ID KC1D_HUMAN Reviewed; 415 AA. AC P48730; A2I2P2; Q96KZ6; Q9BTN5; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 27-JAN-2003, sequence version 2. DT 27-MAR-2024, entry version 226. DE RecName: Full=Casein kinase I isoform delta; DE Short=CKI-delta; DE Short=CKId; DE EC=2.7.11.1 {ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:17562708, ECO:0000269|PubMed:20041275, ECO:0000269|PubMed:20637175, ECO:0000269|PubMed:21422228, ECO:0000269|PubMed:23636092}; DE AltName: Full=Tau-protein kinase CSNK1D; DE EC=2.7.11.26 {ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:16618118, ECO:0000269|PubMed:17562708}; GN Name=CSNK1D; Synonyms=HCKID; 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] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=8786104; DOI=10.1006/geno.1996.0091; RA Kusuda J., Hidari N., Hidari M., Hashimoto K.; RT "Sequence analysis of the cDNA for the human casein kinase I delta (CSNK1D) RT gene and its chromosomal localization."; RL Genomics 32:140-143(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Placenta, and Spleen; 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 [6] RP ACTIVITY REGULATION, AND AUTOPHOSPHORYLATION. RX PubMed=9632646; DOI=10.1074/jbc.273.26.15980; RA Rivers A., Gietzen K.F., Vielhaber E., Virshup D.M.; RT "Regulation of casein kinase I epsilon and casein kinase I delta by an in RT vivo futile phosphorylation cycle."; RL J. Biol. Chem. 273:15980-15984(1998). RN [7] RP FUNCTION AS TP53 KINASE, AND CATALYTIC ACTIVITY. RX PubMed=10606744; DOI=10.1016/s0014-5793(99)01647-6; RA Dumaz N., Milne D.M., Meek D.W.; RT "Protein kinase CK1 is a p53-threonine 18 kinase which requires prior RT phosphorylation of serine 15."; RL FEBS Lett. 463:312-316(1999). RN [8] RP INTERACTION WITH TUBULINS, AND SUBCELLULAR LOCATION. RX PubMed=10826492; DOI=10.1078/s0171-9335(04)70027-8; RA Behrend L., Stoeter M., Kurth M., Rutter G., Heukeshoven J., Deppert W., RA Knippschild U.; RT "Interaction of casein kinase 1 delta (CK1delta) with post-Golgi RT structures, microtubules and the spindle apparatus."; RL Eur. J. Cell Biol. 79:240-251(2000). RN [9] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-38 AND THR-176. RX PubMed=11161704; DOI=10.1006/excr.2000.5100; RA Milne D.M., Looby P., Meek D.W.; RT "Catalytic activity of protein kinase CK1 delta (casein kinase 1delta) is RT essential for its normal subcellular localization."; RL Exp. Cell Res. 263:43-54(2001). RN [10] RP INTERACTION WITH PER1 AND PER2. RX PubMed=11165242; DOI=10.1016/s0014-5793(00)02434-0; RA Camacho F., Cilio M., Guo Y., Virshup D.M., Patel K., Khorkova O., RA Styren S., Morse B., Yao Z., Keesler G.A.; RT "Human casein kinase Idelta phosphorylation of human circadian clock RT proteins period 1 and 2."; RL FEBS Lett. 489:159-165(2001). RN [11] RP FUNCTION AS CONNEXIN-43/GJA1 KINASE, INTERACTION WITH CONNEXIN-43/GJA1, AND RP CATALYTIC ACTIVITY. RX PubMed=12270943; DOI=10.1074/jbc.m209427200; RA Cooper C.D., Lampe P.D.; RT "Casein kinase 1 regulates connexin-43 gap junction assembly."; RL J. Biol. Chem. 277:44962-44968(2002). RN [12] RP INTERACTION WITH AKAP9/AKAP450, AND SUBCELLULAR LOCATION. RX PubMed=12270714; DOI=10.1016/s0022-2836(02)00857-4; RA Sillibourne J.E., Milne D.M., Takahashi M., Ono Y., Meek D.W.; RT "Centrosomal anchoring of the protein kinase CK1delta mediated by RT attachment to the large, coiled-coil scaffolding protein CG-NAP/AKAP450."; RL J. Mol. Biol. 322:785-797(2002). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. 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 [14] RP FUNCTION AS MAPT/TAU KINASE, ACTIVITY REGULATION, INTERACTION WITH RP MAPT/TAU, AND CATALYTIC ACTIVITY. RX PubMed=14761950; DOI=10.1074/jbc.m314116200; RA Li G., Yin H., Kuret J.; RT "Casein kinase 1 delta phosphorylates tau and disrupts its binding to RT microtubules."; RL J. Biol. Chem. 279:15938-15945(2004). RN [15] RP FUNCTION IN MITOTIC SPINDLE FORMATION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, DEVELOPMENTAL STAGE, AND ACTIVITY REGULATION. RX PubMed=16027726; DOI=10.1038/sj.onc.1208941; RA Stoeter M., Bamberger A.-M., Aslan B., Kurth M., Speidel D., Loening T., RA Frank H.-G., Kaufmann P., Loehler J., Henne-Bruns D., Deppert W., RA Knippschild U.; RT "Inhibition of casein kinase I delta alters mitotic spindle formation and RT induces apoptosis in trophoblast cells."; RL Oncogene 24:7964-7975(2005). RN [16] RP CATALYTIC ACTIVITY, AND 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 [17] RP FUNCTION AS PKD2 KINASE, AND CATALYTIC ACTIVITY. RX PubMed=17962809; DOI=10.1038/sj.emboj.7601891; RA von Blume J., Knippschild U., Dequiedt F., Giamas G., Beck A., Auer A., RA Van Lint J., Adler G., Seufferlein T.; RT "Phosphorylation at Ser244 by CK1 determines nuclear localization and RT substrate targeting of PKD2."; RL EMBO J. 26:4619-4633(2007). RN [18] RP FUNCTION AS MAPT/TAU KINASE, AND CATALYTIC ACTIVITY. RX PubMed=17562708; DOI=10.1074/jbc.m703269200; RA Hanger D.P., Byers H.L., Wray S., Leung K.