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Entry version 153 (08 May 2019)
Sequence version 2 (15 Mar 2005)
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Protein

eIF-2-alpha kinase GCN2

Gene

Eif2ak4

Organism
Mus musculus (Mouse)
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/EIF2S1) on 'Ser-52' in response to low amino acid availability (PubMed:10504407, PubMed:10655230, PubMed:12176355, PubMed:12215525, PubMed:15213227, PubMed:16054071, PubMed:16176978, PubMed:16121183, PubMed:15774759, PubMed:16601681, PubMed:26102367). Plays a role as an activator of the integrated stress response (ISR) required for adapatation to amino acid starvation. Converts phosphorylated eIF-2-alpha/EIF2S1 either to a competitive inhibitor of the 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 ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:10655230, PubMed:11106749, PubMed:12176355, PubMed:15213227, PubMed:16176978, PubMed:26102367). Binds uncharged tRNAs (By similarity). Involved in cell cycle arrest by promoting cyclin D1 mRNA translation repression after the unfolded protein response pathway (UPR) activation or cell cycle inhibitor CDKN1A/p21 mRNA translation activation in response to amino acid deprivation (PubMed:16176978, PubMed:26102367). Plays a role in the consolidation of synaptic plasticity, learning as well as formation of long-term memory (PubMed:16121183). Plays a role in neurite outgrowth inhibition (PubMed:23447528). Plays a role in feeding behavior to maintain amino acid homeostasis; contributes to the innate aversion toward diets of imbalanced amino acid composition (PubMed:16054071, PubMed:15774759). Plays a proapoptotic role in response to glucose deprivation (PubMed:20660158). Promotes global cellular protein synthesis repression in response to UV irradiation independently of the stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) and p38 MAPK signaling pathways (PubMed:12176355).By similarity14 Publications
(Microbial infection) Plays a role in the antiviral response against alphavirus infection; impairs early viral mRNA translation of the incoming genomic virus RNA, thus preventing alphavirus replication.1 Publication
(Microbial infection) Plays a role in modulating the adaptive immune response to Yellow fever virus infection; promotes dendritic cells to initiate autophagy and antigene presentation to both CD4+ and CD8+ T-cells under amino acid starvation.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 <a href="http://www.uniprot.org/help/function_section">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

(Microbial infection) Kinase activity is enhanced by alphavirus genomic RNA sequences (PubMed:16601681). Kinase activity is stimulated upon binding to uncharged tRNAs (PubMed:16601681). Activated by serum starvation (in vitro) (PubMed:10504407).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei618ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei846Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi595 – 603ATPPROSITE-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 processActivation of host autophagy by virus, Adaptive immunity, Antiviral defense, Cell cycle, Differentiation, Growth arrest, Host-virus interaction, Immunity, Neurogenesis, Stress response, Translation regulation
LigandATP-binding, Nucleotide-binding

<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_and_taxonomy_section">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 GCN2Curated
Alternative name(s):
Eukaryotic translation initiation factor 2-alpha kinase 4Imported (EC:2.7.11.13 Publications)
GCN2-like protein
Short name:
mGCN2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:Eif2ak4Imported
Synonyms:Gcn2, Kiaa1338
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 2

