ID KC1D_MOUSE Reviewed; 415 AA.
AC Q9DC28; Q3TZK2; Q99KK4;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 27-MAR-2024, entry version 178.
DE RecName: Full=Casein kinase I isoform delta;
DE Short=CKI-delta;
DE Short=CKId;
DE EC=2.7.11.1 {ECO:0000269|PubMed:10848614, ECO:0000269|PubMed:17101137, ECO:0000269|PubMed:19414593, ECO:0000269|PubMed:20192920};
DE AltName: Full=Tau-protein kinase CSNK1D;
DE EC=2.7.11.26 {ECO:0000250|UniProtKB:P48730};
GN Name=Csnk1d; Synonyms=Hckid;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Lung, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP FUNCTION AS PER1 KINASE, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=10848614; DOI=10.1128/mcb.20.13.4888-4899.2000;
RA Vielhaber E., Eide E., Rivers A., Gao Z.-H., Virshup D.M.;
RT "Nuclear entry of the circadian regulator mPER1 is controlled by mammalian
RT casein kinase I epsilon.";
RL Mol. Cell. Biol. 20:4888-4899(2000).
RN [4]
RP IDENTIFICATION IN A COMPLEX WITH CLOCK; PER1; PER2; CRY1; CRY2; CSNK1D AND
RP CSNK1E.
RX PubMed=11779462; DOI=10.1016/s0092-8674(01)00610-9;
RA Lee C., Etchegaray J.-P., Cagampang F.R.A., Loudon A.S.I., Reppert S.M.;
RT "Posttranslational mechanisms regulate the mammalian circadian clock.";
RL Cell 107:855-867(2001).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=12924632; DOI=10.1078/0171-9335-00323;
RA Maritzen T., Loehler J., Deppert W., Knippschild U.;
RT "Casein kinase I delta (CKIdelta) is involved in lymphocyte physiology.";
RL Eur. J. Cell Biol. 82:369-378(2003).
RN [6]
RP FUNCTION IN SYNAPTIC TRANSMISSION.
RX PubMed=16014721; DOI=10.1523/jneurosci.1082-05.2005;
RA Chergui K., Svenningsson P., Greengard P.;
RT "Physiological role for casein kinase 1 in glutamatergic synaptic
RT transmission.";
RL J. Neurosci. 25:6601-6609(2005).
RN [7]
RP FUNCTION AS SNAPIN KINASE, SUBCELLULAR LOCATION, INTERACTION WITH SNAPIN,
RP AND CATALYTIC ACTIVITY.
RX PubMed=17101137; DOI=10.1016/j.febslet.2006.10.068;
RA Wolff S., Stoeter M., Giamas G., Piesche M., Henne-Bruns D., Banting G.,
RA Knippschild U.;
RT "Casein kinase 1 delta (CK1delta) interacts with the SNARE associated
RT protein snapin.";
RL FEBS Lett. 580:6477-6484(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP FUNCTION IN CIRCADIAN CLOCK, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19414593; DOI=10.1128/mcb.00338-09;
RA Etchegaray J.P., Machida K.K., Noton E., Constance C.M., Dallmann R.,
RA Di Napoli M.N., DeBruyne J.P., Lambert C.M., Yu E.A., Reppert S.M.,
RA Weaver D.R.;
RT "Casein kinase 1 delta regulates the pace of the mammalian circadian
RT clock.";
RL Mol. Cell. Biol. 29:3853-3866(2009).
RN [10]
RP FUNCTION IN CIRCADIAN CLOCK, AND DISRUPTION PHENOTYPE.
RX PubMed=19948962; DOI=10.1073/pnas.0906651106;
RA Lee H., Chen R., Lee Y., Yoo S., Lee C.;
RT "Essential roles of CKIdelta and CKIepsilon in the mammalian circadian
RT clock.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:21359-21364(2009).
RN [11]
RP FUNCTION AS DNMT1 KINASE, INTERACTION WITH DNMT1, AND CATALYTIC ACTIVITY.
