KC1A_MOUSE
ID KC1A_MOUSE Reviewed; 337 AA.
AC Q8BK63; Q3UIL0; Q64506; Q80XI2; Q99LY3;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Casein kinase I isoform alpha;
DE Short=CKI-alpha;
DE EC=2.7.11.1;
DE AltName: Full=CK1;
GN Name=Csnk1a1;
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; TISSUE=Liver;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Olfactory epithelium;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 299-325 (ISOFORM 2).
RX PubMed=9522121; DOI=10.3109/10425179709020885;
RA McInnes C., Leader D.P.;
RT "Tissue-specific distribution of the mouse casein kinase I alpha mRNA.";
RL DNA Seq. 8:55-57(1997).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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 [5]
RP FUNCTION AS PER1 AND PER2 KINASE.
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-8, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=25644602; DOI=10.1101/gad.252676.114;
RA Chong Y.C., Mann R.K., Zhao C., Kato M., Beachy P.A.;
RT "Bifurcating action of Smoothened in Hedgehog signaling is mediated by
RT Dlg5.";
RL Genes Dev. 29:262-276(2015).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=31338967; DOI=10.15252/embr.201847495;
RA Fulcher L.J., He Z., Mei L., Macartney T.J., Wood N.T., Prescott A.R.,
RA Whigham A.J., Varghese J., Gourlay R., Ball G., Clarke R., Campbell D.G.,
RA Maxwell C.A., Sapkota G.P.;
RT "FAM83D directs protein kinase CK1alpha to the mitotic spindle for proper
RT spindle positioning.";
RL EMBO Rep. 20:e47495-e47495(2019).
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. Can phosphorylate a large number of proteins. Participates
CC in Wnt signaling. Phosphorylates CTNNB1 at 'Ser-45'. May phosphorylate
CC PER1 and PER2. May play a role in segregating chromosomes during
CC mitosis. May play a role in keratin cytoskeleton disassembly and
CC thereby, it may regulate epithelial cell migration (By similarity).
CC {ECO:0000250|UniProtKB:P48729, ECO:0000269|PubMed:21930935}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with the Axin complex (By similarity). Interacts
CC with TUT1, leading to TUT1 phosphorylation (By similarity). Interacts
CC with FAM83H; recruits CSNK1A1 to keratin filaments (By similarity).
CC Interacts with FAM83D (via N-terminus); in mitotic cells (By
CC similarity). {ECO:0000250|UniProtKB:P48729}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48729}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P48729}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:P48729}. Nucleus speckle
CC {ECO:0000250|UniProtKB:P48729}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:25644602}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:31338967}. Note=Localizes to the centrosome in
CC interphase cells, and to kinetochore fibers during mitosis. Also
CC recruited to the keratin cytoskeleton. {ECO:0000250|UniProtKB:P48729}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BK63-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BK63-2; Sequence=VSP_010252;
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; AK076070; BAC36161.1; -; mRNA.
DR EMBL; AK078398; BAC37255.1; -; mRNA.
DR EMBL; AK146873; BAE27496.1; -; mRNA.
DR EMBL; BC002171; AAH02171.1; -; mRNA.
DR EMBL; BC048081; AAH48081.1; -; mRNA.
DR EMBL; X90945; CAA62440.1; -; mRNA.
DR CCDS; CCDS37838.1; -. [Q8BK63-2]
DR CCDS; CCDS89254.1; -. [Q8BK63-1]
DR RefSeq; XP_006526451.1; XM_006526388.2.
DR AlphaFoldDB; Q8BK63; -.
DR SMR; Q8BK63; -.
DR BioGRID; 220237; 18.
DR ComplexPortal; CPX-103; Beta-catenin destruction core complex, variant 1.
DR ComplexPortal; CPX-448; Beta-catenin destruction core complex, variant 2.
DR ComplexPortal; CPX-449; Beta-catenin destruction core complex, variant 3.
DR ComplexPortal; CPX-452; Beta-catenin destruction core complex, variant 4.
DR ComplexPortal; CPX-453; Beta-catenin destruction core complex, variant 5.
