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UniProtKB/Swiss-Prot entry O00418


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name EF2K_HUMAN
Primary accession number O00418
Secondary accession number Q8N588
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on July 1, 1997 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 85)
Name and origin of the protein
Protein name Elongation factor 2 kinase
Synonyms EC 2.7.11.20
eEF-2 kinase
eEF-2K
Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase
Gene name
Name: EEF2K
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Glial tumor;
DOI=10.1073/pnas.94.10.4884; PubMed=9144159 [NCBI, ExPASy, EBI, Israel, Japan]
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 MRNA], AND VARIANT ARG-23.
TISSUE=Lymph;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASS SPECTROMETRY.
TISSUE=T-cell;
DOI=10.1021/ac035352d; PubMed=15144186 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-27; SER-31; TYR-69; SER-70; SER-470 AND SER-474, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-445, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; THR-348; SER-470; SER-474 AND SER-477, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[9]
VARIANTS [LARGE SCALE ANALYSIS] ARG-23; ALA-75; MET-291; TRP-433 AND HIS-609.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U93850; AAB58270.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC032665; AAH32665.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00011689; -.
RefSeq NP_037434.1; -.
UniGene Hs.633744
3D structure databases
ModBase O00418.
PTM databases
PhosphoSite O00418; -.
Enzyme and pathway databases
BRENDA 2.7.11.20; 247.
Pathway_Interaction_DB p38gammadeltapathway; Signaling mediated by p38-gamma and p38-delta.
Reactome REACT_498; Signaling by Insulin receptor.
Organism-specific databases
GeneCards GC16P022125; -.
H-InvDB HIX0021510; -.
HGNC HGNC:24615; EEF2K.
GenAtlas EEF2K.
HPA CAB007818; -.
MIM 606968; gene. [NCBI / EBI]
PharmGKB PA134992891; -.
Gene expression databases
ArrayExpress O00418; -.
Bgee O00418; -.
CleanEx HS_EEF2K; -.
GermOnline ENSG00000103319; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005516; Molecular function: calmodulin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004686; Molecular function: elongation factor-2 kinase activity (inferred from electronic annotation from EC).
GO:0008135; Molecular function: translation factor activity, nucleic acid binding (traceable author statement from ProtInc).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0006414; Biological process: translational elongation (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR017400; Elongation_factor_2_kinase.
IPR004166; MHCK_EF2_kinase.
IPR006597; Sel1-like.
IPR011990; TPR-like_helical.
Graphical view of domain structure.
Gene3D G3DSA:1.25.40.10; TPR-like_helical; 1.
Pfam PF02816; Alpha_kinase; 1.
PF08238; Sel1; 3.
Pfam graphical view of domain structure.
PIRSF PIRSF038139; Elongation_factor_2_kinase; 1.
SMART SM00811; Alpha_kinase; 1.
SMART graphical view of domain structure.
PROSITE PS51158; ALPHA_KINASE; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE O00418; -.
Genome annotation databases
Ensembl ENSG00000103319; Homo sapiens. [Contig view]
GeneID 29904; -.
KEGG hsa:29904; -.
Phylogenomic databases
HOGENOM O00418; -.
HOVERGEN O00418; -.
Other
NextBio 52478; -.
SOURCE EEF2K; Homo sapiens.
ProtoNet O00418.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Calcium; Calmodulin-binding; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   725  725     Elongation factor 2 kinase. PRO_0000086936
DOMAIN   116   326  211     Alpha-type protein kinase. 
NP_BIND   296   302  7     ATP (By similarity). 
REGION   594   610  17     Calmodulin-binding (Potential). 
REGION   610   627  18     Pseudosubstrate/autoinhibitory domain (Potential). 
MOD_RES   18    18        Phosphoserine. 
MOD_RES   27    27        Phosphoserine. 
MOD_RES   31    31        Phosphoserine. 
MOD_RES   69    69        Phosphotyrosine. 
MOD_RES   70    70        Phosphoserine. 
MOD_RES   71    71        Phosphoserine (By similarity). 
MOD_RES   135   135        Phosphoserine. 
MOD_RES   348   348        Phosphothreonine. 
MOD_RES   445   445        Phosphoserine. 
MOD_RES   470   470        Phosphoserine. 
MOD_RES   474   474        Phosphoserine. 
MOD_RES   477   477        Phosphoserine. 
VARIANT   23    23  1     H -> R (in dbSNP:rs9935059 [NCBI]). VAR_033915 
VARIANT   75    75  1     P -> A (in dbSNP:rs17841292 [NCBI]). VAR_033916 
VARIANT   291   291  1     T -> M (in a colorectal adenocarcinoma sample; somatic mutation). VAR_041534 
VARIANT   433   433  1     R -> W. VAR_041535 
VARIANT   609   609  1     D -> H. VAR_041536 
Sequence information
Length: 725 AA [This is the length of the unprocessed precursor] Molecular weight: 82172 Da [This is the MW of the unprocessed precursor] CRC64: E006FECAF169F70D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MADEDLIFRL EGVDGGQSPR AGHDGDSDGD SDDEEGYFIC PITDDPSSNQ NVNSKVNKYY 

        70         80         90        100        110        120 
SNLTKSERYS SSGSPANSFH FKEAWKHAIQ KAKHMPDPWA EFHLEDIATE RATRHRYNAV 

       130        140        150        160        170        180 
TGEWLDDEVL IKMASQPFGR GAMRECFRTK KLSNFLHAQQ WKGASNYVAK RYIEPVDRDV 

       190        200        210        220        230        240 
YFEDVRLQME AKLWGEEYNR HKPPKQVDIM QMCIIELKDR PGKPLFHLEH YIEGKYIKYN 

       250        260        270        280        290        300 
SNSGFVRDDN IRLTPQAFSH FTFERSGHQL IVVDIQGVGD LYTDPQIHTE TGTDFGDGNL 

       310        320        330        340        350        360 
GVRGMALFFY SHACNRICES MGLAPFDLSP RERDAVNQNT KLLQSAKTIL RGTEEKCGSP 

       370        380        390        400        410        420 
RVRTLSGSRP PLLRPLSENS GDENMSDVTF DSLPSSPSSA TPHSQKLDHL HWPVFSDLDN 

       430        440        450        460        470        480 
MASRDHDHLD NHRESENSGD SGYPSEKRGE LDDPEPREHG HSYSNRKYES DEDSLGSSGR 

       490        500        510        520        530        540 
VCVEKWNLLN SSRLHLPRAS AVALEVQRLN ALDLEKKIGK SILGKVHLAM VRYHEGGRFC 

       550        560        570        580        590        600 
EKGEEWDQES AVFHLEHAAN LGELEAIVGL GLMYSQLPHH ILADVSLKET EENKTKGFDY 

       610        620        630        640        650        660 
LLKAAEAGDR QSMILVARAF DSGQNLSPDR CQDWLEALHW YNTALEMTDC DEGGEYDGMQ 

       670        680        690        700        710        720 
DEPRYMMLAR EAEMLFTGGY GLEKDPQRSG DLYTQAAEAA MEAMKGRLAN QYYQKAEEAW 


AQMEE 

O00418 in FASTA format

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