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Casein kinase I isoform delta (CKI-delta) (CKId) (EC 2.7.11.1) (Tau-protein kinase CSNK1D) (EC 2.7.11.26)

 KC1D_HUMAN              Reviewed;         415 AA.
P48730; A2I2P2; Q96KZ6; Q9BTN5;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
27-JAN-2003, sequence version 2.
12-SEP-2018, entry version 191.
RecName: Full=Casein kinase I isoform delta;
Short=CKI-delta;
Short=CKId;
EC=2.7.11.1;
AltName: Full=Tau-protein kinase CSNK1D;
EC=2.7.11.26;
Name=CSNK1D; Synonyms=HCKID;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=8786104; DOI=10.1006/geno.1996.0091;
Kusuda J., Hidari N., Hidari M., Hashimoto K.;
"Sequence analysis of the cDNA for the human casein kinase I delta
(CSNK1D) gene and its chromosomal localization.";
Genomics 32:140-143(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Hematopoietic stem cell;
PubMed=15070676; DOI=10.1182/blood-2003-08-2768;
Okamura A., Iwata N., Nagata A., Tamekane A., Shimoyama M., Gomyo H.,
Yakushijin K., Urahama N., Hamaguchi M., Fukui C., Chihara K., Ito M.,
Matsui T.;
"Involvement of casein kinase Iepsilon in cytokine-induced
granulocytic differentiation.";
Blood 103:2997-3004(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Placenta, and Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
ACTIVITY REGULATION, AND AUTOPHOSPHORYLATION.
PubMed=9632646; DOI=10.1074/jbc.273.26.15980;
Rivers A., Gietzen K.F., Vielhaber E., Virshup D.M.;
"Regulation of casein kinase I epsilon and casein kinase I delta by an
in vivo futile phosphorylation cycle.";
J. Biol. Chem. 273:15980-15984(1998).
[7]
FUNCTION AS TP53 KINASE.
PubMed=10606744; DOI=10.1016/S0014-5793(99)01647-6;
Dumaz N., Milne D.M., Meek D.W.;
"Protein kinase CK1 is a p53-threonine 18 kinase which requires prior
phosphorylation of serine 15.";
FEBS Lett. 463:312-316(1999).
[8]
INTERACTION WITH TUBULINS, AND SUBCELLULAR LOCATION.
PubMed=10826492; DOI=10.1078/S0171-9335(04)70027-8;
Behrend L., Stoeter M., Kurth M., Rutter G., Heukeshoven J.,
Deppert W., Knippschild U.;
"Interaction of casein kinase 1 delta (CK1delta) with post-Golgi
structures, microtubules and the spindle apparatus.";
Eur. J. Cell Biol. 79:240-251(2000).
[9]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-38 AND THR-176.
PubMed=11161704; DOI=10.1006/excr.2000.5100;
Milne D.M., Looby P., Meek D.W.;
"Catalytic activity of protein kinase CK1 delta (casein kinase 1delta)
is essential for its normal subcellular localization.";
Exp. Cell Res. 263:43-54(2001).
[10]
INTERACTION WITH PER1 AND PER2.
PubMed=11165242; DOI=10.1016/S0014-5793(00)02434-0;
Camacho F., Cilio M., Guo Y., Virshup D.M., Patel K., Khorkova O.,
Styren S., Morse B., Yao Z., Keesler G.A.;
"Human casein kinase Idelta phosphorylation of human circadian clock
proteins period 1 and 2.";
FEBS Lett. 489:159-165(2001).
[11]
FUNCTION AS CONNEXIN-43/GJA1 KINASE, AND INTERACTION WITH
CONNEXIN-43/GJA1.
PubMed=12270943; DOI=10.1074/jbc.M209427200;
Cooper C.D., Lampe P.D.;
"Casein kinase 1 regulates connexin-43 gap junction assembly.";
J. Biol. Chem. 277:44962-44968(2002).
[12]
INTERACTION WITH AKAP9/AKAP450, AND SUBCELLULAR LOCATION.
PubMed=12270714; DOI=10.1016/S0022-2836(02)00857-4;
Sillibourne J.E., Milne D.M., Takahashi M., Ono Y., Meek D.W.;
"Centrosomal anchoring of the protein kinase CK1delta mediated by
attachment to the large, coiled-coil scaffolding protein CG-
NAP/AKAP450.";
J. Mol. Biol. 322:785-797(2002).
[13]
FUNCTION AS MAPT/TAU KINASE, ACTIVITY REGULATION, AND INTERACTION WITH
MAPT/TAU.