RX PubMed=20192920; DOI=10.1042/bj20091856;
RA Sugiyama Y., Hatano N., Sueyoshi N., Suetake I., Tajima S., Kinoshita E.,
RA Kinoshita-Kikuta E., Koike T., Kameshita I.;
RT "The DNA-binding activity of mouse DNA methyltransferase 1 is regulated by
RT phosphorylation with casein kinase 1delta/epsilon.";
RL Biochem. J. 427:489-497(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382 AND SER-383, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP FUNCTION IN CIRCADIAN CLOCK.
RX PubMed=20421981; DOI=10.1371/journal.pone.0010303;
RA Etchegaray J.-P., Yu E.A., Indic P., Dallmann R., Weaver D.R.;
RT "Casein kinase 1 delta (CK1delta) regulates period length of the mouse
RT suprachiasmatic circadian clock in vitro.";
RL PLoS ONE 5:E10303-E10303(2010).
RN [14]
RP FUNCTION IN DOPAMINE RECEPTORS.
RX PubMed=20145109; DOI=10.1073/pnas.0915173107;
RA Zhou M., Rebholz H., Brocia C., Warner-Schmidt J.L., Fienberg A.A.,
RA Nairn A.C., Greengard P., Flajolet M.;
RT "Forebrain overexpression of CK1delta leads to down-regulation of dopamine
RT receptors and altered locomotor activity reminiscent of ADHD.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:4401-4406(2010).
RN [15]
RP FUNCTION IN CIRCADIAN CLOCK, AND DEPHOSPHORYLATION.
RX PubMed=21930935; DOI=10.1073/pnas.1107178108;
RA Lee H.M., Chen R., Kim H., Etchegaray J.P., Weaver D.R., Lee C.;
RT "The period of the circadian oscillator is primarily determined by the
RT balance between casein kinase 1 and protein phosphatase 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:16451-16456(2011).
RN [16]
RP MUTAGENESIS OF THR-44.
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).
RN [17]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-375, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF LYS-38.
RX PubMed=29191835; DOI=10.1074/jbc.m117.802587;
RA Lee K.H., Hwang J.A., Kim S.O., Kim J.H., Shin S.C., Kim E.E., Lee K.S.,
RA Rhee K., Jeon B.H., Bang J.K., Cha-Molstad H., Soung N.K., Jang J.H.,
RA Ko S.K., Lee H.G., Ahn J.S., Kwon Y.T., Kim B.Y.;
RT "Phosphorylation of human enhancer filamentation 1 (HEF1) stimulates
RT interaction with Polo-like kinase 1 leading to HEF1 localization to focal
RT adhesions.";
RL J. Biol. Chem. 293:847-862(2018).
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
CC (PubMed:29191835). EIF6 phosphorylation promotes its nuclear export.
CC Triggers down-regulation of dopamine receptors in the forebrain.
CC Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors
CC DNA cleavable complex formation. May regulate the formation of the
CC mitotic spindle apparatus in extravillous trophoblast. Modulates
CC connexin-43/GJA1 gap junction assembly by phosphorylation. Probably
CC involved in lymphocyte physiology. Regulates fast synaptic transmission
CC mediated by glutamate. {ECO:0000269|PubMed:10848614,
CC ECO:0000269|PubMed:16014721, ECO:0000269|PubMed:17101137,
CC ECO:0000269|PubMed:19414593, ECO:0000269|PubMed:19948962,
CC ECO:0000269|PubMed:20145109, ECO:0000269|PubMed:20192920,
CC ECO:0000269|PubMed:20421981, ECO:0000269|PubMed:21930935,
CC ECO:0000269|PubMed:29191835}.
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:10848614, ECO:0000269|PubMed:17101137,
CC ECO:0000269|PubMed:19414593, ECO:0000269|PubMed:20192920};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000305|PubMed:20192920};
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:10848614,
CC ECO:0000269|PubMed:17101137, ECO:0000269|PubMed:19414593,
CC ECO:0000269|PubMed:20192920};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305|PubMed:20192920};
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:0000250|UniProtKB:P48730};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12802;
CC Evidence={ECO:0000250|UniProtKB:P48730};
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:0000250|UniProtKB:P48730};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53905;
CC Evidence={ECO:0000250|UniProtKB:P48730};
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 (By similarity).
CC {ECO:0000250|UniProtKB:P48730}.