-Y., Saxton M.J., Seereeram A., RA Reynolds C.H., Ward M.A., Anderton B.H.; RT "Novel phosphorylation sites in tau from Alzheimer brain support a role for RT casein kinase 1 in disease pathogenesis."; RL J. Biol. Chem. 282:23645-23654(2007). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [20] RP 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331 AND SER-384, AND RP IDENTIFICATION BY 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 [22] RP ACTIVITY REGULATION, AND CATALYTIC ACTIVITY. RX PubMed=19591487; DOI=10.1021/jm9005127; RA Peifer C., Abadleh M., Bischof J., Hauser D., Schattel V., Hirner H., RA Knippschild U., Laufer S.; RT "3,4-Diaryl-isoxazoles and -imidazoles as potent dual inhibitors of RT p38alpha mitogen activated protein kinase and casein kinase 1delta."; RL J. Med. Chem. 52:7618-7630(2009). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND IDENTIFICATION BY RP 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 [24] RP FUNCTION AS TOP2A KINASE, ACTIVITY REGULATION, AND CATALYTIC ACTIVITY. RX PubMed=19043076; DOI=10.1093/nar/gkn934; RA Grozav A.G., Chikamori K., Kozuki T., Grabowski D.R., Bukowski R.M., RA Willard B., Kinter M., Andersen A.H., Ganapathi R., Ganapathi M.K.; RT "Casein kinase I delta/epsilon phosphorylates topoisomerase IIalpha at RT serine-1106 and modulates DNA cleavage activity."; RL Nucleic Acids Res. 37:382-392(2009). RN [25] RP RETRACTED PAPER. RX PubMed=19339517; DOI=10.1093/nar/gkp136; RA Giamas G., Castellano L., Feng Q., Knippschild U., Jacob J., Thomas R.S., RA Coombes R.C., Smith C.L., Jiao L.R., Stebbing J.; RT "CK1delta modulates the transcriptional activity of ERalpha via AIB1 in an RT estrogen-dependent manner and regulates ERalpha-AIB1 interactions."; RL Nucleic Acids Res. 37:3110-3123(2009). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, 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 [27] RP FUNCTION AS DCK KINASE, AND CATALYTIC ACTIVITY. RX PubMed=20637175; DOI=10.1016/j.abb.2010.07.009; RA Smal C., Vertommen D., Amsailale R., Arts A., Degand H., Morsomme P., RA Rider M.H., Neste E.V., Bontemps F.; RT "Casein kinase 1delta activates human recombinant deoxycytidine kinase by RT Ser-74 phosphorylation, but is not involved in the in vivo regulation of RT its activity."; RL Arch. Biochem. Biophys. 502:44-52(2010). RN [28] RP FUNCTION AS P53/TP53 KINASE, GENE FAMILY, AND CATALYTIC ACTIVITY. RX PubMed=20041275; DOI=10.1007/s00018-009-0236-7; RA Venerando A., Marin O., Cozza G., Bustos V.H., Sarno S., Pinna L.A.; RT "Isoform specific phosphorylation of p53 by protein kinase CK1."; RL Cell. Mol. Life Sci. 67:1105-1118(2010). RN [29] RP FUNCTION AS YAP1 KINASE, AND CATALYTIC ACTIVITY. RX PubMed=20048001; DOI=10.1101/gad.1843810; RA Zhao B., Li L., Tumaneng K., Wang C.-Y., Guan K.-L.; RT "A coordinated phosphorylation by Lats and CK1 regulates YAP stability RT through SCF(beta-TRCP)."; RL Genes Dev. 24:72-85(2010). RN [30] RP FUNCTION AS HIF1A KINASE, AND CATALYTIC ACTIVITY. RX PubMed=20699359; DOI=10.1242/jcs.068122; RA Kalousi A., Mylonis I., Politou A.S., Chachami G., Paraskeva E., Simos G.; RT "Casein kinase 1 regulates human hypoxia-inducible factor HIF-1."; RL J. Cell Sci. 123:2976-2986(2010). RN [31] RP FUNCTION IN CIRCADIAN RHYTHMS, AND ACTIVITY REGULATION. RX PubMed=20696890; DOI=10.1073/pnas.1005101107; RA Meng Q.-J., Maywood E.S., Bechtold D.A., Lu W.-Q., Li J., Gibbs J.E., RA Dupre S.M., Chesham J.E., Rajamohan F., Knafels J., Sneed B., RA Zawadzke L.E., Ohren J.F., Walton K.M., Wager T.T., Hastings M.H., RA Loudon A.S.I.; RT "Entrainment of disrupted circadian behavior through inhibition of casein RT kinase 1 (CK1) enzymes."; RL Proc. Natl. Acad. Sci. U.S.A. 107:15240-15245(2010). RN [32] RP FUNCTION IN CIRCADIAN RHYTHMS, AND ACTIVITY REGULATION. RX PubMed=20407760; DOI=10.1007/s00213-010-1860-5; RA Sprouse J., Reynolds L., Kleiman R., Tate B., Swanson T.A., Pickard G.E.; RT "Chronic treatment with a selective inhibitor of casein kinase I RT delta/epsilon yields cumulative phase delays in circadian rhythms."; RL Psychopharmacology 210:569-576(2010). RN [33] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [34] 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 [35] RP FUNCTION AS EIF6 KINASE, ACTIVITY REGULATION, AND CATALYTIC ACTIVITY. RX PubMed=21084295; DOI=10.1074/jbc.m110.188565; RA Biswas A., Mukherjee S., Das S., Shields