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Casein kinase I isoform epsilon (CKI-epsilon) (CKIe) (EC 2.7.11.1)

 KC1E_MOUSE              Reviewed;         416 AA.
Q9JMK2; Q8R389;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 2.
20-JUN-2018, entry version 152.
RecName: Full=Casein kinase I isoform epsilon;
Short=CKI-epsilon;
Short=CKIe;
EC=2.7.11.1;
Name=Csnk1e;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10640823;
Kusuda J., Hirai M., Tanuma R., Hashimoto K.;
"cDNA cloning and chromosome mapping of the mouse casein kinase I
epsilon gene (Csnk1e).";
Cytogenet. Cell Genet. 87:99-101(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[3]
FUNCTION AS PER1 KINASE, AND MUTAGENESIS OF LYS-38.
PubMed=10848614; DOI=10.1128/MCB.20.13.4888-4899.2000;
Vielhaber E., Eide E., Rivers A., Gao Z.-H., Virshup D.M.;
"Nuclear entry of the circadian regulator mPER1 is controlled by
mammalian casein kinase I epsilon.";
Mol. Cell. Biol. 20:4888-4899(2000).
[4]
INTERACTION WITH ANKRD6.
PubMed=12183362; DOI=10.1101/gad.230402;
Schwarz-Romond T., Asbrand C., Bakkers J., Kuehl M., Schaeffer H.J.,
Huelsken J., Behrens J., Hammerschmidt M., Birchmeier W.;
"The ankyrin repeat protein diversin recruits casein kinase Iepsilon
to the beta-catenin degradation complex and acts in both canonical Wnt
and Wnt/JNK signaling.";
Genes Dev. 16:2073-2084(2002).
[5]
FUNCTION AS PER PROTEINS KINASE.
PubMed=14701732; DOI=10.1128/MCB.24.2.584-594.2004;
Lee C., Weaver D.R., Reppert S.M.;
"Direct association between mouse PERIOD and CKIepsilon is critical
for a functioning circadian clock.";
Mol. Cell. Biol. 24:584-594(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[7]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=16790549; DOI=10.1073/pnas.0604138103;
Partch C.L., Shields K.F., Thompson C.L., Selby C.P., Sancar A.;
"Posttranslational regulation of the mammalian circadian clock by
cryptochrome and protein phosphatase 5.";
Proc. Natl. Acad. Sci. U.S.A. 103:10467-10472(2006).
[8]
DISRUPTION PHENOTYPE, FUNCTION, AND MUTAGENESIS OF ARG-178.
PubMed=18400165; DOI=10.1016/j.neuron.2008.01.019;
Meng Q.J., Logunova L., Maywood E.S., Gallego M., Lebiecki J.,
Brown T.M., Sladek M., Semikhodskii A.S., Glossop N.R., Piggins H.D.,
Chesham J.E., Bechtold D.A., Yoo S.H., Takahashi J.S., Virshup D.M.,
Boot-Handford R.P., Hastings M.H., Loudon A.S.;
"Setting clock speed in mammals: the CK1 epsilon tau mutation in mice
accelerates circadian pacemakers by selectively destabilizing PERIOD
proteins.";
Neuron 58:78-88(2008).
[9]
FUNCTION IN CIRCADIAN CLOCK, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY,
AND SUBCELLULAR LOCATION.
PubMed=19414593; DOI=10.1128/MCB.00338-09;
Etchegaray J.P., Machida K.K., Noton E., Constance C.M., Dallmann R.,
Di Napoli M.N., DeBruyne J.P., Lambert C.M., Yu E.A., Reppert S.M.,
Weaver D.R.;
"Casein kinase 1 delta regulates the pace of the mammalian circadian
clock.";
Mol. Cell. Biol. 29:3853-3866(2009).
[10]
FUNCTION IN CIRCADIAN CLOCK, AND DEPHOSPHORYLATION.
PubMed=21930935; DOI=10.1073/pnas.1107178108;
Lee H.M., Chen R., Kim H., Etchegaray J.P., Weaver D.R., Lee C.;
"The period of the circadian oscillator is primarily determined by the
balance between casein kinase 1 and protein phosphatase 1.";
Proc. Natl. Acad. Sci. U.S.A. 108:16451-16456(2011).
