KC1D_PONAB
ID KC1D_PONAB Reviewed; 415 AA.
AC Q5RC72;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. EIF6 phosphorylation promotes its nuclear
CC export. Triggers down-regulation of dopamine receptors in the
CC forebrain. Activates DCK in vitro by phosphorylation. TOP2A
CC phosphorylation favors DNA cleavable complex formation. May regulate
CC the formation of the mitotic spindle apparatus in extravillous
CC trophoblast. Modulates connexin-43/GJA1 gap junction assembly by
CC phosphorylation. Probably involved in lymphocyte physiology. Regulates
CC fast synaptic transmission mediated by glutamate (By similarity).
CC {ECO:0000250|UniProtKB:P48730}.
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: Exhibits substrate-dependent heparin activation.
CC Drug-mediated inhibition leads to a delay of the oscillations with the
CC magnitude of this effect dependent upon the timing of drug
CC administration. Inhibited by phosphorylation (By similarity).
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 {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell
CC membrane {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC Golgi 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}.
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DR EMBL; CR858408; CAH90635.1; -; mRNA.
DR RefSeq; NP_001125343.1; NM_001131871.1.
DR AlphaFoldDB; Q5RC72; -.
DR SMR; Q5RC72; -.
DR STRING; 9601.ENSPPYP00000009846; -.
DR GeneID; 100172245; -.
DR KEGG; pon:100172245; -.
DR CTD; 1453; -.
DR eggNOG; KOG1164; Eukaryota.
DR InParanoid; Q5RC72; -.
DR OrthoDB; 1097975at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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:0005819; C:spindle; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
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:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
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 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_0000354086"
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; 47304 MW; 627A0F07EE40813A CRC64;
MELRVGNRYR LGRKIGSGSF GDIYLGTDIA AGEEVAIKLE CVKTKPPQLH IESKIYKMMQ
GGVGIPTIRW CGAEGDYNVM VMELLGPSLE DLFNFCSRKF SLKTILLLAD 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