D., Chow C.W., Maitra U.; RT "Opposing action of casein kinase 1 and calcineurin in nucleo-cytoplasmic RT shuttling of mammalian translation initiation factor eIF6."; RL J. Biol. Chem. 286:3129-3138(2011). RN [36] RP FUNCTION AS DVL2 AND DVL3 KINASE, ACTIVITY REGULATION, SUBCELLULAR RP LOCATION, AND CATALYTIC ACTIVITY. RX PubMed=21422228; DOI=10.1083/jcb.201011111; RA Greer Y.E., Rubin J.S.; RT "Casein kinase 1 delta functions at the centrosome to mediate Wnt-3a- RT dependent neurite outgrowth."; RL J. Cell Biol. 192:993-1004(2011). RN [37] RP ACTIVITY REGULATION, AND AUTOPHOSPHORYLATION. RX PubMed=21258417; DOI=10.1038/onc.2010.627; RA Cheong J.K., Nguyen T.H., Wang H., Tan P., Voorhoeve P.M., Lee S.H., RA Virshup D.M.; RT "IC261 induces cell cycle arrest and apoptosis of human cancer cells via RT CK1delta/epsilon and Wnt/beta-catenin independent inhibition of mitotic RT spindle formation."; RL Oncogene 30:2558-2569(2011). RN [38] RP REVIEW ON CIRCADIAN RHYTHMS, AND GENE FAMILY. RX PubMed=21145983; DOI=10.1016/j.biocel.2010.12.004; RA Cheong J.K., Virshup D.M.; RT "Casein kinase 1: Complexity in the family."; RL Int. J. Biochem. Cell Biol. 43:465-469(2011). RN [39] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; SER-331; SER-382; RP SER-384 AND SER-407, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [40] 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 [41] RP INTERACTION WITH DDX3X. 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 [42] RP RETRACTION NOTICE OF PUBMED:19339517. RX PubMed=34718754; DOI=10.1093/nar/gkab845; RA Giamas G., Castellano L., Feng Q., Knippschild U., Jacob J., Thomas R.S., RA Coombes R.C., Smith C.L., Jiao L.R., Stebbing J.; RT "Retraction of 'CK1delta modulates the transcriptional activity of ERalpha RT via AIB1 in an estrogen-dependent manner and regulates ERalpha-AIB1 RT interactions'."; RL Nucleic Acids Res. 49:12006-12006(2021). RN [43] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=9761932; DOI=10.1107/s0907444997011724; RA Longenecker K.L., Roach P.J., Hurley T.D.; RT "Crystallographic studies of casein kinase I delta toward a structural RT understanding of auto-inhibition."; RL Acta Crystallogr. D 54:473-475(1998). RN [44] RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 1-294 IN COMPLEX WITH INHIBITOR, RP AND SUBUNIT. RX PubMed=22168824; DOI=10.1021/jm201387s; RA Long A., Zhao H., Huang X.; RT "Structural basis for the interaction between casein kinase 1 delta and a RT potent and selective inhibitor."; RL J. Med. Chem. 55:956-960(2012). RN [45] RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 1-294 IN COMPLEX WITH INHIBITOR, RP 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 [46] RP VARIANT FASPS2 ALA-44. RX PubMed=15800623; DOI=10.1038/nature03453; RA Xu Y., Padiath Q.S., Shapiro R.E., Jones C.R., Wu S.C., Saigoh N., RA Saigoh K., Ptacek L.J., Fu Y.H.; RT "Functional consequences of a CKIdelta mutation causing familial advanced RT sleep phase syndrome."; RL Nature 434:640-644(2005). RN [47] RP VARIANT [LARGE SCALE ANALYSIS] CYS-97. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [48] RP VARIANTS [LARGE SCALE ANALYSIS] CYS-97 AND ALA-401. 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). RN [49] RP VARIANTS FASPS2 ALA-44 AND ARG-46, CHARACTERIZATION OF VARIANTS FASPS2 RP ALA-44 AND ARG-46, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=23636092; DOI=10.1126/scitranslmed.3005784; RA Brennan K.C., Bates E.A., Shapiro R.E., Zyuzin J., Hallows W.C., Huang Y., RA Lee H.Y., Jones C.R., Fu Y.H., Charles A.C., Ptacek L.J.; RT "Casein kinase idelta mutations in familial migraine and advanced phase."; RL Sci. Transl. Med. 5:183ra56-183ra56(2013). CC -!- FUNCTION: Essential serine/threonine-protein kinase that regulates CC diverse cellular growth and survival processes including Wnt signaling, CC DNA repair and circadian rhythms. It can phosphorylate a large number CC of proteins. Casein kinases are operationally defined by their CC preferential utilization of acidic proteins such as caseins as CC substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, CC TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, CC PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In CC balance with PP1, determines the circadian period length through the CC regulation of the speed and rhythmicity of PER1 and PER2 CC phosphorylation. Controls PER1 and PER2 nuclear transport and CC degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 CC ubiquitin ligase-mediated ubiquitination and subsequent degradation. CC DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation CC of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. CC Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that