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:1353427 Eif2ak4

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

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

Mice are viable, fertile, and exhibit no phenotypic abnormalities under standard growth conditions (PubMed:12215525). Show an increase in prenatal and neonatal mortalities when essential amino acids are absent in the maternal diet during gestation (PubMed:12215525, PubMed:15213227). In response to nutrient deprivation, display reduced abilities to chronically down-regulate hepatic protein synthesis, resulting in preservation of liver mass relative to body size and enhanced skeletal muscle loss (PubMed:15213227). Mice exhibit a lowered threshold for the induction of strong and robust long-term potentiation (LTP) in the CA1 neurons of the hippocampus and the consolidation of long-term memory (PubMed:16121183). Knockout and conditional knockout in the brain result in a diminution of the rate of food consumption and an impairment in the food aversion response in mice fed an imbalanced amino acid diet (PubMed:16054071). Mice are more susceptible to intranasal Sindbis virus infection, with high virus titers in the brain compared to similarly infected control animals (PubMed:16601681). Mice infected with yellow fever virus show a decrease in dendritic cell autophagy and an impairment in their capacity to present antigens to T-cells under amino acid starvation (PubMed:24310610).6 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi618K → R: Inhibits autophosphorylation, eIF-2-alpha phosphorylation and antiviral activity against Sindbis virus. 1 Publication1
Mutagenesisi1142F → L: Decreases autophosphorylation, binding to tRNA and Sindbis virus genomic RNA and eIF-2-alpha phosphorylation in amino acid-starved cells; when associated with I-1143. 1 Publication1
Mutagenesisi1143R → I: Decreases autophosphorylation, binding to tRNA and Sindbis virus genomic RNA and eIF-2-alpha phosphorylation in amino acid-starved cells; when associated with L-1142. 1 Publication1

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000859481 – 1648eIF-2-alpha kinase GCN2Add BLAST1648

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 residuei230PhosphoserineBy similarity1
Modified residuei666PhosphothreonineBy similarity1
Modified residuei869PhosphothreonineBy similarity1
Modified residuei898Phosphothreonine; by autocatalysis2 Publications1
Modified residuei903Phosphothreonine; by autocatalysisBy similarity1
Modified residuei1258N6-acetyllysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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-898 is increased upon amino acid starvation and in UV irradiation cells and inhibited in presence of IMPACT (PubMed:10504407, PubMed:10655230, PubMed:11106749, PubMed:12176355, PubMed:16601681, PubMed:24333428).6 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9QZ05

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

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PaxDbi
Q9QZ05

PeptideAtlas

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PeptideAtlasi
Q9QZ05

PRoteomics IDEntifications database

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PRIDEi
Q9QZ05

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9QZ05

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q9QZ05

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in liver (PubMed:10504407). Expressed predominantly in the hippocampal CA1 region and the dentate gyrus, and to a lesser degree in CA3 (at protein level) (PubMed:16121183). Expressed in liver, lung, brain, kidney, skeletal muscle and testis (PubMed:10504407, PubMed:10655230). Expressed weakly in heart and spleen (PubMed:10655230). Expressed in the hippocampal CA1 and CA3 regions, the dentate gyrus and cerebellum (PubMed:16121183). Isoform 1 is widely expressed (PubMed:12215525). Isoform 1 is expressed in brain, liver, skeletal muscle and testis (PubMed:10655230). Isoform 3 is expressed in lung, brain, testis, prostate and choroid plexus (PubMed:12215525). Isoform 4 is expressed in muscle, lung, kidney, brain, testis and prostate (PubMed:10655230, PubMed:12215525).4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000005102 Expressed in 269 organ(s), highest expression level in secondary oocyte

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9QZ05 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9QZ05 MM

<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_section">'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_section">'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 (By similarity). Interacts with GCN1; this interaction stimulates EIF2AK4/GCN2 kinase activity and is impaired by IMPACT upon a variety of stress conditions, such as amino acid depletion, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation (PubMed:24333428). Interacts with DNAJC3; this interaction inhibits EIF2AK4/GCN2 kinase activity during endoplasmic reticulum (ER), hypothermic and amino acid-starving stress conditions (PubMed:25329545).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
205123, 2 interactors

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000005233

<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

11648
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
Q9QZ05

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q9QZ05

<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_and_domains_section">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>Domaini25 – 137RWDPROSITE-ProRule annotationAdd BLAST113
Domaini286 – 538Protein kinase 1PROSITE-ProRule annotationAdd BLAST253
Domaini589 – 1000Protein kinase 2PROSITE-ProRule annotationAdd BLAST412

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>Regioni1021 – 1492Histidyl-tRNA synthetase-likeAdd BLAST472

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili146 – 205Sequence analysisAdd BLAST60

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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi483 – 490Poly-Leu8

