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O08796 (EF2K_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic elongation factor 2 kinase
Short name=eEF-2 kinase
Short name=eEF-2K
EC=2.7.11.20
Alternative name(s):
Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase
Gene names
Name:Eef2k
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length724 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 TRM7, 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. Ref.1

Catalytic activity

ATP + [elongation factor 2] = ADP + [elongation factor 2] phosphate. Ref.1

Enzyme regulation

Undergoes calcium/calmodulin-dependent intramolecular autophosphorylation, and this results in it becoming partially calcium/calmodulin-independent By similarity.

Subunit structure

Monomer or homodimer Potential.

Tissue specificity

Ubiquitously expressed. Particularly abundant in skeletal muscle and heart.

Domain

The catalytic domain is located to N-terminal region. The neighbor region contains the calmodulin-binding domain By similarity.

Post-translational modification

Autophosphorylated. Phosphorylated by AMP-activated protein kinase AMPK at Ser-397 leading to EEF2K activation and protein synthesis inhibition. Phosphorylated by TRPM7 at Ser-77 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-358 or RPS6KA1 and RPS6KB1 at Ser-365 instead decrease EEF2K activity and promote protein synthesis By similarity. Ref.3 Ref.4

Sequence similarities

Belongs to the protein kinase superfamily. Alpha-type protein kinase family.

Contains 1 alpha-type protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 724724Eukaryotic elongation factor 2 kinase
PRO_0000086937

Regions

Domain115 – 325211Alpha-type protein kinase
Nucleotide binding295 – 3017ATP By similarity
Region593 – 60917Calmodulin-binding Potential
Region609 – 62618Pseudosubstrate/autoinhibitory domain Potential

Amino acid modifications

Modified residue271Phosphoserine Ref.4
Modified residue291Phosphothreonine Ref.4
Modified residue311Phosphoserine Ref.4
Modified residue701Phosphoserine Ref.3
Modified residue771Phosphoserine; by TRPM7 By similarity
Modified residue1341Phosphoserine By similarity
Modified residue3471Phosphothreonine By similarity
Modified residue3581Phosphoserine; by MAPK13 and CDK1 By similarity
Modified residue3651Phosphoserine; by RPS6KA1 and RPS6KB1 By similarity
Modified residue3971Phosphoserine; by AMPK By similarity
Modified residue4441Phosphoserine By similarity
Modified residue4691Phosphoserine Ref.4
Modified residue4731Phosphoserine Ref.4
Modified residue4761Phosphoserine By similarity
Modified residue4991Phosphoserine; by PKA By similarity

Sequences

Sequence LengthMass (Da)Tools
O08796 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: B892D7D547C8E7AE

FASTA72481,739
        10         20         30         40         50         60 
MADEDLIFCL EGVDGGRCSR AGHNADSDTD SDDDEGYFIC PITDDHMSNQ NVSSKVQSYY 

        70         80         90        100        110        120 
SNLTKTECGS TGSPASSFHF KEAWKHAIEK AKHMPDPWAE FHLEDIATEH ATRHRYNAVT 

       130        140        150        160        170        180 
GEWLKDEVLI KMASQPFGRG AMRECFRTKK LSNFLHAQQW KGASNYVAKR YIEPVDRSVY 

       190        200        210        220        230        240 
FEDVQLQMEA KLWGEDYNRH KPPKQVDIMQ MCIIELKDRP GQPLFHLEHY IEGKYIKYNS 

       250        260        270        280        290        300 
NSGFVRDDNI RLTPQAFSHF TFERSGHQLI VVDIQGVGDL YTDPQIHTEK GTDFGDGNLG 

       310        320        330        340        350        360 
VRGMALFFYS HACNRICQSM GLTPFDLSPR EQDAVNQSTR LLQSAKTILR GTEEKCGSPR 