CC controls neurite outgrowth. Phosphorylates NEDD9/HEF1 (By similarity). CC EIF6 phosphorylation promotes its nuclear export. Triggers down- CC regulation of dopamine receptors in the forebrain. Activates DCK in CC vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable CC complex formation. May regulate the formation of the mitotic spindle CC apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap CC junction assembly by phosphorylation. Probably involved in lymphocyte CC physiology. Regulates fast synaptic transmission mediated by glutamate. CC {ECO:0000250|UniProtKB:Q9DC28, ECO:0000269|PubMed:10606744, CC ECO:0000269|PubMed:12270943, ECO:0000269|PubMed:14761950, CC ECO:0000269|PubMed:16027726, ECO:0000269|PubMed:17562708, CC ECO:0000269|PubMed:17962809, ECO:0000269|PubMed:19043076, CC ECO:0000269|PubMed:20041275, ECO:0000269|PubMed:20048001, CC ECO:0000269|PubMed:20407760, ECO:0000269|PubMed:20637175, CC ECO:0000269|PubMed:20696890, ECO:0000269|PubMed:20699359, CC ECO:0000269|PubMed:21084295, ECO:0000269|PubMed:21422228, CC ECO:0000269|PubMed:23636092}. 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 Evidence={ECO:0000269|PubMed:12270943, ECO:0000269|PubMed:14761950, CC ECO:0000269|PubMed:16618118, ECO:0000269|PubMed:17562708, CC ECO:0000269|PubMed:17962809, ECO:0000269|PubMed:19043076, CC ECO:0000269|PubMed:19591487, ECO:0000269|PubMed:20041275, CC ECO:0000269|PubMed:20048001, ECO:0000269|PubMed:20637175, CC ECO:0000269|PubMed:20699359, ECO:0000269|PubMed:21084295, CC ECO:0000269|PubMed:21422228, ECO:0000269|PubMed:23636092}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; CC Evidence={ECO:0000305|PubMed:20637175}; 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:10606744, CC ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:17562708, CC ECO:0000269|PubMed:19591487, ECO:0000269|PubMed:20041275, CC ECO:0000269|PubMed:20637175, ECO:0000269|PubMed:21422228, CC ECO:0000269|PubMed:23636092}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; CC Evidence={ECO:0000305|PubMed:20637175}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl- CC [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA- CC COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26; CC Evidence={ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:16618118, CC ECO:0000269|PubMed:17562708}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12802; CC Evidence={ECO:0000305|PubMed:14761950}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L- CC threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703, CC Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.26; Evidence={ECO:0000269|PubMed:14761950, CC ECO:0000269|PubMed:16618118, ECO:0000269|PubMed:17562708}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53905; CC Evidence={ECO:0000305|PubMed:14761950}; CC -!- ACTIVITY REGULATION: Exhibits substrate-dependent heparin activation. CC Drug-mediated inhibition leads to a delay of the oscillations with the CC magnitude of this effect dependent upon the timing of drug CC administration. Inhibited by phosphorylation. Repressed by 3-[(2,4,6- CC trimethoxyphenyl)methylidenyl]-indolin-2-one (IC261), N-(2-aminoethyl)- CC 5-chloroisoquinoline-8-sulfonamide (CKI-7), 4-[4-(2,3-dihydro- CC benzo[1,4]dioxin-6-yl)-5-pyridin-2-yl-1H-imidazol-2-yl]benzamide CC (D4476), 3,4-diaryl-isoxazoles and -imidazoles, and 4-(3-cyclohexyl-5- CC (4-fluoro-phenyl)-3H-imidazol-4-yl) pyrimidin-2-ylamine (PF670462, CC PF670). {ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:16027726, CC ECO:0000269|PubMed:19043076, ECO:0000269|PubMed:19591487, CC ECO:0000269|PubMed:20407760, ECO:0000269|PubMed:20696890, CC ECO:0000269|PubMed:21084295, ECO:0000269|PubMed:21258417, CC ECO:0000269|PubMed:21422228, ECO:0000269|PubMed:9632646}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=36.5 uM for alpha-casein {ECO:0000269|PubMed:23636092}; CC KM=635.8 uM for PER2 peptide {ECO:0000269|PubMed:23636092}; CC KM=180.6 uM for ATP {ECO:0000269|PubMed:23636092}; CC Note=Maximal velocity nearly identical for the reactions with CC alpha-casein and PER2 peptide.; CC -!