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Eukaryotic elongation factor 2 kinase (eEF-2 kinase) (eEF-2K) (EC 2.7.11.20) (Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase)

 EF2K_HUMAN              Reviewed;         725 AA.
O00418; Q8N588;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
28-JUL-2009, sequence version 2.
18-JUL-2018, entry version 176.
RecName: Full=Eukaryotic elongation factor 2 kinase;
Short=eEF-2 kinase;
Short=eEF-2K;
EC=2.7.11.20 {ECO:0000269|PubMed:11015200, ECO:0000269|PubMed:9144159};
AltName: Full=Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase;
Name=EEF2K;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND VARIANT
ARG-361.
TISSUE=Glial tumor;
PubMed=9144159; DOI=10.1073/pnas.94.10.4884;
Ryazanov A.G., Ward M.D., Mendola C.E., Pavur K.S., Dorovkov M.V.,
Wiedmann M., Erdjument-Bromage H., Tempst P., Parmer T.G.,
Prostko C.R., Germino F.J., Hait W.N.;
"Identification of a new class of protein kinases represented by
eukaryotic elongation factor-2 kinase.";
Proc. Natl. Acad. Sci. U.S.A. 94:4884-4889(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-23 AND
ARG-361.
TISSUE=Lymph;
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).
[4]
CATALYTIC ACTIVITY, IDENTIFICATION OF THE CALMODULIN-BINDING REGION,
AUTOPHOSPHORYLATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11015200; DOI=10.1021/bi0007270;
Pavur K.S., Petrov A.N., Ryazanov A.G.;
"Mapping the functional domains of elongation factor-2 kinase.";
Biochemistry 39:12216-12224(2000).
[5]
PHOSPHORYLATION AT SER-359.
PubMed=11500363; DOI=10.1093/emboj/20.16.4360;
Knebel A., Morrice N., Cohen P.;
"A novel method to identify protein kinase substrates: eEF2 kinase is
phosphorylated and inhibited by SAPK4/p38delta.";
EMBO J. 20:4360-4369(2001).
[6]
PHOSPHORYLATION AT SER-366 BY RPS6KA1 AND RPS6KB1, AND MUTAGENESIS OF
SER-366.
PubMed=11500364; DOI=10.1093/emboj/20.16.4370;
Wang X., Li W., Williams M., Terada N., Alessi D.R., Proud C.G.;
"Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6
kinase.";
EMBO J. 20:4370-4379(2001).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[8]
FUNCTION, AND PHOSPHORYLATION AT SER-398.
PubMed=14709557; DOI=10.1074/jbc.M309773200;
Browne G.J., Finn S.G., Proud C.G.;
"Stimulation of the AMP-activated protein kinase leads to activation
of eukaryotic elongation factor 2 kinase and to its phosphorylation at
a novel site, serine 398.";
J. Biol. Chem. 279:12220-12231(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-474, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-445, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[11]
PHOSPHORYLATION AT SER-359.
PubMed=18337751; DOI=10.1038/emboj.2008.39;
Smith E.M., Proud C.G.;
"cdc2-cyclin B regulates eEF2 kinase activity in a cell cycle- and
amino acid-dependent manner.";
EMBO J. 27:1005-1016(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-348; SER-470; SER-474
AND SER-477, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; THR-348; SER-445;
SER-470 AND SER-474, 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).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION AT SER-78.
PubMed=21112387; DOI=10.1016/j.cellsig.2010.11.011;
Perraud A.L., Zhao X., Ryazanov A.G., Schmitz C.;
"The channel-kinase TRPM7 regulates phosphorylation of the
translational factor eEF2 via eEF2-k.";
Cell. Signal. 23:586-593(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-470, 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).
[19]
PHOSPHORYLATION AT SER-61; SER-66; SER-78; THR-348; THR-353; SER-366;
SER-445; SER-474 AND SER-491, AND MUTAGENESIS OF SER-78; THR-348 AND
SER-366.
