KC1G3_HUMAN
ID KC1G3_HUMAN Reviewed; 447 AA.
AC Q9Y6M4; A8K040; B4DSH2; B7Z9Q4; E7EVD0; Q86WZ7; Q9Y6M3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Casein kinase I isoform gamma-3;
DE Short=CKI-gamma 3;
DE EC=2.7.11.1;
GN Name=CSNK1G3;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RX PubMed=9925945; DOI=10.1159/000015143;
RA Kusuda J., Hirai M., Toyoda A., Tanuma R., Hashimoto K.;
RT "Cloning and chromosome mapping of the human casein kinase I gamma3 gene
RT (CSNK1G3).";
RL Cytogenet. Cell Genet. 83:101-103(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
RC TISSUE=Astrocyte, Brain, and Embryonic 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 [3]
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 [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND IDENTIFICATION BY
RP 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366 (ISOFORM 3),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367 (ISOFORM 4),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291 (ISOFORM 5),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254 (ISOFORM 6), 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [12]
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 [13] {ECO:0007744|PDB:2CHL}
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 35-362 IN COMPLEX WITH THE
RP INHIBITOR TRIAZOLODIAMINE 1, AND ACTIVITY REGULATION.
RA Bunkoczi G., Salah E., Rellos P., Das S., Fedorov O., Savitsky P.,
RA Gileadi O., Sundstrom M., Edwards A., Arrowsmith C., Ugochukwu E.,
RA Weigelt J., Von Delft F., Knapp S.;
RT "Structure of casein kinase 1 gamma 3.";
RL Submitted (MAR-2006) to the PDB data bank.
RN [14] {ECO:0007744|PDB:2IZR, ECO:0007744|PDB:2IZS, ECO:0007744|PDB:2IZT, ECO:0007744|PDB:2IZU}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 35-362 IN COMPLEX WITH
RP INHIBITORS, AND ACTIVITY REGULATION.
RA Bunkoczi G., Salah E., Rellos P., Das S., Fedorov O., Savitsky P.,
RA Debreczeni J.E., Gileadi O., Sundstrom M., Edwards A., Arrowsmith C.,
RA Weigelt J., Von Delft F., Knapp S.;
RT "Inhibitor binding by casein kinases.";
RL Submitted (FEB-2009) to the PDB data bank.
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. Regulates fast
CC synaptic transmission mediated by glutamate (By similarity).
CC {ECO:0000250}.
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: Inhibited by triazolodiamine 1 (5-amino-3-([4-
CC (aminosulfonyl)phenyl]amino)-N-(2,6-difluorophenyl)-1H-1,2,4-triazole-
CC 1-carbothioamide), (S)-propane-1,2-diol, 2-({6-[(3-chlorophenyl)amino]-
CC 9-isopropyl-9H-purin-2-yl}amino)-3-methylbutan-1-ol, N2-[(1R,2S)-2-
CC aminocyclohexyl]-N6-(3-chlorophenyl)-9-ethyl-9H-purine-2,6-diamine and
CC [4-amino-2-(3-chloroanilino)-1,3-thiazol-5-yl](4-
CC fluorophenyl)methanone. {ECO:0000269|Ref.13, ECO:0000269|Ref.14}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Y6M4-3; Q6PGQ1: DRICH1; NbExp=3; IntAct=EBI-11045281, EBI-10253641;
CC Q9Y6M4-3; P60014: KRTAP10-10; NbExp=3; IntAct=EBI-11045281, EBI-11955579;
CC Q9Y6M4-3; Q99750: MDFI; NbExp=3; IntAct=EBI-11045281, EBI-724076;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=3;
CC IsoId=Q9Y6M4-1; Sequence=Displayed;
CC Name=2; Synonyms=3L, CSNK1G3L;
CC IsoId=Q9Y6M4-2; Sequence=VSP_004749;
CC Name=3;
CC IsoId=Q9Y6M4-3; Sequence=VSP_010256, VSP_004749;
CC Name=4;
CC IsoId=Q9Y6M4-4; Sequence=VSP_047055, VSP_010256, VSP_004749;
CC Name=5;
CC IsoId=Q9Y6M4-5; Sequence=VSP_047054, VSP_010256, VSP_004749;
CC Name=6;
CC IsoId=Q9Y6M4-6; Sequence=VSP_047053, VSP_047055, VSP_010256,
CC VSP_004749;
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
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; AF049089; AAD26525.1; -; mRNA.