- SUBUNIT: Monomer (PubMed:22168824, PubMed:23106386). Component of the CC circadian core oscillator, which includes the CRY proteins, CLOCK, or CC NPAS2, ARTNL/BMAL1 or ARTNL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and CC the PER proteins (By similarity). Interacts with DNMT1 and MAP1A (By CC similarity). Interacts directly with PER1 and PER2 which may lead to CC their degradation (PubMed:11165242). Interacts with MAPT/TAU CC (PubMed:14761950). Interacts with SNAPIN (By similarity). Interacts CC with DBNDD2 (PubMed:16618118). Interacts with AKAP9/AKAP450; this CC interaction promotes centrosomal subcellular location CC (PubMed:12270714). Binds to tubulins in mitotic cells upon DNA damage CC (PubMed:10826492). Interacts with GJA1 (PubMed:12270943). Interacts CC with DDX3X; this interaction enhances CSNK1D kinase activity in vitro, CC but it is unclear whether this interaction is physiologically relevant CC (PubMed:29222110). {ECO:0000250|UniProtKB:Q06486, CC ECO:0000250|UniProtKB:Q9DC28, ECO:0000269|PubMed:10826492, CC ECO:0000269|PubMed:11165242, ECO:0000269|PubMed:12270714, CC ECO:0000269|PubMed:12270943, ECO:0000269|PubMed:14761950, CC ECO:0000269|PubMed:16618118, ECO:0000269|PubMed:22168824, CC ECO:0000269|PubMed:23106386, ECO:0000269|PubMed:29222110}. CC -!- INTERACTION: CC P48730; P05067: APP; NbExp=3; IntAct=EBI-751621, EBI-77613; CC P48730; Q49A88-3: CCDC14; NbExp=3; IntAct=EBI-751621, EBI-12105646; CC P48730; Q6PGQ1: DRICH1; NbExp=3; IntAct=EBI-751621, EBI-10253641; CC P48730; Q92997: DVL3; NbExp=4; IntAct=EBI-751621, EBI-739789; CC P48730; O60447: EVI5; NbExp=3; IntAct=EBI-751621, EBI-852291; CC P48730; Q9H2S9: IKZF4; NbExp=3; IntAct=EBI-751621, EBI-1640423; CC P48730; Q96LR2: LURAP1; NbExp=4; IntAct=EBI-751621, EBI-741355; CC P48730; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-751621, EBI-741037; CC P48730; Q00987: MDM2; NbExp=6; IntAct=EBI-751621, EBI-389668; CC P48730; Q9P286: PAK5; NbExp=3; IntAct=EBI-751621, EBI-741896; CC P48730; O15055: PER2; NbExp=4; IntAct=EBI-751621, EBI-1054296; CC P48730; O75382: TRIM3; NbExp=3; IntAct=EBI-751621, EBI-2129889; CC P48730; Q9C026: TRIM9; NbExp=3; IntAct=EBI-751621, EBI-720828; CC P48730; P62258: YWHAE; NbExp=2; IntAct=EBI-751621, EBI-356498; CC P48730; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-751621, EBI-742740; CC P48730; Q5T7W0: ZNF618; NbExp=3; IntAct=EBI-751621, EBI-6255994; CC P48730; Q60838: Dvl2; Xeno; NbExp=2; IntAct=EBI-751621, EBI-641940; CC P48730-2; P05067: APP; NbExp=3; IntAct=EBI-9087876, EBI-77613; CC P48730-2; Q92624: APPBP2; NbExp=3; IntAct=EBI-9087876, EBI-743771; CC P48730-2; Q96GW7: BCAN; NbExp=3; IntAct=EBI-9087876, EBI-2690445; CC P48730-2; Q8IU99: CALHM1; NbExp=3; IntAct=EBI-9087876, EBI-1790341; CC P48730-2; Q03135: CAV1; NbExp=3; IntAct=EBI-9087876, EBI-603614; CC P48730-2; P45973: CBX5; NbExp=3; IntAct=EBI-9087876, EBI-78219; CC P48730-2; P06850: CRH; NbExp=3; IntAct=EBI-9087876, EBI-3870390; CC P48730-2; Q01658: DR1; NbExp=3; IntAct=EBI-9087876, EBI-750300; CC P48730-2; Q9BS26: ERP44; NbExp=3; IntAct=EBI-9087876, EBI-541644; CC P48730-2; P35637: FUS; NbExp=3; IntAct=EBI-9087876, EBI-400434; CC P48730-2; P17302: GJA1; NbExp=3; IntAct=EBI-9087876, EBI-1103439; CC P48730-2; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-9087876, EBI-739467; CC P48730-2; P25098: GRK2; NbExp=3; IntAct=EBI-9087876, EBI-3904795; CC P48730-2; Q00403: GTF2B; NbExp=3; IntAct=EBI-9087876, EBI-389564; CC P48730-2; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-9087876, EBI-1054873; CC P48730-2; P42858: HTT; NbExp=15; IntAct=EBI-9087876, EBI-466029; CC P48730-2; Q14114-3: LRP8; NbExp=3; IntAct=EBI-9087876, EBI-25832196; CC P48730-2; Q5S007: LRRK2; NbExp=3; IntAct=EBI-9087876, EBI-5323863; CC P48730-2; Q16539: MAPK14; NbExp=3; IntAct=EBI-9087876, EBI-73946; CC P48730-2; Q96L34: MARK4; NbExp=3; IntAct=EBI-9087876, EBI-302319; CC P48730-2; P35240-4: NF2; NbExp=3; IntAct=EBI-9087876, EBI-1014514; CC P48730-2; Q6ZW49: PAXIP1; NbExp=3; IntAct=EBI-9087876, EBI-743225; CC P48730-2; O14494: PLPP1; NbExp=3; IntAct=EBI-9087876, EBI-2865290; CC P48730-2; D3DTS7: PMP22; NbExp=3; IntAct=EBI-9087876, EBI-25882629; CC P48730-2; P17612: PRKACA; NbExp=3; IntAct=EBI-9087876, EBI-476586; CC P48730-2; P07602: PSAP; NbExp=3; IntAct=EBI-9087876, EBI-716699; CC P48730-2; P54725: RAD23A; NbExp=3; IntAct=EBI-9087876, EBI-746453; CC P48730-2; P04271: S100B; NbExp=3; IntAct=EBI-9087876, EBI-458391; CC P48730-2; Q8WTV0: SCARB1; NbExp=3; IntAct=EBI-9087876, EBI-78657; CC P48730-2; P50454: SERPINH1; NbExp=3; IntAct=EBI-9087876, EBI-350723; CC P48730-2; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-9087876, EBI-11522811; CC P48730-2; P84022: SMAD3; NbExp=3; IntAct=EBI-9087876, EBI-347161; CC P48730-2; P37840: SNCA; NbExp=3; IntAct=EBI-9087876, EBI-985879; CC P48730-2; P00441: SOD1; NbExp=3; IntAct=EBI-9087876, EBI-990792; CC P48730-2; Q6NUL7: SPTLC1; NbExp=3; IntAct=EBI-9087876, EBI-25912847; CC P48730-2; Q13148: TARDBP; NbExp=6; IntAct=EBI-9087876, EBI-372899; CC P48730-2; P37173: TGFBR2; NbExp=3; IntAct=EBI-9087876, EBI-296151; CC P48730-2; Q9NRS4: TMPRSS4; NbExp=3; IntAct=EBI-9087876, EBI-10313040; CC P48730-2; Q9BVJ6: UTP14A; NbExp=3; IntAct=EBI-9087876, EBI-473284; CC P48730-2; Q9UBQ0-2: VPS29; NbExp=3; IntAct=EBI-9087876, EBI-11141397; CC P48730-2; Q8IUH5: ZDHHC17; NbExp=3; IntAct=EBI-9087876, EBI-524753; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome CC {ECO:0000269|PubMed:14654843}. Cytoplasm, perinuclear region. Cell CC membrane. Cytoplasm, cytoskeleton, spindle. Golgi apparatus. CC Note=Localized at mitotic spindle microtubules, and at the centrosomes CC and interphase in interphase cells. Recruited to the spindle apparatus CC and the centrosomes in response to DNA-damage. Correct subcellular CC localization requires kinase activity. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P48730-1; Sequence=Displayed; CC Name=2; CC IsoId=P48730-2; Sequence=VSP_010253; CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined, including brain, CC heart, lung, liver, pancreas, kidney, placenta and skeletal muscle. CC However, kinase activity is not uniform, with highest kinase activity CC in splenocytes. In blood, highly expressed in hemopoietic cells and CC mature granulocytes. Also found in monocytes and lymphocytes. CC {ECO:0000269|PubMed:15070676, ECO:0000269|PubMed:16027726}. CC -!- DEVELOPMENTAL STAGE: Highly present in extravillous trophoblast cells, CC which are present at the placenta implantation site and invade the CC decidua and decidual vessels. {ECO:0000269|PubMed:16027726}. CC -!- PTM: Autophosphorylated on serine and threonine residues; this CC autophosphorylation represses activity. Reactivated by phosphatase- CC mediated dephosphorylation. May be dephosphorylated by PP1. CC -!- DISEASE: Advanced sleep phase syndrome, familial, 2 (FASPS2) CC [MIM:615224]: An autosomal dominant disorder characterized by very CC early sleep onset and offset. Individuals are 'morning larks' with a 4 CC hours advance of the sleep, temperature and melatonin rhythms. CC {ECO:0000269|PubMed:15800623, ECO:0000269|PubMed:23636092}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: May be involved in Alzheimer disease by phosphorylating CC MAPT/TAU. {ECO:0000305|PubMed:17562708}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}. CC -!- CAUTION: Was shown to phosphorylate and activate DCK in vitro but CC probably not in vivo. {ECO:0000305|PubMed:20637175}. 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; U29171; AAC50807.1; -; mRNA. DR EMBL; U31285; AAC50808.1; -; mRNA. DR EMBL; AB091044; BAC10903.1; -; mRNA. DR EMBL; AK291758; BAF84447.1; -; mRNA. DR EMBL; EF015900; ABM64211.1; -; Genomic_DNA. DR EMBL; BC003558; AAH03558.1; -; mRNA. DR EMBL; BC015775; AAH15775.1; -; mRNA. DR CCDS; CCDS11805.1; -. [P48730-1] DR CCDS; CCDS11806.1; -. [P48730-2] DR PIR; G01876; G01876. DR RefSeq; NP_001884.2; NM_001893.4. [P48730-1] DR RefSeq; NP_620693.1; NM_139062.2. [P48730-2] DR PDB; 3UYS; X-ray; 2.30 A; A/B/C/D=1-294. DR PDB; 3UYT; X-ray; 2.00 A; A/B/C/D=1-294. DR PDB; 3UZP; X-ray; 1.94 A; A/B=1-294. DR PDB; 4HGT; X-ray; 1.80 A; A/B=1-294. DR PDB; 4HNF; X-ray; 2.07 A; A/B=1-294. DR PDB; 4KB8; X-ray; 1.95 A; A/B/C/D=3-317. DR PDB; 4KBA; X-ray; 1.98 A; A/B/C/D=3-317. DR PDB; 4KBC; X-ray; 1.98 A; A/B=1-317. DR PDB; 4KBK; X-ray; 2.10 A; A/B/C/D=3-317. DR PDB; 4TN6; X-ray; 2.41 A; A/B=1-301. DR PDB; 4TW9; X-ray; 2.40 A; A/B=1-295. DR PDB; 4TWC; X-ray; 1.70 A; A/B=1-295. DR PDB; 5IH4; X-ray; 1.90 A; A=1-294. DR PDB; 5IH5; X-ray; 2.25 A; A=1-294. DR PDB; 5IH6; X-ray; 2.30 A; A=1-294. DR PDB; 5MQV; X-ray; 2.15 A; A/B/C/D/E/F=1-294. DR PDB; 5OKT; X-ray; 2.13 A; A/B/C/D=1-294. DR PDB; 5W4W; X-ray; 1.99 A; A/B/C/D=3-317. DR PDB; 6F1W; X-ray; 1.86 A; A/B=1-294. DR PDB; 6F26; X-ray; 1.83 A; A/B=1-294. DR PDB; 6GZM; X-ray; 1.59 A; A/B=1-295. DR PDB; 6HMP; X-ray; 2.04 A; A/B=1-294. DR PDB; 6HMR; X-ray; 1.78 A; A/B=1-294. DR PDB; 6PXN; X-ray; 1.55 A; A/B=1-415. DR PDB; 6PXO; X-ray; 2.00 A; A/B=1-294. DR PDB; 6PXP; X-ray; 2.35 A; A/B=1-294. DR PDB; 6RCG; X-ray; 1.40 A; A=1-294. DR PDB; 6RCH; X-ray; 1.45 A; A/B=1-294. DR PDB; 6RU6; X-ray; 2.05 A; A/B=1-294. DR PDB; 6RU7; X-ray; 2.08 A; A/B=1-294. DR PDB; 6RU8; X-ray; 1.92 A; A/B/C/D=1-294. DR PDB; 7NZY; X-ray; 1.85 A; A/B/C/D=1-294. DR PDB; 7P7F; X-ray; 1.96 A; A/B/C/D=1-294. DR PDB; 7P7G; X-ray; 1.70 A; A/B=1-294. DR PDB; 7P7H; X-ray; 2.40 A; A/B=1-294. DR PDB; 7QR9; X-ray; 2.30 A; A/B/C/D=1-294. DR PDB; 7QRA; X-ray; 2.40 A; A/B/C/D=1-294. DR PDB; 7QRB; X-ray; 2.60 A; A/B/C/D=1-294. DR PDB; 8D7M; X-ray; 2.25 A; A/B=1-294. DR PDB; 8D7N; X-ray; 1.66 A; A/B=1-294. DR PDB; 8D7O; X-ray; 1.65 A; A/B=1-294. DR PDB; 8D7P; X-ray; 2.25 A; A/B=1-294. DR PDBsum; 3UYS; -. DR PDBsum; 3UYT; -. DR PDBsum; 3UZP; -. DR PDBsum; 4HGT; -. DR PDBsum; 4HNF; -. DR PDBsum; 4KB8; -. DR PDBsum; 4KBA; -. DR PDBsum; 4KBC; -. DR PDBsum; 4KBK; -. DR PDBsum; 4TN6; -. DR PDBsum; 4TW9; -. DR