PubMed=14761950; DOI=10.1074/jbc.M314116200;
Li G., Yin H., Kuret J.;
"Casein kinase 1 delta phosphorylates tau and disrupts its binding to
microtubules.";
J. Biol. Chem. 279:15938-15945(2004).
[14]
FUNCTION IN MITOTIC SPINDLE FORMATION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND ACTIVITY REGULATION.
PubMed=16027726; DOI=10.1038/sj.onc.1208941;
Stoeter M., Bamberger A.-M., Aslan B., Kurth M., Speidel D.,
Loening T., Frank H.-G., Kaufmann P., Loehler J., Henne-Bruns D.,
Deppert W., Knippschild U.;
"Inhibition of casein kinase I delta alters mitotic spindle formation
and induces apoptosis in trophoblast cells.";
Oncogene 24:7964-7975(2005).
[15]
CATALYTIC ACTIVITY, AND INTERACTION WITH DBNDD2.
PubMed=16618118; DOI=10.1021/bi052354e;
Yin H., Laguna K.A., Li G., Kuret J.;
"Dysbindin structural homologue CK1BP is an isoform-selective binding
partner of human casein kinase-1.";
Biochemistry 45:5297-5308(2006).
[16]
FUNCTION AS PKD2 KINASE.
PubMed=17962809; DOI=10.1038/sj.emboj.7601891;
von Blume J., Knippschild U., Dequiedt F., Giamas G., Beck A.,
Auer A., Van Lint J., Adler G., Seufferlein T.;
"Phosphorylation at Ser244 by CK1 determines nuclear localization and
substrate targeting of PKD2.";
EMBO J. 26:4619-4633(2007).
[17]
FUNCTION AS MAPT/TAU KINASE.
PubMed=17562708; DOI=10.1074/jbc.M703269200;
Hanger D.P., Byers H.L., Wray S., Leung K.-Y., Saxton M.J.,
Seereeram A., Reynolds C.H., Ward M.A., Anderton B.H.;
"Novel phosphorylation sites in tau from Alzheimer brain support a
role for casein kinase 1 in disease pathogenesis.";
J. Biol. Chem. 282:23645-23654(2007).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331 AND SER-384, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[21]
ACTIVITY REGULATION.
PubMed=19591487; DOI=10.1021/jm9005127;
Peifer C., Abadleh M., Bischof J., Hauser D., Schattel V., Hirner H.,
Knippschild U., Laufer S.;
"3,4-Diaryl-isoxazoles and -imidazoles as potent dual inhibitors of
p38alpha mitogen activated protein kinase and casein kinase 1delta.";
J. Med. Chem. 52:7618-7630(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[23]
FUNCTION AS TOP2A KINASE, AND ACTIVITY REGULATION.
PubMed=19043076; DOI=10.1093/nar/gkn934;
Grozav A.G., Chikamori K., Kozuki T., Grabowski D.R., Bukowski R.M.,
Willard B., Kinter M., Andersen A.H., Ganapathi R., Ganapathi M.K.;
"Casein kinase I delta/epsilon phosphorylates topoisomerase IIalpha at
serine-1106 and modulates DNA cleavage activity.";
Nucleic Acids Res. 37:382-392(2009).
[24]
FUNCTION AS AIB1/NCOA3 AND ESR1 KINASE, AND INTERACTION WITH
AIB1/NCOA3 AND ESR1.
PubMed=19339517; DOI=10.1093/nar/gkp136;
Giamas G., Castellano L., Feng Q., Knippschild U., Jacob J.,
Thomas R.S., Coombes R.C., Smith C.L., Jiao L.R., Stebbing J.;
"CK1delta modulates the transcriptional activity of ERalpha via AIB1
in an estrogen-dependent manner and regulates ERalpha-AIB1
interactions.";
Nucleic Acids Res. 37:3110-3123(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[26]
FUNCTION AS DCK KINASE.
