KC1A_BOVIN
ID KC1A_BOVIN Reviewed; 325 AA.
AC P67827; P35506; Q9GLY1; Q9GLY2; Q9GLY3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Casein kinase I isoform alpha;
DE Short=CKI-alpha;
DE EC=2.7.11.1;
DE AltName: Full=CK1;
GN Name=CSNK1A1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=1946367; DOI=10.1073/pnas.88.21.9548;
RA Rowles J., Slaughter C., Moomaw C., Hsu J., Cobb M.H.;
RT "Purification of casein kinase I and isolation of cDNAs encoding multiple
RT casein kinase I-like enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9548-9552(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Hereford, Holstein, and Jersey; TISSUE=Blood;
RA Yamamoto N.;
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
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. Phosphorylates CTNNB1 at 'Ser-45'. May
CC phosphorylate PER1 and PER2. May play a role in segregating chromosomes
CC during mitosis. May play a role in keratin cytoskeleton disassembly and
CC thereby, it may regulate epithelial cell migration.
CC {ECO:0000250|UniProtKB:P48729}.
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: Interacts with the Axin complex (By similarity). Interacts
CC with TUT1, leading to TUT1 phosphorylation (By similarity). Interacts
CC with FAM83H; recruits CSNK1A1 to keratin filaments (By similarity).
CC Interacts with FAM83D (via N-terminus); in mitotic cells (By
CC similarity). {ECO:0000250|UniProtKB:P48729}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48729}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P48729}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:P48729}. Nucleus speckle
CC {ECO:0000250|UniProtKB:P48729}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q8BK63}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q8BK63}. Note=Localizes to the centrosome in
CC interphase cells, and to kinetochore fibers during mitosis. Also
CC recruited to the keratin cytoskeleton. {ECO:0000250|UniProtKB:P48729}.
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; M76543; AAA30451.1; -; mRNA.
DR EMBL; AB050943; BAB17767.1; -; Genomic_DNA.
DR EMBL; AB050944; BAB17768.1; -; Genomic_DNA.
DR EMBL; AB050946; BAB17806.1; -; Genomic_DNA.
DR PIR; A56406; A56406.
DR RefSeq; NP_777136.1; NM_174711.2.
DR AlphaFoldDB; P67827; -.
DR SMR; P67827; -.
DR STRING; 9913.ENSBTAP00000035028; -.
DR BindingDB; P67827; -.
DR ChEMBL; CHEMBL3337329; -.
DR PaxDb; P67827; -.
DR PRIDE; P67827; -.
DR Ensembl; ENSBTAT00000007007; ENSBTAP00000007007; ENSBTAG00000005326.
DR GeneID; 282684; -.
DR KEGG; bta:282684; -.
DR CTD; 1452; -.
DR VEuPathDB; HostDB:ENSBTAG00000005326; -.
DR VGNC; VGNC:55205; CSNK1A1.
DR eggNOG; KOG1163; Eukaryota.
DR GeneTree; ENSGT00940000153700; -.
DR HOGENOM; CLU_019279_2_7_1; -.
DR InParanoid; P67827; -.
DR OrthoDB; 1097975at2759; -.
DR BRENDA; 2.7.11.1; 908.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000005326; Expressed in neutrophil and 109 other tissues.
DR ExpressionAtlas; P67827; baseline and differential.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IDA:AgBase.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:AgBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:AgBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell cycle; Cell division; Cell projection;
KW Centromere; Chromosome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Kinase; Kinetochore; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P48729"
FT CHAIN 2..325
FT /note="Casein kinase I isoform alpha"
FT /id="PRO_0000192821"
FT DOMAIN 17..285
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
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 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P48729"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48729"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48729"
FT VARIANT 60
FT /note="E -> Q (in strain: Holstein)"
FT VARIANT 67
FT /note="L -> P (in strain: Jersey)"
FT VARIANT 96
FT /note="S -> T (in strain: Hereford)"
FT VARIANT 216
FT /note="R -> T (in strain: Jersey)"
FT CONFLICT 2
FT /note="A -> G (in Ref. 2; BAB17767/BAB17768/BAB17806)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="G -> R (in Ref. 2; BAB17767/BAB17768/BAB17806)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="I -> M (in Ref. 2; BAB17767/BAB17768/BAB17806)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="Y -> C (in Ref. 2; BAB17767/BAB17768/BAB17806)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="G -> E (in Ref. 2; BAB17767/BAB17768/BAB17806)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="E -> Q (in Ref. 2; BAB17767/BAB17768/BAB17806)"
FT /evidence="ECO:0000305"
FT CONFLICT 121..122
FT /note="IS -> MG (in Ref. 2; BAB17767/BAB17768)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="N -> S (in Ref. 2; BAB17767/BAB17768/BAB17806)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="Q -> H (in Ref. 2; BAB17767/BAB17768/BAB17806)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="R -> H (in Ref. 2; BAB17767/BAB17768/BAB17806)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="F -> S (in Ref. 2; BAB17767/BAB17768/BAB17806)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 37567 MW; B84DC84BDDC17854 CRC64;
MASSSGSKAE FIVGGKYKLV RKIGSGSFGD IYLAINITNG EEVAVKLESQ KARHPQLLYE
SKLYKILQGG VGIPHIRWYG QEKDYNVLVM DLLGPSLEDL FNFCSRRFTM KTVLMLADQM
ISRIEYVHTK NFIHRDIKPD NFLMGIGRHC NKLFLIDFGL AKKYRDNRTR QHIPYREDKN
LTGTARYASI NAHLGIEQSR RDDMESLGYV LMYFNRTSLP WQGLKAATKK QKYEKISEKK
MSTPVEVLCK GFPAEFAMYL NYCRGLRFEE APDYMYLRQL FRILFRTLNH QYDYTFDWTM
LKQKAAQQAA SSSGQGQQAQ TPTGF