PDBsum; 4TWC; -. DR PDBsum; 5IH4; -. DR PDBsum; 5IH5; -. DR PDBsum; 5IH6; -. DR PDBsum; 5MQV; -. DR PDBsum; 5OKT; -. DR PDBsum; 5W4W; -. DR PDBsum; 6F1W; -. DR PDBsum; 6F26; -. DR PDBsum; 6GZM; -. DR PDBsum; 6HMP; -. DR PDBsum; 6HMR; -. DR PDBsum; 6PXN; -. DR PDBsum; 6PXO; -. DR PDBsum; 6PXP; -. DR PDBsum; 6RCG; -. DR PDBsum; 6RCH; -. DR PDBsum; 6RU6; -. DR PDBsum; 6RU7; -. DR PDBsum; 6RU8; -. DR PDBsum; 7NZY; -. DR PDBsum; 7P7F; -. DR PDBsum; 7P7G; -. DR PDBsum; 7P7H; -. DR PDBsum; 7QR9; -. DR PDBsum; 7QRA; -. DR PDBsum; 7QRB; -. DR PDBsum; 8D7M; -. DR PDBsum; 8D7N; -. DR PDBsum; 8D7O; -. DR PDBsum; 8D7P; -. DR AlphaFoldDB; P48730; -. DR SMR; P48730; -. DR BioGRID; 107837; 260. DR DIP; DIP-39735N; -. DR IntAct; P48730; 164. DR MINT; P48730; -. DR STRING; 9606.ENSP00000381531; -. DR BindingDB; P48730; -. DR ChEMBL; CHEMBL2828; -. DR DrugCentral; P48730; -. DR GuidetoPHARMACOLOGY; 1997; -. DR iPTMnet; P48730; -. DR PhosphoSitePlus; P48730; -. DR BioMuta; CSNK1D; -. DR DMDM; 27923980; -. DR CPTAC; CPTAC-3148; -. DR CPTAC; CPTAC-3149; -. DR EPD; P48730; -. DR jPOST; P48730; -. DR MassIVE; P48730; -. DR MaxQB; P48730; -. DR PaxDb; 9606-ENSP00000324464; -. DR PeptideAtlas; P48730; -. DR ProteomicsDB; 55930; -. [P48730-1] DR ProteomicsDB; 55931; -. [P48730-2] DR Pumba; P48730; -. DR TopDownProteomics; P48730-1; -. [P48730-1] DR Antibodypedia; 4210; 410 antibodies from 40 providers. DR DNASU; 1453; -. DR Ensembl; ENST00000314028.11; ENSP00000324464.6; ENSG00000141551.15. [P48730-1] DR Ensembl; ENST00000392334.7; ENSP00000376146.2; ENSG00000141551.15. [P48730-2] DR GeneID; 1453; -. DR KEGG; hsa:1453; -. DR MANE-Select; ENST00000314028.11; ENSP00000324464.6; NM_001893.6; NP_001884.2. DR UCSC; uc002kei.4; human. [P48730-1] DR AGR; HGNC:2452; -. DR CTD; 1453; -. DR DisGeNET; 1453; -. DR GeneCards; CSNK1D; -. DR HGNC; HGNC:2452; CSNK1D. DR HPA; ENSG00000141551; Low tissue specificity. DR MalaCards; CSNK1D; -. DR MIM; 600864; gene. DR MIM; 615224; phenotype. DR neXtProt; NX_P48730; -. DR OpenTargets; ENSG00000141551; -. DR Orphanet; 164736; Familial advanced sleep-phase syndrome. DR PharmGKB; PA26952; -. DR VEuPathDB; HostDB:ENSG00000141551; -. DR eggNOG; KOG1164; Eukaryota. DR GeneTree; ENSGT00940000153536; -. DR HOGENOM; CLU_019279_2_2_1; -. DR InParanoid; P48730; -. DR OMA; IFDWTFL; -. DR OrthoDB; 1534388at2759; -. DR PhylomeDB; P48730; -. DR TreeFam; TF300544; -. DR BRENDA; 2.7.11.1; 2681. DR BRENDA; 2.7.11.26; 2681. DR PathwayCommons; P48730; -. DR Reactome; R-HSA-204005; COPII-mediated vesicle transport. 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; P48730; -. DR SignaLink; P48730; -. DR SIGNOR; P48730; -. DR BioGRID-ORCS; 1453; 26 hits in 1201 CRISPR screens. DR ChiTaRS; CSNK1D; human. DR GeneWiki; CSNK1D; -. DR GenomeRNAi; 1453; -. DR Pharos; P48730; Tchem. DR PRO; PR:P48730; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P48730; Protein. DR Bgee; ENSG00000141551; Expressed in left testis and 205 other cell types or tissues. DR ExpressionAtlas; P48730; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0036064; C:ciliary basal body; IDA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005819; C:spindle; IDA:UniProtKB. DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; IDA:UniProtKB. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0050321; F:tau-protein kinase activity; IDA:UniProtKB. DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl. DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB. DR GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome. DR GO; GO:0006897; P:endocytosis; IBA:GO_Central. DR GO; GO:0007030; P:Golgi organization; IMP:SYSCILIA_CCNET. DR GO; GO:0007020; P:microtubule nucleation; IMP:SYSCILIA_CCNET. DR GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; ISS:ParkinsonsUK-UCL. DR GO; GO:1905515; P:non-motile cilium assembly; IMP:SYSCILIA_CCNET. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:BHF-UCL. DR GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; ISS:ParkinsonsUK-UCL. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:BHF-UCL. DR GO; GO:0071539; P:protein localization to centrosome; IMP:SYSCILIA_CCNET. DR GO; GO:0061512; P:protein localization to cilium; IMP:SYSCILIA_CCNET. DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:SYSCILIA_CCNET. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR GO; GO:0051225; P:spindle assembly; IDA:UniProtKB. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. 