KC1A_HUMAN
ID KC1A_HUMAN Reviewed; 337 AA.
AC P48729; D3DQG0; D3DQG1; Q4JJA0; Q5U046; Q5U047; Q6FGA2; Q71TU5; Q96HD2;
AC Q9UDK3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 218.
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 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=8050587; DOI=10.1016/0014-5793(94)00679-2;
RA Tapia C., Featherstone T., Gomez C., Taillon-Miller P., Allende C.C.,
RA Allende J.E.;
RT "Cloning and chromosomal localization of the gene coding for human protein
RT kinase CK1.";
RL FEBS Lett. 349:307-312(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=7797465; DOI=10.1074/jbc.270.25.14875;
RA Fish K.J., Cegielska A., Getman M.E., Landes G.M., Virshup D.M.;
RT "Isolation and characterization of human casein kinase I epsilon (CKI), a
RT novel member of the CKI gene family.";
RL J. Biol. Chem. 270:14875-14883(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
RA Huang B., Li H., Yang S.;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP PROTEIN SEQUENCE OF 65-83; 111-152 AND 179-204, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=1409656; DOI=10.1073/pnas.89.20.9454;
RA Brockman J.L., Gross S.D., Sussman M.R., Anderson R.A.;
RT "Cell cycle-dependent localization of casein kinase I to mitotic
RT spindles.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9454-9458(1992).
RN [12]
RP ROLE IN WNT SIGNALING, AND INTERACTION WITH AXIN COMPLEX.
RX PubMed=11955436; DOI=10.1016/s0092-8674(02)00685-2;
RA Liu C., Li Y., Semenov M., Han C., Baeg G.-H., Tan Y., Zhang Z., Lin X.,
RA He X.;
RT "Control of beta-catenin phosphorylation/degradation by a dual-kinase
RT mechanism.";
RL Cell 108:837-847(2002).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [14]
RP FUNCTION, INTERACTION WITH TUT1, AND SUBCELLULAR LOCATION.
RX PubMed=18305108; DOI=10.1074/jbc.m800656200;
RA Gonzales M.L., Mellman D.L., Anderson R.A.;
RT "CKIalpha is associated with and phosphorylates star-PAP and is also
RT required for expression of select star-PAP target messenger RNAs.";
RL J. Biol. Chem. 283:12665-12673(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 (ISOFORM 2), AND
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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-321 (ISOFORM 3), AND
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 [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [22]
RP FUNCTION, INTERACTION WITH FAM83H, AND SUBCELLULAR LOCATION.
RX PubMed=23902688; DOI=10.1242/jcs.129684;
RA Kuga T., Kume H., Kawasaki N., Sato M., Adachi J., Shiromizu T.,
RA Hoshino I., Nishimori T., Matsubara H., Tomonaga T.;
RT "A novel mechanism of keratin cytoskeleton organization through casein
RT kinase Ialpha and FAM83H in colorectal cancer.";
RL J. Cell Sci. 126:4721-4731(2013).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [24]
RP INTERACTION WITH FAM83D.
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).
RN [25]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-297.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. It can phosphorylate a large number of proteins.
CC Participates in Wnt signaling. Phosphorylates CTNNB1 at 'Ser-45'. May
CC phosphorylate PER1 and PER2. May play a role in segregating chromosomes
CC during mitosis (PubMed:11955436, PubMed:1409656, PubMed:18305108). May
CC play a role in keratin cytoskeleton disassembly and thereby, it may
CC regulate epithelial cell migration (PubMed:23902688).
CC {ECO:0000269|PubMed:11955436, ECO:0000269|PubMed:1409656,
CC ECO:0000269|PubMed:18305108, ECO:0000269|PubMed:23902688}.
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 (PubMed:11955436). Interacts
CC with TUT1, leading to TUT1 phosphorylation (PubMed:1409656). Interacts
CC with FAM83H; recruits CSNK1A1 to keratin filaments (PubMed:23902688).
CC Interacts with FAM83D (via N-terminus); in mitotic cells
CC (PubMed:31338967). {ECO:0000269|PubMed:11955436,
CC ECO:0000269|PubMed:1409656, ECO:0000269|PubMed:23902688,
CC ECO:0000269|PubMed:31338967}.