PubMed=20637175; DOI=10.1016/j.abb.2010.07.009;
Smal C., Vertommen D., Amsailale R., Arts A., Degand H., Morsomme P.,
Rider M.H., Neste E.V., Bontemps F.;
"Casein kinase 1delta activates human recombinant deoxycytidine kinase
by Ser-74 phosphorylation, but is not involved in the in vivo
regulation of its activity.";
Arch. Biochem. Biophys. 502:44-52(2010).
[27]
FUNCTION AS P53/TP53 KINASE, AND GENE FAMILY.
PubMed=20041275; DOI=10.1007/s00018-009-0236-7;
Venerando A., Marin O., Cozza G., Bustos V.H., Sarno S., Pinna L.A.;
"Isoform specific phosphorylation of p53 by protein kinase CK1.";
Cell. Mol. Life Sci. 67:1105-1118(2010).
[28]
FUNCTION AS YAP1 KINASE.
PubMed=20048001; DOI=10.1101/gad.1843810;
Zhao B., Li L., Tumaneng K., Wang C.-Y., Guan K.-L.;
"A coordinated phosphorylation by Lats and CK1 regulates YAP stability
through SCF(beta-TRCP).";
Genes Dev. 24:72-85(2010).
[29]
FUNCTION AS HIF1A KINASE.
PubMed=20699359; DOI=10.1242/jcs.068122;
Kalousi A., Mylonis I., Politou A.S., Chachami G., Paraskeva E.,
Simos G.;
"Casein kinase 1 regulates human hypoxia-inducible factor HIF-1.";
J. Cell Sci. 123:2976-2986(2010).
[30]
FUNCTION IN CIRCADIAN RHYTHMS, AND ACTIVITY REGULATION.
PubMed=20696890; DOI=10.1073/pnas.1005101107;
Meng Q.-J., Maywood E.S., Bechtold D.A., Lu W.-Q., Li J., Gibbs J.E.,
Dupre S.M., Chesham J.E., Rajamohan F., Knafels J., Sneed B.,
Zawadzke L.E., Ohren J.F., Walton K.M., Wager T.T., Hastings M.H.,
Loudon A.S.I.;
"Entrainment of disrupted circadian behavior through inhibition of
casein kinase 1 (CK1) enzymes.";
Proc. Natl. Acad. Sci. U.S.A. 107:15240-15245(2010).
[31]
FUNCTION IN CIRCADIAN RHYTHMS, AND ACTIVITY REGULATION.
PubMed=20407760; DOI=10.1007/s00213-010-1860-5;
Sprouse J., Reynolds L., Kleiman R., Tate B., Swanson T.A.,
Pickard G.E.;
"Chronic treatment with a selective inhibitor of casein kinase I
delta/epsilon yields cumulative phase delays in circadian rhythms.";
Psychopharmacology 210:569-576(2010).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[34]
FUNCTION AS EIF6 KINASE, AND ACTIVITY REGULATION.
PubMed=21084295; DOI=10.1074/jbc.M110.188565;
Biswas A., Mukherjee S., Das S., Shields D., Chow C.W., Maitra U.;
"Opposing action of casein kinase 1 and calcineurin in nucleo-
cytoplasmic shuttling of mammalian translation initiation factor
eIF6.";
J. Biol. Chem. 286:3129-3138(2011).
[35]
FUNCTION AS DVL2 AND DVL3 KINASE, ACTIVITY REGULATION, AND SUBCELLULAR
LOCATION.
PubMed=21422228; DOI=10.1083/jcb.201011111;
Greer Y.E., Rubin J.S.;
"Casein kinase 1 delta functions at the centrosome to mediate Wnt-3a-
dependent neurite outgrowth.";
J. Cell Biol. 192:993-1004(2011).
[36]
ACTIVITY REGULATION, AND AUTOPHOSPHORYLATION.
PubMed=21258417; DOI=10.1038/onc.2010.627;
Cheong J.K., Nguyen T.H., Wang H., Tan P., Voorhoeve P.M., Lee S.H.,
Virshup D.M.;
"IC261 induces cell cycle arrest and apoptosis of human cancer cells
via CK1delta/epsilon and Wnt/beta-catenin independent inhibition of
mitotic spindle formation.";
Oncogene 30:2558-2569(2011).
[37]
REVIEW ON CIRCADIAN RHYTHMS, AND GENE FAMILY.
