 interactors
DIPiDIP-2346N
IntActiP15442, 27 interactors
MINTiP15442
STRINGi4932.YDR283C

PTM databases

iPTMnetiP15442

Proteomic databases

MaxQBiP15442
PaxDbiP15442
PRIDEiP15442

Genome annotation databases

EnsemblFungiiYDR283C_mRNA; YDR283C; YDR283C
GeneIDi851877
KEGGisce:YDR283C

Organism-specific databases

SGDiS000002691, GCN2
VEuPathDBiFungiDB:YDR283C

Phylogenomic databases

eggNOGiKOG1035, Eukaryota
GeneTreeiENSGT00940000158121
HOGENOMiCLU_001222_2_0_1
InParanoidiP15442
OMAiGSEMIYE

Enzyme and pathway databases

BRENDAi2.7.11.20, 984
ReactomeiR-SCE-381042, PERK regulates gene expression

Miscellaneous databases

EvolutionaryTraceiP15442

Protein Ontology

More...
PROi
PR:P15442
RNActiP15442, protein

Family and domain databases

CDDicd00773, HisRS-like_core, 1 hit
Gene3Di3.10.110.10, 1 hit
3.40.50.800, 1 hit
InterProiView protein in InterPro
IPR036621, Anticodon-bd_dom_sf
IPR016255, Gcn2
IPR041715, HisRS-like_core
IPR024435, HisRS-related_dom
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR006575, RWD-domain
IPR008271, Ser/Thr_kinase_AS
IPR016135, UBQ-conjugating_enzyme/RWD
PfamiView protein in Pfam
PF12745, HGTP_anticodon2, 1 hit
PF00069, Pkinase, 3 hits
PF05773, RWD, 1 hit
PF13393, tRNA-synt_His, 1 hit
PIRSFiPIRSF000660, Ser/Thr_PK_GCN2, 1 hit
SMARTiView protein in SMART
SM00591, RWD, 1 hit
SM00220, S_TKc, 1 hit
SUPFAMiSSF54495, SSF54495, 1 hit
SSF56112, SSF56112, 2 hits
PROSITEiView protein in PROSITE
PS00107, PROTEIN_KINASE_ATP, 1 hit
PS50011, PROTEIN_KINASE_DOM, 2 hits
PS00108, PROTEIN_KINASE_ST, 1 hit
PS50908, RWD, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGCN2_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P15442
Secondary accession number(s): D6VSR3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: September 5, 2006
Last modified: June 2, 2021
This is version 227 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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