KC1A_RAT
ID KC1A_RAT Reviewed; 325 AA.
AC P97633; P97634;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 161.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Sprague-Dawley;
RX PubMed=8973207; DOI=10.1021/bi9614444;
RA Zhang J., Gross S.D., Schroeder M.D., Anderson R.A.;
RT "Casein kinase I alpha and alpha L: alternative splicing-generated kinases
RT exhibit different catalytic properties.";
RL Biochemistry 35:16319-16327(1996).
RN [2]
RP ROLE IN WNT SIGNALING.
RX PubMed=11955436; DOI=10.1016/s0092-8674(02)00685-2;
RA Liu C., Li Y., Semenov M., Han C., Baeg G.-H., Tan Y., Zhang Z., Lin X.,
RA He X.;
RT "Control of beta-catenin phosphorylation/degradation by a dual-kinase
RT mechanism.";
RL Cell 108:837-847(2002).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P48729, ECO:0000269|PubMed:11955436}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Isoforms exhibit differences in binding and activity toward
CC common CKI substrates.;
CC Name=1; Synonyms=CKI-alpha;
CC IsoId=P97633-1; Sequence=Displayed;
CC Name=2; Synonyms=CKI-alpha-L;
CC IsoId=P97633-2; Sequence=VSP_004745;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U77582; AAB19227.1; -; mRNA.
DR EMBL; U77583; AAB19228.1; -; Genomic_DNA.
DR RefSeq; NP_446067.1; NM_053615.1. [P97633-1]
DR AlphaFoldDB; P97633; -.
DR SMR; P97633; -.
DR BioGRID; 250223; 2.
DR IntAct; P97633; 2.
DR MINT; P97633; -.
DR STRING; 10116.ENSRNOP00000051516; -.
DR BindingDB; P97633; -.
DR iPTMnet; P97633; -.
DR PhosphoSitePlus; P97633; -.
DR jPOST; P97633; -.
DR PeptideAtlas; P97633; -.
DR PRIDE; P97633; -.
DR GeneID; 113927; -.
DR KEGG; rno:113927; -.
DR UCSC; RGD:71098; rat. [P97633-1]
DR CTD; 1452; -.
DR RGD; 71098; Csnk1a1.
DR eggNOG; KOG1163; Eukaryota.
DR InParanoid; P97633; -.
DR OrthoDB; 1097975at2759; -.
DR BRENDA; 2.7.11.1; 5301.
DR Reactome; R-RNO-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-RNO-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-RNO-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-RNO-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-RNO-5635838; Activation of SMO.
DR PRO; PR:P97633; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030877; C:beta-catenin destruction complex; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0016607; C:nuclear speck; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0000287; F:magnesium ion binding; IDA:RGD.
DR GO; GO:0042277; F:peptide binding; IDA:RGD.
DR GO; GO:0051219; F:phosphoprotein binding; IDA:RGD.
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:ParkinsonsUK-UCL.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR GO; GO:0007030; P:Golgi organization; ISO:RGD.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
DR GO; GO:1904424; P:regulation of GTP binding; ISO:RGD.
DR GO; GO:0043278; P:response to morphine; IEP:RGD.
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; Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Cell projection; Centromere; Chromosome; Cytoplasm; Cytoskeleton; Kinase;
KW 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_0000192826"
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 VAR_SEQ 152
FT /note="K -> KCLESPVGKRKRSMTVSPSQDPSFSGLNQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8973207"
FT /id="VSP_004745"
FT MOD_RES P97633-2:156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 325 AA; 37495 MW; 484DC84B33F99BDB CRC64;
MASSSGSKAE FIVGGKYKLV RKIGSGSFGD IYLAINITNG EEVAVKLESQ KARHPQLLYE
SKLYKILQGG VGIPHIRWYG QGKDYNVLVM DLLGPSLEDL FNFCSRRFTM KTVLMLADQM
ISRIEYVHTK NFIHRDIKPD NFLMGIGRHC NKLFLIDFGL AKKYRDNRTR QHIPYREDKN
LTGTARYASI NAHLGIEQSR RDDMESLGYV LMYFNRTSLP WQGLKAATKK QKYEKISEKK
MSTPVEVLCK GFPAEFAMYL NYCRGLRFEE APDYMYLRQL FRILFRTLNH QYDYTFDWTM
LKQKAAQQAA SSSGQGQQAQ TPTGF