DR EMBL; AF049090; AAD26526.1; -; mRNA.
DR EMBL; AK289405; BAF82094.1; -; mRNA.
DR EMBL; AK299739; BAG61634.1; -; mRNA.
DR EMBL; AK316019; BAH14390.1; -; mRNA.
DR EMBL; AC008541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471086; EAW48872.1; -; Genomic_DNA.
DR EMBL; BC047567; AAH47567.1; -; mRNA.
DR CCDS; CCDS34218.1; -. [Q9Y6M4-3]
DR CCDS; CCDS4135.1; -. [Q9Y6M4-1]
DR CCDS; CCDS43355.1; -. [Q9Y6M4-2]
DR CCDS; CCDS59491.1; -. [Q9Y6M4-4]
DR CCDS; CCDS59492.1; -. [Q9Y6M4-5]
DR CCDS; CCDS59493.1; -. [Q9Y6M4-6]
DR RefSeq; NP_001026982.1; NM_001031812.3. [Q9Y6M4-3]
DR RefSeq; NP_001038188.1; NM_001044723.2. [Q9Y6M4-2]
DR RefSeq; NP_001257501.1; NM_001270572.1. [Q9Y6M4-4]
DR RefSeq; NP_001257502.1; NM_001270573.1. [Q9Y6M4-5]
DR RefSeq; NP_001257503.1; NM_001270574.1. [Q9Y6M4-6]
DR RefSeq; NP_004375.2; NM_004384.4. [Q9Y6M4-1]
DR RefSeq; XP_005271949.1; XM_005271892.2. [Q9Y6M4-2]
DR RefSeq; XP_005271951.1; XM_005271894.2. [Q9Y6M4-1]
DR RefSeq; XP_005271952.1; XM_005271895.2. [Q9Y6M4-4]
DR RefSeq; XP_016864558.1; XM_017009069.1. [Q9Y6M4-4]
DR PDB; 2CHL; X-ray; 1.95 A; A=35-362.
DR PDB; 2IZR; X-ray; 1.30 A; A=35-362.
DR PDB; 2IZS; X-ray; 1.95 A; A=35-362.
DR PDB; 2IZT; X-ray; 2.00 A; A=35-362.
DR PDB; 2IZU; X-ray; 1.85 A; A=35-362.
DR PDB; 4G16; X-ray; 2.30 A; A=34-362.
DR PDB; 4G17; X-ray; 2.10 A; A=34-362.
DR PDB; 4HGL; X-ray; 2.40 A; A=34-362.
DR PDB; 4HGS; X-ray; 2.40 A; A=34-362.
DR PDB; 6GRO; X-ray; 1.45 A; A=33-362.
DR PDBsum; 2CHL; -.
DR PDBsum; 2IZR; -.
DR PDBsum; 2IZS; -.
DR PDBsum; 2IZT; -.
DR PDBsum; 2IZU; -.
DR PDBsum; 4G16; -.
DR PDBsum; 4G17; -.
DR PDBsum; 4HGL; -.
DR PDBsum; 4HGS; -.
DR PDBsum; 6GRO; -.
DR AlphaFoldDB; Q9Y6M4; -.
DR SMR; Q9Y6M4; -.
DR BioGRID; 107840; 121.
DR IntAct; Q9Y6M4; 43.
DR MINT; Q9Y6M4; -.