DR ComplexPortal; CPX-456; Beta-catenin destruction core complex, variant 6.
DR ComplexPortal; CPX-457; Beta-catenin destruction core complex, variant 7.
DR ComplexPortal; CPX-458; Beta-catenin destruction core complex, variant 8.
DR DIP; DIP-32408N; -.
DR IntAct; Q8BK63; 9.
DR MINT; Q8BK63; -.
DR STRING; 10090.ENSMUSP00000128871; -.
DR ChEMBL; CHEMBL5148; -.
DR iPTMnet; Q8BK63; -.
DR PhosphoSitePlus; Q8BK63; -.
DR EPD; Q8BK63; -.
DR MaxQB; Q8BK63; -.
DR PaxDb; Q8BK63; -.
DR PRIDE; Q8BK63; -.
DR ProteomicsDB; 263393; -. [Q8BK63-1]
DR ProteomicsDB; 263394; -. [Q8BK63-2]
DR Antibodypedia; 27829; 664 antibodies from 39 providers.
DR Ensembl; ENSMUST00000165123; ENSMUSP00000128871; ENSMUSG00000024576. [Q8BK63-2]
DR Ensembl; ENSMUST00000165721; ENSMUSP00000132083; ENSMUSG00000024576. [Q8BK63-1]
DR UCSC; uc008fcc.1; mouse. [Q8BK63-1]
DR MGI; MGI:1934950; Csnk1a1.
DR VEuPathDB; HostDB:ENSMUSG00000024576; -.
DR eggNOG; KOG1163; Eukaryota.
DR GeneTree; ENSGT00940000153700; -.
DR HOGENOM; CLU_019279_2_7_1; -.
DR InParanoid; Q8BK63; -.
DR OrthoDB; 1097975at2759; -.
DR TreeFam; TF354246; -.
DR BRENDA; 2.7.11.1; 3474.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5635838; Activation of SMO.
DR BioGRID-ORCS; 93687; 25 hits in 75 CRISPR screens.
DR ChiTaRS; Csnk1a1; mouse.
DR PRO; PR:Q8BK63; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8BK63; protein.
DR Bgee; ENSMUSG00000024576; Expressed in renal corpuscle and 265 other tissues.
DR ExpressionAtlas; Q8BK63; baseline and differential.
DR Genevisible; Q8BK63; MM.
DR GO; GO:0030877; C:beta-catenin destruction complex; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045095; C:keratin filament; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000902; P:cell morphogenesis; IGI:MGI.
DR GO; GO:0007030; P:Golgi organization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:ParkinsonsUK-UCL.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:1904424; P:regulation of GTP binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 Acetylation; Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Cell projection; Centromere; Chromosome; Cytoplasm; Cytoskeleton; Kinase;
KW Kinetochore; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CHAIN 2..337
FT /note="Casein kinase I isoform alpha"
FT /id="PRO_0000192823"
FT DOMAIN 17..285
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 309..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 23..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48729"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 325..337
FT /note="KQTDKTKSNMKGF -> F (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9522121"
FT /id="VSP_010252"
FT CONFLICT 126
FT /note="Y -> N (in Ref. 2; AAH48081)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="R -> K (in Ref. 1; BAC36161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 38915 MW; 1B2085AE33CAFAC2 CRC64;
MASSSGSKAE FIVGGKYKLV RKIGSGSFGD IYLAINITNG EEVAVKLESQ KARHPQLLYE
SKLYKILQGG VGIPHIRWYG QEKDYNVLVM DLLGPSLEDL FNFCSRRFTM KTVLMLADQM
ISRIEYVHTK NFIHRDIKPD NFLMGIGRHC NKLFLIDFGL AKKYRDNRTR QHIPYREDKN
LTGTARYASI NAHLGIEQSR RDDMESLGYV LMYFNRTSLP WQGLKAATKK QKYEKISEKK
MSTPVEVLCK GFPAEFAMYL NYCRGLRFEE APDYMYLRQL FRILFRTLNH QYDYTFDWTM
LKQKAAQQAA SSSGQGQQAQ TPTGKQTDKT KSNMKGF
