LOCUS       NP_001399258             724 aa            linear   ROD 14-FEB-2025
DEFINITION  eukaryotic elongation factor 2 kinase isoform a [Mus musculus].
ACCESSION   NP_001399258 XP_006507405
VERSION     NP_001399258.1
DBSOURCE    REFSEQ: accession NM_001412329.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Ruggiero,A., Heim,L.R., Susman,L., Hreaky,D., Shapira,I.,
            Katsenelson,M., Rosenblum,K. and Slutsky,I.
  TITLE     NMDA receptors regulate the firing rate set point of hippocampal
            circuits without altering single-cell dynamics
  JOURNAL   Neuron 113 (2), 244-259 (2025)
   PUBMED   39515323
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Xu,Y., Sun,F., Tian,Y., Zeng,G., Lei,G., Bai,Z., Wang,Y., Ge,X.,
            Wang,J., Xiao,C., Wang,Z., Hu,M., Song,J., Yang,P. and Liu,R.
  TITLE     Enhanced NK cell activation via eEF2K-mediated potentiation of the
            cGAS-STING pathway in hepatocellular carcinoma
  JOURNAL   Int Immunopharmacol 129, 111628 (2024)
   PUBMED   38320351
  REMARK    GeneRIF: Enhanced NK cell activation via eEF2K-mediated
            potentiation of the cGAS-STING pathway in hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 724)
  AUTHORS   Iyyappan,R., Aleshkina,D., Ming,H., Dvoran,M., Kakavand,K.,
            Jansova,D., Del Llano,E., Gahurova,L., Bruce,A.W., Masek,T.,
            Pospisek,M., Horvat,F., Kubelka,M., Jiang,Z. and Susor,A.
  TITLE     The translational oscillation in oocyte and early embryo
            development
  JOURNAL   Nucleic Acids Res 51 (22), 12076-12091 (2023)
   PUBMED   37950888
REFERENCE   4  (residues 1 to 724)
  AUTHORS   Peng,H.Y., Wang,L., Das,J.K., Kumar,A., Ballard,D.J., Ren,Y.,
            Xiong,X., de Figueiredo,P., Yang,J.M. and Song,J.
  TITLE     Control of CD4+ T cells to restrain inflammatory diseases via
            eukaryotic elongation factor 2 kinase
  JOURNAL   Signal Transduct Target Ther 8 (1), 415 (2023)
   PUBMED   37875468
  REMARK    GeneRIF: Control of CD4[+] T cells to restrain inflammatory
            diseases via eukaryotic elongation factor 2 kinase.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 724)
  AUTHORS   Knight,J.R.P., Proud,C.G., Mallucci,G., von der Haar,T.,
            Smales,C.M., Willis,A.E. and Sansom,O.J.
  TITLE     Eukaryotic Elongation Factor 2 Kinase Activity Is Required for the
            Phenotypes of the Rpl24Bst Mouse
  JOURNAL   J Invest Dermatol 142 (12), 3346-3348 (2022)
   PUBMED   35850210
  REMARK    GeneRIF: Eukaryotic Elongation Factor 2 Kinase Activity Is Required
            for the Phenotypes of the Rpl24[Bst] Mouse.
REFERENCE   6  (residues 1 to 724)
  AUTHORS   Boyce,M., Py,B.F., Ryazanov,A.G., Minden,J.S., Long,K., Ma,D. and
            Yuan,J.
  TITLE     A pharmacoproteomic approach implicates eukaryotic elongation
            factor 2 kinase in ER stress-induced cell death
  JOURNAL   Cell Death Differ 15 (3), 589-599 (2008)
   PUBMED   18188169
REFERENCE   7  (residues 1 to 724)
  AUTHORS   Sakagami,H., Nishimura,H., Saito,R. and Kondo,H.
  TITLE     Transient up-regulation of elongation factor-2 kinase
            (Ca2+/calmodulin-dependent protein kinase III) messenger RNA in
            developing mouse brain
  JOURNAL   Neurosci Lett 330 (1), 41-44 (2002)
   PUBMED   12213630
  REMARK    GeneRIF: During late embryonic and early postnatal stages,
            elongation factor 2 kinase is up-regulated in the cerebral cortex
            and hippocampal pyramidal cell layer.
REFERENCE   8  (residues 1 to 724)
  AUTHORS   Ryazanov,A.G., Pavur,K.S. and Dorovkov,M.V.
