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Protein

Interferon-induced, double-stranded RNA-activated protein kinase

Gene

EIF2AK2

Organism
Homo sapiens (Human)
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

IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1). Inhibits viral replication via phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (EIF2S1), this phosphorylation impairs the recycling of EIF2S1 between successive rounds of initiation leading to inhibition of translation which eventually results in shutdown of cellular and viral protein synthesis. Also phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11. In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteosomal degradation. Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding proinflammatory cytokines and IFNs. Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6. Can act as both a positive and negative regulator of the insulin signaling pathway (ISP). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes. Can trigger apoptosis via FADD-mediated activation of CASP8. Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin.24 Publications

<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 ‘Function’ 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

Initially produced in an inactive form and is activated by binding to viral dsRNA, which causes dimerization and autophosphorylation in the activation loop and stimulation of function. ISGylation can activate it in the absence of viral infection. Can also be activated by heparin, proinflammatory stimuli, growth factors, cytokines, oxidative stress and the cellular protein PRKRA. Activity is markedly stimulated by manganese ions. Activation is blocked by the viral components HIV-1 Tat protein and large amounts of HIV-1 trans-activation response (TAR) RNA element as well as by the cellular proteins TARBP2, DUS2L, NPM1, NCK1 and ADAR. Down-regulated by Toscana virus (TOS) and Rift valley fever virus (RVFV) NSS which promote its proteasomal degradation. Inhibited by vaccinia virus protein E3, probably via dsRNA sequestering.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei296ATP1
<p>This subsection of the ‘Function’ 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 sitei414Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi273 – 281ATPPROSITE-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

  • ATP binding Source: UniProtKB-KW
  • double-stranded RNA binding Source: MGI
  • eukaryotic translation initiation factor 2alpha kinase activity Source: UniProtKB
  • identical protein binding Source: IntAct
  • non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  • protein kinase activity Source: UniProtKB
  • protein phosphatase regulator activity Source: ProtInc
  • protein serine/threonine kinase activity Source: ProtInc
  • RNA binding Source: UniProtKB

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 functionKinase, RNA-binding, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase
Biological processAntiviral defense, Host-virus interaction, Immunity, Innate immunity, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1169408 ISG15 antiviral mechanism
R-HSA-169131 Inhibition of PKR

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P19525

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P19525

<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:
Interferon-induced, double-stranded RNA-activated protein kinase (EC:2.7.11.1)
Alternative name(s):
Eukaryotic translation initiation factor 2-alpha kinase 2
Short name:
eIF-2A protein kinase 2
Interferon-inducible RNA-dependent protein kinase
P1/eIF-2A protein kinase
Protein kinase RNA-activated
Short name:
PKR
Short name:
Protein kinase R1 Publication
Tyrosine-protein kinase EIF2AK2 (EC:2.7.10.2)
p68 kinase
<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:EIF2AK2
Synonyms:PKR, PRKR
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000055332.16

Human Gene Nomenclature Database

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HGNCi
HGNC:9437 EIF2AK2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
176871 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P19525

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<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

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>Mutagenesisi59 – 60SK → AA in FL-PKR-2AI; moderate loss of activity but no effect on dsRNA binding. 1 Publication2
Mutagenesisi60K → A: Impairs dsRNA binding but not dimerization or activity. 1 Publication1
Mutagenesisi67A → E: Significant loss of activity; loss of dsRNA binding and dimerization. 1 Publication1
Mutagenesisi83S → A: No effect on enzymatic activity; when associated with A-88; A-89 and A-90. 1 Publication1
Mutagenesisi88T → A: No effect on enzymatic activity; when associated with A-83; A-89 and A-90. 1 Publication1
Mutagenesisi89T → A: No effect on enzymatic activity; when associated with A-83; A-88 and A-90. 1 Publication1
Mutagenesisi90T → A: No effect on enzymatic activity; when associated with A-83; A-88 and A-89. 1 Publication1
Mutagenesisi149 – 150TK → AA in FL-PKR-2AII; no effect on activity. 1 Publication2
Mutagenesisi242S → A: Moderate loss of activity; when associated with A-255 and A-258. 1 Publication1
Mutagenesisi244 – 296Missing : Loss of activity. 1 PublicationAdd BLAST53
Mutagenesisi255T → A: Moderate loss of activity; when associated with A-242 and A-255. 1 Publication1
Mutagenesisi258T → A: Moderate loss of activity. 1 Publication1
Mutagenesisi296K → R: Loss of activity. 1 Publication1
Mutagenesisi446T → A: Significant loss of activity and impairs autophosphorylation of T-451. 1 Publication1
Mutagenesisi451T → A: Loss of activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
5610