[11]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-382, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Casein kinases are operationally defined by their
preferential utilization of acidic proteins such as caseins as
substrates. Can phosphorylate a large number of proteins.
Participates in Wnt signaling. Phosphorylates DVL1. Central
component of the circadian clock. In balance with PP1, determines
the circadian period length, through the regulation of the speed
and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1
and PER2 nuclear transport and degradation. Inhibits cytokine-
induced granuloytic differentiation. {ECO:0000269|PubMed:10848614,
ECO:0000269|PubMed:14701732, ECO:0000269|PubMed:18400165,
ECO:0000269|PubMed:19414593, ECO:0000269|PubMed:21930935}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:19414593}.
-!- ENZYME REGULATION: Phosphorylation leads to a decrease in the
catalytic activity. {ECO:0000250}.
-!- SUBUNIT: Monomer. Component of the circadian core oscillator,
which includes the CRY proteins, CLOCK, or NPAS2, ARTNL/BMAL1 or
ARTNL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins.
Interacts with ANKRD6, DBNDD2, LRP5, LRP6 and SOCS3. Interacts
with SNAI1 (via zinc fingers). Interacts with DDX3X; the
interaction greatly improves CSNK1E affinity for ATP and enhances
DVL2 phosphorylation (By similarity).
{ECO:0000250|UniProtKB:P49674, ECO:0000269|PubMed:12183362}.
-!- INTERACTION:
O08785:Clock; NbExp=2; IntAct=EBI-771709, EBI-79859;
O35973:Per1; NbExp=2; IntAct=EBI-771709, EBI-1266764;
O54943:Per2; NbExp=4; IntAct=EBI-771709, EBI-1266779;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000269|PubMed:19414593}.
-!- TISSUE SPECIFICITY: Expressed in all tissues examined, including
brain, heart, lung, liver, pancreas, kidney, placenta and skeletal
muscle. Expressed in monocytes and lymphocytes but not in
granulocytes. {ECO:0000269|PubMed:16790549}.
-!- INDUCTION: Down-regulated during granulocytic differentiation.
Does not show circadian oscillations.
{ECO:0000269|PubMed:16790549}.
-!- PTM: Autophosphorylated. Partially dephosphorylated by PPP5C. May
be dephosphorylated by PP1.
-!- DISRUPTION PHENOTYPE: No visible phenotype. Has no apparent effect
on circadian oscillation of protein levels. Mice exhibit a small
but significant increase in circadian period length.
{ECO:0000269|PubMed:18400165, ECO:0000269|PubMed:19414593}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB028736; BAA88107.2; -; mRNA.
EMBL; BC026127; AAH26127.1; -; mRNA.
CCDS; CCDS27640.1; -.
PIR; S47616; S47616.
RefSeq; NP_001276827.1; NM_001289898.1.
RefSeq; NP_038795.3; NM_013767.6.
RefSeq; XP_017172146.1; XM_017316657.1.
RefSeq; XP_017172147.1; XM_017316658.1.
RefSeq; XP_017172148.1; XM_017316659.1.
UniGene; Mm.30199; -.
ProteinModelPortal; Q9JMK2; -.
SMR; Q9JMK2; -.
BioGrid; 205180; 49.
DIP; DIP-32410N; -.
IntAct; Q9JMK2; 58.
MINT; Q9JMK2; -.
STRING; 10090.ENSMUSP00000113341; -.
iPTMnet; Q9JMK2; -.
PhosphoSitePlus; Q9JMK2; -.
MaxQB; Q9JMK2; -.
PaxDb; Q9JMK2; -.
PeptideAtlas; Q9JMK2; -.
PRIDE; Q9JMK2; -.
Ensembl; ENSMUST00000117786; ENSMUSP00000113341; ENSMUSG00000022433.
Ensembl; ENSMUST00000120859; ENSMUSP00000113975; ENSMUSG00000022433.
GeneID; 27373; -.
KEGG; mmu:27373; -.
UCSC; uc007wtl.2; mouse.
CTD; 1454; -.