<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 histidyl-tRNA synthetase-like region and protein kinase domains are necessary for eIF-2-alpha kinase activity and eIF-2-alpha-mediated translational control (PubMed:10655230). The histidyl-tRNA synthetase-like domain is necessary for binding to uncharged tRNAs (PubMed:16601681). Kinase domain 1 is a degenerate kinase domain (PubMed:10504407).2 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

Coiled coil, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1035 Eukaryota
COG0124 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156798

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9QZ05

KEGG Orthology (KO)

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KOi
K16196

Database of Orthologous Groups

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OrthoDBi
64059at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9QZ05

Family and domain databases

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, 2 hits

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_length">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>Sequences (6+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

This entry describes 6 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 6 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9QZ05-1) [UniParc]FASTAAdd to basket
Also known as: GCN2beta

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAGGRGASGR GRAEPQESYS QRQDHELQAL EAIYGSDFQD LRPDARGRVR
60 70 80 90 100
EPPEINLVLY PQGLAGEEVY VQVELQVKCP PTYPDVVPEI ELKNAKGLSN
110 120 130 140 150
ESVNLLKSHL EELAKKQCGE VMIFELAHHV QSFLSEHNKP PPKSFHEEML
160 170 180 190 200
ERQAQEKQQR LLEARRKEEQ EQREILHEIQ RRKEEIKEEK KRKEMAKQER
210 220 230 240 250
LEITSLTNQD YASKRDPAGH RAAAILHGGS PDFVGNGKAR TYSSGRSRRE
260 270 280 290 300
RQYSVCSGEP SPGSCDILHF SVGSPDQLMV HKGRCVGSDE QLGKVVYNAL
310 320 330 340 350
ETATGSFVLL HEWVLQWQKM GPCLTSQEKE KIDKCKRQIQ GAETEFSSLV
360 370 380 390 400
KLSHPNIVRY FAMNSREEED SIVIDILAEH VSGISLATHL SHSGPVPAHQ
410 420 430 440 450
LRKYTAQLLA GLDYLHSNSV VHKVLSASSV LVDAEGTVKI TDYSISKRLA
460 470 480 490 500
DICKEDVFEQ ARVRFSDSAL PYKTGKKGDV WRLGLLLLSL SQGQECGEYP
510 520 530 540 550
VTIPSDLPAD FQDFLKKCVC LDDKERWSPQ QLLKHSFINP QPKLPLVEQS
560 570 580 590 600
PEDSGGQDYI ETVIPSNQLP SAAFFSETQK QFSRYFIEFE ELQLLGKGAF
610 620 630 640 650
GAVIKVQNKL DGCCYAVKRI PINPASRHFR RIKGEVTLLS RLHHENIVRY
660 670 680 690 700
YNAWIERHER PAVPGTPPPD CTPQAQDSPA TCGKTSGDTE ELGSVEAAAP
710 720 730 740 750
PPILSSSVEW STSAERSTST RFPVTGQDSS SDEEDEDERD GVFSQSFLPA
760 770 780 790 800
SDSDSDIIFD NEDENSKSQN QDEDCNQKDG SHEIEPSVTA EAVHYLYIQM
810 820 830 840 850
EYCEKSTLRD TIDQGLFRDT SRLWRLFREI LDGLAYIHEK GMIHRDLKPV
860 870 880 890 900
NIFLDSDDHV KIGDFGLATD HLAFTAEGKQ DDQAGDGVIK SDPSGHLTGM
910 920 930 940 950
VGTALYVSPE VQGSTKSAYN QKVDLFSLGI IFFEMSYHPM VTASERIFVL
960 970 980 990 1000
NQLRDPTSPK FPDDFDDGEH TKQKSVISWL LNHDPAKRPT AMELLKSELL
1010 1020 1030 1040 1050
PPPQMEESEL HEVLHHTLAN IDGKAYRTMM SQIFCQHISP AIDYTYDSDI
1060 1070 1080 1090 1100
LKGNFLIRTA KIQQLVCETI VRVFKRHGAV QLCTPLLLPR NRQIYEHNEA
1110 1120 1130 1140 1150
ALFMDHSGML VMLPFDLRVP FARYVARNNI LNLKRYCIER VFRPRKLDRF
1160 1170 1180 1190 1200
HPKELLECAF DIVTSTTNSS LPTAETIYTI YEIIQEFPAL QERNYSIYLN
1210 1220 1230 1240 1250
HTMLLKAILL HCGIPEDKLS QVYVILYDAV TEKLTRREVE AKFCNLSLSS
1260 1270 1280 1290 1300
NSLCRLYKFI EQKGDLQDLT PTINSLIKQK TGVAQLVKYS LKDLEDVVGL
1310 1320 1330 1340 1350
LKKLGVKLQV SINLGLVYKV QQHTGIIFQF LAFSKRRQRV VPEILAAGGR
1360 1370 1380 1390 1400
YDLLIPKFRG PQTVGPVPTA VGVSIAIDKI FAAVLNMEEP VTVSSCDLLV
1410 1420 1430 1440 1450
VSVGQMSMSR AINLTQKLWT AGITAEIMYD WSQSQEELQE YCRHHEITYV
1460 1470 1480 1490 1500
ALVSDKEGSH VKVKSFEKER QTEKRVLESD LVDHVMQKLR TKVGDERNFR
1510 1520 1530 1540 1550
DASDNLAVQT LKGSFSNASG LFEIHGTTVV PNVIVLAPEK LSASTRRRHE
1560 1570 1580 1590 1600
IQVQTRLQTT LANLHQKSSE IEILAVDLPK ETILQFLSLE WDADEQAFNT
1610 1620 1630 1640
TVKQLLSRLP KQRYLKLVCD EIYNIKVEKK VSVLFLYSYR DDYYRILF
Length:1,648
Mass (Da):186,487
Last modified:March 15, 2005 - v2
<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:iF27841DDB317EFCB
GO
Isoform 2 (identifier: Q9QZ05-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-112: Missing.
     113-120: LAKKQCGE → MPTYIPRC

