KC1D_HUMAN
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 03-AUG-2022, entry version 217.
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. EIF6 phosphorylation promotes its nuclear
CC export. Triggers down-regulation of dopamine receptors in the
CC forebrain. Activates DCK in vitro by phosphorylation. TOP2A
CC phosphorylation favors DNA cleavable complex formation. May regulate
CC the formation of the mitotic spindle apparatus in extravillous
CC trophoblast. Modulates connexin-43/GJA1 gap junction assembly by
CC phosphorylation. Probably involved in lymphocyte physiology. Regulates
CC fast synaptic transmission mediated by glutamate.
CC {ECO:0000269|PubMed:10606744, ECO:0000269|PubMed:12270943,
CC ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:16027726,
CC ECO:0000269|PubMed:17562708, ECO:0000269|PubMed:17962809,
CC ECO:0000269|PubMed:19043076, ECO:0000269|PubMed:20041275,
CC ECO:0000269|PubMed:20048001, ECO:0000269|PubMed:20407760,
CC ECO:0000269|PubMed:20637175, ECO:0000269|PubMed:20696890,
CC ECO:0000269|PubMed:20699359, ECO:0000269|PubMed:21084295,
CC ECO:0000269|PubMed:21422228, 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 alpha-
CC 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; 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]: A disorder characterized by very early sleep onset and
CC offset. Individuals are 'morning larks' with a 4 hours advance of the
CC sleep, temperature and melatonin rhythms. {ECO:0000269|PubMed:15800623,
CC ECO:0000269|PubMed:23636092}. Note=The disease is caused by variants
CC affecting the gene represented in this 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}.
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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; 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 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; 7P7F; -.
DR PDBsum; 7P7G; -.
DR PDBsum; 7P7H; -.
DR AlphaFoldDB; P48730; -.
DR SMR; P48730; -.
DR BioGRID; 107837; 214.
DR DIP; DIP-39735N; -.
DR IntAct; P48730; 161.
DR MINT; P48730; -.
DR STRING; 9606.ENSP00000324464; -.
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 EPD; P48730; -.
DR jPOST; P48730; -.
DR MassIVE; P48730; -.
DR MaxQB; P48730; -.
DR PaxDb; P48730; -.
DR PeptideAtlas; P48730; -.
DR PRIDE; P48730; -.
DR ProteomicsDB; 55930; -. [P48730-1]
DR ProteomicsDB; 55931; -. [P48730-2]
DR TopDownProteomics; P48730-1; -. [P48730-1]
DR Antibodypedia; 4210; 376 antibodies from 40 providers.
DR DNASU; 1453; -.
DR Ensembl; ENST00000314028.11; ENSP00000324464.6; ENSG00000141551.15. [P48730-1]
DR Ensembl; ENST00000392334.6; 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 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; 1097975at2759; -.
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; 24 hits in 1120 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 203 other tissues.
DR ExpressionAtlas; P48730; baseline and differential.
DR Genevisible; P48730; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA: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:0043005; C:neuron projection; IEA:Ensembl.
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:0007030; P:Golgi organization; IMP:SYSCILIA_CCNET.
DR GO; GO:0007020; P:microtubule nucleation; IMP:SYSCILIA_CCNET.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:SYSCILIA_CCNET.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
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:1905426; P:positive regulation of Wnt-mediated midbrain dopaminergic neuron differentiation; IC:ParkinsonsUK-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 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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
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:4TWC"
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
