ID KC1D_BOVIN Reviewed; 415 AA. AC P35508; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 24-JAN-2024, entry version 177. DE RecName: Full=Casein kinase I isoform delta; DE Short=CKI-delta; DE Short=CKId; DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P48730}; DE AltName: Full=Tau-protein kinase CSNK1D; DE EC=2.7.11.26 {ECO:0000250|UniProtKB:P48730}; GN Name=CSNK1D; Synonyms=HCKID; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford; RX PubMed=19390049; DOI=10.1126/science.1169588; RG The bovine genome sequencing and analysis consortium; RT "The genome sequence of taurine cattle: a window to ruminant biology and RT evolution."; RL Science 324:522-528(2009). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 137-178. 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). CC -!- FUNCTION: Essential serine/threonine-protein kinase that regulates CC diverse cellular growth and survival processes including Wnt signaling, CC DNA repair and circadian rhythms. It can phosphorylate a large number CC of proteins. Casein kinases are operationally defined by their CC preferential utilization of acidic proteins such as caseins as CC substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, CC TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, CC PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In CC balance with PP1, determines the circadian period length through the CC regulation of the speed and rhythmicity of PER1 and PER2 CC phosphorylation. Controls PER1 and PER2 nuclear transport and CC degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 CC ubiquitin ligase-mediated ubiquitination and subsequent degradation. CC DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation CC of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. CC Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that CC controls neurite outgrowth. Phosphorylates NEDD9/HEF1 (By similarity). CC EIF6 phosphorylation promotes its nuclear export. Triggers down- CC regulation of dopamine receptors in the forebrain. Activates DCK in CC vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable CC complex formation. May regulate the formation of the mitotic spindle CC apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap CC junction assembly by phosphorylation. Probably involved in lymphocyte CC physiology. Regulates fast synaptic transmission mediated by glutamate CC (By similarity). {ECO:0000250|UniProtKB:P48730, CC ECO:0000250|UniProtKB:Q9DC28}. 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 Evidence={ECO:0000250|UniProtKB:P48730}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; CC Evidence={ECO:0000250|UniProtKB:P48730}; 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; Evidence={ECO:0000250|UniProtKB:P48730}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; CC Evidence={ECO:0000250|UniProtKB:P48730}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl- CC [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA- CC COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26; CC Evidence={ECO:0000250|UniProtKB:P48730}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12802; CC Evidence={ECO:0000250|UniProtKB:P48730}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L- CC threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703, CC Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.26; Evidence={ECO:0000250|UniProtKB:P48730}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53905; CC Evidence={ECO:0000250|UniProtKB:P48730}; CC -!- ACTIVITY REGULATION: Drug-mediated inhibition leads to a delay of the CC oscillations with the magnitude of this effect dependent upon the CC timing of drug administration. Inhibited by phosphorylation (By CC similarity). Exhibits substrate-dependent heparin activation. CC {ECO:0000250|UniProtKB:P48730}. CC -!- SUBUNIT: Monomer (By similarity). Component of the circadian core CC oscillator, which includes the CRY proteins, CLOCK, or NPAS2, CC ARTNL/BMAL1 or ARTNL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER CC proteins (By similarity). Interacts with DNMT1 and MAP1A (By CC similarity). Interacts directly with PER1 and PER2 which may lead to CC their degradation (By similarity). Interacts with MAPT/TAU, SNAPIN, CC DBNDD2, AIB1/NCOA3 and ESR1 (By similarity). Interacts with CC AKAP9/AKAP450; this interaction promotes centrosomal subcellular CC location (By similarity). Binds to tubulins in mitotic cells upon DNA CC damage (By similarity). Interacts with GJA1 (By similarity). Interacts CC with DDX3X; this interaction enhances CSNK1D kinase activity in vitro, CC but it is unclear whether this interaction is physiologically relevant CC (By similarity). {ECO:0000250|UniProtKB:P48730, CC ECO:0000250|UniProtKB:Q06486, ECO:0000250|UniProtKB:Q9DC28}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. CC Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Golgi CC apparatus {ECO:0000250}. Note=Localized at mitotic spindle CC microtubules, and at the centrosomes and interphase in interphase CC cells. Recruited to the spindle apparatus and the centrosomes in CC response to DNA-damage. Correct subcellular localization requires CC kinase activity (By similarity). {ECO:0000250}. CC -!