DR STRING; 9606.ENSP00000353904; -.
DR BindingDB; Q9Y6M4; -.
DR ChEMBL; CHEMBL5084; -.
DR DrugBank; DB07489; 4-Amino-2-[(3-chlorophenyl)amino]-5-(4-fluorobenzoyl)-1,3-thiazol-3-ium.
DR DrugBank; DB07664; K-00546.
DR DrugBank; DB04751; Purvalanol A.
DR DrugBank; DB07488; {4-Amino-2-[(4-methoxyphenyl)amino]-1,3-thiazol-5-yl}(4-methoxyphenyl)methanone.
DR DrugCentral; Q9Y6M4; -.
DR iPTMnet; Q9Y6M4; -.
DR PhosphoSitePlus; Q9Y6M4; -.
DR SwissPalm; Q9Y6M4; -.
DR BioMuta; CSNK1G3; -.
DR DMDM; 47117932; -.
DR EPD; Q9Y6M4; -.
DR jPOST; Q9Y6M4; -.
DR MassIVE; Q9Y6M4; -.
DR MaxQB; Q9Y6M4; -.
DR PaxDb; Q9Y6M4; -.
DR PeptideAtlas; Q9Y6M4; -.
DR PRIDE; Q9Y6M4; -.
DR ProteomicsDB; 1831; -.
DR ProteomicsDB; 18613; -.
DR ProteomicsDB; 5025; -.
DR ProteomicsDB; 86730; -. [Q9Y6M4-1]
DR ProteomicsDB; 86731; -. [Q9Y6M4-2]
DR ProteomicsDB; 86732; -. [Q9Y6M4-3]
DR Antibodypedia; 25674; 172 antibodies from 28 providers.
DR DNASU; 1456; -.
DR Ensembl; ENST00000345990.8; ENSP00000334735.4; ENSG00000151292.17. [Q9Y6M4-3]
DR Ensembl; ENST00000360683.6; ENSP00000353904.2; ENSG00000151292.17. [Q9Y6M4-2]
DR Ensembl; ENST00000361991.6; ENSP00000354942.2; ENSG00000151292.17. [Q9Y6M4-1]
DR Ensembl; ENST00000510842.6; ENSP00000423838.2; ENSG00000151292.17. [Q9Y6M4-4]
DR Ensembl; ENST00000511130.6; ENSP00000421385.2; ENSG00000151292.17. [Q9Y6M4-6]
DR Ensembl; ENST00000512718.7; ENSP00000421998.3; ENSG00000151292.17. [Q9Y6M4-5]
DR Ensembl; ENST00000521364.5; ENSP00000429412.1; ENSG00000151292.17. [Q9Y6M4-3]
DR GeneID; 1456; -.
DR KEGG; hsa:1456; -.
DR UCSC; uc003ktn.5; human. [Q9Y6M4-1]
DR CTD; 1456; -.
DR DisGeNET; 1456; -.
DR GeneCards; CSNK1G3; -.
DR HGNC; HGNC:2456; CSNK1G3.
DR HPA; ENSG00000151292; Low tissue specificity.
DR MIM; 604253; gene.
DR neXtProt; NX_Q9Y6M4; -.
DR OpenTargets; ENSG00000151292; -.
DR PharmGKB; PA26956; -.
DR VEuPathDB; HostDB:ENSG00000151292; -.
DR eggNOG; KOG1165; Eukaryota.
DR GeneTree; ENSGT00940000160646; -.
DR HOGENOM; CLU_019279_2_0_1; -.
DR InParanoid; Q9Y6M4; -.
DR OMA; TGFQKFM; -.
DR OrthoDB; 889559at2759; -.
DR PhylomeDB; Q9Y6M4; -.
DR TreeFam; TF313349; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; Q9Y6M4; -.
DR SignaLink; Q9Y6M4; -.
DR BioGRID-ORCS; 1456; 10 hits in 1117 CRISPR screens.
