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Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Serine/threonine-protein kinase TIK) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)

 E2AK2_MOUSE             Reviewed;         515 AA.
Q03963; Q61742; Q62026;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
20-JUN-2018, entry version 173.
RecName: Full=Interferon-induced, double-stranded RNA-activated protein kinase;
EC=2.7.11.1;
AltName: Full=Eukaryotic translation initiation factor 2-alpha kinase 2;
Short=eIF-2A protein kinase 2;
AltName: Full=Interferon-inducible RNA-dependent protein kinase;
AltName: Full=P1/eIF-2A protein kinase;
AltName: Full=Protein kinase RNA-activated;
Short=PKR;
Short=Protein kinase R {ECO:0000303|PubMed:20478537};
AltName: Full=Serine/threonine-protein kinase TIK;
AltName: Full=Tyrosine-protein kinase EIF2AK2;
EC=2.7.10.2;
AltName: Full=p68 kinase;
Name=Eif2ak2; Synonyms=Pkr, Prkr, Tik;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1714905;
Icely P.L., Gros P., Bergeron J.J.M., Devault A., Afar D.E.H.,
Bell J.C.;
"TIK, a novel serine/threonine kinase, is recognized by antibodies
directed against phosphotyrosine.";
J. Biol. Chem. 266:16073-16077(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary carcinoma;
PubMed=1351683; DOI=10.1073/pnas.89.12.5447;
Feng G.S., Chong K., Kumar A., Williams B.R.G.;
"Identification of double-stranded RNA-binding domains in the
interferon-induced double-stranded RNA-activated p68 kinase.";
Proc. Natl. Acad. Sci. U.S.A. 89:5447-5451(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DBA/2J; TISSUE=Liver;
PubMed=7914700; DOI=10.1073/pnas.91.17.7995;
Tanaka H., Samuel C.E.;
"Mechanism of interferon action: structure of the mouse PKR gene
encoding the interferon-inducible RNA-dependent protein kinase.";
Proc. Natl. Acad. Sci. U.S.A. 91:7995-7999(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DBA/2J; TISSUE=Liver;
PubMed=7533117; DOI=10.1016/0378-1119(94)00821-9;
Tanaka H., Samuel C.E.;
"Sequence of the murine interferon-inducible RNA-dependent protein
kinase (PKR) deduced from genomic clones.";
Gene 153:283-284(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Skin;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
INTERACTION WITH IKBKB.
PubMed=10848580; DOI=10.1128/MCB.20.13.4532-4542.2000;
Bonnet M.C., Weil R., Dam E., Hovanessian A.G., Meurs E.F.;
"PKR stimulates NF-kappaB irrespective of its kinase function by
interacting with the IkappaB kinase complex.";
Mol. Cell. Biol. 20:4532-4542(2000).
[7]
INTERACTION WITH NPM1.
PubMed=12882984; DOI=10.1074/jbc.M301392200;
Pang Q., Christianson T.A., Koretsky T., Carlson H., David L.,
Keeble W., Faulkner G.R., Speckhart A., Bagby G.C.;
"Nucleophosmin interacts with and inhibits the catalytic function of
eukaryotic initiation factor 2 kinase PKR.";
J. Biol. Chem. 278:41709-41717(2003).
[8]
INTERACTION WITH ADAR.
PubMed=17079286; DOI=10.1128/JVI.01527-06;
Nie Y., Hammond G.L., Yang J.H.;
"Double-stranded RNA deaminase ADAR1 increases host susceptibility to
virus infection.";
J. Virol. 81:917-923(2007).
[9]
FUNCTION IN SFV RESTRICTION.
PubMed=19264662; DOI=10.1099/vir.0.007336-0;
Barry G., Breakwell L., Fragkoudis R., Attarzadeh-Yazdi G.,
Rodriguez-Andres J., Kohl A., Fazakerley J.K.;
"PKR acts early in infection to suppress Semliki Forest virus
production and strongly enhances the type I interferon response.";
J. Gen. Virol. 90:1382-1391(2009).
[10]
FUNCTION, AND INTERACTION WITH DHX9.
PubMed=19229320; DOI=10.1371/journal.ppat.1000311;
Sadler A.J., Latchoumanin O., Hawkes D., Mak J., Williams B.R.;
"An antiviral response directed by PKR phosphorylation of the RNA
helicase A.";
PLoS Pathog. 5:E1000311-E1000311(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
FUNCTION.