Open Targets

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OpenTargetsi
ENSG00000055332

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA33779

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5785

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2016

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
EIF2AK2

Domain mapping of disease mutations (DMDM)

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DMDMi
125527

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<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_00000859452 – 551Interferon-induced, double-stranded RNA-activated protein kinaseAdd BLAST550

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 residuei2N-acetylalanineCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki69Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)1 Publication
Modified residuei83PhosphoserineCombined sources1 Publication1
Modified residuei88Phosphothreonine; by autocatalysis1 Publication1
Modified residuei89Phosphothreonine; by autocatalysis1 Publication1
Modified residuei90Phosphothreonine; by autocatalysis1 Publication1
Modified residuei101Phosphotyrosine; by autocatalysis1 Publication1
Cross-linki159Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)1 Publication
Modified residuei162Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei242Phosphoserine; by autocatalysis1 Publication1
Modified residuei255Phosphothreonine; by autocatalysis1 Publication1
Modified residuei258Phosphothreonine; by autocatalysis1 Publication1
Modified residuei293Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei446Phosphothreonine; by autocatalysis2 Publications1
Modified residuei451Phosphothreonine; by autocatalysis2 Publications1
Modified residuei456PhosphoserineCombined sources1
Modified residuei542PhosphoserineCombined sources1

<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 on several Ser, Thr and Tyr residues. Autophosphorylation of Thr-451 is dependent on Thr-446 and is stimulated by dsRNA binding and dimerization. Autophosphorylation apparently leads to the activation of the kinase. Tyrosine autophosphorylation is essential for efficient dsRNA-binding, dimerization, and kinase activation.7 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P19525

MaxQB - The MaxQuant DataBase

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MaxQBi
P19525

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

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PaxDbi
P19525

PeptideAtlas

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PeptideAtlasi
P19525

PRoteomics IDEntifications database

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PRIDEi
P19525

ProteomicsDB human proteome resource

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ProteomicsDBi
53670

Consortium for Top Down Proteomics

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TopDownProteomicsi
P19525-1 [P19525-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P19525

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

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PhosphoSitePlusi
P19525

SwissPalm database of S-palmitoylation events

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SwissPalmi
P19525

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P19525

<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

Highly expressed in thymus, spleen and bone marrow compared to non-hematopoietic tissues such as small intestine, liver, or kidney tissues. Colocalizes with GSK3B and TAU in the Alzheimer disease (AD) brain. Elevated levels seen in breast and colon carcinomas,and which correlates with tumor progression and invasiveness or risk of progression.2 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By type I interferons.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000055332 Expressed in 238 organ(s), highest expression level in oviduct epithelium

CleanEx database of gene expression profiles

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CleanExi
HS_EIF2AK2

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P19525 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P19525 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB003845
HPA019795
HPA063893

<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. Interacts with STRBP (By similarity). Interacts with DNAJC3. Forms a complex with FANCA, FANCC, FANCG and HSP70. Interacts with ADAR/ADAR1. Interacts with IRS1 (By similarity). The inactive form interacts with NCK1 and GSN. Interacts (via the kinase catalytic domain) with STAT3 (via SH2 domain), TRAF2 (C-terminus), TRAF5 (C-terminus) and TRAF6 (C-terminus). Interacts with MAP2K6, IKBKB/IKKB, NPM1, TARBP2, NLRP1, NLRP3, NLRC4 and AIM2. Interacts (via DRBM 1 domain) with DUS2L (via DRBM domain). Interacts with DHX9 (via N-terminus) and this interaction is dependent upon activation of the kinase.By similarity19 Publications
(Microbial infection) Interacts with human herpes simplex virus 1 (HHV-1) protein US11 in an RNA-dependent manner.1 Publication
(Microbial infection) The inactive form interacts with Toscana virus (TOS) NSS.1 Publication
(Microbial infection) Interacts with herpes virus 8 protein v-IRF2; this interaction inhibits EIF2AK2 activation.1 Publication
(Microbial infection) Interacts with vaccinia protein E3.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111596, 181 interactors