CC -!- INTERACTION:
CC P48729; Q9BXL7: CARD11; NbExp=5; IntAct=EBI-1383726, EBI-7006141;
CC P48729; Q96SW2: CRBN; NbExp=3; IntAct=EBI-1383726, EBI-2510250;
CC P48729; Q5T0W9: FAM83B; NbExp=8; IntAct=EBI-1383726, EBI-2556565;
CC P48729; Q9BQN1: FAM83C; NbExp=6; IntAct=EBI-1383726, EBI-1220251;
CC P48729; Q9H4H8: FAM83D; NbExp=5; IntAct=EBI-1383726, EBI-2556127;
CC P48729; Q2M2I3: FAM83E; NbExp=6; IntAct=EBI-1383726, EBI-21993639;
CC P48729; Q8NEG4: FAM83F; NbExp=7; IntAct=EBI-1383726, EBI-1563144;
CC P48729; A6ND36: FAM83G; NbExp=13; IntAct=EBI-1383726, EBI-1047240;
CC P48729; Q6ZRV2: FAM83H; NbExp=11; IntAct=EBI-1383726, EBI-2556538;
CC P48729; P08238: HSP90AB1; NbExp=2; IntAct=EBI-1383726, EBI-352572;
CC P48729; Q9UDY8: MALT1; NbExp=7; IntAct=EBI-1383726, EBI-1047372;
CC P48729; Q00987: MDM2; NbExp=3; IntAct=EBI-1383726, EBI-389668;
CC P48729; O15151: MDM4; NbExp=2; IntAct=EBI-1383726, EBI-398437;
CC P48729; Q13546: RIPK1; NbExp=5; IntAct=EBI-1383726, EBI-358507;
CC P48729-1; Q9BXL7: CARD11; NbExp=5; IntAct=EBI-10106282, EBI-7006141;
CC P48729-1; Q5S007: LRRK2; NbExp=2; IntAct=EBI-10106282, EBI-5323863;
CC P48729-2; Q00987: MDM2; NbExp=3; IntAct=EBI-2040168, EBI-389668;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1409656}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:1409656}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:1409656}. Nucleus speckle
CC {ECO:0000303|PubMed:18305108}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q8BK63}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q8BK63}. Note=Localizes to the centrosome in
CC interphase cells, and to kinetochore fibers during mitosis. Also
CC recruited to the keratin cytoskeleton (PubMed:23902688).
CC {ECO:0000269|PubMed:1409656, ECO:0000269|PubMed:23902688}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P48729-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48729-2; Sequence=VSP_035455;
CC Name=3;
CC IsoId=P48729-3; Sequence=VSP_055131;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CSNK1A1ID40168ch5q32.html";
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DR EMBL; X80693; CAA56710.1; -; mRNA.
DR EMBL; L37042; AAC41760.1; -; mRNA.
DR EMBL; AF218004; AAG17246.1; -; mRNA.
DR EMBL; AK294942; BAG58018.1; -; mRNA.
DR EMBL; CR542206; CAG47002.1; -; mRNA.
DR EMBL; BT019829; AAV38632.1; -; mRNA.
DR EMBL; BT019830; AAV38633.1; -; mRNA.
DR EMBL; DQ082865; AAY84562.1; -; mRNA.
DR EMBL; AC021078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61767.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61769.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61773.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61774.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61776.1; -; Genomic_DNA.
DR EMBL; BC008717; AAH08717.1; -; mRNA.
DR CCDS; CCDS47303.1; -. [P48729-1]
DR CCDS; CCDS47304.1; -. [P48729-2]
DR CCDS; CCDS64291.1; -. [P48729-3]
DR PIR; A57011; A57011.
DR PIR; S46254; S46254.
DR RefSeq; NP_001020276.1; NM_001025105.2. [P48729-2]
DR RefSeq; NP_001258670.1; NM_001271741.1. [P48729-3]
DR RefSeq; NP_001258671.1; NM_001271742.1.
DR RefSeq; NP_001883.4; NM_001892.5. [P48729-1]
DR PDB; 5FQD; X-ray; 2.45 A; C/F=1-337.
DR PDB; 6GZD; X-ray; 2.28 A; A=1-337.
DR PDBsum; 5FQD; -.
DR PDBsum; 6GZD; -.
DR AlphaFoldDB; P48729; -.
DR SMR; P48729; -.
DR BioGRID; 107836; 293.
DR ComplexPortal; CPX-107; Beta-catenin destruction core complex, variant 5.
DR ComplexPortal; CPX-109; Beta-catenin destruction core complex, variant 1.
DR ComplexPortal; CPX-439; Beta-catenin destruction core complex, variant 3.
DR ComplexPortal; CPX-440; Beta-catenin destruction core complex, variant 4.
DR ComplexPortal; CPX-441; Beta-catenin destruction core complex, variant 7.
DR ComplexPortal; CPX-442; Beta-catenin destruction core complex, variant 6.
DR ComplexPortal; CPX-443; Beta-catenin destruction core complex, variant 8.
DR ComplexPortal; CPX-99; Beta-catenin destruction core complex, variant 2.
DR DIP; DIP-40367N; -.
DR IntAct; P48729; 121.
DR MINT; P48729; -.
DR STRING; 9606.ENSP00000421689; -.
DR BindingDB; P48729; -.
DR ChEMBL; CHEMBL2793; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; P48729; -.
DR GuidetoPHARMACOLOGY; 1995; -.
DR iPTMnet; P48729; -.
DR MetOSite; P48729; -.
DR PhosphoSitePlus; P48729; -.
DR SwissPalm; P48729; -.
DR BioMuta; CSNK1A1; -.
DR DMDM; 31077177; -.
DR EPD; P48729; -.
DR jPOST; P48729; -.
DR MassIVE; P48729; -.
DR MaxQB; P48729; -.
DR PeptideAtlas; P48729; -.
DR PRIDE; P48729; -.
DR ProteomicsDB; 55928; -. [P48729-1]
DR ProteomicsDB; 55929; -. [P48729-2]
DR ProteomicsDB; 68630; -.