PubMed=20478537; DOI=10.1016/j.chom.2010.04.007;
Schulz O., Pichlmair A., Rehwinkel J., Rogers N.C., Scheuner D.,
Kato H., Takeuchi O., Akira S., Kaufman R.J., Reis e Sousa C.;
"Protein kinase R contributes to immunity against specific viruses by
regulating interferon mRNA integrity.";
Cell Host Microbe 7:354-361(2010).
[13]
FUNCTION.
PubMed=21123651; DOI=10.1101/gad.1965010;
Harashima A., Guettouche T., Barber G.N.;
"Phosphorylation of the NFAR proteins by the dsRNA-dependent protein
kinase PKR constitutes a novel mechanism of translational regulation
and cellular defense.";
Genes Dev. 24:2640-2653(2010).
[14]
FUNCTION.
PubMed=20038207; DOI=10.1089/jir.2009.0051;
Minor R.A., Limmon G.V., Miller-DeGraff L., Dixon D., Andrews D.M.,
Kaufman R.J., Imani F.;
"Double-stranded RNA-activated protein kinase regulates early innate
immune responses during respiratory syncytial virus infection.";
J. Interferon Cytokine Res. 30:263-272(2010).
[15]
FUNCTION.
PubMed=20631127; DOI=10.1128/JVI.00625-10;
Rojas M., Arias C.F., Lopez S.;
"Protein kinase R is responsible for the phosphorylation of eIF2alpha
in rotavirus infection.";
J. Virol. 84:10457-10466(2010).
[16]
FUNCTION IN LCMV RESTRICTION.
PubMed=20585572; DOI=10.1371/journal.ppat.1000966;
Nakayama Y., Plisch E.H., Sullivan J., Thomas C., Czuprynski C.J.,
Williams B.R., Suresh M.;
"Role of PKR and Type I IFNs in viral control during primary and
secondary infection.";
PLoS Pathog. 6:E1000966-E1000966(2010).
[17]
FUNCTION.
PubMed=21994357; DOI=10.1128/CVI.05476-11;
Thakur S.A., Zalinger Z.B., Johnson T.R., Imani F.;
"Protein kinase R is a novel mediator of CD40 signaling and plays a
critical role in modulating immunoglobulin expression during
respiratory syncytial virus infection.";
Clin. Vaccine Immunol. 18:2060-2066(2011).
[18]
REVIEW.
PubMed=21300116; DOI=10.1016/j.jhep.2010.11.037;
Marsollier N., Ferre P., Foufelle F.;
"Novel insights in the interplay between inflammation and metabolic
diseases: a role for the pathogen sensing kinase PKR.";
J. Hepatol. 54:1307-1309(2011).
[19]
FUNCTION, AND INTERACTION WITH IRS1.
PubMed=22948222; DOI=10.1210/en.2012-1400;
Carvalho-Filho M.A., Carvalho B.M., Oliveira A.G., Guadagnini D.,
Ueno M., Dias M.M., Tsukumo D.M., Hirabara S.M., Reis L.F., Curi R.,
Carvalheira J.B., Saad M.J.;
"Double-stranded RNA-activated protein kinase is a key modulator of
insulin sensitivity in physiological conditions and in obesity in
mice.";
Endocrinology 153:5261-5274(2012).
[20]
FUNCTION, AND INTERACTION WITH GSN.
PubMed=22633459; DOI=10.1016/j.immuni.2012.02.020;
Irving A.T., Wang D., Vasilevski O., Latchoumanin O., Kozer N.,
Clayton A.H., Szczepny A., Morimoto H., Xu D., Williams B.R.,
Sadler A.J.;
"Regulation of actin dynamics by protein kinase R control of gelsolin
enforces basal innate immune defense.";
Immunity 36:795-806(2012).
[21]
FUNCTION, INTERACTION WITH NLRP3, AND AUTOPHOSPHORYLATION.
PubMed=22801494; DOI=10.1038/nature11290;
Lu B., Nakamura T., Inouye K., Li J., Tang Y., Lundbaeck P.,
Valdes-Ferrer S.I., Olofsson P.S., Kalb T., Roth J., Zou Y.,
Erlandsson-Harris H., Yang H., Ting J.P., Wang H., Andersson U.,
Antoine D.J., Chavan S.S., Hotamisligil G.S., Tracey K.J.;
"Novel role of PKR in inflammasome activation and HMGB1 release.";
Nature 488:670-674(2012).
[22]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23403623; DOI=10.1182/blood-2012-09-456400;
Liu X., Bennett R.L., Cheng X., Byrne M., Reinhard M.K., May W.S. Jr.;
"PKR regulates proliferation, differentiation and survival of murine
hematopoietic stem/progenitor cells.";
Blood 121:3364-3374(2013).