PubMed=22216903; DOI=10.1042/BJ20111530;
Pyr Dit Ruys S., Wang X., Smith E.M., Herinckx G., Hussain N.,
Rider M.H., Vertommen D., Proud C.G.;
"Identification of autophosphorylation sites in eukaryotic elongation
factor-2 kinase.";
Biochem. J. 442:681-692(2012).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-70; SER-72;
SER-74; SER-78; SER-243; THR-348; THR-353; SER-435; SER-445; SER-470;
SER-474; SER-477 AND SER-491, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; THR-348; SER-445 AND
SER-474, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
VARIANTS [LARGE SCALE ANALYSIS] ARG-23; ALA-75; MET-291; TRP-433 AND
HIS-609.
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: Threonine kinase that regulates protein synthesis by
controlling the rate of peptide chain elongation. Upon activation
by a variety of upstream kinases including AMPK or TRPM7,
phosphorylates the elongation factor EEF2 at a single site,
renders it unable to bind ribosomes and thus inactive. In turn,
the rate of protein synthesis is reduced.
{ECO:0000269|PubMed:14709557, ECO:0000269|PubMed:9144159}.
-!- CATALYTIC ACTIVITY: ATP + [elongation factor 2] = ADP +
[elongation factor 2] phosphate. {ECO:0000269|PubMed:11015200,
ECO:0000269|PubMed:9144159}.
-!- ENZYME REGULATION: Undergoes calcium/calmodulin-dependent
intramolecular autophosphorylation, and this results in it
becoming partially calcium/calmodulin-independent. {ECO:0000250}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.2 uM for EEF2 {ECO:0000269|PubMed:11015200};
Vmax=4 nmol/min/mg enzyme {ECO:0000269|PubMed:11015200};
-!- SUBUNIT: Monomer or homodimer (Probable). Interacts with
Calmodulin/CALM1; this interaction is strictly required for
phosphorylation activity (PubMed:11015200).
{ECO:0000269|PubMed:11015200, ECO:0000305}.
-!- PTM: Autophosphorylated at multiple residues, Thr-348 being the
major site. Phosphorylated by AMP-activated protein kinase AMPK at
Ser-398 leading to EEF2K activation and protein synthesis
inhibition. Phosphorylated by TRPM7 at Ser-78 resulting in
improved protein stability, higher EE2F phosphorylated and
subsequently reduced rate of protein synthesis. Phosphorylation by
other kinases such as CDK1 and MAPK13 at Ser-359 or RPS6KA1 and
RPS6KB1 at Ser-366 instead decrease EEF2K activity and promote
protein synthesis. {ECO:0000269|PubMed:11015200,
ECO:0000269|PubMed:11500363, ECO:0000269|PubMed:11500364,
ECO:0000269|PubMed:14709557, ECO:0000269|PubMed:18337751,
ECO:0000269|PubMed:21112387, ECO:0000269|PubMed:22216903}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
protein kinase family. {ECO:0000305}.
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EMBL; U93850; AAB58270.1; -; mRNA.
EMBL; AC009034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC032665; AAH32665.1; -; mRNA.
CCDS; CCDS10604.1; -.
RefSeq; NP_037434.1; NM_013302.3.
RefSeq; XP_005276554.1; XM_005276497.3.
RefSeq; XP_016878682.1; XM_017023193.1.
UniGene; Hs.498892; -.
PDB; 5J8H; NMR; -; B=74-100.
PDB; 5KS5; NMR; -; A=627-725.
PDBsum; 5J8H; -.
PDBsum; 5KS5; -.
ProteinModelPortal; O00418; -.
SMR; O00418; -.
BioGrid; 118953; 34.
ELM; O00418; -.
IntAct; O00418; 14.
MINT; O00418; -.
STRING; 9606.ENSP00000263026; -.
BindingDB; O00418; -.
ChEMBL; CHEMBL5026; -.
GuidetoPHARMACOLOGY; 2014; -.
iPTMnet; O00418; -.
PhosphoSitePlus; O00418; -.
BioMuta; EEF2K; -.
EPD; O00418; -.
MaxQB; O00418; -.
