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

 KC1E_HUMAN              Reviewed;         416 AA.
P49674;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
18-JUL-2018, entry version 193.
RecName: Full=Casein kinase I isoform epsilon;
Short=CKI-epsilon;
Short=CKIe;
EC=2.7.11.1;
Name=CSNK1E;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=7797465; DOI=10.1074/jbc.270.25.14875;
Fish K.J., Cegielska A., Getman M.E., Landes G.M., Virshup D.M.;
"Isolation and characterization of human casein kinase I epsilon
(CKI), a novel member of the CKI gene family.";
J. Biol. Chem. 270:14875-14883(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Ono K., Murata-Hori M., Hosoya H.;
"Casein kinase I epsilon from HeLa cell.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SOCS3, INDUCTION, AND
FUNCTION.
TISSUE=Hematopoietic stem cell;
PubMed=15070676; DOI=10.1182/blood-2003-08-2768;
Okamura A., Iwata N., Nagata A., Tamekane A., Shimoyama M., Gomyo H.,
Yakushijin K., Urahama N., Hamaguchi M., Fukui C., Chihara K., Ito M.,
Matsui T.;
"Involvement of casein kinase Iepsilon in cytokine-induced
granulocytic differentiation.";
Blood 103:2997-3004(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[7]
INTERACTION WITH PER1.
PubMed=10790862; DOI=10.1097/00001756-200004070-00011;
Keesler G.A., Camacho F., Guo Y., Virshup D., Mondadori C., Yao Z.;
"Phosphorylation and destabilization of human period I clock protein
by human casein kinase I epsilon.";
NeuroReport 11:951-955(2000).
[8]
ROLE IN WNT SIGNALING.
PubMed=12556519; DOI=10.1074/jbc.M213265200;
Hino S., Michiue T., Asashima M., Kikuchi A.;
"Casein kinase I epsilon enhances the binding of Dvl-1 to Frat-1 and
is essential for Wnt-3a-induced accumulation of beta-catenin.";
J. Biol. Chem. 278:14066-14073(2003).
[9]
FUNCTION AS PER1 KINASE.
PubMed=15917222; DOI=10.1074/jbc.M502862200;
Shirogane T., Jin J., Ang X.L., Harper J.W.;
"SCFbeta-TRCP controls clock-dependent transcription via casein kinase
1-dependent degradation of the mammalian period-1 (Per1) protein.";
J. Biol. Chem. 280:26863-26872(2005).
[10]
INTERACTION WITH DBNDD2.
PubMed=16618118; DOI=10.1021/bi052354e;
Yin H., Laguna K.A., Li G., Kuret J.;
"Dysbindin structural homologue CK1BP is an isoform-selective binding
partner of human casein kinase-1.";
Biochemistry 45:5297-5308(2006).
[11]
INTERACTION WITH LRP5 AND LRP6.
PubMed=16513652; DOI=10.1074/jbc.M510580200;
Swiatek W., Kang H., Garcia B.A., Shabanowitz J., Coombs G.S.,
Hunt D.F., Virshup D.M.;
"Negative regulation of LRP6 function by casein kinase I epsilon
phosphorylation.";
J. Biol. Chem. 281:12233-12241(2006).
[12]
FUNCTION, AUTOPHOSPHORYLATION, DEPHOSPHORYLATION BY PPP5C, AND ENZYME
REGULATION.
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343; SER-354; THR-362
AND SER-363, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, 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).
[15]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-354, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, 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).
[18]
INTERACTION WITH SNAI1.
PubMed=20305697; DOI=10.1038/onc.2010.77;
Xu Y., Lee S.H., Kim H.S., Kim N.H., Piao S., Park S.H., Jung Y.S.,
Yook J.I., Park B.J., Ha N.C.;
"Role of CK1 in GSK3beta-mediated phosphorylation and degradation of
snail.";
Oncogene 29:3124-3133(2010).
[19]
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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, 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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389; SER-405 AND
SER-408, 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]
FUNCTION, AND INTERACTION WITH DDX3X.
PubMed=23413191; DOI=10.1126/science.1231499;
Cruciat C.M., Dolde C., de Groot R.E., Ohkawara B., Reinhard C.,
Korswagen H.C., Niehrs C.;
"RNA helicase DDX3 is a regulatory subunit of casein kinase 1 in Wnt-
beta-catenin signaling.";
Science 339:1436-1441(2013).
[23]
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).
[24]
X-RAY CRYSTALLOGRAPHY (2.74 ANGSTROMS) OF 1-294 ALONE AND IN COMPLEX
WITH INHIBITOR.