[23]
FUNCTION.
PubMed=23401008; DOI=10.1002/eji.201243187;
He Y., Franchi L., Nunez G.;
"The protein kinase PKR is critical for LPS-induced iNOS production
but dispensable for inflammasome activation in macrophages.";
Eur. J. Immunol. 43:1147-1152(2013).
[24]
ISGYLATION.
PubMed=23229543; DOI=10.1074/jbc.M112.401851;
Okumura F., Okumura A.J., Uematsu K., Hatakeyama S., Zhang D.E.,
Kamura T.;
"Activation of double-stranded RNA-activated protein kinase (PKR) by
interferon-stimulated gene 15 (ISG15) modification down-regulates
protein translation.";
J. Biol. Chem. 288:2839-2847(2013).
[25]
FUNCTION.
PubMed=23392680; DOI=10.1523/JNEUROSCI.2322-12.2013;
Stern E., Chinnakkaruppan A., David O., Sonenberg N., Rosenblum K.;
"Blocking the eIF2? kinase (PKR) enhances positive and negative forms
of cortex-dependent taste memory.";
J. Neurosci. 33:2517-2525(2013).
[26]
STRUCTURE BY NMR OF 1-171.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the first and second DSRM domain in interferon-
induced, double-stranded RNA-activated protein kinase.";
Submitted (NOV-2005) to the PDB data bank.
-!- FUNCTION: 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 west nile virus (WNV), sindbis virus (SV), foot-
and-mouth virus (FMDV), semliki Forest virus (SFV) and lymphocytic
choriomeningitis virus (LCMV). 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 and IRS1. 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. Regulates
proliferation, differentiation and survival of hematopoietic
stem/progenitor cells, induction of cytokines and chemokines and
plays a role in cortex-dependent memory consolidation.
{ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:19264662,
ECO:0000269|PubMed:20038207, ECO:0000269|PubMed:20478537,
ECO:0000269|PubMed:20585572, ECO:0000269|PubMed:20631127,
ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:21994357,
ECO:0000269|PubMed:22633459, ECO:0000269|PubMed:22801494,
ECO:0000269|PubMed:22948222, ECO:0000269|PubMed:23392680,
ECO:0000269|PubMed:23401008, ECO:0000269|PubMed:23403623}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10027}.
-!- ENZYME REGULATION: 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 cellular proteins
TARBP2, DUS2L, NPM1, NCK1 and ADAR (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with DNAJC3 and STRBP (By
similarity). Forms a complex with FANCA, FANCC, FANCG and HSP70
(By similarity). Interacts with ADAR/ADAR1. The inactive form
interacts with NCK1. Interacts (via the kinase catalytic domain)
with STAT3 (via SH2 domain), TRAF2 (C-terminus), TRAF5 (C-
terminus) and TRAF6 (C-terminus). Interacts with MAP2K6, TARBP2,
NLRP1, NLRC4 and AIM2. Interacts (via DRBM 1 domain) with DUS2L
(via DRBM domain) (By similarity). Interacts with DHX9 (via N-
terminus) and this interaction is dependent upon activation of the
kinase. The inactive form interacts with GSN. Interacts with
IKBKB/IKKB, NPM1, NLRP3 and IRS1. {ECO:0000250,
ECO:0000269|PubMed:10848580, ECO:0000269|PubMed:12882984,
ECO:0000269|PubMed:17079286, ECO:0000269|PubMed:19229320,
ECO:0000269|PubMed:22633459, ECO:0000269|PubMed:22801494,
ECO:0000269|PubMed:22948222}.
-!- INTERACTION:
P35569:Irs1; NbExp=2; IntAct=EBI-2603444, EBI-400825;
Q8R4B8:Nlrp3; NbExp=3; IntAct=EBI-2603444, EBI-6910832;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in heart, lung, brain, kidney,
testes, thymus and bone marrow.
-!- INDUCTION: By type I interferons. {ECO:0000250}.
-!- PTM: Autophosphorylated on several Ser, Thr and Tyr residues.
Autophosphorylation of Thr-414 is dependent on Thr-409 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 (By similarity).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice have significantly elevated numbers of
bone marrow derived hematopoietic stem/progenitor cells (HSPCs)
and which are more actively proliferating and resistant to stress.
{ECO:0000269|PubMed:23403623}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. GCN2 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; M65029; AAA40150.1; -; mRNA.
EMBL; M93567; AAA39885.1; -; mRNA.
EMBL; U09928; AAC24729.1; -; Genomic_DNA.