Note: No experimental confirmation available.
Show »
Length:1,536
Mass (Da):174,179
Checksum:i71FE1EBAFBAB53A9
GO
Isoform 3 (identifier: Q9QZ05-3) [UniParc]FASTAAdd to basket
Also known as: GCN2gamma

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.
     79-86: CPPTYPDV → MRTQRALL

Show »
Length:1,570
Mass (Da):177,919
Checksum:i673582EE560E4421
GO
Isoform 4 (identifier: Q9QZ05-4) [UniParc]FASTAAdd to basket
Also known as: GCN2alpha

The sequence of this isoform differs from the canonical sequence as follows:
     1-278: Missing.

Show »
Length:1,370
Mass (Da):154,948
Checksum:iCD2E9DFB9920FD0F
GO
Isoform 5 (identifier: Q9QZ05-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-801: Missing.
     802-840: YCEKSTLRDT...LDGLAYIHEK → MGEDSSSGHH...VDGLFIVFQQ
     1120-1148: PFARYVARNNILNLKRYCIERVFRPRKLD → SWDAAPLKTRPSQTPPLQPYPGEPHVGNT
     1149-1648: Missing.

Show »
Length:347
Mass (Da):38,820
Checksum:i46136A7A0F53C392
GO
Isoform 6 (identifier: Q9QZ05-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-121: Missing.
     607-653: QNKLDGCCYA...HENIVRYYNA → RQGCPQSLLS...EAGSTFTSRS
     654-1648: Missing.