Database of interacting proteins

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DIPi
DIP-2657N

Protein interaction database and analysis system

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IntActi
P19525, 72 interactors

Molecular INTeraction database

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MINTi
P19525

STRING: functional protein association networks

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STRINGi
9606.ENSP00000233057

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P19525

<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

1551
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P19525

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

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SMRi
P19525

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
P19525

<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>Domaini9 – 77DRBM 1PROSITE-ProRule annotationAdd BLAST69
Domaini100 – 167DRBM 2PROSITE-ProRule annotationAdd BLAST68
Domaini267 – 538Protein kinasePROSITE-ProRule annotationAdd BLAST272
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati331 – 3431Add BLAST13
Repeati345 – 3572Add BLAST13

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>Regioni266 – 551Interaction with TRAF51 PublicationAdd BLAST286
Regioni331 – 3572 X 13 AA approximate repeatsAdd BLAST27

<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
KOG1033 Eukaryota
ENOG410XS0B LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000160736

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000234351

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG051430

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P19525

KEGG Orthology (KO)

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KOi
K16195

Identification of Orthologs from Complete Genome Data

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OMAi
ELLYICP

Database of Orthologous Groups

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OrthoDBi
EOG091G088F

Database for complete collections of gene phylogenies

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PhylomeDBi
P19525

TreeFam database of animal gene trees

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TreeFami
TF317576

Family and domain databases

Conserved Domains Database

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CDDi
cd00048 DSRM, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR014720 dsRBD_dom
IPR011009 Kinase-like_dom_sf
IPR033366 PKR
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

The PANTHER Classification System

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PANTHERi
PTHR11042:SF102 PTHR11042:SF102, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00035 dsrm, 2 hits
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00358 DSRM, 2 hits
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50137 DS_RBD, 2 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <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 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P19525-1) [UniParc]FASTAAdd to basket

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
MAGDLSAGFF MEELNTYRQK QGVVLKYQEL PNSGPPHDRR FTFQVIIDGR
60 70 80 90 100
EFPEGEGRSK KEAKNAAAKL AVEILNKEKK AVSPLLLTTT NSSEGLSMGN
110 120 130 140 150
YIGLINRIAQ KKRLTVNYEQ CASGVHGPEG FHYKCKMGQK EYSIGTGSTK
160 170 180 190 200
QEAKQLAAKL AYLQILSEET SVKSDYLSSG SFATTCESQS NSLVTSTLAS
210 220 230 240 250
ESSSEGDFSA DTSEINSNSD SLNSSSLLMN GLRNNQRKAK RSLAPRFDLP
260 270 280 290 300
DMKETKYTVD KRFGMDFKEI ELIGSGGFGQ VFKAKHRIDG KTYVIKRVKY
310 320 330 340 350
NNEKAEREVK ALAKLDHVNI VHYNGCWDGF DYDPETSDDS LESSDYDPEN
360 370 380 390 400
SKNSSRSKTK CLFIQMEFCD KGTLEQWIEK RRGEKLDKVL ALELFEQITK
410 420 430 440 450
GVDYIHSKKL IHRDLKPSNI FLVDTKQVKI GDFGLVTSLK NDGKRTRSKG
460 470 480 490 500
TLRYMSPEQI SSQDYGKEVD LYALGLILAE LLHVCDTAFE TSKFFTDLRD
510 520 530 540 550
GIISDIFDKK EKTLLQKLLS KKPEDRPNTS EILRTLTVWK KSPEKNERHT

C
Length:551
Mass (Da):62,094
Last modified:May 1, 1991 - 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:i815AD83ACAB45DA3
GO
Isoform 2 (identifier: P19525-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     263-303: Missing.