EMBL; U09914; AAC24729.1; JOINED; Genomic_DNA.
EMBL; U09915; AAC24729.1; JOINED; Genomic_DNA.
EMBL; U09916; AAC24729.1; JOINED; Genomic_DNA.
EMBL; U09917; AAC24729.1; JOINED; Genomic_DNA.
EMBL; U09918; AAC24729.1; JOINED; Genomic_DNA.
EMBL; U09919; AAC24729.1; JOINED; Genomic_DNA.
EMBL; U09920; AAC24729.1; JOINED; Genomic_DNA.
EMBL; U09921; AAC24729.1; JOINED; Genomic_DNA.
EMBL; U09922; AAC24729.1; JOINED; Genomic_DNA.
EMBL; U09923; AAC24729.1; JOINED; Genomic_DNA.
EMBL; U09924; AAC24729.1; JOINED; Genomic_DNA.
EMBL; U09925; AAC24729.1; JOINED; Genomic_DNA.
EMBL; U09926; AAC24729.1; JOINED; Genomic_DNA.
EMBL; U09927; AAC24729.1; JOINED; Genomic_DNA.
EMBL; AK028602; BAC26027.1; -; mRNA.
CCDS; CCDS28980.1; -.
PIR; A59309; A59309.
RefSeq; NP_035293.1; NM_011163.4.
UniGene; Mm.378990; -.
PDB; 1X48; NMR; -; A=96-170.
PDB; 1X49; NMR; -; A=1-84.
PDBsum; 1X48; -.
PDBsum; 1X49; -.
ProteinModelPortal; Q03963; -.
SMR; Q03963; -.
BioGrid; 202376; 2.
DIP; DIP-41411N; -.
IntAct; Q03963; 4.
STRING; 10090.ENSMUSP00000024884; -.
ChEMBL; CHEMBL1795121; -.
iPTMnet; Q03963; -.
PhosphoSitePlus; Q03963; -.
SwissPalm; Q03963; -.
EPD; Q03963; -.
MaxQB; Q03963; -.
PaxDb; Q03963; -.
PeptideAtlas; Q03963; -.
PRIDE; Q03963; -.
Ensembl; ENSMUST00000024884; ENSMUSP00000024884; ENSMUSG00000024079.
GeneID; 19106; -.
KEGG; mmu:19106; -.
UCSC; uc008dph.2; mouse.
CTD; 5610; -.
MGI; MGI:1353449; Eif2ak2.
eggNOG; KOG1033; Eukaryota.
eggNOG; ENOG410XS0B; LUCA.
GeneTree; ENSGT00530000062984; -.
HOGENOM; HOG000234351; -.
HOVERGEN; HBG051430; -.
InParanoid; Q03963; -.
KO; K16195; -.
OMA; ELLYICP; -.
OrthoDB; EOG091G088F; -.
PhylomeDB; Q03963; -.
TreeFam; TF317576; -.
EvolutionaryTrace; Q03963; -.
PRO; PR:Q03963; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024079; -.
Genevisible; Q03963; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0000186; P:activation of MAPKK activity; ISS:UniProtKB.
GO; GO:0034198; P:cellular response to amino acid starvation; ISO:MGI.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IDA:MGI.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; IGI:MGI.
GO; GO:0033689; P:negative regulation of osteoblast proliferation; ISS:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0032722; P:positive regulation of chemokine production; IMP:UniProtKB.
GO; GO:0001819; P:positive regulation of cytokine production; IMP:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:1901532; P:regulation of hematopoietic progenitor cell differentiation; IMP:UniProtKB.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; IMP:UniProtKB.
GO; GO:1902033; P:regulation of hematopoietic stem cell proliferation; IMP:UniProtKB.
GO; GO:1900225; P:regulation of NLRP3 inflammasome complex assembly; IMP:UniProtKB.
GO; GO:0035455; P:response to interferon-alpha; ISS:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
GO; GO:0009636; P:response to toxic substance; ISO:MGI.
GO; GO:0009615; P:response to virus; ISS:UniProtKB.
GO; GO:0033197; P:response to vitamin E; ISO:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006412; P:translation; IDA:MGI.
InterPro; IPR014720; dsRBD_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR033366; PKR.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR11042:SF102; PTHR11042:SF102; 1.
Pfam; PF00035; dsrm; 2.
Pfam; PF00069; Pkinase; 1.