- PTM: Autophosphorylated on serine and threonine residues; this CC autophosphorylation represses activity. Reactivated by phosphatase- CC mediated dephosphorylation. May be dephosphorylated by PP1 (By CC similarity). {ECO:0000250}. 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; M76545; AAA30453.1; -; mRNA. DR PIR; C56406; C56406. DR RefSeq; XP_005221107.1; XM_005221050.2. DR AlphaFoldDB; P35508; -. DR SMR; P35508; -. DR STRING; 9913.ENSBTAP00000059105; -. DR PaxDb; 9913-ENSBTAP00000026621; -. DR Ensembl; ENSBTAT00000026621.5; ENSBTAP00000026621.4; ENSBTAG00000019986.5. DR GeneID; 523542; -. DR VEuPathDB; HostDB:ENSBTAG00000019986; -. DR VGNC; VGNC:27766; CSNK1D. DR eggNOG; KOG1164; Eukaryota. DR GeneTree; ENSGT00940000153536; -. DR InParanoid; P35508; -. DR OMA; IFDWTFL; -. DR TreeFam; TF300544; -. DR Reactome; R-BTA-204005; COPII-mediated vesicle transport. DR Reactome; R-BTA-2565942; Regulation of PLK1 Activity at G2/M Transition. DR Reactome; R-BTA-380259; Loss of Nlp from mitotic centrosomes. DR Reactome; R-BTA-380270; Recruitment of mitotic centrosome proteins and complexes. DR Reactome; R-BTA-380284; Loss of proteins required for interphase microtubule organization from the centrosome. DR Reactome; R-BTA-380320; Recruitment of NuMA to mitotic centrosomes. DR Reactome; R-BTA-5620912; Anchoring of the basal body to the plasma membrane. DR Reactome; R-BTA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR Reactome; R-BTA-8854518; AURKA Activation by TPX2. DR Proteomes; UP000009136; Chromosome 19. DR Bgee; ENSBTAG00000019986; Expressed in myometrium and 105 other cell types or tissues. DR ExpressionAtlas; P35508; baseline. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl. DR GO; GO:0000139; C:Golgi membrane; IDA:AgBase. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central. 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:Ensembl. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:AgBase. DR GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC. DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB. DR GO; GO:0006897; P:endocytosis; IBA:GO_Central. DR GO; GO:0007030; P:Golgi organization; IEA:Ensembl. DR GO; GO:0007020; P:microtubule nucleation; IEA:Ensembl. DR GO; GO:1905515; P:non-motile cilium assembly; IBA:GO_Central. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:AgBase. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl. DR GO; GO:0071539; P:protein localization to centrosome; IEA:Ensembl. DR GO; GO:0061512; P:protein localization to cilium; IEA:Ensembl. DR GO; GO:0034067; P:protein localization to Golgi apparatus; IEA:Ensembl. DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB. DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR CDD; cd14125; STKc_CK1_delta_epsilon; 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:SF18; CASEIN KINASE I ISOFORM DELTA; 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 ATP-binding; Biological rhythms; Cell membrane; Cytoplasm; Cytoskeleton; KW Golgi apparatus; Kinase; Membrane; Methylation; Nucleotide-binding; KW Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase; Wnt signaling pathway. FT CHAIN 1..415 FT /note="Casein kinase I isoform delta" FT /id="PRO_0000192832" FT DOMAIN 9..277 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 278..364 FT /note="Centrosomal localization signal (CLS)" FT /evidence="ECO:0000250" FT REGION 301..415 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 317..342 FT /note="Autoinhibitory" FT /evidence="ECO:0000250" FT COMPBIAS 301..320 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 342..359 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 380..415 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 128 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 15..23 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 38 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 328 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48730" FT MOD_RES 331 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48730" FT MOD_RES 370 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q06486" FT MOD_RES 375 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9DC28" FT MOD_RES 382 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48730" FT MOD_RES 383 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48730" FT MOD_RES 384 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48730" FT MOD_RES 407 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48730" FT MOD_RES 411 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48730" SQ SEQUENCE 415 AA; 47330 MW; B97F1717A52466D2 CRC64; MELRVGNRYR LGRKIGSGSF GDIYLGTDIA AGEEVAIKLE CVKTKHPQLH IESKIYKMMQ GGVGIPTIRW CGAEGDYNVM VMELLGPSLE DLFNFCSRKF SLKTVLLLAD QMISRIEYIH SKNFIHRDVK PDNFLMGLGK KGNLVYIIDF GLAKKYRDAR THQHIPYREN KNLTGTARYA SINTHLGIEQ SRRDDLESLG YVLMYFNLGS LPWQGLKAAT KRQKYERISE KKMSTPIEVL CKGYPSEFAT YLNFCRSLRF DDKPDYSYLR QLFRNLFHRQ GFSYDYVFDW NMLKFGASRA ADDAERERRD REERLRHSRN PATRGLPSTA SGRLRGTQEV APPTPLTPTS HTANTSPRPV SGMERERKVS MRLHRGAPVN ISSSDLTGRQ DTSRMSTSQI PGRVASSGLQ SVVHR //