MGI; MGI:1351660; Csnk1e.
eggNOG; KOG1164; Eukaryota.
eggNOG; ENOG410XPGP; LUCA.
GeneTree; ENSGT00920000148982; -.
HOGENOM; HOG000182055; -.
HOVERGEN; HBG000176; -.
InParanoid; Q9JMK2; -.
KO; K08960; -.
OrthoDB; EOG091G0AFG; -.
PhylomeDB; Q9JMK2; -.
TreeFam; TF300544; -.
BRENDA; 2.7.11.1; 3474.
Reactome; R-MMU-201688; WNT mediated activation of DVL.
Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-MMU-8854518; AURKA Activation by TPX2.
PRO; PR:Q9JMK2; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022433; -.
CleanEx; MM_CSNK1E; -.
ExpressionAtlas; Q9JMK2; baseline and differential.
Genevisible; Q9JMK2; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030426; C:growth cone; ISO:MGI.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:MGI.
GO; GO:0034613; P:cellular protein localization; IDA:MGI.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
GO; GO:0048512; P:circadian behavior; ISO:MGI.
GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
GO; GO:0007623; P:circadian rhythm; TAS:MGI.
GO; GO:0006897; P:endocytosis; IBA:GO_Central.
GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IGI:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISO:MGI.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IGI:MGI.
GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; IGI:ParkinsonsUK-UCL.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IGI:ParkinsonsUK-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
GO; GO:1903827; P:regulation of cellular protein localization; IMP:ParkinsonsUK-UCL.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Biological rhythms; Complete proteome; Cytoplasm; Kinase;
Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Wnt signaling pathway.
CHAIN 1 416 Casein kinase I isoform epsilon.
/FTId=PRO_0000192838.
DOMAIN 9 277 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 15 23 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 128 128 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 38 38 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000250|UniProtKB:P49674}.
MOD_RES 354 354 Phosphoserine.
{ECO:0000250|UniProtKB:P49674}.
MOD_RES 362 362 Phosphothreonine.
{ECO:0000250|UniProtKB:P49674}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000250|UniProtKB:P49674}.
MOD_RES 382 382 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 389 389 Phosphoserine.
{ECO:0000250|UniProtKB:P49674}.
MOD_RES 405 405 Phosphoserine.
{ECO:0000250|UniProtKB:P49674}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000250|UniProtKB:P49674}.
MUTAGEN 38 38 K->A: Decreases PER1 phosphorylation.
{ECO:0000269|PubMed:10848614}.
MUTAGEN 38 38 K->R: Increases PER1 nuclear import.
{ECO:0000269|PubMed:10848614}.
MUTAGEN 178 178 R->C: Shortens circadian rhythm.
Accelerates PER2 degradation.
{ECO:0000269|PubMed:18400165}.
CONFLICT 28 28 N -> D (in Ref. 1; BAA88107).
{ECO:0000305}.
CONFLICT 310 310 E -> G (in Ref. 1; BAA88107).
{ECO:0000305}.
CONFLICT 379 379 R -> G (in Ref. 1; BAA88107).
{ECO:0000305}.
SEQUENCE 416 AA; 47322 MW; 38CC5299BB9040D7 CRC64;
MELRVGNKYR LGRKIGSGSF GDIYLGANIA SGEEVAIKLE CVKTKHPQLH IESKFYKMMQ
GGVGIPSIKW CGAEGDYNVM VMELLGPSLE DLFNFCSRKF SLKTVLLLAD QMISRIEYIH
SKNFIHRDVK PDNFLMGLGK KGNLVYIIDF GLAKKYRDAR THQHIPYREN KNLTGTARYA
SINTHLGIEQ SRRDDLESLG YVLMYFNLGS LPWQGLKAAT KRQKYERISE KKMSTPIEVL
CKGYPSEFST YLNFCRSLRF DDKPDYSYLR QLFRNLFHRQ GFSYDYVFDW NMLKFGAARN
PEDVDRERRE HEREERMGQL RGSATRALPP GPPTGATANR LRSAAEPVAS TPASRIQQTG
NTSPRAISRA DRERKVSMRL HRGAPANVSS SDLTGRQEVS RLAASQTSVP FDHLGK


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