KC1G3_MOUSE
ID KC1G3_MOUSE Reviewed; 424 AA.
AC Q8C4X2; Q8BM57; Q8C001; Q8K079;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Casein kinase I isoform gamma-3;
DE Short=CKI-gamma 3;
DE EC=2.7.11.1;
GN Name=Csnk1g3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-210 AND 238-424.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryoid bodies;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-210.
RC TISSUE=Melanocyte;
RX PubMed=15782199; DOI=10.1038/nmeth719;
RA Watahiki A., Waki K., Hayatsu N., Shiraki T., Kondo S., Nakamura M.,
RA Sasaki D., Arakawa T., Kawai J., Harbers M., Hayashizaki Y., Carninci P.;
RT "Libraries enriched for alternatively spliced exons reveal splicing
RT patterns in melanocytes and melanomas.";
RL Nat. Methods 1:233-239(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-424.
RC TISSUE=Eye;
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 [5]
RP FUNCTION IN SYNAPTIC TRANSMISSION, AND TISSUE SPECIFICITY.
RX PubMed=16014721; DOI=10.1523/jneurosci.1082-05.2005;
RA Chergui K., Svenningsson P., Greengard P.;
RT "Physiological role for casein kinase 1 in glutamatergic synaptic
RT transmission.";
RL J. Neurosci. 25:6601-6609(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 Regulates fast synaptic transmission mediated by glutamate.
CC {ECO:0000250, ECO:0000269|PubMed:16014721}.
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: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in both the striatum and the neocortex.
CC {ECO:0000269|PubMed:16014721}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: Triazolodiamine 1 is a commercial name for 5-amino-3-
CC ([4-(aminosulfonyl)phenyl]amino)-N-(2,6-difluorophenyl)-1H-1,2,4-
CC triazole-1-carbothioamide.
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; AC115124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK032675; BAC27983.1; -; mRNA.
DR EMBL; AK034842; BAC28850.1; -; mRNA.
DR EMBL; AK080491; BAC37932.1; -; mRNA.
DR EMBL; AK218008; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC033601; AAH33601.2; -; mRNA.
DR CCDS; CCDS37823.1; -.
DR RefSeq; NP_690022.2; NM_152809.2.
DR AlphaFoldDB; Q8C4X2; -.
DR SMR; Q8C4X2; -.
DR STRING; 10090.ENSMUSP00000070259; -.
DR iPTMnet; Q8C4X2; -.
DR PhosphoSitePlus; Q8C4X2; -.
DR SwissPalm; Q8C4X2; -.
DR EPD; Q8C4X2; -.
DR jPOST; Q8C4X2; -.
DR MaxQB; Q8C4X2; -.
DR PaxDb; Q8C4X2; -.
DR PeptideAtlas; Q8C4X2; -.
DR PRIDE; Q8C4X2; -.
DR ProteomicsDB; 269449; -.
DR Antibodypedia; 25674; 172 antibodies from 28 providers.
DR DNASU; 70425; -.
DR Ensembl; ENSMUST00000069597; ENSMUSP00000070259; ENSMUSG00000073563.
DR GeneID; 70425; -.
DR KEGG; mmu:70425; -.
DR UCSC; uc008eya.1; mouse.
DR CTD; 1456; -.
DR MGI; MGI:1917675; Csnk1g3.
DR VEuPathDB; HostDB:ENSMUSG00000073563; -.
DR eggNOG; KOG1165; Eukaryota.
DR GeneTree; ENSGT00940000160646; -.
DR HOGENOM; CLU_019279_2_0_1; -.
DR InParanoid; Q8C4X2; -.
DR OrthoDB; 889559at2759; -.
DR PhylomeDB; Q8C4X2; -.
DR TreeFam; TF313349; -.
DR BioGRID-ORCS; 70425; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Csnk1g3; mouse.
DR PRO; PR:Q8C4X2; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8C4X2; protein.
DR Bgee; ENSMUSG00000073563; Expressed in superior cervical ganglion and 224 other tissues.
DR ExpressionAtlas; Q8C4X2; baseline and differential.
DR Genevisible; Q8C4X2; MM.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
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 Acetylation; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Wnt signaling pathway.
FT CHAIN 1..424
FT /note="Casein kinase I isoform gamma-3"
FT /id="PRO_0000305924"
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 337..390
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 359..385
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:0000250|UniProtKB:Q9Y6M4"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 62..84
FT /note="NLYTNEYVAIKLEPMKSRAPQLH -> IVLFIPLCEEQFKNEYTCKRVFL
FT (in Ref. 2; BAC37932)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="L -> V (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="T -> A (in Ref. 2; AK218008)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="N -> K (in Ref. 2; AK218008)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 48938 MW; A0A0789CE718F3C0 CRC64;
MDNKKKDKDK SDDRMARPSG RSGHSTRGTG SSSSGVLMVG PNFRVGKKIG CGNFGELRLG
KNLYTNEYVA IKLEPMKSRA PQLHLEYRFY KQLGSGDGIP QVYYFGPCGK YNAMVLELLG
PSLEDLFDLC DRTFSLKTVL MIAIQLISRM EYVHSKNLIY RDVKPENFLI GRPGNKAQQV
IHIIDFGLAK EYIDPETKKH IPYREHKSLT GTARYMSINT HLGKEQSRRD DLEALGHMFM
YFLRGSLPWQ GLKADTLKER YQKIGDTKRA TPIEVLCENF PEEMATYLRY VRRLDFFEKP
DYDYLRKLFT DLFDRKGYMF DYEYDWIGKQ LPTPVGAVQQ DPALSSNREA HQHRDKIQQS
KNQVVSSTNG ELNTDDPTAG RSNAPITAPT EVEVMDETNC QKVLNMWCCC FFKRRKRKTI
QRHK