Note: No experimental confirmation available.
Show »
Length:532
Mass (Da):59,991
Checksum:iB0E034754953EB1B
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A2AUM0A2AUM0_MOUSE
eIF-2-alpha kinase GCN2
Eif2ak4
1,648Annotation score:

Annotation score:2 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>
A2AUM1A2AUM1_MOUSE
eIF-2-alpha kinase GCN2
Eif2ak4
1,570Annotation score:

Annotation score:2 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>
A2AUM2A2AUM2_MOUSE
eIF-2-alpha kinase GCN2
Eif2ak4
1,527Annotation score:

Annotation score:2 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>
A2AUL9A2AUL9_MOUSE
eIF-2-alpha kinase GCN2
Eif2ak4
653Annotation score:

Annotation score:1 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 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 conflicti76Q → R in BAB28984 (PubMed:16141072).Curated1
Sequence conflicti91E → D in BAB28984 (PubMed:16141072).Curated1
Sequence conflicti262P → L (PubMed:16141072).Curated1
Sequence conflicti262P → L in AAH23958 (PubMed:15489334).Curated1
Sequence conflicti517 – 539KCVCL…HSFIN → NPRRPKRRPQETSQEVWFC in BAC98144 (PubMed:14621295).CuratedAdd BLAST23
Sequence conflicti682C → Y in AAG22589 (PubMed:10655230).Curated1
Sequence conflicti682C → Y in AAG22590 (PubMed:10655230).Curated1
Sequence conflicti682C → Y in AAG22591 (PubMed:10655230).Curated1
Sequence conflicti682C → Y in BAC98144 (PubMed:14621295).Curated1
Sequence conflicti725 – 727TGQ → MGE (PubMed:16141072).Curated3
Sequence conflicti784I → V in AAG22589 (PubMed:10655230).Curated1
Sequence conflicti784I → V in AAG22590 (PubMed:10655230).Curated1
Sequence conflicti784I → V in AAG22591 (PubMed:10655230).Curated1
Sequence conflicti784I → V in BAC98144 (PubMed:14621295).Curated1
Sequence conflicti853F → I in AAH72637 (PubMed:15489334).Curated1
Sequence conflicti882D → G in AAG22589 (PubMed:10655230).Curated1
Sequence conflicti882D → G in AAG22590 (PubMed:10655230).Curated1
Sequence conflicti882D → G in AAG22591 (PubMed:10655230).Curated1
Sequence conflicti887G → R in AAG22589 (PubMed:10655230).Curated1
Sequence conflicti887G → R in AAG22590 (PubMed:10655230).Curated1
Sequence conflicti887G → R in AAG22591 (PubMed:10655230).Curated1
Sequence conflicti887G → R in BAC98144 (PubMed:14621295).Curated1
Sequence conflicti895G → C in BAC98144 (PubMed:14621295).Curated1
Sequence conflicti1021I → T in AAG22589 (PubMed:10655230).Curated1
Sequence conflicti1021I → T in AAG22590 (PubMed:10655230).Curated1
Sequence conflicti1021I → T in AAG22591 (PubMed:10655230).Curated1
Sequence conflicti1033I → L in AAG22589 (PubMed:10655230).Curated1
Sequence conflicti1033I → L in AAG22590 (PubMed:10655230).Curated1
Sequence conflicti1033I → L in AAG22591 (PubMed:10655230).Curated1
Sequence conflicti1038I → S in AAG22589 (PubMed:10655230).Curated1
Sequence conflicti1038I → S in AAG22590 (PubMed:10655230).Curated1
Sequence conflicti1038I → S in AAG22591 (PubMed:10655230).Curated1
Sequence conflicti1167T → A in AAG22589 (PubMed:10655230).Curated1
Sequence conflicti1167T → A in AAG22590 (PubMed:10655230).Curated1
