KC1AL_HUMAN
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 03-AUG-2022, entry version 158.
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; 57.
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 BioMuta; CSNK1A1L; -.
DR DMDM; 212286065; -.
DR jPOST; Q8N752; -.
DR MassIVE; Q8N752; -.
DR MaxQB; Q8N752; -.
DR PaxDb; Q8N752; -.
DR PeptideAtlas; Q8N752; -.
DR PRIDE; Q8N752; -.
DR ProteomicsDB; 72263; -.
DR Antibodypedia; 42131; 184 antibodies from 25 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 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; WLIELVH; -.
DR OrthoDB; 614259at2759; -.
DR PhylomeDB; Q8N752; -.
DR TreeFam; TF354246; -.
DR PathwayCommons; Q8N752; -.
DR SignaLink; Q8N752; -.
DR SIGNOR; Q8N752; -.
DR BioGRID-ORCS; 122011; 6 hits in 1075 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: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: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:0018105; P:peptidyl-serine phosphorylation; 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; 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; 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 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
