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Eukaryotic translation initiation factor 2-alpha kinase 3 (EC 2.7.11.1) (PRKR-like endoplasmic reticulum kinase) (Pancreatic eIF2-alpha kinase) (HsPEK)

 E2AK3_HUMAN             Reviewed;        1116 AA.
Q9NZJ5; A0AVH1; A0AVH2; B2RCU9; O95846; Q53QY0; Q53SB1;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
20-JUN-2018, entry version 182.
RecName: Full=Eukaryotic translation initiation factor 2-alpha kinase 3;
EC=2.7.11.1;
AltName: Full=PRKR-like endoplasmic reticulum kinase;
AltName: Full=Pancreatic eIF2-alpha kinase;
Short=HsPEK;
Flags: Precursor;
Name=EIF2AK3; Synonyms=PEK, PERK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND VARIANTS ARG-166 AND
SER-704.
TISSUE=Liver, Pancreas, and Testis;
PubMed=10026192; DOI=10.1074/jbc.274.9.5723;
Shi Y., An J., Liang J., Hayes S.E., Sandusky G.E., Stramm L.E.,
Yang N.N.;
"Characterization of a mutant pancreatic eIF-2alpha kinase, PEK, and
co-localization with somatostatin in islet delta cells.";
J. Biol. Chem. 274:5723-5730(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND VARIANTS ARG-166 AND
SER-704.
TISSUE=Brain, and Pancreas;
PubMed=10677345; DOI=10.1042/bj3460281;
Sood R., Porter A.C., Ma K., Quilliam L.A., Wek R.C.;
"Pancreatic eukaryotic initiation factor-2alpha kinase (PEK)
homologues in humans, Drosophila melanogaster and Caenorhabditis
elegans that mediate translational control in response to endoplasmic
reticulum stress.";
Biochem. J. 346:281-293(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT WRS GLN-588, AND VARIANT
CYS-136.
PubMed=10932183; DOI=10.1038/78085;
Delepine M., Nicolino M., Barrett T., Golamaully M., Lathrop G.M.,
Julier C.;
"EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is
mutated in patients with Wolcott-Rallison syndrome.";
Nat. Genet. 25:406-409(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-166 AND
SER-704.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-715, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[8]
PHOSPHORYLATION AT TYR-619, AND DEPHOSPHORYLATION AT TYR-619.
PubMed=22169477; DOI=10.1126/scisignal.2002329;
Krishnan N., Fu C., Pappin D.J., Tonks N.K.;
"H2s-induced sulfhydration of the phosphatase PTP1B and its role in
the endoplasmic reticulum stress response.";
Sci. Signal. 4:RA86-RA86(2011).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1094, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[10]
ADP-RIBOSYLATION BY PARP16.
PubMed=23103912; DOI=10.1038/ncb2593;
Jwa M., Chang P.;
"PARP16 is a tail-anchored endoplasmic reticulum protein required for
the PERK-and IRE1alpha-mediated unfolded protein response.";
Nat. Cell Biol. 14:1223-1230(2012).
[11]
INTERACTION WITH PDIA6.
PubMed=24508390; DOI=10.1016/j.molcel.2014.01.004;
Eletto D., Eletto D., Dersh D., Gidalevitz T., Argon Y.;
"Protein disulfide isomerase A6 controls the decay of IRE1alpha
signaling via disulfide-dependent association.";
Mol. Cell 53:562-576(2014).
[12]
INTERACTION WITH TMEM33.
PubMed=26268696; DOI=10.1007/s10549-015-3536-7;
Sakabe I., Hu R., Jin L., Clarke R., Kasid U.N.;
"TMEM33: a new stress-inducible endoplasmic reticulum transmembrane
protein and modulator of the unfolded protein response signaling.";
Breast Cancer Res. Treat. 153:285-297(2015).
[13]
VARIANTS [LARGE SCALE ANALYSIS] CYS-136; VAL-566 AND LEU-716.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Metabolic-stress sensing protein kinase that
phosphorylates the alpha subunit of eukaryotic translation
initiation factor 2 (eIF-2-alpha/EIF2S1) on 'Ser-52' during the
unfolded protein response (UPR) and in response to low amino acid
availability. Converts phosphorylated eIF-2-alpha/EIF2S1 either in
a global protein synthesis inhibitor, leading to a reduced overall
utilization of amino acids, or to a translation initiation
activator 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.
Serves as a critical effector of unfolded protein response (UPR)-
induced G1 growth arrest due to the loss of cyclin-D1 (CCND1).
Involved in control of mitochondrial morphology and function.