PubMed=21145983; DOI=10.1016/j.biocel.2010.12.004;
Cheong J.K., Virshup D.M.;
"Casein kinase 1: Complexity in the family.";
Int. J. Biochem. Cell Biol. 43:465-469(2011).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; SER-331; SER-382;
SER-384 AND SER-407, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[40]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=9761932; DOI=10.1107/S0907444997011724;
Longenecker K.L., Roach P.J., Hurley T.D.;
"Crystallographic studies of casein kinase I delta toward a structural
understanding of auto-inhibition.";
Acta Crystallogr. D 54:473-475(1998).
[41]
X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 1-294 IN COMPLEX WITH
INHIBITOR.
PubMed=22168824; DOI=10.1021/jm201387s;
Long A., Zhao H., Huang X.;
"Structural basis for the interaction between casein kinase 1 delta
and a potent and selective inhibitor.";
J. Med. Chem. 55:956-960(2012).
[42]
X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 1-294 IN COMPLEX WITH
INHIBITOR.
PubMed=23106386; DOI=10.1021/jm301336n;
Long A.M., Zhao H., Huang X.;
"Structural basis for the potent and selective inhibition of casein
kinase 1 epsilon.";
J. Med. Chem. 55:10307-10311(2012).
[43]
VARIANT FASPS2 ALA-44.
PubMed=15800623; DOI=10.1038/nature03453;
Xu Y., Padiath Q.S., Shapiro R.E., Jones C.R., Wu S.C., Saigoh N.,
Saigoh K., Ptacek L.J., Fu Y.H.;
"Functional consequences of a CKIdelta mutation causing familial
advanced sleep phase syndrome.";
Nature 434:640-644(2005).
[44]
VARIANT [LARGE SCALE ANALYSIS] CYS-97.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[45]
VARIANTS [LARGE SCALE ANALYSIS] CYS-97 AND ALA-401.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[46]
VARIANTS FASPS2 ALA-44 AND ARG-46, CHARACTERIZATION OF VARIANTS FASPS2
ALA-44 AND ARG-46, FUNCTION, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=23636092; DOI=10.1126/scitranslmed.3005784;
Brennan K.C., Bates E.A., Shapiro R.E., Zyuzin J., Hallows W.C.,
Huang Y., Lee H.Y., Jones C.R., Fu Y.H., Charles A.C., Ptacek L.J.;
"Casein kinase idelta mutations in familial migraine and advanced
phase.";
Sci. Transl. Med. 5:183ra56-183ra56(2013).
-!- FUNCTION: Essential serine/threonine-protein kinase that regulates
diverse cellular growth and survival processes including Wnt
signaling, DNA repair and circadian rhythms. It can phosphorylate
a large number of proteins. Casein kinases are operationally
defined by their preferential utilization of acidic proteins such
as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A,
SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3,
ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central
component of the circadian clock. In balance with PP1, determines
the circadian period length through the regulation of the speed
and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1
and PER2 nuclear transport and degradation. YAP1 phosphorylation
promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated
ubiquitination and subsequent degradation. DNMT1 phosphorylation
reduces its DNA-binding activity. Phosphorylation of ESR1 and
AIB1/NCOA3 stimulates their activity and coactivation.
Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway
that controls neurite outgrowth. EIF6 phosphorylation promotes its
nuclear export. Triggers down-regulation of dopamine receptors in
the forebrain. Activates DCK in vitro by phosphorylation. TOP2A
phosphorylation favors DNA cleavable complex formation. May
regulate the formation of the mitotic spindle apparatus in
extravillous trophoblast. Modulates connexin-43/GJA1 gap junction
assembly by phosphorylation. Probably involved in lymphocyte
physiology. Regulates fast synaptic transmission mediated by
glutamate. {ECO:0000269|PubMed:10606744,
ECO:0000269|PubMed:12270943, ECO:0000269|PubMed:14761950,
ECO:0000269|PubMed:16027726, ECO:0000269|PubMed:17562708,
ECO:0000269|PubMed:17962809, ECO:0000269|PubMed:19043076,
ECO:0000269|PubMed:19339517, ECO:0000269|PubMed:20041275,
ECO:0000269|PubMed:20048001, ECO:0000269|PubMed:20407760,
ECO:0000269|PubMed:20637175, ECO:0000269|PubMed:20696890,
ECO:0000269|PubMed:20699359, ECO:0000269|PubMed:21084295,
ECO:0000269|PubMed:21422228, ECO:0000269|PubMed:23636092}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- CATALYTIC ACTIVITY: ATP + [tau protein] = ADP + [tau protein]
phosphate.
