KC1G1_HUMAN
ID KC1G1_HUMAN Reviewed; 422 AA.
AC Q9HCP0; Q5JPH1; Q96AE9; Q9HCP1;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Casein kinase I isoform gamma-1;
DE Short=CKI-gamma 1;
DE EC=2.7.11.1;
GN Name=CSNK1G1;
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 1L AND 1S).
RX PubMed=11124537; DOI=10.1159/000056792;
RA Kusuda J., Hirai M., Tanuma R., Hashimoto K.;
RT "Cloning, expression analysis and chromosome mapping of human casein kinase
RT 1 gamma1 (CSNK1G1): identification of two types of cDNA encoding the kinase
RT protein associated with heterologous carboxy-terminal sequences.";
RL Cytogenet. Cell Genet. 90:298-302(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1L).
RC TISSUE=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 [5]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, 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 [7]
RP FUNCTION AS CLSPN KINASE, AND MUTAGENESIS OF ASN-169.
RX PubMed=21680713; DOI=10.1091/mbc.e11-01-0048;
RA Meng Z., Capalbo L., Glover D.M., Dunphy W.G.;
RT "Role for casein kinase 1 in the phosphorylation of Claspin on critical
RT residues necessary for the activation of Chk1.";
RL Mol. Biol. Cell 22:2834-2847(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 45-352 IN COMPLEX WITH DB08325.
RA Bunkoczi G., Rellos P., Das S., Savitsky P., Niesen F., Sobott F.,
RA Fedorov O., Pike A.C.W., Von Delft F., Sundstrom M., Arrowsmith C.,
RA Edwards A., Weigelt J., Knapp S.;
RT "Structure of human casein kinase 1 gamma-1 in complex with (3-
RT chloroanilino)-9-isopropylpurine (casp target).";
RL Submitted (JUL-2011) to the PDB data bank.
RN [9]
RP VARIANTS [LARGE SCALE ANALYSIS] LYS-206 AND ILE-329.
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).
RN [10]
RP VARIANT TRP-230.
RX PubMed=24463883; DOI=10.1093/hmg/ddu030;
RG WGS500 Consortium;
RA Martin H.C., Kim G.E., Pagnamenta A.T., Murakami Y., Carvill G.L.,
RA Meyer E., Copley R.R., Rimmer A., Barcia G., Fleming M.R., Kronengold J.,
RA Brown M.R., Hudspith K.A., Broxholme J., Kanapin A., Cazier J.B.,
RA Kinoshita T., Nabbout R., Bentley D., McVean G., Heavin S., Zaiwalla Z.,
RA McShane T., Mefford H.C., Shears D., Stewart H., Kurian M.A.,
RA Scheffer I.E., Blair E., Donnelly P., Kaczmarek L.K., Taylor J.C.;
RT "Clinical whole-genome sequencing in severe early-onset epilepsy reveals
RT new genes and improves molecular diagnosis.";
RL Hum. Mol. Genet. 23:3200-3211(2014).
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 Phosphorylates CLSPN. {ECO:0000250, ECO:0000269|PubMed:21680713}.
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: Repressed by 2-(2-hydroxyethylamino)-6-(3-
CC chloroanilino)-9-isopropylpurine (DB08325).
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9HCP0; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-1383814, EBI-742887;
CC Q9HCP0; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-1383814, EBI-10172290;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1L;
CC IsoId=Q9HCP0-1; Sequence=Displayed;
CC Name=1S;
CC IsoId=Q9HCP0-2; Sequence=VSP_004748;
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 1S]: May be produced at very low levels due to
CC a premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
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; AB042563; BAB17839.1; -; mRNA.
DR EMBL; AB042562; BAB17838.1; -; mRNA.
DR EMBL; AL832551; CAI46142.1; -; mRNA.
DR EMBL; CH471082; EAW77670.1; -; Genomic_DNA.
DR EMBL; BC017236; AAH17236.2; -; mRNA.
DR EMBL; BC130613; AAI30614.1; -; mRNA.
DR EMBL; BC136504; AAI36505.1; -; mRNA.
DR CCDS; CCDS10192.2; -. [Q9HCP0-1]
DR RefSeq; NP_001316535.1; NM_001329606.1. [Q9HCP0-1]
DR RefSeq; NP_071331.2; NM_022048.4. [Q9HCP0-1]
DR PDB; 2CMW; X-ray; 1.75 A; A=45-352.
DR PDBsum; 2CMW; -.
DR AlphaFoldDB; Q9HCP0; -.
DR SMR; Q9HCP0; -.
DR BioGRID; 119824; 24.
DR IntAct; Q9HCP0; 23.
DR MINT; Q9HCP0; -.
DR STRING; 9606.ENSP00000305777; -.
DR BindingDB; Q9HCP0; -.
DR ChEMBL; CHEMBL2426; -.
DR DrugBank; DB08325; 2-({6-[(3-Chlorophenyl)amino]-9-isopropyl-9H-purin-2-yl}amino)ethanol.
DR DrugCentral; Q9HCP0; -.
DR GuidetoPHARMACOLOGY; 1999; -.
DR iPTMnet; Q9HCP0; -.
DR PhosphoSitePlus; Q9HCP0; -.
DR SwissPalm; Q9HCP0; -.
DR BioMuta; CSNK1G1; -.
DR DMDM; 18202957; -.
DR EPD; Q9HCP0; -.
DR jPOST; Q9HCP0; -.
DR MassIVE; Q9HCP0; -.
DR MaxQB; Q9HCP0; -.
DR PaxDb; Q9HCP0; -.
DR PeptideAtlas; Q9HCP0; -.