{ECO:0000250|UniProtKB:Q9Z2B5}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Perturbation in protein folding in the
endoplasmic reticulum (ER) promotes reversible dissociation from
HSPA5/BIP and oligomerization, resulting in
transautophosphorylation and kinase activity induction.
{ECO:0000250}.
-!- SUBUNIT: Forms dimers with HSPA5/BIP in resting cells (By
similarity). Oligomerizes in ER-stressed cells (By similarity).
Interacts with DNAJC3 and MFN2 (By similarity). Interacts with
TMEM33 (PubMed:26268696). Interacts with PDIA6 (PubMed:24508390).
{ECO:0000250|UniProtKB:Q9Z2B5, ECO:0000269|PubMed:24508390,
ECO:0000269|PubMed:26268696}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-766076, EBI-766076;
P11021:HSPA5; NbExp=4; IntAct=EBI-766076, EBI-354921;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
type I membrane protein.
-!- TISSUE SPECIFICITY: Ubiquitous. A high level expression is seen in
secretory tissues.
-!- INDUCTION: By endoplasmic reticulum stress.
-!- DOMAIN: The lumenal domain senses perturbations in protein folding
in the ER, probably through reversible interaction with HSPA5/BIP.
{ECO:0000250}.
-!- PTM: Oligomerization of the N-terminal ER luminal domain by ER
stress promotes PERK trans-autophosphorylation of the C-terminal
cytoplasmic kinase domain at multiple residues including Thr-982
on the kinase activation loop (By similarity). Autophosphorylated.
Phosphorylated at Tyr-619 following endoplasmic reticulum stress,
leading to activate its tyrosine-protein kinase activity.
Dephosphorylated by PTPN1/TP1B, leading to inactivate its enzyme
activity. {ECO:0000250, ECO:0000269|PubMed:22169477}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- PTM: ADP-ribosylated by PARP16 upon ER stress, which increases
kinase activity.
-!- DISEASE: Wolcott-Rallison syndrome (WRS) [MIM:226980]: A rare
autosomal recessive disorder, characterized by permanent neonatal
or early infancy insulin-dependent diabetes and, at a later age,
epiphyseal dysplasia, osteoporosis, growth retardation and other
multisystem manifestations, such as hepatic and renal
dysfunctions, mental retardation and cardiovascular abnormalities.
{ECO:0000269|PubMed:10932183}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. GCN2 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; AF110146; AAD19961.1; -; mRNA.
EMBL; AF193339; AAF61199.1; -; mRNA.
EMBL; AF284615; AAF91480.1; -; Genomic_DNA.
EMBL; AF284604; AAF91480.1; JOINED; Genomic_DNA.
EMBL; AF284605; AAF91480.1; JOINED; Genomic_DNA.
EMBL; AF284606; AAF91480.1; JOINED; Genomic_DNA.
EMBL; AF284607; AAF91480.1; JOINED; Genomic_DNA.
EMBL; AF284608; AAF91480.1; JOINED; Genomic_DNA.
EMBL; AF284609; AAF91480.1; JOINED; Genomic_DNA.
EMBL; AF284610; AAF91480.1; JOINED; Genomic_DNA.
EMBL; AF284611; AAF91480.1; JOINED; Genomic_DNA.
EMBL; AF284612; AAF91480.1; JOINED; Genomic_DNA.
EMBL; AF284613; AAF91480.1; JOINED; Genomic_DNA.
EMBL; AF284614; AAF91480.1; JOINED; Genomic_DNA.
EMBL; AK315287; BAG37696.1; -; mRNA.
EMBL; AC062029; AAY14777.1; -; Genomic_DNA.
EMBL; AC104134; AAY24331.1; -; Genomic_DNA.
EMBL; BC126354; AAI26355.1; -; mRNA.
EMBL; BC126356; AAI26357.1; -; mRNA.
CCDS; CCDS33241.1; -.
RefSeq; NP_004827.4; NM_004836.6.
UniGene; Hs.591589; -.
PDB; 4G31; X-ray; 2.28 A; A=588-1093.
PDB; 4G34; X-ray; 2.70 A; A=588-1093.
PDB; 4M7I; X-ray; 2.34 A; A=588-1093.
PDB; 4X7H; X-ray; 2.00 A; A=575-1094.
PDB; 4X7J; X-ray; 2.30 A; A=575-1094.
PDB; 4X7K; X-ray; 1.80 A; A=575-1094.
PDB; 4X7L; X-ray; 1.90 A; A=575-1094.
PDB; 4X7N; X-ray; 2.35 A; A=575-1094.