-!- ACTIVITY REGULATION: Exhibits substrate-dependent heparin
activation. Drug-mediated inhibition leads to a delay of the
oscillations with the magnitude of this effect dependent upon the
timing of drug administration. Inhibited by phosphorylation.
Repressed by 3-[(2,4,6-trimethoxyphenyl)methylidenyl]-indolin-2-
one (IC261), N-(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamide
(CKI-7), 4-[4-(2,3-dihydro-benzo[1,4]dioxin-6-yl)-5-pyridin-2-yl-
1H-imidazol-2-yl]benzamide (D4476), 3,4-diaryl-isoxazoles and
-imidazoles, and 4-(3-cyclohexyl-5-(4-fluoro-phenyl)-3H-imidazol-
4-yl) pyrimidin-2-ylamine (PF670462, PF670).
{ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:16027726,
ECO:0000269|PubMed:19043076, ECO:0000269|PubMed:19591487,
ECO:0000269|PubMed:20407760, ECO:0000269|PubMed:20696890,
ECO:0000269|PubMed:21084295, ECO:0000269|PubMed:21258417,
ECO:0000269|PubMed:21422228, ECO:0000269|PubMed:9632646}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=36.5 uM for alpha-casein {ECO:0000269|PubMed:23636092};
KM=635.8 uM for PER2 peptide {ECO:0000269|PubMed:23636092};
KM=180.6 uM for ATP {ECO:0000269|PubMed:23636092};
Note=Maximal velocity nearly identical for the reactions with
alpha-casein and PER2 peptide.;
-!- SUBUNIT: Binds to DNMT1 and MAP1A (By similarity). Monomer.
Component of the circadian core oscillator, which includes the CRY
proteins, CLOCK, or NPAS2, ARTNL/BMAL1 or ARTNL2/BMAL2, CSNK1D
and/or CSNK1E, TIMELESS and the PER proteins. Interacts directly
with PER1 and PER2 which may lead to their degradation. Interacts
with MAPT/TAU, SNAPIN, DBNDD2, AIB1/NCOA3 and ESR1. AKAP9/AKAP450
binding promotes centrosomal subcellular location. Binds to
tubulins in mitotic cells upon DNA damage. {ECO:0000250,
ECO:0000269|PubMed:10826492, ECO:0000269|PubMed:11165242,
ECO:0000269|PubMed:12270714, ECO:0000269|PubMed:12270943,
ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:16618118,
ECO:0000269|PubMed:19339517, ECO:0000269|PubMed:22168824,
ECO:0000269|PubMed:23106386}.
-!- INTERACTION:
Q60838:Dvl2 (xeno); NbExp=2; IntAct=EBI-751621, EBI-641940;
Q92997:DVL3; NbExp=4; IntAct=EBI-751621, EBI-739789;
Q96LR2:LURAP1; NbExp=4; IntAct=EBI-751621, EBI-741355;
Q00987:MDM2; NbExp=6; IntAct=EBI-751621, EBI-389668;
O15055:PER2; NbExp=3; IntAct=EBI-751621, EBI-1054296;
Q9C026:TRIM9; NbExp=3; IntAct=EBI-751621, EBI-720828;
Q8IUH5:ZDHHC17; NbExp=3; IntAct=EBI-9087876, EBI-524753;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome. Cytoplasm, perinuclear
region. Cell membrane. Cytoplasm, cytoskeleton, spindle. Golgi
apparatus. Note=Localized at mitotic spindle microtubules, and at
the centrosomes and interphase in interphase cells. Recruited to
the spindle apparatus and the centrosomes in response to DNA-
damage. Correct subcellular localization requires kinase activity.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P48730-1; Sequence=Displayed;
Name=2;
IsoId=P48730-2; Sequence=VSP_010253;
-!- TISSUE SPECIFICITY: Expressed in all tissues examined, including
brain, heart, lung, liver, pancreas, kidney, placenta and skeletal
muscle. However, kinase activity is not uniform, with highest
kinase activity in splenocytes. In blood, highly expressed in
hemopoietic cells and mature granulocytes. Also found in monocytes
and lymphocytes. {ECO:0000269|PubMed:15070676,
ECO:0000269|PubMed:16027726}.