  TITLE     Alpha-kinases: a new class of protein kinases with a novel
            catalytic domain
  JOURNAL   Curr Biol 9 (2), R43-R45 (1999)
   PUBMED   10021370
REFERENCE   9  (residues 1 to 724)
  AUTHORS   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. and Hait,W.N.
  TITLE     Identification of a new class of protein kinases represented by
            eukaryotic elongation factor-2 kinase
  JOURNAL   Proc Natl Acad Sci U S A 94 (10), 4884-4889 (1997)
   PUBMED   9144159
REFERENCE   10 (residues 1 to 724)
  AUTHORS   Gschwendt,M., Kittstein,W. and Marks,F.
  TITLE     Elongation factor-2 kinase: effective inhibition by the novel
            protein kinase inhibitor rottlerin and relative insensitivity
            towards staurosporine
  JOURNAL   FEBS Lett 338 (1), 85-88 (1994)
   PUBMED   8307162
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC122214.4 and AC122248.5.
            
            On Sep 29, 2022 this sequence version replaced XP_006507405.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR13422601.1979248.1,
                                           SRR13422598.421786.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849379
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 64.95 cM"
     Protein         1..724
                     /product="eukaryotic elongation factor 2 kinase isoform a"
                     /EC_number="2.7.11.20"
                     /note="eukaroytic elongation factor 2 kinase; eEF-2
                     kinase; calcium/calmodulin-dependent eukaryotic elongation
                     factor 2 kinase"
                     /calculated_mol_wt=81608
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:O00418; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00418; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:O00418; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00418; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Region          80..93
                     /region_name="Calmodulin-binding.
                     /evidence=ECO:0000250|UniProtKB:O00418"
                     /note="propagated from UniProtKB/Swiss-Prot (O08796.1)"
     Region          102..317
                     /region_name="Alpha_kinase_eEF2K"
                     /note="Alpha-kinase domain of eukaryotic elongation
                     factor-2 kinase; cd16967"
                     /db_xref="CDD:341217"
     Site            order(138..143,145,167,169,209,228..231,273,275,283)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:341217"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00418; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:O00418; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:O00418; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Region          353..476
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08796.1)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK13 and CDK1.
                     /evidence=ECO:0000250|UniProtKB:O00418; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis, RPS6KA1 and
                     RPS6KB1. /evidence=ECO:0000250|UniProtKB:O00418;
                     propagated from UniProtKB/Swiss-Prot (O08796.1)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:O00418; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00418; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00418; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:O00418; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00418; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:P70531; propagated from
                     UniProtKB/Swiss-Prot (O08796.1)"
     Region          502..535
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          <531..694
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          542..575
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          592..621
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     CDS             1..724
                     /gene="Eef2k"
                     /gene_synonym="eEF-2K"
                     /coded_by="NM_001412329.1:390..2564"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="GeneID:13631"
                     /db_xref="MGI:MGI:1195261"
ORIGIN      
        1 madedlifcl egvdggrcsr aghnadsdtd sdddegyfic pitddhmsnq nvsskvqsyy
       61 snltktecgs tgspassfhf keawkhaiek akhmpdpwae fhlediateh atrhrynavt
      121 gewlkdevli kmasqpfgrg amrecfrtkk lsnflhaqqw kgasnyvakr yiepvdrsvy
      181 fedvqlqmea klwgedynrh kppkqvdimq mciielkdrp gqplfhlehy iegkyikyns
      241 nsgfvrddni rltpqafshf tfersghqli vvdiqgvgdl ytdpqihtek gtdfgdgnlg
      301 vrgmalffys hacnricqsm gltpfdlspr eqdavnqstr llqsaktilr gteekcgspr
      361 irtlsssrpp lllrlsensg denmsdvtfd slpsspssat phsqkldhlh wpvfgdldnm
      421 gprdhdrmdn hrdsensgds gypsekrsdl ddpeprehgh sngnrrhesd edslgssgrv
      481 cvetwnllnp srlhlprpsa valevqrlna ldlgrkigks vlgkvhlamv ryheggrfce
      541 kdeewdresa ifhlehaadl geleaivglg lmysqlphhi ladvslkete enktkgfdyl
      601 lkaaeagdrh smilvarafd tglnlspdrc qdwsealhwy ntalettdcd eggeydgiqd
      661 epqyallare aemlltggfg ldknpqrsgd lytqaaeaam eamkgrlanq yyekaeeawa
      721 qmee
//