DR TopDownProteomics; P48729-1; -. [P48729-1]
DR Antibodypedia; 27829; 664 antibodies from 39 providers.
DR DNASU; 1452; -.
DR Ensembl; ENST00000261798.10; ENSP00000261798.6; ENSG00000113712.19. [P48729-2]
DR Ensembl; ENST00000377843.8; ENSP00000367074.2; ENSG00000113712.19. [P48729-1]
DR Ensembl; ENST00000657001.1; ENSP00000499757.1; ENSG00000113712.19. [P48729-3]
DR GeneID; 1452; -.
DR KEGG; hsa:1452; -.
DR MANE-Select; ENST00000377843.8; ENSP00000367074.2; NM_001892.6; NP_001883.4.
DR UCSC; uc003lqw.3; human. [P48729-1]
DR CTD; 1452; -.
DR DisGeNET; 1452; -.
DR GeneCards; CSNK1A1; -.
DR HGNC; HGNC:2451; CSNK1A1.
DR HPA; ENSG00000113712; Low tissue specificity.
DR MIM; 600505; gene.
DR neXtProt; NX_P48729; -.
DR OpenTargets; ENSG00000113712; -.
DR PharmGKB; PA26951; -.
DR VEuPathDB; HostDB:ENSG00000113712; -.
DR eggNOG; KOG1163; Eukaryota.
DR GeneTree; ENSGT00940000153700; -.
DR HOGENOM; CLU_019279_2_7_1; -.
DR InParanoid; P48729; -.
DR OMA; PAEFPMY; -.
DR OrthoDB; 614259at2759; -.
DR PhylomeDB; P48729; -.
DR TreeFam; TF354246; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; P48729; -.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-HSA-5339716; Signaling by GSK3beta mutants.
DR Reactome; R-HSA-5358747; CTNNB1 S33 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358749; CTNNB1 S37 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358751; CTNNB1 S45 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358752; CTNNB1 T41 mutants aren't phosphorylated.
DR Reactome; R-HSA-5467337; APC truncation mutants have impaired AXIN binding.
DR Reactome; R-HSA-5467340; AXIN missense mutants destabilize the destruction complex.
DR Reactome; R-HSA-5467348; Truncations of AMER1 destabilize the destruction complex.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5635838; Activation of SMO.
DR Reactome; R-HSA-9694631; Maturation of nucleoprotein.
DR SignaLink; P48729; -.
DR SIGNOR; P48729; -.
DR BioGRID-ORCS; 1452; 629 hits in 1127 CRISPR screens.
DR ChiTaRS; CSNK1A1; human.
DR GeneWiki; Casein_kinase_1,_alpha_1; -.
DR GenomeRNAi; 1452; -.
DR Pharos; P48729; Tchem.
DR PRO; PR:P48729; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P48729; protein.
DR Bgee; ENSG00000113712; Expressed in stromal cell of endometrium and 200 other tissues.
DR ExpressionAtlas; P48729; baseline and differential.
DR Genevisible; P48729; HS.
DR GO; GO:0030877; C:beta-catenin destruction complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007030; P:Golgi organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:WormBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:FlyBase.
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; IMP:ParkinsonsUK-UCL.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR GO; GO:0016055; P:Wnt signaling pathway; TAS:Reactome.
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; Acetylation; Alternative splicing; ATP-binding; Cell cycle;
KW Cell division; Cell projection; Centromere; Chromosome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Kinase; Kinetochore; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..337
FT /note="Casein kinase I isoform alpha"
FT /id="PRO_0000192822"
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:19369195,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 152
FT /note="K -> KCLESPVGKRKRSMTVSTSQDPSFSGLNQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_035455"
FT VAR_SEQ 324..335
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15498874"
FT /id="VSP_055131"
FT VARIANT 297
FT /note="D -> H (in a breast pleomorphic lobular carcinoma
FT sample; somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042073"
FT CONFLICT 45
FT /note="V -> L (in Ref. 1; CAA56710)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="P -> T (in Ref. 6; AAV38633)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="S -> A (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="T -> TK (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="Q -> K (in Ref. 10; AAH08717)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="K -> E (in Ref. 7; AAY84562)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="T -> S (in Ref. 1; CAA56710 and 6; AAV38632/
FT AAV38633)"
FT /evidence="ECO:0000305"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:6GZD"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:6GZD"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:6GZD"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:6GZD"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:6GZD"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:6GZD"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:6GZD"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:6GZD"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:6GZD"
FT HELIX 110..129
FT /evidence="ECO:0007829|PDB:6GZD"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:6GZD"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6GZD"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:6GZD"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6GZD"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:6GZD"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:6GZD"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:6GZD"
FT HELIX 200..216
FT /evidence="ECO:0007829|PDB:6GZD"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:6GZD"
FT HELIX 229..242
FT /evidence="ECO:0007829|PDB:6GZD"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:6GZD"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:6GZD"
FT HELIX 254..265
FT /evidence="ECO:0007829|PDB:6GZD"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:6GZD"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:6GZD"
FT MOD_RES P48729-2:156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES P48729-3:321
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
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