-!- DEVELOPMENTAL STAGE: Highly present in extravillous trophoblast
cells, which are present at the placenta implantation site and
invade the decidua and decidual vessels.
{ECO:0000269|PubMed:16027726}.
-!- PTM: Autophosphorylated on serine and threonine residues; this
autophosphorylation represses activity. Reactivated by
phosphatase-mediated dephosphorylation. May be dephosphorylated by
PP1.
-!- DISEASE: Advanced sleep phase syndrome, familial, 2 (FASPS2)
[MIM:615224]: A disorder characterized by very early sleep onset
and offset. Individuals are 'morning larks' with a 4 hours advance
of the sleep, temperature and melatonin rhythms.
{ECO:0000269|PubMed:15800623, ECO:0000269|PubMed:23636092}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: May be involved in Alzheimer disease by
phosphorylating MAPT/TAU. {ECO:0000305|PubMed:17562708}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
-!- CAUTION: Was shown to phosphorylate and activate DCK in vitro but
probably not in vivo. {ECO:0000305|PubMed:20637175}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U29171; AAC50807.1; -; mRNA.
EMBL; U31285; AAC50808.1; -; mRNA.
EMBL; AB091044; BAC10903.1; -; mRNA.
EMBL; AK291758; BAF84447.1; -; mRNA.
EMBL; EF015900; ABM64211.1; -; Genomic_DNA.
EMBL; BC003558; AAH03558.1; -; mRNA.
EMBL; BC015775; AAH15775.1; -; mRNA.
CCDS; CCDS11805.1; -. [P48730-1]
CCDS; CCDS11806.1; -. [P48730-2]
PIR; G01876; G01876.
RefSeq; NP_001884.2; NM_001893.4. [P48730-1]
RefSeq; NP_620693.1; NM_139062.2. [P48730-2]
UniGene; Hs.631725; -.
PDB; 3UYS; X-ray; 2.30 A; A/B/C/D=1-294.
PDB; 3UYT; X-ray; 2.00 A; A/B/C/D=1-294.
PDB; 3UZP; X-ray; 1.94 A; A/B=1-294.
PDB; 4HGT; X-ray; 1.80 A; A/B=1-294.
PDB; 4HNF; X-ray; 2.07 A; A/B=1-294.
PDB; 4KB8; X-ray; 1.95 A; A/B/C/D=3-317.
PDB; 4KBA; X-ray; 1.98 A; A/B/C/D=3-317.
PDB; 4KBC; X-ray; 1.98 A; A/B=1-317.
PDB; 4KBK; X-ray; 2.10 A; A/B/C/D=3-317.
PDB; 4TN6; X-ray; 2.41 A; A/B=1-301.
PDB; 4TW9; X-ray; 2.40 A; A/B=1-295.
PDB; 4TWC; X-ray; 1.70 A; A/B=1-295.
PDB; 5IH4; X-ray; 1.90 A; A=1-294.
PDB; 5IH5; X-ray; 2.25 A; A=1-294.
PDB; 5IH6; X-ray; 2.30 A; A=1-294.
PDB; 5MQV; X-ray; 2.15 A; A/B/C/D/E/F=1-294.
PDB; 5OKT; X-ray; 2.13 A; A/B/C/D=1-294.
PDB; 5W4W; X-ray; 1.99 A; A/B/C/D=3-317.
PDBsum; 3UYS; -.
PDBsum; 3UYT; -.
PDBsum; 3UZP; -.
PDBsum; 4HGT; -.
PDBsum; 4HNF; -.
PDBsum; 4KB8; -.
PDBsum; 4KBA; -.
PDBsum; 4KBC; -.
PDBsum; 4KBK; -.
PDBsum; 4TN6; -.
PDBsum; 4TW9; -.
PDBsum; 4TWC; -.
PDBsum; 5IH4; -.
PDBsum; 5IH5; -.
PDBsum; 5IH6; -.
PDBsum; 5MQV; -.
PDBsum; 5OKT; -.
PDBsum; 5W4W; -.
ProteinModelPortal; P48730; -.
SMR; P48730; -.