Note: No experimental confirmation available.
Show »
Length:510
Mass (Da):57,391
Checksum:i6EC61AFC54DEFCA4
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8WBH4F8WBH4_HUMAN
Interferon-induced, double-stranded...
EIF2AK2
102Annotation 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>
C9JZT2C9JZT2_HUMAN
Interferon-induced, double-stranded...
EIF2AK2
141Annotation 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>

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 conflicti102I → M in AAP57628 (Ref. 7) Curated1
Sequence conflicti224S → R in AAP57628 (Ref. 7) Curated1
Sequence conflicti512K → E in AAF13156 (PubMed:9726442).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_040474428V → E1 PublicationCorresponds to variant dbSNP:rs56219559Ensembl.1
Natural variantiVAR_040475439L → V in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_040476506I → V1 PublicationCorresponds to variant dbSNP:rs34821155Ensembl.1

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_046177263 – 303Missing in isoform 2. 1 PublicationAdd BLAST41

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
M35663 mRNA Translation: AAA36409.1
M85294 mRNA Translation: AAA18253.1
U50648
, U50634, U50635, U50636, U50637, U50638, U50639, U50640, U50641, U50642, U50643, U50644, U50645, U50646, U50647 Genomic DNA Translation: AAC50768.1
AF167472
, AF167460, AF167462, AF167463, AF167464, AF167465, AF167466, AF167468, AF167470 Genomic DNA Translation: AAF13156.1
AY302136 mRNA Translation: AAP57628.1
AK290655 mRNA Translation: BAF83344.1
AK313818 mRNA Translation: BAG36554.1
AY228338 Genomic DNA Translation: AAO38055.1
AC007899 Genomic DNA Translation: AAY24317.1
CH471053 Genomic DNA Translation: EAX00407.1
CH471053 Genomic DNA Translation: EAX00408.1
CH471053 Genomic DNA Translation: EAX00409.1
BC093676 mRNA Translation: AAH93676.1
BC101475 mRNA Translation: AAI01476.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS1786.1 [P19525-1]
CCDS46259.1 [P19525-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
JC5225

NCBI Reference Sequences

More...
RefSeqi
NP_001129123.1, NM_001135651.2 [P19525-1]
NP_001129124.1, NM_001135652.2 [P19525-2]
NP_002750.1, NM_002759.3 [P19525-1]
XP_011531289.1, XM_011532987.2 [P19525-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.131431

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000233057; ENSP00000233057; ENSG00000055332 [P19525-1]
ENST00000395127; ENSP00000378559; ENSG00000055332 [P19525-1]
ENST00000405334; ENSP00000385014; ENSG00000055332 [P19525-2]
ENST00000647926; ENSP00000497534; ENSG00000055332 [P19525-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5610

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5610

UCSC genome browser

More...
UCSCi
uc010fab.3 human [P19525-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35663 mRNA Translation: AAA36409.1
M85294 mRNA Translation: AAA18253.1
U50648
, U50634, U50635, U50636, U50637, U50638, U50639, U50640, U50641, U50642, U50643, U50644, U50645, U50646, U50647 Genomic DNA Translation: AAC50768.1
AF167472
, AF167460, AF167462, AF167463, AF167464, AF167465, AF167466, AF167468, AF167470 Genomic DNA Translation: AAF13156.1
AY302136 mRNA Translation: AAP57628.1
AK290655 mRNA Translation: BAF83344.1
AK313818 mRNA Translation: BAG36554.1
AY228338 Genomic DNA Translation: AAO38055.1
AC007899 Genomic DNA Translation: AAY24317.1
CH471053 Genomic DNA Translation: EAX00407.1
CH471053 Genomic DNA Translation: EAX00408.1
CH471053 Genomic DNA Translation: EAX00409.1
BC093676 mRNA Translation: AAH93676.1
BC101475 mRNA Translation: AAI01476.1
CCDSiCCDS1786.1 [P19525-1]
CCDS46259.1 [P19525-2]
PIRiJC5225
RefSeqiNP_001129123.1, NM_001135651.2 [P19525-1]
NP_001129124.1, NM_001135652.2 [P19525-2]
NP_002750.1, NM_002759.3 [P19525-1]
XP_011531289.1, XM_011532987.2 [P19525-1]
UniGeneiHs.131431