PDB; 4X7O; X-ray; 2.65 A; A=575-1094.
PDB; 4YZS; X-ray; 3.14 A; A/B=104-403.
PDB; 5SV7; X-ray; 3.21 A; A/B/C/D=95-420.
PDBsum; 4G31; -.
PDBsum; 4G34; -.
PDBsum; 4M7I; -.
PDBsum; 4X7H; -.
PDBsum; 4X7J; -.
PDBsum; 4X7K; -.
PDBsum; 4X7L; -.
PDBsum; 4X7N; -.
PDBsum; 4X7O; -.
PDBsum; 4YZS; -.
PDBsum; 5SV7; -.
ProteinModelPortal; Q9NZJ5; -.
SMR; Q9NZJ5; -.
BioGrid; 114840; 50.
IntAct; Q9NZJ5; 10.
MINT; Q9NZJ5; -.
STRING; 9606.ENSP00000307235; -.
BindingDB; Q9NZJ5; -.
ChEMBL; CHEMBL6030; -.
GuidetoPHARMACOLOGY; 2017; -.
iPTMnet; Q9NZJ5; -.
PhosphoSitePlus; Q9NZJ5; -.
BioMuta; EIF2AK3; -.
DMDM; 296439367; -.
EPD; Q9NZJ5; -.
MaxQB; Q9NZJ5; -.
PaxDb; Q9NZJ5; -.
PeptideAtlas; Q9NZJ5; -.
PRIDE; Q9NZJ5; -.
ProteomicsDB; 83416; -.
Ensembl; ENST00000303236; ENSP00000307235; ENSG00000172071.
GeneID; 9451; -.
KEGG; hsa:9451; -.
UCSC; uc002stc.5; human.
CTD; 9451; -.
DisGeNET; 9451; -.
EuPathDB; HostDB:ENSG00000172071.11; -.
GeneCards; EIF2AK3; -.
H-InvDB; HIX0023925; -.
H-InvDB; HIX0030379; -.
HGNC; HGNC:3255; EIF2AK3.
HPA; CAB009204; -.
HPA; HPA015737; -.
MalaCards; EIF2AK3; -.
MIM; 226980; phenotype.
MIM; 604032; gene.
neXtProt; NX_Q9NZJ5; -.
OpenTargets; ENSG00000172071; -.
Orphanet; 1667; Wolcott-Rallison syndrome.
PharmGKB; PA27687; -.
eggNOG; KOG1033; Eukaryota.
eggNOG; ENOG410XS0B; LUCA.
GeneTree; ENSGT00530000062984; -.
HOVERGEN; HBG051431; -.
InParanoid; Q9NZJ5; -.
KO; K08860; -.
OMA; KWKPLIH; -.
OrthoDB; EOG091G01X1; -.
PhylomeDB; Q9NZJ5; -.
TreeFam; TF101511; -.
Reactome; R-HSA-381042; PERK regulates gene expression.
SignaLink; Q9NZJ5; -.
SIGNOR; Q9NZJ5; -.
ChiTaRS; EIF2AK3; human.
GeneWiki; EIF2AK3; -.
GenomeRNAi; 9451; -.
PRO; PR:Q9NZJ5; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000172071; -.
CleanEx; HS_EIF2AK3; -.
ExpressionAtlas; Q9NZJ5; baseline and differential.
Genevisible; Q9NZJ5; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; NAS:ParkinsonsUK-UCL.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IDA:UniProtKB.
GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; TAS:ParkinsonsUK-UCL.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; IMP:ParkinsonsUK-UCL.
GO; GO:0030282; P:bone mineralization; ISS:UniProtKB.
GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
GO; GO:0034198; P:cellular response to amino acid starvation; IMP:UniProtKB.
GO; GO:0070417; P:cellular response to cold; IMP:UniProtKB.
GO; GO:0042149; P:cellular response to glucose starvation; IMP:ParkinsonsUK-UCL.
GO; GO:0002063; P:chondrocyte development; ISS:UniProtKB.
GO; GO:0036492; P:eiF2alpha phosphorylation in response to endoplasmic reticulum stress; IMP:UniProtKB.
GO; GO:0031018; P:endocrine pancreas development; IMP:UniProtKB.
GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IDA:UniProtKB.
GO; GO:0006983; P:ER overload response; IDA:UniProtKB.
GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0031642; P:negative regulation of myelination; ISS:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; TAS:UniProtKB.
GO; GO:0032057; P:negative regulation of translational initiation in response to stress; TAS:UniProtKB.
GO; GO:0001503; P:ossification; IMP:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:ParkinsonsUK-UCL.