CC -!- SUBUNIT: Monomer (By similarity). Component of the circadian core
CC oscillator, which includes the CRY proteins, CLOCK, or NPAS2, BMAL1 or
CC BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins
CC (PubMed:11779462). Interacts directly with PER1 and PER2 which may lead
CC to their degradation (By similarity). Interacts with MAP1A (By
CC similarity). Interacts with MAPT/TAU, DBNDD2, AIB1/NCOA3 and ESR1 (By
CC similarity). Interacts with AKAP9/AKAP450; this interaction promotes
CC centrosomal subcellular location (By similarity). Binds to tubulins in
CC mitotic cells upon DNA damage (By similarity). Interacts with GJA1 (By
CC similarity). Interacts with SNAPIN (PubMed:17101137). Interacts with
CC DNMT1 (PubMed:20192920). Interacts with DDX3X; this interaction
CC enhances CSNK1D kinase activity in vitro, but it is unclear whether
CC this interaction is physiologically relevant (By similarity).
CC {ECO:0000250|UniProtKB:P48730, ECO:0000250|UniProtKB:Q06486,
CC ECO:0000269|PubMed:11779462, ECO:0000269|PubMed:17101137,
CC ECO:0000269|PubMed:20192920}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:10848614, ECO:0000269|PubMed:17101137,
CC ECO:0000269|PubMed:19414593}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250}. Golgi apparatus {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DC28-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DC28-2; Sequence=VSP_010254;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. However, kinase activity is
CC not uniform, with highest kinase activity in splenocytes.
CC {ECO:0000269|PubMed:12924632}.
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 -!- DISRUPTION PHENOTYPE: Lethal. There are fewer embryos than expected at
CC late stages of gestation; they weigh about 30% less than control
CC animals, but appear otherwise normal. Mice die shortly after birth.
CC Tissue-specific disruption increases the half-life of PER2 protein and
CC alters circadian protein expression dynamics.
CC {ECO:0000269|PubMed:19414593, ECO:0000269|PubMed:19948962}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
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DR EMBL; AK004606; BAB23405.1; -; mRNA.
DR EMBL; AK088642; BAC40472.1; -; mRNA.
DR EMBL; AK152721; BAE31444.1; -; mRNA.
DR EMBL; AK157812; BAE34206.1; -; mRNA.
DR EMBL; BC004604; AAH04604.1; -; mRNA.
DR CCDS; CCDS25762.1; -. [Q9DC28-1]
DR CCDS; CCDS25763.1; -. [Q9DC28-2]
DR PIR; S47616; S47616.
DR RefSeq; NP_620690.1; NM_139059.2. [Q9DC28-1]
DR PDB; 4JJR; X-ray; 2.41 A; A/B=1-299.
DR PDB; 5X17; X-ray; 2.00 A; A/B=1-294.
DR PDBsum; 4JJR; -.
DR PDBsum; 5X17; -.
DR AlphaFoldDB; Q9DC28; -.
DR SMR; Q9DC28; -.
DR BioGRID; 222545; 24.
DR DIP; DIP-47809N; -.
DR IntAct; Q9DC28; 21.
DR MINT; Q9DC28; -.
DR STRING; 10090.ENSMUSP00000018274; -.
DR ChEMBL; CHEMBL5175; -.
DR GlyGen; Q9DC28; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9DC28; -.
DR PhosphoSitePlus; Q9DC28; -.
DR SwissPalm; Q9DC28; -.
DR EPD; Q9DC28; -.
DR jPOST; Q9DC28; -.
DR MaxQB; Q9DC28; -.
DR PaxDb; 10090-ENSMUSP00000018274; -.
DR PeptideAtlas; Q9DC28; -.
DR ProteomicsDB; 263482; -. [Q9DC28-1]
DR ProteomicsDB; 263483; -. [Q9DC28-2]
DR Pumba; Q9DC28; -.
DR Antibodypedia; 4210; 410 antibodies from 40 providers.
DR DNASU; 104318; -.
DR Ensembl; ENSMUST00000018274.10; ENSMUSP00000018274.4; ENSMUSG00000025162.19. [Q9DC28-1]
DR Ensembl; ENSMUST00000070575.14; ENSMUSP00000070721.8; ENSMUSG00000025162.19. [Q9DC28-2]
DR GeneID; 104318; -.
