ID   KC1AL_HUMAN             Reviewed;         337 AA.
AC   Q8N752; Q5T2N2;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   08-NOV-2023, entry version 165.
DE   RecName: Full=Casein kinase I isoform alpha-like;
DE            Short=CKI-alpha-like;
DE            EC=2.7.11.1;
DE   AltName: Full=CK1;
GN   Name=CSNK1A1L;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-42.
RC   TISSUE=Testis;
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   [4]
RP   VARIANT [LARGE SCALE ANALYSIS] GLN-21.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [5]
RP   VARIANTS [LARGE SCALE ANALYSIS] GLY-5; TRP-21; SER-170; LYS-177; LEU-220;
RP   ASN-230 AND THR-257.
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: Casein kinases are operationally defined by their
CC       preferential utilization of acidic proteins such as caseins as
CC       substrates. It can phosphorylate a large number of proteins.
CC       Participates in Wnt signaling (By similarity). {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   -!- SUBCELLULAR LOCATION: Cytoplasm {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; AL391383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471075; EAX08587.1; -; Genomic_DNA.
DR   EMBL; BC028723; AAH28723.1; -; mRNA.
DR   CCDS; CCDS9363.1; -.
DR   RefSeq; NP_660204.2; NM_145203.5.
DR   AlphaFoldDB; Q8N752; -.
DR   SMR; Q8N752; -.
DR   BioGRID; 125755; 66.
DR   IntAct; Q8N752; 18.
DR   MINT; Q8N752; -.
DR   STRING; 9606.ENSP00000369126; -.
DR   BindingDB; Q8N752; -.
DR   ChEMBL; CHEMBL5520; -.
DR   DrugCentral; Q8N752; -.
DR   iPTMnet; Q8N752; -.
DR   PhosphoSitePlus; Q8N752; -.
DR   SwissPalm; Q8N752; -.
DR   BioMuta; CSNK1A1L; -.
DR   DMDM; 212286065; -.
DR   jPOST; Q8N752; -.
DR   MassIVE; Q8N752; -.
DR   MaxQB; Q8N752; -.
DR   PaxDb; 9606-ENSP00000369126; -.
DR   PeptideAtlas; Q8N752; -.
DR   ProteomicsDB; 72263; -.
DR   Pumba; Q8N752; -.
DR   Antibodypedia; 42131; 195 antibodies from 26 providers.
DR   DNASU; 122011; -.
DR   Ensembl; ENST00000379800.4; ENSP00000369126.3; ENSG00000180138.7.
DR   GeneID; 122011; -.
DR   KEGG; hsa:122011; -.
DR   MANE-Select; ENST00000379800.4; ENSP00000369126.3; NM_145203.6; NP_660204.2.
DR   UCSC; uc001uwm.2; human.
DR   AGR; HGNC:20289; -.
DR   CTD; 122011; -.
DR   DisGeNET; 122011; -.
DR   GeneCards; CSNK1A1L; -.
DR   HGNC; HGNC:20289; CSNK1A1L.
DR   HPA; ENSG00000180138; Tissue enriched (testis).
DR   neXtProt; NX_Q8N752; -.
DR   OpenTargets; ENSG00000180138; -.
DR   PharmGKB; PA134917108; -.
DR   VEuPathDB; HostDB:ENSG00000180138; -.
DR   eggNOG; KOG1163; Eukaryota.
DR   GeneTree; ENSGT00940000164967; -.
DR   HOGENOM; CLU_019279_2_7_1; -.
DR   InParanoid; Q8N752; -.
DR   OMA; CPPRIRT; -.
DR   OrthoDB; 1534388at2759; -.
DR   PhylomeDB; Q8N752; -.
DR   TreeFam; TF354246; -.
DR   PathwayCommons; Q8N752; -.
DR   SignaLink; Q8N752; -.
DR   SIGNOR; Q8N752; -.
DR   BioGRID-ORCS; 122011; 7 hits in 1147 CRISPR screens.
DR   GenomeRNAi; 122011; -.
DR   Pharos; Q8N752; Tdark.
DR   PRO; PR:Q8N752; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; Q8N752; Protein.
DR   Bgee; ENSG00000180138; Expressed in blood and 11 other tissues.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; 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; IBA:GO_Central.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd14128; STKc_CK1_alpha; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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:SF139; CASEIN KINASE I ISOFORM ALPHA-LIKE; 1.
DR   PANTHER; PTHR11909; CASEIN KINASE-RELATED; 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   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Wnt signaling pathway.
FT   CHAIN           1..337
FT                   /note="Casein kinase I isoform alpha-like"
FT                   /id="PRO_0000192830"
FT   DOMAIN          17..285
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          309..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        136
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         23..31
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         8
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P48729"
FT   VARIANT         5
FT                   /note="S -> G (in dbSNP:rs56224973)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042074"
FT   VARIANT         21
FT                   /note="R -> Q (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs373362769)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036450"
FT   VARIANT         21
FT                   /note="R -> W (in dbSNP:rs56158728)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042075"
FT   VARIANT         42
FT                   /note="D -> E (in dbSNP:rs9576175)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_042076"
FT   VARIANT         170
FT                   /note="R -> S (in dbSNP:rs17773251)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_034047"
FT   VARIANT         177
FT                   /note="E -> K (in dbSNP:rs17054882)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042077"
FT   VARIANT         220
FT                   /note="P -> L (in dbSNP:rs56252856)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042078"
FT   VARIANT         230
FT                   /note="K -> N (in dbSNP:rs56252523)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042079"
FT   VARIANT         257
FT                   /note="A -> T (in dbSNP:rs55895045)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042080"
FT   CONFLICT        225
FT                   /note="R -> K (in Ref. 3; AAH28723)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   337 AA;  39086 MW;  6110F854D739B142 CRC64;
     MTNNSGSKAE LVVGGKYKLV RKIGSGSFGD VYLGITTTNG EDVAVKLESQ KVKHPQLLYE
     SKLYTILQGG VGIPHMHWYG QEKDNNVLVM DLLGPSLEDL FNFCSRRFTM KTVLMLADQM
     ISRIEYVHTK NFLHRDIKPD NFLMGTGRHC NKLFLIDFGL AKKYRDNRTR QHIPYREDKH
     LIGTVRYASI NAHLGIEQSR RDDMESLGYV FMYFNRTSLP WQGLRAMTKK QKYEKISEKK
     MSTPVEVLCK GFPAEFAMYL NYCRGLRFEE VPDYMYLRQL FRILFRTLNH QYDYTFDWTM
     LKQKAAQQAA SSSGQGQQAQ TQTGKQTEKN KNNVKDN
//