PaxDb; O00418; -.
PeptideAtlas; O00418; -.
PRIDE; O00418; -.
ProteomicsDB; 47876; -.
DNASU; 29904; -.
Ensembl; ENST00000263026; ENSP00000263026; ENSG00000103319.
GeneID; 29904; -.
KEGG; hsa:101930123; -.
KEGG; hsa:29904; -.
UCSC; uc002dki.4; human.
CTD; 29904; -.
DisGeNET; 101930123; -.
DisGeNET; 29904; -.
EuPathDB; HostDB:ENSG00000103319.11; -.
GeneCards; EEF2K; -.
HGNC; HGNC:24615; EEF2K.
HPA; CAB007818; -.
HPA; HPA056061; -.
MIM; 606968; gene.
neXtProt; NX_O00418; -.
OpenTargets; ENSG00000103319; -.
PharmGKB; PA134992891; -.
eggNOG; ENOG410IFRY; Eukaryota.
eggNOG; ENOG410YE3S; LUCA.
GeneTree; ENSGT00800000124135; -.
HOGENOM; HOG000022023; -.
HOVERGEN; HBG002318; -.
InParanoid; O00418; -.
KO; K08292; -.
OMA; FICPITD; -.
OrthoDB; EOG091G09CK; -.
PhylomeDB; O00418; -.
TreeFam; TF316085; -.
BRENDA; 2.7.11.20; 2681.
Reactome; R-HSA-166208; mTORC1-mediated signalling.
SIGNOR; O00418; -.
ChiTaRS; EEF2K; human.
GeneWiki; EEF2K; -.
PRO; PR:O00418; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103319; -.
CleanEx; HS_EEF2K; -.
ExpressionAtlas; O00418; baseline and differential.
Genevisible; O00418; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
GO; GO:0004686; F:elongation factor-2 kinase activity; IDA:UniProtKB.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0008135; F:translation factor activity, RNA binding; TAS:ProtInc.
GO; GO:0071454; P:cellular response to anoxia; IEA:Ensembl.
GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; IEA:Ensembl.
GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IEA:Ensembl.
GO; GO:0045807; P:positive regulation of endocytosis; IEA:Ensembl.
GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0031952; P:regulation of protein autophosphorylation; IEA:Ensembl.
GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
GO; GO:1990637; P:response to prolactin; IEA:Ensembl.
GO; GO:0006414; P:translational elongation; TAS:ProtInc.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR017400; eEF-2K.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR004166; MHCK_EF2_kinase.
InterPro; IPR006597; Sel1-like.
InterPro; IPR011990; TPR-like_helical_dom_sf.
Pfam; PF02816; Alpha_kinase; 1.
Pfam; PF08238; Sel1; 3.
PIRSF; PIRSF038139; Elongation_factor_2_kinase; 1.
SMART; SM00811; Alpha_kinase; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51158; ALPHA_KINASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Calcium; Calmodulin-binding;
Complete proteome; Kinase; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 725 Eukaryotic elongation factor 2 kinase.
/FTId=PRO_0000086936.
DOMAIN 116 326 Alpha-type protein kinase.
{ECO:0000255|PROSITE-ProRule:PRU00501}.
NP_BIND 296 302 ATP. {ECO:0000250}.
REGION 81 94 Calmodulin-binding.
{ECO:0000269|PubMed:11015200}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 61 61 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:22216903}.
MOD_RES 66 66 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:22216903}.
MOD_RES 70 70 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 71 71 Phosphoserine.
{ECO:0000250|UniProtKB:O08796}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 74 74 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 78 78 Phosphoserine; by autocatalysis and
TRPM7. {ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:21112387,
ECO:0000269|PubMed:22216903}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 348 348 Phosphothreonine; by autocatalysis.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:22216903}.
MOD_RES 353 353 Phosphothreonine; by autocatalysis.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:22216903}.
MOD_RES 359 359 Phosphoserine; by MAPK13 and CDK1.
{ECO:0000269|PubMed:11500363,
ECO:0000269|PubMed:18337751}.