PubMed=23106386; DOI=10.1021/jm301336n;
Long A.M., Zhao H., Huang X.;
"Structural basis for the potent and selective inhibition of casein
kinase 1 epsilon.";
J. Med. Chem. 55:10307-10311(2012).
[25]
VARIANTS [LARGE SCALE ANALYSIS] LEU-256 AND ARG-413.
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: 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 and DVL2.
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:12556519, ECO:0000269|PubMed:15070676,
ECO:0000269|PubMed:15917222, ECO:0000269|PubMed:16790549,
ECO:0000269|PubMed:23413191}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Phosphorylation leads to a decrease of the
catalytic activity. {ECO:0000269|PubMed:16790549}.
-!- 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 (PubMed:23413191).
{ECO:0000269|PubMed:10790862, ECO:0000269|PubMed:15070676,
ECO:0000269|PubMed:16513652, ECO:0000269|PubMed:16618118,
ECO:0000269|PubMed:20305697, ECO:0000269|PubMed:23106386,
ECO:0000269|PubMed:23413191}.
-!- INTERACTION:
P25054:APC; NbExp=8; IntAct=EBI-749343, EBI-727707;
O15169:AXIN1; NbExp=5; IntAct=EBI-749343, EBI-710484;
O70239:Axin1 (xeno); NbExp=7; IntAct=EBI-749343, EBI-6857773;
O14640:DVL1; NbExp=6; IntAct=EBI-749343, EBI-723489;
Q60838:Dvl2 (xeno); NbExp=3; IntAct=EBI-749343, EBI-641940;
Q92997:DVL3; NbExp=8; IntAct=EBI-749343, EBI-739789;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-749343, EBI-352572;
P23508:MCC; NbExp=4; IntAct=EBI-749343, EBI-307531;
Q00987:MDM2; NbExp=3; IntAct=EBI-749343, EBI-389668;
Q16625:OCLN; NbExp=7; IntAct=EBI-749343, EBI-2903088;
O15055:PER2; NbExp=4; IntAct=EBI-749343, EBI-1054296;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- 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.
-!- INDUCTION: Down-regulated during granulocytic differentiation.
{ECO:0000269|PubMed:15070676}.
-!- PTM: Autophosphorylated. Partially dephosphorylated by PPP5C. May
be dephosphorylated by PP1.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
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EMBL; L37043; AAC41761.1; -; mRNA.
EMBL; AB024597; BAA92345.1; -; mRNA.
EMBL; AB091043; BAC10902.1; -; mRNA.
EMBL; CR456429; CAG30315.1; -; mRNA.
EMBL; AL020993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006490; AAH06490.1; -; mRNA.
CCDS; CCDS13970.1; -.
PIR; I61744; I61744.
RefSeq; NP_001276841.1; NM_001289912.1.
RefSeq; NP_001885.1; NM_001894.4.
RefSeq; NP_689407.1; NM_152221.2.
UniGene; Hs.474833; -.
UniGene; Hs.720223; -.
PDB; 4HNI; X-ray; 2.74 A; A/B=1-294.
PDB; 4HOK; X-ray; 2.77 A; A/C/E/G/I/K/M/O/Q/S/U/W=1-294.
PDBsum; 4HNI; -.
PDBsum; 4HOK; -.
ProteinModelPortal; P49674; -.
SMR; P49674; -.
BioGrid; 107838; 182.
DIP; DIP-38050N; -.
IntAct; P49674; 113.
MINT; P49674; -.
STRING; 9606.ENSP00000352929; -.
BindingDB; P49674; -.
ChEMBL; CHEMBL4937; -.
GuidetoPHARMACOLOGY; 1998; -.
iPTMnet; P49674; -.
PhosphoSitePlus; P49674; -.
BioMuta; CSNK1E; -.
DMDM; 1346369; -.
EPD; P49674; -.
PaxDb; P49674; -.
PeptideAtlas; P49674; -.
PRIDE; P49674; -.
ProteomicsDB; 56045; -.
DNASU; 1454; -.
Ensembl; ENST00000359867; ENSP00000352929; ENSG00000213923.
Ensembl; ENST00000396832; ENSP00000380044; ENSG00000213923.
Ensembl; ENST00000403904; ENSP00000384074; ENSG00000213923.
GeneID; 102800317; -.
GeneID; 1454; -.
KEGG; hsa:102800317; -.
KEGG; hsa:1454; -.
CTD; 102800317; -.
CTD; 1454; -.
DisGeNET; 102800317; -.
DisGeNET; 1454; -.
EuPathDB; HostDB:ENSG00000213923.10; -.
