ID KC1E_HUMAN Reviewed; 416 AA. AC P49674; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 226. DE RecName: Full=Casein kinase I isoform epsilon; DE Short=CKI-epsilon; DE Short=CKIe; DE EC=2.7.11.1 {ECO:0000269|PubMed:29222110}; GN Name=CSNK1E; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX PubMed=7797465; DOI=10.1074/jbc.270.25.14875; RA Fish K.J., Cegielska A., Getman M.E., Landes G.M., Virshup D.M.; RT "Isolation and characterization of human casein kinase I epsilon (CKI), a RT novel member of the CKI gene family."; RL J. Biol. Chem. 270:14875-14883(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Ono K., Murata-Hori M., Hosoya H.; RT "Casein kinase I epsilon from HeLa cell."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SOCS3, INDUCTION, AND RP FUNCTION. RC TISSUE=Hematopoietic stem cell; RX PubMed=15070676; DOI=10.1182/blood-2003-08-2768; RA Okamura A., Iwata N., Nagata A., Tamekane A., Shimoyama M., Gomyo H., RA Yakushijin K., Urahama N., Hamaguchi M., Fukui C., Chihara K., Ito M., RA Matsui T.; RT "Involvement of casein kinase Iepsilon in cytokine-induced granulocytic RT differentiation."; RL Blood 103:2997-3004(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP INTERACTION WITH PER1. RX PubMed=10790862; DOI=10.1097/00001756-200004070-00011; RA Keesler G.A., Camacho F., Guo Y., Virshup D., Mondadori C., Yao Z.; RT "Phosphorylation and destabilization of human period I clock protein by RT human casein kinase I epsilon."; RL NeuroReport 11:951-955(2000). RN [8] RP ROLE IN WNT SIGNALING. RX PubMed=12556519; DOI=10.1074/jbc.m213265200; RA Hino S., Michiue T., Asashima M., Kikuchi A.; RT "Casein kinase I epsilon enhances the binding of Dvl-1 to Frat-1 and is RT essential for Wnt-3a-induced accumulation of beta-catenin."; RL J. Biol. Chem. 278:14066-14073(2003). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [10] RP FUNCTION AS PER1 KINASE. RX PubMed=15917222; DOI=10.1074/jbc.m502862200; RA Shirogane T., Jin J., Ang X.L., Harper J.W.; RT "SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1- RT dependent degradation of the mammalian period-1 (Per1) protein."; RL J. Biol. Chem. 280:26863-26872(2005). RN [11] RP INTERACTION WITH DBNDD2. RX PubMed=16618118; DOI=10.1021/bi052354e; RA Yin H., Laguna K.A., Li G., Kuret J.; RT "Dysbindin structural homologue CK1BP is an isoform-selective binding RT partner of human casein kinase-1."; RL Biochemistry 45:5297-5308(2006). RN [12] RP INTERACTION WITH LRP5 AND LRP6. RX PubMed=16513652; DOI=10.1074/jbc.m510580200; RA Swiatek W., Kang H., Garcia B.A., Shabanowitz J., Coombs G.S., Hunt D.F., RA Virshup D.M.; RT "Negative regulation of LRP6 function by casein kinase I epsilon RT phosphorylation."; RL J. Biol. Chem. 281:12233-12241(2006). RN [13] RP FUNCTION, AUTOPHOSPHORYLATION, DEPHOSPHORYLATION BY PPP5C, AND ACTIVITY RP REGULATION. RX PubMed=16790549; DOI=10.1073/pnas.0604138103; RA Partch C.L., Shields K.F., Thompson C.L., Selby C.P., Sancar A.; RT "Posttranslational regulation of the mammalian circadian clock by RT cryptochrome and protein phosphatase 5."; RL Proc. Natl. Acad. Sci. U.S.A. 103:10467-10472(2006). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343; SER-354; THR-362 AND RP SER-363, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-354, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [19] RP INTERACTION WITH SNAI1. RX PubMed=20305697; DOI=10.1038/onc.2010.77; RA Xu Y., Lee S.H., Kim H.S., Kim N.H., Piao S., Park S.H., Jung Y.S., RA Yook J.I., Park B.J., Ha N.C.; RT "Role of CK1 in GSK3beta-mediated phosphorylation and degradation of RT snail."; RL Oncogene 29:3124-3133(2010). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389; SER-405 AND SER-408, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [23] RP FUNCTION, AND INTERACTION WITH DDX3X. RX PubMed=23413191; DOI=10.1126/science.1231499; RA Cruciat C.M., Dolde C., de Groot R.E., Ohkawara B., Reinhard C., RA Korswagen H.C., Niehrs C.; RT "RNA helicase DDX3 is a regulatory subunit of casein kinase 1 in Wnt-beta- RT catenin signaling."; RL Science 339:1436-1441(2013). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [25] RP INTERACTION WITH DDX3X, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-38. RX PubMed=29222110; DOI=10.1242/jcs.207316; RA Dolde C., Bischof J., Grueter S., Montada A., Halekotte J., Peifer C., RA Kalbacher H., Baumann U., Knippschild U., Suter B.; RT "A CK1 FRET biosensor reveals that DDX3X is an essential activator of RT CK1epsilon."; RL J. Cell Sci. 131:0-0(2018). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.74 ANGSTROMS) OF 1-294 ALONE AND IN COMPLEX WITH RP INHIBITOR, AND SUBUNIT. RX PubMed=23106386; DOI=10.1021/jm301336n; RA Long A.M., Zhao H., Huang X.; RT "Structural basis for the potent and selective inhibition of casein kinase RT 1 epsilon."; RL J. Med. Chem. 55:10307-10311(2012). RN [27] RP VARIANTS [LARGE SCALE ANALYSIS] LEU-256 AND ARG-413. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Casein kinases are operationally defined by their CC preferential utilization of acidic proteins such as caseins as CC substrates (Probable). Participates in Wnt signaling (PubMed:12556519, CC PubMed:23413191). Phosphorylates DVL1 (PubMed:12556519). Phosphorylates CC DVL2 (PubMed:23413191). Phosphorylates NEDD9/HEF1 (By similarity). CC Central component of the circadian clock (PubMed:16790549). In balance CC with PP1, determines the circadian period length, through the CC regulation of the speed and rhythmicity of PER1 and PER2 CC phosphorylation (PubMed:15917222, PubMed:16790549). Controls PER1 and CC PER2 nuclear transport and degradation (By similarity). Inhibits CC cytokine-induced granuloytic differentiation (PubMed:15070676). CC {ECO:0000250|UniProtKB:Q9JMK2, ECO:0000269|PubMed:12556519, CC ECO:0000269|PubMed:15070676, ECO:0000269|PubMed:15917222, CC ECO:0000269|PubMed:16790549, ECO:0000269|PubMed:23413191, CC ECO:0000305|PubMed:7797465}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:29222110}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; CC Evidence={ECO:0000269|PubMed:29222110}; CC -!- ACTIVITY REGULATION: Phosphorylation leads to a decrease of the CC catalytic activity. {ECO:0000269|PubMed:16790549}. CC -!- SUBUNIT: Monomer (PubMed:23106386). Component of the circadian core CC oscillator, which includes the CRY proteins, CLOCK, or NPAS2, CC ARTNL/BMAL1 or ARTNL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER CC proteins (By similarity). Interacts with PER1 (PubMed:10790862). CC Interacts with ANKRD6 (By similarity). Interacts with DBNDD2 CC (PubMed:16618118). Interacts with LRP5 and LRP6 (PubMed:16513652). CC Interacts with SOCS3 (PubMed:15070676). Interacts with SNAI1 (via zinc CC fingers) (PubMed:20305697). Interacts with DDX3X; this interaction CC greatly enhances CSNK1E affinity for ATP and DVL2 phosphorylation, but CC inhibits DDX3X ATPase/helicase activity. In the presence of RNA, the CC interaction is decreased (PubMed:23413191, PubMed:29222110). CC {ECO:0000250|UniProtKB:Q9JMK2, ECO:0000269|PubMed:10790862, CC ECO:0000269|PubMed:15070676, ECO:0000269|PubMed:16513652, CC ECO:0000269|PubMed:16618118, ECO:0000269|PubMed:20305697, CC ECO:0000269|PubMed:23106386, ECO:0000269|PubMed:23413191, CC ECO:0000269|PubMed:29222110}. CC -!