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
1QU6NMR-A1-170[»]
2A19X-ray2.50B/C258-550[»]
2A1AX-ray2.80B258-550[»]
3UIUX-ray2.90A/B254-551[»]
ProteinModelPortaliP19525
SMRiP19525
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111596, 181 interactors
DIPiDIP-2657N
IntActiP19525, 72 interactors
MINTiP19525
STRINGi9606.ENSP00000233057

Chemistry databases

BindingDBiP19525
ChEMBLiCHEMBL5785
GuidetoPHARMACOLOGYi2016

PTM databases

iPTMnetiP19525
PhosphoSitePlusiP19525
SwissPalmiP19525

Polymorphism and mutation databases

BioMutaiEIF2AK2
DMDMi125527

Proteomic databases

EPDiP19525
MaxQBiP19525
PaxDbiP19525
PeptideAtlasiP19525
PRIDEiP19525
ProteomicsDBi53670
TopDownProteomicsiP19525-1 [P19525-1]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5610
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000233057; ENSP00000233057; ENSG00000055332 [P19525-1]
ENST00000395127; ENSP00000378559; ENSG00000055332 [P19525-1]
ENST00000405334; ENSP00000385014; ENSG00000055332 [P19525-2]
ENST00000647926; ENSP00000497534; ENSG00000055332 [P19525-1]
GeneIDi5610
KEGGihsa:5610
UCSCiuc010fab.3 human [P19525-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5610
DisGeNETi5610
EuPathDBiHostDB:ENSG00000055332.16

GeneCards: human genes, protein and diseases

More...
GeneCardsi
EIF2AK2
HGNCiHGNC:9437 EIF2AK2
HPAiCAB003845
HPA019795
HPA063893
MIMi176871 gene
neXtProtiNX_P19525
OpenTargetsiENSG00000055332
PharmGKBiPA33779

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1033 Eukaryota
ENOG410XS0B LUCA
GeneTreeiENSGT00940000160736
HOGENOMiHOG000234351
HOVERGENiHBG051430
InParanoidiP19525
KOiK16195
OMAiELLYICP
OrthoDBiEOG091G088F
PhylomeDBiP19525
TreeFamiTF317576

Enzyme and pathway databases

ReactomeiR-HSA-1169408 ISG15 antiviral mechanism
R-HSA-169131 Inhibition of PKR
SignaLinkiP19525
SIGNORiP19525

Miscellaneous databases

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

More...
ChiTaRSi
EIF2AK2 human
EvolutionaryTraceiP19525

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Protein_kinase_R

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
5610
PMAP-CutDBiP19525

Protein Ontology

More...
PROi
PR:P19525

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000055332 Expressed in 238 organ(s), highest expression level in oviduct epithelium
CleanExiHS_EIF2AK2
ExpressionAtlasiP19525 baseline and differential
GenevisibleiP19525 HS

Family and domain databases

CDDicd00048 DSRM, 2 hits
InterProiView protein in InterPro
IPR014720 dsRBD_dom
IPR011009 Kinase-like_dom_sf
IPR033366 PKR
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR11042:SF102 PTHR11042:SF102, 1 hit
PfamiView protein in Pfam
PF00035 dsrm, 2 hits
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00358 DSRM, 2 hits
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50137 DS_RBD, 2 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 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 nameiE2AK2_HUMAN
<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: P19525
Secondary accession number(s): A8K3P0
, D6W584, E9PC80, Q52M43, Q7Z6F6, Q9UIR4
<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: February 1, 1991
Last sequence update: May 1, 1991
Last modified: December 5, 2018
This is version 221 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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 chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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