Sequence conflicti1167T → A in AAG22591 (PubMed:10655230).Curated1
Sequence conflicti1183I → V in AAG22589 (PubMed:10655230).Curated1
Sequence conflicti1183I → V in AAG22590 (PubMed:10655230).Curated1
Sequence conflicti1183I → V in AAG22591 (PubMed:10655230).Curated1
Sequence conflicti1275S → A in BAB27580 (PubMed:16141072).Curated1
Sequence conflicti1283V → I in AAG22589 (PubMed:10655230).Curated1
Sequence conflicti1283V → I in AAG22590 (PubMed:10655230).Curated1
Sequence conflicti1283V → I in AAG22591 (PubMed:10655230).Curated1
Sequence conflicti1296D → E in AAG22589 (PubMed:10655230).Curated1
Sequence conflicti1296D → E in AAG22590 (PubMed:10655230).Curated1
Sequence conflicti1296D → E in AAG22591 (PubMed:10655230).Curated1
Sequence conflicti1324T → N in AAG22589 (PubMed:10655230).Curated1
Sequence conflicti1324T → N in AAG22590 (PubMed:10655230).Curated1
Sequence conflicti1324T → N in AAG22591 (PubMed:10655230).Curated1
Sequence conflicti1363 – 1364TV → AL in AAG22589 (PubMed:10655230).Curated2
Sequence conflicti1363 – 1364TV → AL in AAG22590 (PubMed:10655230).Curated2
Sequence conflicti1383A → V in CAB58363 (PubMed:10504407).Curated1
Sequence conflicti1383A → V in BAC98144 (PubMed:14621295).Curated1
Sequence conflicti1388E → G in AAG22589 (PubMed:10655230).Curated1
Sequence conflicti1388E → G in AAG22590 (PubMed:10655230).Curated1
Sequence conflicti1388E → G in AAG22591 (PubMed:10655230).Curated1
Sequence conflicti1403V → A in AAG22589 (PubMed:10655230).Curated1
Sequence conflicti1403V → A in AAG22590 (PubMed:10655230).Curated1
Sequence conflicti1403V → A in AAG22591 (PubMed:10655230).Curated1
Sequence conflicti1467E → G in BAB27580 (PubMed:16141072).Curated1
Sequence conflicti1532 – 1537NVIVLA → TVSVIS in AAG22589 (PubMed:10655230).Curated6
Sequence conflicti1532 – 1537NVIVLA → TVSVIS in AAG22590 (PubMed:10655230).Curated6
Sequence conflicti1540K → M in BAB27580 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0130391 – 801Missing in isoform 5. 1 PublicationAdd BLAST801
Alternative sequenceiVSP_0130401 – 278Missing in isoform 4. 1 PublicationAdd BLAST278
Alternative sequenceiVSP_0130411 – 121Missing in isoform 6. 1 PublicationAdd BLAST121
Alternative sequenceiVSP_0130421 – 112Missing in isoform 2. 1 PublicationAdd BLAST112
Alternative sequenceiVSP_0130431 – 78Missing in isoform 3. 1 PublicationAdd BLAST78
Alternative sequenceiVSP_01304479 – 86CPPTYPDV → MRTQRALL in isoform 3. 1 Publication8
Alternative sequenceiVSP_013045113 – 120LAKKQCGE → MPTYIPRC in isoform 2. 1 Publication8
Alternative sequenceiVSP_013046607 – 653QNKLD…RYYNA → RQGCPQSLLSFLFPFHGLTG LVSILGVEREVNKIRLFEAG STFTSRS in isoform 6. 1 PublicationAdd BLAST47
Alternative sequenceiVSP_013047654 – 1648Missing in isoform 6. 1 PublicationAdd BLAST995
Alternative sequenceiVSP_013048802 – 840YCEKS…YIHEK → MGEDSSSGHHNPLPLKSGNR VLSSVWEEAVDGLFIVFQQ in isoform 5. 1 PublicationAdd BLAST39
Alternative sequenceiVSP_0130491120 – 1148PFARY…PRKLD → SWDAAPLKTRPSQTPPLQPY PGEPHVGNT in isoform 5. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_0130501149 – 1648Missing in isoform 5. 1 PublicationAdd BLAST500