SMART; SM00358; DSRM; 2.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50137; DS_RBD; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Antiviral defense; ATP-binding;
Complete proteome; Cytoplasm; Immunity; Innate immunity;
Isopeptide bond; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; RNA-binding;
Serine/threonine-protein kinase; Transcription;
Transcription regulation; Transferase; Tyrosine-protein kinase;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P19525}.
CHAIN 2 515 Interferon-induced, double-stranded RNA-
activated protein kinase.
/FTId=PRO_0000085946.
DOMAIN 8 76 DRBM 1. {ECO:0000255|PROSITE-
ProRule:PRU00266}.
DOMAIN 95 162 DRBM 2. {ECO:0000255|PROSITE-
ProRule:PRU00266}.
DOMAIN 242 504 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 248 256 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 241 515 Interaction with TRAF5. {ECO:0000250}.
COMPBIAS 183 187 Poly-Ser.
COMPBIAS 241 247 Asp/Glu-rich (acidic).
ACT_SITE 376 376 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 271 271 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P19525}.
MOD_RES 84 84 Phosphothreonine.
{ECO:0000250|UniProtKB:P19525}.
MOD_RES 96 96 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P19525}.
MOD_RES 157 157 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P19525}.
MOD_RES 233 233 Phosphothreonine.
{ECO:0000250|UniProtKB:P19525}.
MOD_RES 268 268 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P19525}.
MOD_RES 409 409 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:P19525}.
MOD_RES 414 414 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:P19525}.
MOD_RES 419 419 Phosphoserine.
{ECO:0000250|UniProtKB:P19525}.
CROSSLNK 68 68 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15).
{ECO:0000250}.
CROSSLNK 154 154 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15).
{ECO:0000250}.
CONFLICT 52 52 P -> G (in Ref. 1; AAA40150).
{ECO:0000305}.
CONFLICT 60 60 Q -> T (in Ref. 1; AAA40150).
{ECO:0000305}.
CONFLICT 87 87 S -> C (in Ref. 1; AAA40150).
{ECO:0000305}.
CONFLICT 144 144 T -> I (in Ref. 2; AAA39885).
{ECO:0000305}.
CONFLICT 281 282 EH -> DR (in Ref. 2; AAA39885).
{ECO:0000305}.
CONFLICT 510 510 K -> E (in Ref. 1; AAA40150).
{ECO:0000305}.
CONFLICT 512 515 RNTC -> KHMLGPF (in Ref. 1; AAA40150).
{ECO:0000305}.
HELIX 8 20 {ECO:0000244|PDB:1X49}.
STRAND 24 33 {ECO:0000244|PDB:1X49}.
STRAND 35 37 {ECO:0000244|PDB:1X49}.
STRAND 39 48 {ECO:0000244|PDB:1X49}.
STRAND 54 58 {ECO:0000244|PDB:1X49}.
HELIX 59 74 {ECO:0000244|PDB:1X49}.
HELIX 96 106 {ECO:0000244|PDB:1X48}.
STRAND 111 115 {ECO:0000244|PDB:1X48}.
STRAND 119 123 {ECO:0000244|PDB:1X48}.
STRAND 126 134 {ECO:0000244|PDB:1X48}.
STRAND 136 144 {ECO:0000244|PDB:1X48}.
HELIX 145 162 {ECO:0000244|PDB:1X48}.
SEQUENCE 515 AA; 58280 MW; 7A116F7D8DB9B847 CRC64;
MASDTPGFYM DKLNKYRQMH GVAITYKELS TSGPPHDRRF TFQVLIDEKE FPEAKGRSKQ
EARNAAAKLA VDILDNENKV DCHTSASEQG LFVGNYIGLV NSFAQKKKLS VNYEQCEPNS
ELPQRFICKC KIGQTMYGTG SGVTKQEAKQ LAAKEAYQKL LKSPPKTAGT SSSVVTSTFS
GFSSSSSMTS NGVSQSAPGS FSSENVFTNG LGENKRKSGV KVSPDDVQRN KYTLDARFNS
DFEDIEEIGL GGFGQVFKAK HRIDGKRYAI KRVKYNTEKA EHEVQALAEL NHVNIVQYHS
CWEGVDYDPE HSMSDTSRYK TRCLFIQMEF CDKGTLEQWM RNRNQSKVDK ALILDLYEQI
VTGVEYIHSK GLIHRDLKPG NIFLVDERHI KIGDFGLATA LENDGKSRTR RTGTLQYMSP
EQLFLKHYGK EVDIFALGLI LAELLHTCFT ESEKIKFFES LRKGDFSNDI FDNKEKSLLK
KLLSEKPKDR PETSEILKTL AEWRNISEKK KRNTC


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