- INTERACTION: CC P49674; P25054: APC; NbExp=8; IntAct=EBI-749343, EBI-727707; CC P49674; O15169: AXIN1; NbExp=5; IntAct=EBI-749343, EBI-710484; CC P49674; O14640: DVL1; NbExp=6; IntAct=EBI-749343, EBI-723489; CC P49674; O14641: DVL2; NbExp=4; IntAct=EBI-749343, EBI-740850; CC P49674; Q92997: DVL3; NbExp=9; IntAct=EBI-749343, EBI-739789; CC P49674; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-749343, EBI-1752811; CC P49674; Q1W6H9: FAM110C; NbExp=3; IntAct=EBI-749343, EBI-3942563; CC P49674; Q86UY5: FAM83A; NbExp=4; IntAct=EBI-749343, EBI-1384254; CC P49674; P08238: HSP90AB1; NbExp=2; IntAct=EBI-749343, EBI-352572; CC P49674; P23508: MCC; NbExp=4; IntAct=EBI-749343, EBI-307531; CC P49674; Q00987: MDM2; NbExp=3; IntAct=EBI-749343, EBI-389668; CC P49674; Q16625: OCLN; NbExp=8; IntAct=EBI-749343, EBI-2903088; CC P49674; O15055: PER2; NbExp=6; IntAct=EBI-749343, EBI-1054296; CC P49674; O75382: TRIM3; NbExp=3; IntAct=EBI-749343, EBI-2129889; CC P49674; P62258: YWHAE; NbExp=3; IntAct=EBI-749343, EBI-356498; CC P49674; Q04917: YWHAH; NbExp=3; IntAct=EBI-749343, EBI-306940; CC P49674; Q5T7W0: ZNF618; NbExp=5; IntAct=EBI-749343, EBI-6255994; CC P49674; O70239: Axin1; Xeno; NbExp=7; IntAct=EBI-749343, EBI-6857773; CC P49674; Q60838: Dvl2; Xeno; NbExp=3; IntAct=EBI-749343, EBI-641940; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined, including brain, CC heart, lung, liver, pancreas, kidney, placenta and skeletal muscle. CC Expressed in monocytes and lymphocytes but not in granulocytes. CC -!- INDUCTION: Down-regulated during granulocytic differentiation. CC {ECO:0000269|PubMed:15070676}. CC -!- PTM: Autophosphorylated. Partially dephosphorylated by PPP5C. May be CC dephosphorylated by PP1. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L37043; AAC41761.1; -; mRNA. DR EMBL; AB024597; BAA92345.1; -; mRNA. DR EMBL; AB091043; BAC10902.1; -; mRNA. DR EMBL; CR456429; CAG30315.1; -; mRNA. DR EMBL; AL020993; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC006490; AAH06490.1; -; mRNA. DR PIR; I61744; I61744. DR RefSeq; NP_001276841.1; NM_001289912.1. DR RefSeq; NP_001885.1; NM_001894.4. DR RefSeq; NP_689407.1; NM_152221.2. DR PDB; 4HNI; X-ray; 2.74 A; A/B=1-294. DR PDB; 4HOK; X-ray; 2.77 A; A/C/E/G/I/K/M/O/Q/S/U/W=1-294. DR PDBsum; 4HNI; -. DR PDBsum; 4HOK; -. DR AlphaFoldDB; P49674; -. DR SMR; P49674; -. DR BioGRID; 107838; 315. DR BioGRID; 3196631; 5. DR DIP; DIP-38050N; -. DR IntAct; P49674; 164. DR MINT; P49674; -. DR STRING; 9606.ENSP00000380044; -. DR BindingDB; P49674; -. DR ChEMBL; CHEMBL4937; -. DR DrugBank; DB06195; Seliciclib. DR DrugBank; DB14989; Umbralisib. DR DrugCentral; P49674; -. DR GuidetoPHARMACOLOGY; 1998; -. DR iPTMnet; P49674; -. DR PhosphoSitePlus; P49674; -. DR BioMuta; CSNK1E; -. DR DMDM; 1346369; -. DR CPTAC; CPTAC-3155; -. DR EPD; P49674; -. DR jPOST; P49674; -. DR MassIVE; P49674; -. DR PaxDb; 9606-ENSP00000380044; -. DR