DR PRIDE; Q9HCP0; -.
DR ProteomicsDB; 81782; -. [Q9HCP0-1]
DR ProteomicsDB; 81783; -. [Q9HCP0-2]
DR Antibodypedia; 13388; 447 antibodies from 32 providers.
DR DNASU; 53944; -.
DR Ensembl; ENST00000303052.13; ENSP00000305777.7; ENSG00000169118.18. [Q9HCP0-1]
DR Ensembl; ENST00000606225.1; ENSP00000475325.1; ENSG00000169118.18. [Q9HCP0-2]
DR GeneID; 53944; -.
DR KEGG; hsa:53944; -.
DR MANE-Select; ENST00000303052.13; ENSP00000305777.7; NM_022048.5; NP_071331.2.
DR UCSC; uc002anf.4; human. [Q9HCP0-1]
DR CTD; 53944; -.
DR DisGeNET; 53944; -.
DR GeneCards; CSNK1G1; -.
DR HGNC; HGNC:2454; CSNK1G1.
DR HPA; ENSG00000169118; Tissue enhanced (testis).
DR MIM; 606274; gene.
DR neXtProt; NX_Q9HCP0; -.
DR OpenTargets; ENSG00000169118; -.
DR PharmGKB; PA26954; -.
DR VEuPathDB; HostDB:ENSG00000169118; -.
DR eggNOG; KOG1165; Eukaryota.
DR GeneTree; ENSGT00940000155628; -.
DR HOGENOM; CLU_019279_2_0_1; -.
DR InParanoid; Q9HCP0; -.
DR OMA; DWMHLNG; -.
DR PhylomeDB; Q9HCP0; -.
DR TreeFam; TF313349; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; Q9HCP0; -.
DR SignaLink; Q9HCP0; -.
DR SIGNOR; Q9HCP0; -.
DR BioGRID-ORCS; 53944; 11 hits in 1115 CRISPR screens.
DR ChiTaRS; CSNK1G1; human.
DR EvolutionaryTrace; Q9HCP0; -.
DR GenomeRNAi; 53944; -.
DR Pharos; Q9HCP0; Tchem.
DR PRO; PR:Q9HCP0; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9HCP0; protein.
DR Bgee; ENSG00000169118; Expressed in secondary oocyte and 191 other tissues.
DR ExpressionAtlas; Q9HCP0; baseline and differential.
DR Genevisible; Q9HCP0; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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: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: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; 2.
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; Alternative splicing; ATP-binding; Cytoplasm;
KW Disease variant; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Wnt signaling pathway.
FT CHAIN 1..422
FT /note="Casein kinase I isoform gamma-1"
FT /id="PRO_0000192839"
FT DOMAIN 44..315
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 351..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 50..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 370..422
FT /note="VVSSTNGELNVDDPTGAHSNAPITAHAEVEVVEEAKCCCFFKRKRKKTAQRH
FT K -> SLRTVTAEHYDVNNSAIWHRGRGT (in isoform 1S)"
FT /evidence="ECO:0000303|PubMed:11124537"
FT /id="VSP_004748"
FT VARIANT 206
FT /note="R -> K (in dbSNP:rs55799101)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042084"
FT VARIANT 230
FT /note="R -> W (probable disease-associated variant found in
FT a patient with non-syndromic early-onset epilepsy
FT associated with severe developmental delay and
FT microcephaly; dbSNP:rs587777544)"
FT /evidence="ECO:0000269|PubMed:24463883"
FT /id="VAR_078686"
FT VARIANT 329
FT /note="V -> I (in dbSNP:rs55699712)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042085"
FT MUTAGEN 169
FT /note="N->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:21680713"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:2CMW"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:2CMW"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:2CMW"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:2CMW"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:2CMW"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:2CMW"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:2CMW"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:2CMW"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:2CMW"
FT HELIX 138..157
FT /evidence="ECO:0007829|PDB:2CMW"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:2CMW"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2CMW"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:2CMW"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2CMW"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:2CMW"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:2CMW"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:2CMW"
FT HELIX 230..246
FT /evidence="ECO:0007829|PDB:2CMW"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:2CMW"
FT HELIX 259..272
FT /evidence="ECO:0007829|PDB:2CMW"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:2CMW"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:2CMW"
FT HELIX 284..295
FT /evidence="ECO:0007829|PDB:2CMW"
FT HELIX 304..317
FT /evidence="ECO:0007829|PDB:2CMW"
FT TURN 327..330
FT /evidence="ECO:0007829|PDB:2CMW"
SQ SEQUENCE 422 AA; 48511 MW; B875922349B97645 CRC64;
MDHPSREKDE RQRTTKPMAQ RSAHCSRPSG SSSSSGVLMV GPNFRVGKKI GCGNFGELRL
GKNLYTNEYV AIKLEPIKSR APQLHLEYRF YKQLGSAGEG LPQVYYFGPC GKYNAMVLEL
LGPSLEDLFD LCDRTFTLKT VLMIAIQLLS RMEYVHSKNL IYRDVKPENF LIGRQGNKKE
HVIHIIDFGL AKEYIDPETK KHIPYREHKS LTGTARYMSI NTHLGKEQSR RDDLEALGHM
FMYFLRGSLP WQGLKADTLK ERYQKIGDTK RNTPIEALCE NFPEEMATYL RYVRRLDFFE
KPDYEYLRTL FTDLFEKKGY TFDYAYDWVG RPIPTPVGSV HVDSGASAIT RESHTHRDRP
SQQQPLRNQV VSSTNGELNV DDPTGAHSNA PITAHAEVEV VEEAKCCCFF KRKRKKTAQR
HK