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AJ243533 mRNA Translation: CAB58363.1
AF193342 mRNA Translation: AAG22589.1
AF193343 mRNA Translation: AAG22590.1
AF193344 mRNA Translation: AAG22591.1
AK011380 mRNA Translation: BAB27580.1
AK013758 mRNA Translation: BAB28984.1
AK077199 mRNA Translation: BAC36677.1
AL929163 Genomic DNA No translation available.
BC023958 mRNA Translation: AAH23958.1
BC072637 mRNA Translation: AAH72637.1
AK129334 Transcribed RNA Translation: BAC98144.2

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS16576.1 [Q9QZ05-1]
CCDS50669.1 [Q9QZ05-2]

NCBI Reference Sequences

More...
RefSeqi
NP_001171277.1, NM_001177806.1 [Q9QZ05-2]
NP_038747.2, NM_013719.3
XP_006499688.1, XM_006499625.3 [Q9QZ05-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000102527; ENSMUSP00000099586; ENSMUSG00000005102 [Q9QZ05-2]
ENSMUST00000110869; ENSMUSP00000106493; ENSMUSG00000005102 [Q9QZ05-5]
ENSMUST00000110870; ENSMUSP00000106494; ENSMUSG00000005102 [Q9QZ05-4]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
27103

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:27103

UCSC genome browser

More...
UCSCi
uc008lrx.2 mouse [Q9QZ05-2]
uc008lry.1 mouse [Q9QZ05-1]
uc008lrz.1 mouse [Q9QZ05-5]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AJ243533 mRNA Translation: CAB58363.1
AF193342 mRNA Translation: AAG22589.1
AF193343 mRNA Translation: AAG22590.1
AF193344 mRNA Translation: AAG22591.1
AK011380 mRNA Translation: BAB27580.1
AK013758 mRNA Translation: BAB28984.1
AK077199 mRNA Translation: BAC36677.1
AL929163 Genomic DNA No translation available.
BC023958 mRNA Translation: AAH23958.1
BC072637 mRNA Translation: AAH72637.1
AK129334 Transcribed RNA Translation: BAC98144.2
CCDSiCCDS16576.1 [Q9QZ05-1]
CCDS50669.1 [Q9QZ05-2]
RefSeqiNP_001171277.1, NM_001177806.1 [Q9QZ05-2]
NP_038747.2, NM_013719.3
XP_006499688.1, XM_006499625.3 [Q9QZ05-2]

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
1UKXNMR-A17-139[»]
4OTNX-ray1.90A/B1514-1648[»]
SMRiQ9QZ05
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205123, 2 interactors
STRINGi10090.ENSMUSP00000005233

PTM databases

iPTMnetiQ9QZ05
PhosphoSitePlusiQ9QZ05

Proteomic databases

jPOSTiQ9QZ05
PaxDbiQ9QZ05
PeptideAtlasiQ9QZ05
PRIDEiQ9QZ05

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102527; ENSMUSP00000099586; ENSMUSG00000005102 [Q9QZ05-2]
ENSMUST00000110869; ENSMUSP00000106493; ENSMUSG00000005102 [Q9QZ05-5]
ENSMUST00000110870; ENSMUSP00000106494; ENSMUSG00000005102 [Q9QZ05-4]
GeneIDi27103
KEGGimmu:27103
UCSCiuc008lrx.2 mouse [Q9QZ05-2]
uc008lry.1 mouse [Q9QZ05-1]
uc008lrz.1 mouse [Q9QZ05-5]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
440275
MGIiMGI:1353427 Eif2ak4

Rodent Unidentified Gene-Encoded large proteins database

More...
Rougei
Search...

Phylogenomic databases

eggNOGiKOG1035 Eukaryota
COG0124 LUCA
GeneTreeiENSGT00940000156798
InParanoidiQ9QZ05
KOiK16196
OrthoDBi64059at2759
PhylomeDBiQ9QZ05

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Eif2ak4 mouse
EvolutionaryTraceiQ9QZ05

Protein Ontology

More...
PROi
PR:Q9QZ05

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000005102 Expressed in 269 organ(s), highest expression level in secondary oocyte
ExpressionAtlasiQ9QZ05 baseline and differential
GenevisibleiQ9QZ05 MM

Family and domain databases

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, 2 hits
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiE2AK4_MOUSE
<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: Q9QZ05
Secondary accession number(s): A2AUM3
, A2AUM4, Q6GQT4, Q6ZPT5, Q8C5S0, Q8CIF5, Q9CT30, Q9CUV9, Q9ESB6, Q9ESB7, Q9ESB8
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: May 8, 2019
This is version 153 of the entry and version 2 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 programChordata 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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