DR KEGG; mmu:104318; -.
DR UCSC; uc007mvb.1; mouse. [Q9DC28-1]
DR AGR; MGI:1355272; -.
DR CTD; 1453; -.
DR MGI; MGI:1355272; Csnk1d.
DR VEuPathDB; HostDB:ENSMUSG00000025162; -.
DR eggNOG; KOG1164; Eukaryota.
DR GeneTree; ENSGT00940000153536; -.
DR HOGENOM; CLU_019279_2_2_1; -.
DR InParanoid; Q9DC28; -.
DR OMA; IFDWTFL; -.
DR OrthoDB; 1534388at2759; -.
DR PhylomeDB; Q9DC28; -.
DR TreeFam; TF300544; -.
DR BRENDA; 2.7.11.1; 3474.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 104318; 3 hits in 82 CRISPR screens.
DR ChiTaRS; Csnk1d; mouse.
DR PRO; PR:Q9DC28; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9DC28; Protein.
DR Bgee; ENSMUSG00000025162; Expressed in paneth cell and 277 other cell types or tissues.
DR ExpressionAtlas; Q9DC28; baseline and differential.
DR Genevisible; Q9DC28; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005819; C:spindle; ISO:MGI.
DR GO; GO:0005876; C:spindle microtubule; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; ISO:MGI.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0050321; F:tau-protein kinase activity; ISO:MGI.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR GO; GO:0007020; P:microtubule nucleation; ISO:MGI.
DR GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; IGI:ParkinsonsUK-UCL.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; IGI:ParkinsonsUK-UCL.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IGI:ParkinsonsUK-UCL.
DR GO; GO:0071539; P:protein localization to centrosome; ISO:MGI.
DR GO; GO:0061512; P:protein localization to cilium; ISO:MGI.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0051225; P:spindle assembly; ISO:MGI.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Biological rhythms;
KW Cell membrane; Cytoplasm; Cytoskeleton; Golgi apparatus; Kinase; Membrane;
KW 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_0000192834"
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 /evidence="ECO:0000250"
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:0000250|UniProtKB:P48730"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48730"
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:0007744|PubMed:24129315"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48730"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48730"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48730"
FT VAR_SEQ 400..415
FT /note="IPGRVASSGLQSVVHR -> NSIPFEHHGK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010254"
FT MUTAGEN 38
FT /note="K->M: Abolishes NEDD9 phosphorylation."
FT /evidence="ECO:0000269|PubMed:29191835"
FT MUTAGEN 44
FT /note="T->A: Increases pain sensitivity; reduces threshold
FT for induction of cortical spreading depression; increases
FT arterial dilation during cortical spreading depression and
FT increases spontaneous and evoked calcium signaling in
FT astrocytes."
FT /evidence="ECO:0000269|PubMed:23636092"
FT CONFLICT 313
FT /note="E -> G (in Ref. 1; BAB23405)"
FT /evidence="ECO:0000305"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:5X17"
FT STRAND 9..16
FT /evidence="ECO:0007829|PDB:5X17"
FT STRAND 19..28
FT /evidence="ECO:0007829|PDB:5X17"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:5X17"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:5X17"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:5X17"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:5X17"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:5X17"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:5X17"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:5X17"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:5X17"
FT HELIX 102..121
FT /evidence="ECO:0007829|PDB:5X17"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:5X17"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:5X17"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:5X17"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:5X17"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:5X17"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:5X17"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:5X17"
FT HELIX 192..208
FT /evidence="ECO:0007829|PDB:5X17"
FT TURN 212..215
FT /evidence="ECO:0007829|PDB:5X17"
FT HELIX 221..233
FT /evidence="ECO:0007829|PDB:5X17"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:5X17"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:5X17"
FT HELIX 247..257
FT /evidence="ECO:0007829|PDB:5X17"
FT HELIX 266..279
FT /evidence="ECO:0007829|PDB:5X17"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:5X17"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:4JJR"
FT MOD_RES Q9DC28-2:401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 415 AA; 47316 MW; B97F04AF9EB466D2 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 VSSSDLTGRQ DTSRMSTSQI PGRVASSGLQ SVVHR
//