BioGrid; 107837; 95.
DIP; DIP-39735N; -.
IntAct; P48730; 45.
MINT; P48730; -.
STRING; 9606.ENSP00000324464; -.
BindingDB; P48730; -.
ChEMBL; CHEMBL2828; -.
GuidetoPHARMACOLOGY; 1997; -.
iPTMnet; P48730; -.
PhosphoSitePlus; P48730; -.
BioMuta; CSNK1D; -.
DMDM; 27923980; -.
EPD; P48730; -.
MaxQB; P48730; -.
PaxDb; P48730; -.
PeptideAtlas; P48730; -.
PRIDE; P48730; -.
ProteomicsDB; 55930; -.
ProteomicsDB; 55931; -. [P48730-2]
TopDownProteomics; P48730-1; -. [P48730-1]
DNASU; 1453; -.
Ensembl; ENST00000314028; ENSP00000324464; ENSG00000141551. [P48730-1]
Ensembl; ENST00000392334; ENSP00000376146; ENSG00000141551. [P48730-2]
GeneID; 1453; -.
KEGG; hsa:1453; -.
UCSC; uc002kei.4; human. [P48730-1]
CTD; 1453; -.
DisGeNET; 1453; -.
EuPathDB; HostDB:ENSG00000141551.14; -.
GeneCards; CSNK1D; -.
HGNC; HGNC:2452; CSNK1D.
HPA; CAB015410; -.
MalaCards; CSNK1D; -.
MIM; 600864; gene.
MIM; 615224; phenotype.
neXtProt; NX_P48730; -.
OpenTargets; ENSG00000141551; -.
Orphanet; 164736; Familial advanced sleep-phase syndrome.
PharmGKB; PA26952; -.
eggNOG; KOG1164; Eukaryota.
eggNOG; ENOG410XPGP; LUCA.
GeneTree; ENSGT00920000148982; -.
HOGENOM; HOG000182055; -.
HOVERGEN; HBG000176; -.
InParanoid; P48730; -.
KO; K08959; -.
PhylomeDB; P48730; -.
TreeFam; TF300544; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-204005; COPII-mediated vesicle transport.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
SABIO-RK; P48730; -.
SignaLink; P48730; -.
SIGNOR; P48730; -.
ChiTaRS; CSNK1D; human.
GeneWiki; CSNK1D; -.
GenomeRNAi; 1453; -.
PRO; PR:P48730; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000141551; Expressed in 227 organ(s), highest expression level in adenohypophysis.
CleanEx; HS_CSNK1D; -.
ExpressionAtlas; P48730; baseline and differential.
Genevisible; P48730; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005819; C:spindle; IDA:UniProtKB.
GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0042277; F:peptide binding; IEA:Ensembl.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0006897; P:endocytosis; IBA:GO_Central.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0007030; P:Golgi organization; IMP:SYSCILIA_CCNET.
GO; GO:0007020; P:microtubule nucleation; IMP:SYSCILIA_CCNET.
GO; GO:1905515; P:non-motile cilium assembly; IMP:SYSCILIA_CCNET.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; ISS:ParkinsonsUK-UCL.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:BHF-UCL.
GO; GO:1905426; P:positive regulation of Wnt-mediated midbrain dopaminergic neuron differentiation; IC:ParkinsonsUK-UCL.
GO; GO:0071539; P:protein localization to centrosome; IMP:SYSCILIA_CCNET.
GO; GO:0061512; P:protein localization to cilium; IMP:SYSCILIA_CCNET.
GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:SYSCILIA_CCNET.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0051225; P:spindle assembly; IDA:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Biological rhythms;
Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton;
Disease mutation; Golgi apparatus; Kinase; Membrane; Methylation;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Wnt signaling pathway.
CHAIN 1 415 Casein kinase I isoform delta.
/FTId=PRO_0000192833.
DOMAIN 9 277 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 15 23 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 278 364 Centrosomal localization signal (CLS).
REGION 317 342 Autoinhibitory. {ECO:0000250}.
ACT_SITE 128 128 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 38 38 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 331 331 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 370 370 Phosphoserine.
{ECO:0000250|UniProtKB:Q06486}.
MOD_RES 375 375 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9DC28}.
MOD_RES 382 382 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 383 383 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 384 384 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 407 407 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
VAR_SEQ 400 415 IPGRVASSGLQSVVHR -> NSIPFEHHGK (in
isoform 2). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_010253.
VARIANT 44 44 T -> A (in FASPS2; strongly reduces
kinase activity; dbSNP:rs104894561).
{ECO:0000269|PubMed:15800623,
ECO:0000269|PubMed:23636092}.
/FTId=VAR_029075.
VARIANT 46 46 H -> R (in FASPS2; strongly reduces
kinase activity; dbSNP:rs397514693).
{ECO:0000269|PubMed:23636092}.
/FTId=VAR_069801.
VARIANT 97 97 S -> C (in breast cancer samples;
infiltrating ductal carcinoma; somatic
mutation). {ECO:0000269|PubMed:16959974,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_036451.
VARIANT 401 401 P -> A (in dbSNP:rs56124628).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042081.
MUTAGEN 38 38 K->M: Impaired kinase activity and
abnormal subcellular localization with
exclusive accumulation to the nucleus.
{ECO:0000269|PubMed:11161704}.
MUTAGEN 176 176 T->I: Impaired kinase activity and
abnormal subcellular localization with
exclusive accumulation to the nucleus.
{ECO:0000269|PubMed:11161704}.
CONFLICT 330 330 A -> D (in Ref. 1; AAC50807).
{ECO:0000305}.
STRAND 3 5 {ECO:0000244|PDB:4TWC}.
TURN 6 8 {ECO:0000244|PDB:4TWC}.
STRAND 9 16 {ECO:0000244|PDB:4TWC}.
STRAND 21 28 {ECO:0000244|PDB:4TWC}.
TURN 29 32 {ECO:0000244|PDB:4TWC}.
STRAND 33 41 {ECO:0000244|PDB:4TWC}.
STRAND 44 46 {ECO:0000244|PDB:4TWC}.
HELIX 49 59 {ECO:0000244|PDB:4TWC}.
STRAND 68 74 {ECO:0000244|PDB:4TWC}.
STRAND 77 83 {ECO:0000244|PDB:4TWC}.
HELIX 89 95 {ECO:0000244|PDB:4TWC}.
TURN 96 98 {ECO:0000244|PDB:4TWC}.
HELIX 102 121 {ECO:0000244|PDB:4TWC}.
HELIX 131 133 {ECO:0000244|PDB:4TWC}.
STRAND 134 136 {ECO:0000244|PDB:4TWC}.
HELIX 139 141 {ECO:0000244|PDB:4TWC}.
STRAND 145 147 {ECO:0000244|PDB:4TWC}.
STRAND 154 157 {ECO:0000244|PDB:4TWC}.
TURN 159 161 {ECO:0000244|PDB:4TWC}.
HELIX 177 179 {ECO:0000244|PDB:4TWC}.
HELIX 182 185 {ECO:0000244|PDB:4TWC}.
HELIX 192 208 {ECO:0000244|PDB:4TWC}.
TURN 212 215 {ECO:0000244|PDB:4KB8}.
STRAND 219 221 {ECO:0000244|PDB:5OKT}.
HELIX 223 234 {ECO:0000244|PDB:4TWC}.
HELIX 237 240 {ECO:0000244|PDB:4TWC}.
TURN 241 243 {ECO:0000244|PDB:4TWC}.
HELIX 247 257 {ECO:0000244|PDB:4TWC}.
HELIX 266 279 {ECO:0000244|PDB:4TWC}.
TURN 289 292 {ECO:0000244|PDB:4TWC}.
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


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EIAAB11065 130 kDa diacylglycerol kinase,DAG kinase delta,DGKD,DGK-delta,Diacylglycerol kinase delta,Diglyceride kinase delta,Homo sapiens,Human,KIAA0145
CSB-EL006067RA Rat casein kinase 1, delta (CSNK1D) ELISA kit, Species Rat, Sample Type serum, plasma 96T
E10128r Rat ELISA Kit FOR Casein kinase I isoform delta 96T
AHP796 GOAT ANTI HUMAN CASEIN KINASE 1 DELTA (C_TERMINAL), Product Type Polyclonal Antibody, Specificity CASEIN KINASE 1 DELTA , Target Species Human, Host Goat, Format Purified, Isotypes Polyclonal Ig 0.1 ml


 

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