GeneCards; CSNK1E; -.
H-InvDB; HIX0080286; -.
HGNC; HGNC:2453; CSNK1E.
HPA; CAB009626; -.
HPA; HPA026288; -.
MIM; 600863; gene.
neXtProt; NX_P49674; -.
OpenTargets; ENSG00000213923; -.
PharmGKB; PA26953; -.
eggNOG; KOG1164; Eukaryota.
eggNOG; ENOG410XPGP; LUCA.
GeneTree; ENSGT00920000148982; -.
HOGENOM; HOG000182055; -.
HOVERGEN; HBG000176; -.
InParanoid; P49674; -.
KO; K08960; -.
OrthoDB; EOG091G0AFG; -.
PhylomeDB; P49674; -.
TreeFam; TF300544; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-201688; WNT mediated activation of DVL.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
SABIO-RK; P49674; -.
SignaLink; P49674; -.
SIGNOR; P49674; -.
ChiTaRS; CSNK1E; human.
GeneWiki; CSNK1E; -.
PRO; PR:P49674; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000213923; -.
CleanEx; HS_CSNK1E; -.
ExpressionAtlas; P49674; baseline and differential.
Genevisible; P49674; HS.
GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:WormBase.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0006281; P:DNA repair; TAS:ProtInc.
GO; GO:0006897; P:endocytosis; IBA:GO_Central.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0032091; P:negative regulation of protein binding; IDA:ParkinsonsUK-UCL.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; IC:ParkinsonsUK-UCL.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:1905426; P:positive regulation of Wnt-mediated midbrain dopaminergic neuron differentiation; NAS: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; IDA:ParkinsonsUK-UCL.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0016055; P:Wnt signaling pathway; IBA:GO_Central.
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;
3D-structure; ATP-binding; Biological rhythms; Complete proteome;
Cytoplasm; Kinase; Methylation; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 416 Casein kinase I isoform epsilon.
/FTId=PRO_0000192837.
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:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 354 354 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 362 362 Phosphothreonine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:21406692}.
MOD_RES 382 382 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9JMK2}.
MOD_RES 389 389 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 405 405 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 256 256 R -> L (in a lung adenocarcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042082.
VARIANT 413 413 H -> R (in dbSNP:rs35665927).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042083.
TURN 6 8 {ECO:0000244|PDB:4HNI}.
STRAND 14 16 {ECO:0000244|PDB:4HNI}.
STRAND 22 28 {ECO:0000244|PDB:4HNI}.
TURN 29 31 {ECO:0000244|PDB:4HNI}.
STRAND 35 41 {ECO:0000244|PDB:4HNI}.
HELIX 51 56 {ECO:0000244|PDB:4HNI}.
TURN 57 61 {ECO:0000244|PDB:4HNI}.
STRAND 68 74 {ECO:0000244|PDB:4HNI}.
STRAND 77 83 {ECO:0000244|PDB:4HNI}.
HELIX 89 95 {ECO:0000244|PDB:4HNI}.
TURN 96 98 {ECO:0000244|PDB:4HNI}.
HELIX 102 120 {ECO:0000244|PDB:4HNI}.
TURN 121 123 {ECO:0000244|PDB:4HNI}.
HELIX 131 133 {ECO:0000244|PDB:4HNI}.
STRAND 134 136 {ECO:0000244|PDB:4HNI}.
HELIX 139 141 {ECO:0000244|PDB:4HNI}.
STRAND 145 147 {ECO:0000244|PDB:4HNI}.
STRAND 154 157 {ECO:0000244|PDB:4HNI}.
TURN 159 161 {ECO:0000244|PDB:4HNI}.
HELIX 177 179 {ECO:0000244|PDB:4HNI}.
HELIX 182 185 {ECO:0000244|PDB:4HNI}.
HELIX 192 208 {ECO:0000244|PDB:4HNI}.
TURN 212 215 {ECO:0000244|PDB:4HOK}.
HELIX 221 234 {ECO:0000244|PDB:4HNI}.
HELIX 237 240 {ECO:0000244|PDB:4HNI}.
TURN 241 243 {ECO:0000244|PDB:4HNI}.
HELIX 246 255 {ECO:0000244|PDB:4HNI}.
HELIX 266 280 {ECO:0000244|PDB:4HNI}.
HELIX 289 291 {ECO:0000244|PDB:4HNI}.
SEQUENCE 416 AA; 47315 MW; EE1B1698AE914324 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 TPASRIQPAG
NTSPRAISRV DRERKVSMRL HRGAPANVSS SDLTGRQEVS RIPASQTSVP FDHLGK


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