GO; GO:0036499; P:PERK-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IMP:ParkinsonsUK-UCL.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISS:ParkinsonsUK-UCL.
GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IMP:ParkinsonsUK-UCL.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:ParkinsonsUK-UCL.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0060734; P:regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation; ISS:UniProtKB.
GO; GO:1902235; P:regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0010998; P:regulation of translational initiation by eIF2 alpha phosphorylation; ISS:ParkinsonsUK-UCL.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:BHF-UCL.
GO; GO:1990737; P:response to manganese-induced endoplasmic reticulum stress; IEA:Ensembl.
GO; GO:0001501; P:skeletal system development; ISS:UniProtKB.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
Pfam; PF00069; Pkinase; 2.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF50998; SSF50998; 2.
SUPFAM; SSF56112; SSF56112; 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; ADP-ribosylation; ATP-binding; Complete proteome;
Diabetes mellitus; Disease mutation; Endoplasmic reticulum;
Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Signal; Stress response; Transferase; Translation regulation;
Transmembrane; Transmembrane helix; Unfolded protein response.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 1116 Eukaryotic translation initiation factor
2-alpha kinase 3.
/FTId=PRO_0000024322.
TOPO_DOM 30 514 Lumenal. {ECO:0000255}.
TRANSMEM 515 535 Helical. {ECO:0000255}.
TOPO_DOM 536 1116 Cytoplasmic. {ECO:0000255}.
DOMAIN 593 1077 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 599 607 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 49 52 Poly-Ala.
ACT_SITE 937 937 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 622 622 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 619 619 Phosphotyrosine.
{ECO:0000269|PubMed:22169477}.
MOD_RES 715 715 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 982 982 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Z2B5}.
MOD_RES 1094 1094 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 136 136 S -> C (in dbSNP:rs867529).
{ECO:0000269|PubMed:10932183,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_011409.
VARIANT 166 166 Q -> R (in dbSNP:rs13045).
{ECO:0000269|PubMed:10026192,
ECO:0000269|PubMed:10677345,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_011410.
VARIANT 566 566 D -> V (in dbSNP:rs55791823).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040477.
VARIANT 588 588 R -> Q (in WRS; dbSNP:rs121908569).
{ECO:0000269|PubMed:10932183}.
/FTId=VAR_011408.
VARIANT 704 704 A -> S (in dbSNP:rs1805165).
{ECO:0000269|PubMed:10026192,
ECO:0000269|PubMed:10677345,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_011411.
VARIANT 716 716 P -> L (in dbSNP:rs55861585).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040478.
CONFLICT 14 14 Missing (in Ref. 1; AAD19961, 2;
AAF61199, 3; AAF91480, 4; BAG37696 and 6;
AAI26357). {ECO:0000305}.
CONFLICT 490 490 N -> H (in Ref. 2; AAF61199).
{ECO:0000305}.
STRAND 105 110 {ECO:0000244|PDB:4YZS}.
STRAND 113 118 {ECO:0000244|PDB:4YZS}.
TURN 120 123 {ECO:0000244|PDB:4YZS}.
STRAND 126 131 {ECO:0000244|PDB:4YZS}.
STRAND 137 139 {ECO:0000244|PDB:4YZS}.
STRAND 152 158 {ECO:0000244|PDB:4YZS}.
STRAND 161 164 {ECO:0000244|PDB:4YZS}.
STRAND 166 169 {ECO:0000244|PDB:4YZS}.
STRAND 171 173 {ECO:0000244|PDB:4YZS}.
HELIX 178 182 {ECO:0000244|PDB:4YZS}.
STRAND 193 204 {ECO:0000244|PDB:4YZS}.
STRAND 207 209 {ECO:0000244|PDB:4YZS}.
STRAND 215 217 {ECO:0000244|PDB:4YZS}.
STRAND 220 222 {ECO:0000244|PDB:4YZS}.
STRAND 237 248 {ECO:0000244|PDB:4YZS}.
TURN 250 252 {ECO:0000244|PDB:4YZS}.
STRAND 255 267 {ECO:0000244|PDB:4YZS}.
STRAND 308 310 {ECO:0000244|PDB:4YZS}.
TURN 314 317 {ECO:0000244|PDB:4YZS}.
STRAND 321 323 {ECO:0000244|PDB:4YZS}.
TURN 324 326 {ECO:0000244|PDB:4YZS}.
STRAND 339 346 {ECO:0000244|PDB:4YZS}.
STRAND 349 352 {ECO:0000244|PDB:4YZS}.
HELIX 375 383 {ECO:0000244|PDB:4YZS}.