DR ChiTaRS; CSNK1G3; human.
DR EvolutionaryTrace; Q9Y6M4; -.
DR GenomeRNAi; 1456; -.
DR Pharos; Q9Y6M4; Tchem.
DR PRO; PR:Q9Y6M4; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9Y6M4; protein.
DR Bgee; ENSG00000151292; Expressed in calcaneal tendon and 199 other tissues.
DR ExpressionAtlas; Q9Y6M4; baseline and differential.
DR Genevisible; Q9Y6M4; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0004672; F:protein kinase activity; TAS:ProtInc.
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:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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 Pfam; PF12605; CK1gamma_C; 1.
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; Cytoplasm;
KW Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
FT CHAIN 1..447
FT /note="Casein kinase I isoform gamma-3"
FT /id="PRO_0000192846"
FT DOMAIN 43..313
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 49..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 1..113
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047053"
FT VAR_SEQ 1..75
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047054"
FT VAR_SEQ 282
FT /note="E -> EE (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047055"
FT VAR_SEQ 363..394
FT /note="Missing (in isoform 3, isoform 4, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_010256"
FT VAR_SEQ 430
FT /note="K -> NCQKVLNMW (in isoform 2, isoform 3, isoform 4,
FT isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9925945"
FT /id="VSP_004749"
FT CONFLICT 91
FT /note="K -> E (in Ref. 5; AAH47567)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="G -> R (in Ref. 1; AAD26525/AAD26526)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="Y -> C (in Ref. 2; BAH14390)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="D -> E (in Ref. 1; AAD26525/AAD26526)"
FT /evidence="ECO:0000305"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:2IZR"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:2IZR"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2IZS"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:2IZR"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:2IZR"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:2IZR"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:2IZR"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:2IZR"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:2IZR"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:2IZR"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:2IZR"
FT HELIX 136..155
FT /evidence="ECO:0007829|PDB:2IZR"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:2IZR"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2IZR"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:2IZR"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:6GRO"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:2IZR"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:2IZR"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:2IZR"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:2IZU"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:2IZR"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:2IZR"
FT HELIX 228..244
FT /evidence="ECO:0007829|PDB:2IZR"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:2IZR"
FT HELIX 257..270
FT /evidence="ECO:0007829|PDB:2IZR"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:2IZR"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:2IZR"
FT HELIX 281..292
FT /evidence="ECO:0007829|PDB:2IZR"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:2IZR"
FT TURN 324..327
FT /evidence="ECO:0007829|PDB:2IZR"
FT MOD_RES Q9Y6M4-3:366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q9Y6M4-4:367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q9Y6M4-5:291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q9Y6M4-6:254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
SQ SEQUENCE 447 AA; 51389 MW; 6FAEDD605579ED3A CRC64;
MENKKKDKDK SDDRMARPSG RSGHNTRGTG SSSSGVLMVG PNFRVGKKIG CGNFGELRLG
KNLYTNEYVA IKLEPMKSRA PQLHLEYRFY KQLGSGDGIP QVYYFGPCGK YNAMVLELLG
PSLEDLFDLC DRTFSLKTVL MIAIQLISRM EYVHSKNLIY RDVKPENFLI GRPGNKTQQV
IHIIDFGLAK EYIDPETKKH IPYREHKSLT GTARYMSINT HLGKEQSRRD DLEALGHMFM
YFLRGSLPWQ GLKADTLKER YQKIGDTKRA TPIEVLCENF PEMATYLRYV RRLDFFEKPD
YDYLRKLFTD LFDRKGYMFD YEYDWIGKQL PTPVGAVQQD PALSSNREAH QHRDKMQQSK
NQSADHRAAW DSQQANPHHL RAHLAADRHG GSVQVVSSTN GELNTDDPTA GRSNAPITAP
TEVEVMDETK CCCFFKRRKR KTIQRHK