PeptideAtlas; P49674; -. DR ProteomicsDB; 56045; -. DR Pumba; P49674; -. DR Antibodypedia; 4043; 541 antibodies from 38 providers. DR DNASU; 1454; -. DR Ensembl; ENST00000359867.7; ENSP00000352929.3; ENSG00000213923.13. DR Ensembl; ENST00000396832.6; ENSP00000380044.1; ENSG00000213923.13. DR Ensembl; ENST00000403904.5; ENSP00000384074.1; ENSG00000213923.13. DR GeneID; 102800317; -. DR GeneID; 1454; -. DR KEGG; hsa:102800317; -. DR KEGG; hsa:1454; -. DR MANE-Select; ENST00000396832.6; ENSP00000380044.1; NM_152221.3; NP_689407.1. DR AGR; HGNC:2453; -. DR AGR; HGNC:53829; -. DR CTD; 102800317; -. DR CTD; 1454; -. DR DisGeNET; 102800317; -. DR DisGeNET; 1454; -. DR GeneCards; CSNK1E; -. DR HGNC; HGNC:2453; CSNK1E. DR HPA; ENSG00000213923; Low tissue specificity. DR MalaCards; CSNK1E; -. DR MIM; 600863; gene. DR neXtProt; NX_P49674; -. DR OpenTargets; ENSG00000213923; -. DR PharmGKB; PA26953; -. DR VEuPathDB; HostDB:ENSG00000213923; -. DR eggNOG; KOG1164; Eukaryota. DR GeneTree; ENSGT00940000153536; -. DR HOGENOM; CLU_019279_2_2_1; -. DR InParanoid; P49674; -. DR OMA; XISRIEY; -. DR OrthoDB; 1534388at2759; -. DR PhylomeDB; P49674; -. DR TreeFam; TF300544; -. DR BRENDA; 2.7.11.1; 2681. DR PathwayCommons; P49674; -. DR Reactome; R-HSA-201688; WNT mediated activation of DVL. DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition. DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes. DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes. DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome. DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes. DR Reactome; R-HSA-400253; Circadian Clock. DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane. DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR Reactome; R-HSA-8854518; AURKA Activation by TPX2. DR SABIO-RK; P49674; -. DR SignaLink; P49674; -. DR SIGNOR; P49674; -. DR BioGRID-ORCS; 102800317; 1 hit in 108 CRISPR screens. DR BioGRID-ORCS; 1454; 11 hits in 1186 CRISPR screens. DR ChiTaRS; CSNK1E; human. DR GeneWiki; CSNK1E; -. DR Pharos; P49674; Tclin. DR PRO; PR:P49674; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; P49674; Protein. DR Bgee; ENSG00000213923; Expressed in cortical plate and 199 other cell types or tissues. DR ExpressionAtlas; P49674; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0030426; C:growth cone; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004672; F:protein kinase activity; IDA:WormBase. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:WormBase. DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl. DR GO; GO:0048512; P:circadian behavior; IEA:Ensembl. DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB. DR GO; GO:0006281; P:DNA repair; TAS:ProtInc. DR GO; GO:0006897; P:endocytosis; IBA:GO_Central. DR GO; GO:0032091; P:negative regulation of protein binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IEA:Ensembl. DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; IEA:Ensembl. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central. DR GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; IC:ParkinsonsUK-UCL. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB. DR GO; GO:0008104; P:protein localization; IEA:Ensembl. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB. DR GO; GO:0032880; P:regulation of protein localization; IDA:ParkinsonsUK-UCL. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd14125; STKc_CK1_delta_epsilon; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR11909:SF428; CASEIN KINASE I ISOFORM EPSILON; 1. DR PANTHER; PTHR11909; CASEIN KINASE-RELATED; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; P49674; HS. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Biological rhythms; Cytoplasm; Kinase; KW Methylation; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..416 FT /note="Casein kinase I isoform epsilon" FT /id="PRO_0000192837" FT DOMAIN 9..277 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 301..416 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 301..320 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 387..407 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 128 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 15..23 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 38 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 343 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195" FT MOD_RES 354 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195" FT MOD_RES 362 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 363 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:21406692" FT MOD_RES 382 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9JMK2" FT MOD_RES 389 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 405 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 408 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VARIANT 256 FT /note="R -> L (in a lung adenocarcinoma sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042082" FT VARIANT 413 FT /note="H -> R (in dbSNP:rs35665927)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042083" FT MUTAGEN 38 FT /note="K->R: Loss of kinase activity." FT /evidence="ECO:0000269|PubMed:29222110" FT TURN 6..8 FT /evidence="ECO:0007829|PDB:4HNI" FT STRAND 14..16 FT /evidence="ECO:0007829|PDB:4HNI" FT STRAND 22..28 FT /evidence="ECO:0007829|PDB:4HNI" FT TURN 29..31 FT /evidence="ECO:0007829|PDB:4HNI" FT STRAND 35..41 FT /evidence="ECO:0007829|PDB:4HNI" FT HELIX 51..56 FT /evidence="ECO:0007829|PDB:4HNI" FT TURN 57..61 FT /evidence="ECO:0007829|PDB:4HNI" FT STRAND 68..74 FT /evidence="ECO:0007829|PDB:4HNI" FT STRAND 77..83 FT /evidence="ECO:0007829|PDB:4HNI" FT HELIX 89..95 FT /evidence="ECO:0007829|PDB:4HNI" FT TURN 96..98 FT /evidence="ECO:0007829|PDB:4HNI" FT HELIX 102..120 FT /evidence="ECO:0007829|PDB:4HNI" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:4HNI" FT HELIX 131..133 FT /evidence="ECO:0007829|PDB:4HNI" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:4HNI" FT HELIX 139..141 FT /evidence="ECO:0007829|PDB:4HNI" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:4HNI" FT STRAND 154..157 FT /evidence="ECO:0007829|PDB:4HNI" FT TURN 159..161 FT /evidence="ECO:0007829|PDB:4HNI" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:4HNI" FT HELIX 182..185 FT /evidence="ECO:0007829|PDB:4HNI" FT HELIX 192..208 FT /evidence="ECO:0007829|PDB:4HNI" FT TURN 212..215 FT /evidence="ECO:0007829|PDB:4HOK" FT HELIX 221..234 FT /evidence="ECO:0007829|PDB:4HNI" FT HELIX 237..240 FT /evidence="ECO:0007829|PDB:4HNI" FT TURN 241..243 FT /evidence="ECO:0007829|PDB:4HNI" FT HELIX 246..255 FT /evidence="ECO:0007829|PDB:4HNI" FT HELIX 266..280 FT /evidence="ECO:0007829|PDB:4HNI" FT HELIX 289..291 FT /evidence="ECO:0007829|PDB:4HNI" SQ 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 //