STRAND 387 390 {ECO:0000244|PDB:4YZS}.
STRAND 392 398 {ECO:0000244|PDB:4YZS}.
HELIX 588 592 {ECO:0000244|PDB:4X7K}.
STRAND 593 602 {ECO:0000244|PDB:4X7K}.
STRAND 605 612 {ECO:0000244|PDB:4X7K}.
TURN 613 615 {ECO:0000244|PDB:4X7K}.
STRAND 618 625 {ECO:0000244|PDB:4X7K}.
HELIX 630 644 {ECO:0000244|PDB:4X7K}.
STRAND 654 660 {ECO:0000244|PDB:4X7K}.
STRAND 883 889 {ECO:0000244|PDB:4X7K}.
HELIX 896 901 {ECO:0000244|PDB:4X7K}.
HELIX 906 908 {ECO:0000244|PDB:4X7K}.
HELIX 911 930 {ECO:0000244|PDB:4X7K}.
HELIX 940 942 {ECO:0000244|PDB:4X7K}.
STRAND 943 945 {ECO:0000244|PDB:4X7K}.
STRAND 951 953 {ECO:0000244|PDB:4X7K}.
HELIX 993 996 {ECO:0000244|PDB:4X7K}.
HELIX 1004 1018 {ECO:0000244|PDB:4X7K}.
HELIX 1024 1035 {ECO:0000244|PDB:4X7K}.
HELIX 1041 1046 {ECO:0000244|PDB:4X7K}.
HELIX 1048 1057 {ECO:0000244|PDB:4X7K}.
HELIX 1062 1064 {ECO:0000244|PDB:4X7K}.
HELIX 1068 1072 {ECO:0000244|PDB:4X7K}.
HELIX 1075 1077 {ECO:0000244|PDB:4X7K}.
SEQUENCE 1116 AA; 125216 MW; 95FEB5DAE8D3D452 CRC64;
MERAISPGLL VRALLLLLLL LGLAARTVAA GRARGLPAPT AEAAFGLGAA AAPTSATRVP
AAGAVAAAEV TVEDAEALPA AAGEQEPRGP EPDDETELRP RGRSLVIIST LDGRIAALDP
ENHGKKQWDL DVGSGSLVSS SLSKPEVFGN KMIIPSLDGA LFQWDQDRES METVPFTVES
LLESSYKFGD DVVLVGGKSL TTYGLSAYSG KVRYICSALG CRQWDSDEME QEEDILLLQR
TQKTVRAVGP RSGNEKWNFS VGHFELRYIP DMETRAGFIE STFKPNENTE ESKIISDVEE
QEAAIMDIVI KVSVADWKVM AFSKKGGHLE WEYQFCTPIA SAWLLKDGKV IPISLFDDTS
YTSNDDVLED EEDIVEAARG ATENSVYLGM YRGQLYLQSS VRISEKFPSS PKALESVTNE
NAIIPLPTIK WKPLIHSPSR TPVLVGSDEF DKCLSNDKFS HEEYSNGALS ILQYPYDNGY
YLPYYKRERN KRSTQITVRF LDNPHYNKNI RKKDPVLLLH WWKEIVATIL FCIIATTFIV
RRLFHPHPHR QRKESETQCQ TENKYDSVSG EANDSSWNDI KNSGYISRYL TDFEPIQCLG
RGGFGVVFEA KNKVDDCNYA IKRIRLPNRE LAREKVMREV KALAKLEHPG IVRYFNAWLE
APPEKWQEKM DEIWLKDEST DWPLSSPSPM DAPSVKIRRM DPFATKEHIE IIAPSPQRSR
SFSVGISCDQ TSSSESQFSP LEFSGMDHED ISESVDAAYN LQDSCLTDCD VEDGTMDGND
EGHSFELCPS EASPYVRSRE RTSSSIVFED SGCDNASSKE EPKTNRLHIG NHCANKLTAF
KPTSSKSSSE ATLSISPPRP TTLSLDLTKN TTEKLQPSSP KVYLYIQMQL CRKENLKDWM
NGRCTIEERE RSVCLHIFLQ IAEAVEFLHS KGLMHRDLKP SNIFFTMDDV VKVGDFGLVT
AMDQDEEEQT VLTPMPAYAR HTGQVGTKLY MSPEQIHGNS YSHKVDIFSL GLILFELLYP
FSTQMERVRT LTDVRNLKFP PLFTQKYPCE YVMVQDMLSP SPMERPEAIN IIENAVFEDL
DFPGKTVLRQ RSRSLSSSGT KHSRQSNNSH SPLPSN


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