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:SF18; CASEIN KINASE I ISOFORM DELTA; 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; P48730; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Biological rhythms; KW Cell membrane; Cytoplasm; Cytoskeleton; Disease variant; Golgi apparatus; KW Kinase; Membrane; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase; KW Wnt signaling pathway. FT CHAIN 1..415 FT /note="Casein kinase I isoform delta" FT /id="PRO_0000192833" FT DOMAIN 9..277 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 278..364 FT /note="Centrosomal localization signal (CLS)" FT REGION 301..415 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 317..342 FT /note="Autoinhibitory" FT /evidence="ECO:0000250" FT COMPBIAS 301..320 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 342..359 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 380..415 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 328 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 331 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 370 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q06486" FT MOD_RES 375 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9DC28" FT MOD_RES 382 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 383 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 384 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 407 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 411 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195" FT VAR_SEQ 400..415 FT /note="IPGRVASSGLQSVVHR -> NSIPFEHHGK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_010253" FT VARIANT 44 FT /note="T -> A (in FASPS2; strongly reduces kinase activity; FT dbSNP:rs104894561)" FT /evidence="ECO:0000269|PubMed:15800623, FT ECO:0000269|PubMed:23636092" FT /id="VAR_029075" FT VARIANT 46 FT /note="H -> R (in FASPS2; strongly reduces kinase activity; FT dbSNP:rs397514693)" FT /evidence="ECO:0000269|PubMed:23636092" FT /id="VAR_069801" FT VARIANT 97 FT /note="S -> C (in breast cancer samples; infiltrating FT ductal carcinoma; somatic mutation)" FT /evidence="ECO:0000269|PubMed:16959974, FT ECO:0000269|PubMed:17344846" FT /id="VAR_036451" FT VARIANT 401 FT /note="P -> A (in dbSNP:rs56124628)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042081" FT MUTAGEN 38 FT /note="K->M: Impaired kinase activity and abnormal FT subcellular localization with exclusive accumulation to the FT nucleus." FT /evidence="ECO:0000269|PubMed:11161704" FT MUTAGEN 176 FT /note="T->I: Impaired kinase activity and abnormal FT subcellular localization with exclusive accumulation to the FT nucleus." FT /evidence="ECO:0000269|PubMed:11161704" FT CONFLICT 330 FT /note="A -> D (in Ref. 1; AAC50807)" FT /evidence="ECO:0000305" FT STRAND 3..5 FT /evidence="ECO:0007829|PDB:6RCG" FT TURN 6..8 FT /evidence="ECO:0007829|PDB:6RCG" FT STRAND 9..18 FT /evidence="ECO:0007829|PDB:6RCG" FT STRAND 21..28 FT /evidence="ECO:0007829|PDB:6RCG" FT TURN 29..32 FT /evidence="ECO:0007829|PDB:6RCG" FT STRAND 33..41 FT /evidence="ECO:0007829|PDB:6RCG" FT STRAND 44..46 FT /evidence="ECO:0007829|PDB:6RCG" FT HELIX 49..59 FT /evidence="ECO:0007829|PDB:6RCG" FT STRAND 68..74 FT /evidence="ECO:0007829|PDB:6RCG" FT STRAND 77..83 FT /evidence="ECO:0007829|PDB:6RCG" FT HELIX 89..95 FT /evidence="ECO:0007829|PDB:6RCG" FT TURN 96..98 FT /evidence="ECO:0007829|PDB:6RCG" FT HELIX 102..121 FT /evidence="ECO:0007829|PDB:6RCG" FT HELIX 131..133 FT /evidence="ECO:0007829|PDB:6RCG" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:6RCG" FT HELIX 139..141 FT /evidence="ECO:0007829|PDB:6RCG" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:6RCG" FT STRAND 154..157 FT /evidence="ECO:0007829|PDB:8D7O" FT TURN 159..161 FT /evidence="ECO:0007829|PDB:6RCG" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:6RCG" FT HELIX 182..185 FT /evidence="ECO:0007829|PDB:6RCG" FT HELIX 192..208 FT /evidence="ECO:0007829|PDB:6RCG" FT TURN 212..215 FT /evidence="ECO:0007829|PDB:6RCH" FT STRAND 217..219 FT /evidence="ECO:0007829|PDB:6RCG" FT HELIX 221..233 FT /evidence="ECO:0007829|PDB:6RCG" FT HELIX 237..240 FT /evidence="ECO:0007829|PDB:6RCG" FT TURN 241..243 FT /evidence="ECO:0007829|PDB:6RCG" FT HELIX 247..257 FT /evidence="ECO:0007829|PDB:6RCG" FT HELIX 266..279 FT /evidence="ECO:0007829|PDB:6RCG" FT HELIX 280..283 FT /evidence="ECO:0007829|PDB:6F1W" FT HELIX 289..292 FT /evidence="ECO:0007829|PDB:6RCG" SQ SEQUENCE 415 AA; 47330 MW; B97F1717A52466D2 CRC64; MELRVGNRYR LGRKIGSGSF GDIYLGTDIA AGEEVAIKLE CVKTKHPQLH IESKIYKMMQ GGVGIPTIRW CGAEGDYNVM VMELLGPSLE DLFNFCSRKF SLKTVLLLAD QMISRIEYIH SKNFIHRDVK PDNFLMGLGK KGNLVYIIDF GLAKKYRDAR THQHIPYREN KNLTGTARYA SINTHLGIEQ SRRDDLESLG YVLMYFNLGS LPWQGLKAAT KRQKYERISE KKMSTPIEVL CKGYPSEFAT YLNFCRSLRF DDKPDYSYLR QLFRNLFHRQ GFSYDYVFDW NMLKFGASRA ADDAERERRD REERLRHSRN PATRGLPSTA SGRLRGTQEV APPTPLTPTS HTANTSPRPV SGMERERKVS MRLHRGAPVN ISSSDLTGRQ DTSRMSTSQI PGRVASSGLQ SVVHR //