       370        380        390        400        410        420 
IRTLSSSRPP LLLRLSENSG DENMSDVTFD SLPSSPSSAT PHSQKLDHLH WPVFGDLDNM 

       430        440        450        460        470        480 
GPRDHDRMDN HRDSENSGDS GYPSEKRSDL DDPEPREHGH SNGNRRHESD EDSLGSSGRV 

       490        500        510        520        530        540 
CVETWNLLNP SRLHLPRPSA VALEVQRLNA LDLGRKIGKS VLGKVHLAMV RYHEGGRFCE 

       550        560        570        580        590        600 
KDEEWDRESA IFHLEHAADL GELEAIVGLG LMYSQLPHHI LADVSLKETE ENKTKGFDYL 

       610        620        630        640        650        660 
LKAAEAGDRH SMILVARAFD TGLNLSPDRC QDWSEALHWY NTALETTDCD EGGEYDGIQD 

       670        680        690        700        710        720 
EPQYALLARE AEMLLTGGFG LDKNPQRSGD LYTQAAEAAM EAMKGRLANQ YYEKAEEAWA 


QMEE

« Hide

References

« Hide 'large scale' references
[1]"Identification of a new class of protein kinases represented by eukaryotic elongation factor-2 kinase."
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.
Proc. Natl. Acad. Sci. U.S.A. 94:4884-4889(1997) [PubMed: 9144159] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION.
Strain: BALB/c.
Tissue: Spleen.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary gland.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, MASS SPECTROMETRY.
Tissue: Liver.
[4]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; THR-29; SER-31; SER-469 AND SER-473, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U93848 mRNA. Translation: AAB58271.1.
BC003433 mRNA. Translation: AAH03433.1.
IPIIPI00115681.
RefSeqNP_001238755.1. NM_001251826.1.
NP_031934.1. NM_007908.3.
UniGeneMm.25997.
Mm.361795.

3D structure databases

ProteinModelPortalO08796.
SMRO08796. Positions 103-323, 526-646.
ModBaseSearch...

Protein-protein interaction databases

STRINGO08796.

PTM databases

PhosphoSiteO08796.

Proteomic databases

PRIDEO08796.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000047875; ENSMUSP00000046595; ENSMUSG00000035064.
ENSMUST00000106488; ENSMUSP00000102097; ENSMUSG00000035064.
ENSMUST00000106489; ENSMUSP00000102098; ENSMUSG00000035064.
GeneID13631.
KEGGmmu:13631.
UCSCuc009jnb.1. mouse.

Organism-specific databases

CTD29904.
MGIMGI:1195261. Eef2k.

Phylogenomic databases

eggNOGroNOG08138.
HOGENOMHBG717344.
HOVERGENHBG002318.
InParanoidO08796.
OMAHKPPKQV.
OrthoDBEOG43TZTX.
PhylomeDBO08796.

Enzyme and pathway databases

BRENDA2.7.11.20. 3474.

Gene expression databases

ArrayExpressO08796.
BgeeO08796.
CleanExMM_EEF2K.
GenevestigatorO08796.
GermOnlineENSMUSG00000035064. Mus musculus.

Family and domain databases

InterProIPR017400. Elongation_factor_2_kinase.
IPR011009. Kinase-like_dom.
IPR004166. MHCK_EF2_kinase.
IPR006597. Sel1-like.
IPR011990. TPR-like_helical.
[Graphical view]
Gene3DG3DSA:1.25.40.10. TPR-like_helical. 1 hit.
KOK08292.
PfamPF02816. Alpha_kinase. 1 hit.
PF08238. Sel1. 4 hits.
[Graphical view]
PIRSFPIRSF038139. Elongation_factor_2_kinase. 1 hit.
SMARTSM00811. Alpha_kinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS51158. ALPHA_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284316.
SOURCESearch...

Entry information

Entry nameEF2K_MOUSE
AccessionPrimary (citable) accession number: O08796
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: December 14, 2011
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents