ID KC1G2_HUMAN Reviewed; 415 AA.
AC P78368; B5BU42; O00704; Q8WUB1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 27-MAR-2024, entry version 216.
DE RecName: Full=Casein kinase I isoform gamma-2;
DE Short=CKI-gamma 2;
DE EC=2.7.11.1;
GN Name=CSNK1G2; Synonyms=CK1G2;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=9403068; DOI=10.1006/geno.1997.4991;
RA Kitabayashi A.N., Kusuda J., Hirai M., Hashimoto K.;
RT "Cloning and chromosomal mapping of human casein kinase I gamma 2
RT (CSNK1G2).";
RL Genomics 46:133-137(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Muscle;
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 [7]
RP FUNCTION AS MTA1 KINASE, INTERACTION WITH MTA1, SUBCELLULAR LOCATION, AND
RP ACTIVITY REGULATION.
RX PubMed=15077195; DOI=10.1038/sj.onc.1207569;
RA Mishra S.K., Yang Z., Mazumdar A., Talukder A.H., Larose L., Kumar R.;
RT "Metastatic tumor antigen 1 short form (MTA1s) associates with casein
RT kinase I-gamma2, an estrogen-responsive kinase.";
RL Oncogene 23:4422-4429(2004).
RN [8]
RP FUNCTION IN PER1 STABILITY.
RX PubMed=15917222; DOI=10.1074/jbc.m502862200;
RA Shirogane T., Jin J., Ang X.L., Harper J.W.;
RT "SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-
RT dependent degradation of the mammalian period-1 (Per1) protein.";
RL J. Biol. Chem. 280:26863-26872(2005).
RN [9]
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 [10]
RP FUNCTION AS SMAD3 KINASE, INTERACTION WITH SMAD3, AND PHOSPHORYLATION.
RX PubMed=18794808; DOI=10.1038/onc.2008.337;
RA Guo X., Waddell D.S., Wang W., Wang Z., Liberati N.T., Yong S., Liu X.,
RA Wang X.-F.;
RT "Ligand-dependent ubiquitination of Smad3 is regulated by casein kinase 1
RT gamma 2, an inhibitor of TGF-beta signaling.";
RL Oncogene 27:7235-7247(2008).
RN [11]
RP FUNCTION AS COL4A3BP/CERT KINASE.
RX PubMed=19005213; DOI=10.1091/mbc.e08-07-0669;
RA Tomishige N., Kumagai K., Kusuda J., Nishijima M., Hanada K.;
RT "Casein kinase I{gamma}2 down-regulates trafficking of ceramide in the
RT synthesis of sphingomyelin.";
RL Mol. Biol. Cell 20:348-357(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP SUBCELLULAR LOCATION, DOMAIN, AND PHOSPHORYLATION.
RX PubMed=26481050; DOI=10.1016/j.devcel.2015.09.016;
RA Bailey M.J., Prehoda K.E.;
RT "Establishment of Par-Polarized Cortical Domains via Phosphoregulated
RT Membrane Motifs.";
RL Dev. Cell 35:199-210(2015).
RN [16]
RP FUNCTION, AND INTERACTION WITH DUOXA2.
RX PubMed=37099597; DOI=10.1371/journal.pgen.1010740;
RA Hu Y., Xu Z., Pan Q., Ma L.;
RT "Casein kinase 1 gamma regulates oxidative stress response via interacting
RT with the NADPH dual oxidase complex.";
RL PLoS Genet. 19:e1010740-e1010740(2023).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 43-353 IN COMPLEX WITH
RP 5-IODOTUBERCIDIN.
RA Bunkoczi G., Rellos P., Das S., Ugochukwu E., Fedorov O., Sobott F.,
RA Eswaran J., Amos A., Ball L., Von Delft F., Bullock A., Debreczeni J.,
RA Turnbull A., Sundstrom M., Weigelt J., Arrowsmith C., Edwards A., Knapp S.;
RT "The structure of casein kinase 1 gamma 2.";
RL Submitted (JUL-2011) to the PDB data bank.
RN [18]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-189; GLY-194; THR-196; CYS-206;
RP HIS-206; SER-207; GLN-208; CYS-217 AND MET-223.
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: Serine/threonine-protein kinase. Casein kinases are
CC operationally defined by their preferential utilization of acidic
CC proteins such as caseins as substrates. It can phosphorylate a large
CC number of proteins. Participates in Wnt signaling (By similarity).
CC Phosphorylates COL4A3BP/CERT, MTA1 and SMAD3. SMAD3 phosphorylation
CC promotes its ligand-dependent ubiquitination and subsequent proteasome
CC degradation, thus inhibiting SMAD3-mediated TGF-beta responses.
CC Hyperphosphorylation of the serine-repeat motif of COL4A3BP/CERT leads
CC to its inactivation by dissociation from the Golgi complex, thus down-
CC regulating ER-to-Golgi transport of ceramide and sphingomyelin
CC synthesis. Triggers PER1 proteasomal degradation probably through
CC phosphorylation (PubMed:15077195, PubMed:15917222, PubMed:18794808,
CC PubMed:19005213). Involved in brain development and vesicular
CC trafficking and neurotransmitter releasing from small synaptic
CC vesicles. Regulates fast synaptic transmission mediated by glutamate
CC (By similarity). Involved in regulation of reactive oxygen species
CC (ROS) levels (PubMed:37099597). {ECO:0000250|UniProtKB:P48729,
CC ECO:0000250|UniProtKB:Q8BVP5, ECO:0000269|PubMed:15077195,
CC ECO:0000269|PubMed:15917222, ECO:0000269|PubMed:18794808,
CC ECO:0000269|PubMed:19005213, ECO:0000269|PubMed:37099597}.
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 -!- ACTIVITY REGULATION: Stimulated by estrogen. Repressed by 5-
CC iodotubercidin (DB04604). {ECO:0000269|PubMed:15077195}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with MTA1 (short isoform)
CC in the cytoplasm (PubMed:15077195). Interacts with SMAD3
CC (PubMed:18794808). Interacts with DUOXA2 (PubMed:37099597).
CC {ECO:0000250|UniProtKB:P48730, ECO:0000269|PubMed:15077195,
CC ECO:0000269|PubMed:18794808, ECO:0000269|PubMed:37099597}.
CC -!- INTERACTION:
CC P78368; Q92624: APPBP2; NbExp=3; IntAct=EBI-748380, EBI-743771;
CC P78368; Q9Y5P4: CERT1; NbExp=5; IntAct=EBI-748380, EBI-739994;
CC P78368; Q9Y5P4-2: CERT1; NbExp=4; IntAct=EBI-748380, EBI-11156432;
CC P78368; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-748380, EBI-10172290;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:26481050}. Cytoplasm {ECO:0000269|PubMed:15077195,
CC ECO:0000269|PubMed:26481050}.
CC -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:9403068}.
CC -!- DOMAIN: The phospho-regulated basic and hydrophobic (PRBH) motif is
CC sufficient and important for interaction with phospholipids permitting
CC cortical localization (PubMed:26481050). Phosphorylation of the PRBH
CC motif by aPKC inhibits the association of the protein with the cortical
CC membrane (PubMed:26481050). {ECO:0000269|PubMed:26481050}.
CC -!- PTM: Autophosphorylated (PubMed:18794808). Phosphorylated by aPKC which
CC promotes dissociation from the cell cortex (PubMed:26481050).
CC {ECO:0000269|PubMed:18794808, ECO:0000269|PubMed:26481050}.
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; U89896; AAB88627.1; -; mRNA.
DR EMBL; BT009922; AAP88924.1; -; mRNA.
DR EMBL; AF001177; AAC00212.1; -; Transcribed_RNA.
DR EMBL; AB451278; BAG70092.1; -; mRNA.
DR EMBL; AB451410; BAG70224.1; -; mRNA.
DR EMBL; AC005306; AAC26983.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69430.1; -; Genomic_DNA.
DR EMBL; BC018693; AAH18693.1; -; mRNA.
DR EMBL; BC018699; AAH18699.1; -; mRNA.
DR EMBL; BC020972; AAH20972.1; -; mRNA.
DR CCDS; CCDS12077.1; -.
DR RefSeq; NP_001310.3; NM_001319.6.
DR PDB; 2C47; X-ray; 2.40 A; A/B/C/D=43-353.
DR PDBsum; 2C47; -.
DR AlphaFoldDB; P78368; -.
DR SMR; P78368; -.
DR BioGRID; 107839; 130.
DR IntAct; P78368; 62.
DR MINT; P78368; -.
DR STRING; 9606.ENSP00000255641; -.
DR BindingDB; P78368; -.
DR ChEMBL; CHEMBL2543; -.
DR DrugBank; DB04604; 5-iodotubercidin.
DR DrugBank; DB03083; IC261.
DR DrugBank; DB03693; N-(2-Aminoethyl)-5-Chloroisoquinoline-8-Sulfonamide.
DR DrugCentral; P78368; -.
DR GuidetoPHARMACOLOGY; 2000; -.
DR iPTMnet; P78368; -.
DR PhosphoSitePlus; P78368; -.
DR SwissPalm; P78368; -.
DR BioMuta; CSNK1G2; -.
DR DMDM; 3024060; -.
DR EPD; P78368; -.
DR jPOST; P78368; -.
DR MassIVE; P78368; -.
DR MaxQB; P78368; -.
DR PaxDb; 9606-ENSP00000255641; -.
DR PeptideAtlas; P78368; -.
DR ProteomicsDB; 57596; -.
DR Pumba; P78368; -.
DR Antibodypedia; 22865; 562 antibodies from 31 providers.
DR DNASU; 1455; -.
DR Ensembl; ENST00000255641.13; ENSP00000255641.7; ENSG00000133275.16.
DR GeneID; 1455; -.
DR KEGG; hsa:1455; -.
DR MANE-Select; ENST00000255641.13; ENSP00000255641.7; NM_001319.7; NP_001310.3.
DR UCSC; uc002lul.5; human.
DR AGR; HGNC:2455; -.
DR CTD; 1455; -.
DR DisGeNET; 1455; -.
DR GeneCards; CSNK1G2; -.
DR HGNC; HGNC:2455; CSNK1G2.
DR HPA; ENSG00000133275; Low tissue specificity.
DR MIM; 602214; gene.
DR neXtProt; NX_P78368; -.
DR OpenTargets; ENSG00000133275; -.
DR PharmGKB; PA26955; -.
DR VEuPathDB; HostDB:ENSG00000133275; -.
DR eggNOG; KOG1165; Eukaryota.
DR GeneTree; ENSGT00940000156470; -.
DR InParanoid; P78368; -.
DR OMA; AANNKHK; -.
DR OrthoDB; 1534388at2759; -.
DR PhylomeDB; P78368; -.
DR TreeFam; TF313349; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; P78368; -.
DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR SignaLink; P78368; -.
DR SIGNOR; P78368; -.
DR BioGRID-ORCS; 1455; 24 hits in 1195 CRISPR screens.
DR ChiTaRS; CSNK1G2; human.
DR EvolutionaryTrace; P78368; -.
DR GenomeRNAi; 1455; -.
DR Pharos; P78368; Tchem.
DR PRO; PR:P78368; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P78368; Protein.
DR Bgee; ENSG00000133275; Expressed in left testis and 202 other cell types or tissues.
DR ExpressionAtlas; P78368; baseline and differential.
DR Genevisible; P78368; HS.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd14126; STKc_CK1_gamma; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR022247; Casein_kinase-1_gamma_C.
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:SF157; CASEIN KINASE I ISOFORM GAMMA-2; 1.
DR PANTHER; PTHR11909; CASEIN KINASE-RELATED; 1.
DR Pfam; PF12605; CK1gamma_C; 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; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Wnt signaling pathway.
FT CHAIN 1..415
FT /note="Casein kinase I isoform gamma-2"
FT /id="PRO_0000192842"
FT DOMAIN 46..316
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..415
FT /note="Phospho-regulated basic and hydrophobic (PRBH)
FT motif"
FT /evidence="ECO:0000269|PubMed:26481050"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 52..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VARIANT 189
FT /note="F -> L (in dbSNP:rs55702630)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042086"
FT VARIANT 194
FT /note="E -> G (in dbSNP:rs55780547)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042087"
FT VARIANT 196
FT /note="I -> T (in dbSNP:rs55923222)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042088"
FT VARIANT 206
FT /note="Y -> C (in dbSNP:rs56264133)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042089"
FT VARIANT 206
FT /note="Y -> H (in dbSNP:rs56108438)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042090"
FT VARIANT 207
FT /note="R -> S (in dbSNP:rs56340103)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042091"
FT VARIANT 208
FT /note="E -> Q (in dbSNP:rs55818316)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042092"
FT VARIANT 217
FT /note="R -> C (in dbSNP:rs55754218)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042093"
FT VARIANT 223
FT /note="T -> M (in dbSNP:rs56038081)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042094"
FT CONFLICT 113
FT /note="K -> N (in Ref. 2; AAP88924 and 6; AAH20972)"
FT /evidence="ECO:0000305"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:2C47"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:2C47"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:2C47"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:2C47"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:2C47"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:2C47"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:2C47"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:2C47"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:2C47"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:2C47"
FT HELIX 139..158
FT /evidence="ECO:0007829|PDB:2C47"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:2C47"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2C47"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:2C47"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:2C47"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:2C47"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:2C47"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:2C47"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:2C47"
FT HELIX 231..247
FT /evidence="ECO:0007829|PDB:2C47"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:2C47"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:2C47"
FT HELIX 260..272
FT /evidence="ECO:0007829|PDB:2C47"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:2C47"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:2C47"
FT HELIX 285..295
FT /evidence="ECO:0007829|PDB:2C47"
FT HELIX 305..318
FT /evidence="ECO:0007829|PDB:2C47"
FT TURN 328..331
FT /evidence="ECO:0007829|PDB:2C47"
SQ SEQUENCE 415 AA; 47457 MW; 036A39148A1DA038 CRC64;
MDFDKKGGKG ETEEGRRMSK AGGGRSSHGI RSSGTSSGVL MVGPNFRVGK KIGCGNFGEL
RLGKNLYTNE YVAIKLEPIK SRAPQLHLEY RFYKQLSATE GVPQVYYFGP CGKYNAMVLE
LLGPSLEDLF DLCDRTFTLK TVLMIAIQLI TRMEYVHTKS LIYRDVKPEN FLVGRPGTKR
QHAIHIIDFG LAKEYIDPET KKHIPYREHK SLTGTARYMS INTHLGKEQS RRDDLEALGH
MFMYFLRGSL PWQGLKADTL KERYQKIGDT KRATPIEVLC ENFPEEMATY LRYVRRLDFF
EKPDYDYLRK LFTDLFDRSG FVFDYEYDWA GKPLPTPIGT VHTDLPSQPQ LRDKTQPHSK
NQALNSTNGE LNADDPTAGH SNAPITAPAE VEVADETKCC CFFKRRKRKS LQRHK
//