MOD_RES 366 366 Phosphoserine; by autocatalysis, RPS6KA1
and RPS6KB1.
{ECO:0000269|PubMed:11500364,
ECO:0000269|PubMed:22216903}.
MOD_RES 392 392 Phosphoserine.
{ECO:0000250|UniProtKB:O08796}.
MOD_RES 398 398 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:14709557}.
MOD_RES 435 435 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 445 445 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:22216903}.
MOD_RES 470 470 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 474 474 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:22216903}.
MOD_RES 477 477 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 491 491 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:22216903}.
MOD_RES 500 500 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P70531}.
VARIANT 23 23 H -> R (in dbSNP:rs9935059).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_033915.
VARIANT 75 75 P -> A (in dbSNP:rs17841292).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_033916.
VARIANT 291 291 T -> M (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs147978363).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041534.
VARIANT 361 361 Q -> R (in dbSNP:rs4783453).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9144159}.
/FTId=VAR_058405.
VARIANT 433 433 R -> W (in dbSNP:rs56137739).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041535.
VARIANT 609 609 D -> H. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041536.
MUTAGEN 78 78 S->A: Decreased kinase activity.
{ECO:0000269|PubMed:22216903}.
MUTAGEN 348 348 T->A: Decreased kinase activity.
{ECO:0000269|PubMed:22216903}.
MUTAGEN 366 366 S->A: Abrogates phosphorylation by
RPS6KB1. {ECO:0000269|PubMed:11500364,
ECO:0000269|PubMed:22216903}.
MUTAGEN 366 366 S->A: Decreased kinase activity.
{ECO:0000269|PubMed:11500364,
ECO:0000269|PubMed:22216903}.
STRAND 78 80 {ECO:0000244|PDB:5J8H}.
HELIX 81 91 {ECO:0000244|PDB:5J8H}.
HELIX 633 640 {ECO:0000244|PDB:5KS5}.
HELIX 664 676 {ECO:0000244|PDB:5KS5}.
HELIX 686 702 {ECO:0000244|PDB:5KS5}.
HELIX 706 721 {ECO:0000244|PDB:5KS5}.
SEQUENCE 725 AA; 82144 MW; 9D2900E50EFF12DA CRC64;
MADEDLIFRL EGVDGGQSPR AGHDGDSDGD SDDEEGYFIC PITDDPSSNQ NVNSKVNKYY
SNLTKSERYS SSGSPANSFH FKEAWKHAIQ KAKHMPDPWA EFHLEDIATE RATRHRYNAV
TGEWLDDEVL IKMASQPFGR GAMRECFRTK KLSNFLHAQQ WKGASNYVAK RYIEPVDRDV
YFEDVRLQME AKLWGEEYNR HKPPKQVDIM QMCIIELKDR PGKPLFHLEH YIEGKYIKYN
SNSGFVRDDN IRLTPQAFSH FTFERSGHQL IVVDIQGVGD LYTDPQIHTE TGTDFGDGNL
GVRGMALFFY SHACNRICES MGLAPFDLSP RERDAVNQNT KLLQSAKTIL RGTEEKCGSP
QVRTLSGSRP PLLRPLSENS GDENMSDVTF DSLPSSPSSA TPHSQKLDHL HWPVFSDLDN
MASRDHDHLD NHRESENSGD SGYPSEKRGE LDDPEPREHG HSYSNRKYES DEDSLGSSGR
VCVEKWNLLN SSRLHLPRAS AVALEVQRLN ALDLEKKIGK SILGKVHLAM VRYHEGGRFC
EKGEEWDQES AVFHLEHAAN LGELEAIVGL GLMYSQLPHH ILADVSLKET EENKTKGFDY
LLKAAEAGDR QSMILVARAF DSGQNLSPDR CQDWLEALHW YNTALEMTDC DEGGEYDGMQ
DEPRYMMLAR EAEMLFTGGY GLEKDPQRSG DLYTQAAEAA MEAMKGRLAN QYYQKAEEAW
AQMEE


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