ID   Q59FJ7_HUMAN            Unreviewed;       342 AA.
AC   Q59FJ7;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Casein kinase I isoform delta {ECO:0000256|ARBA:ARBA00041017};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.26 {ECO:0000256|ARBA:ARBA00012407};
DE   AltName: Full=Tau-protein kinase CSNK1D {ECO:0000256|ARBA:ARBA00041797};
DE   Flags: Fragment;
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 {ECO:0000313|EMBL:BAD92700.1};
RN   [1] {ECO:0000313|EMBL:BAD92700.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:BAD92700.1};
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001127};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC         Evidence={ECO:0000256|ARBA:ARBA00001127};
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:0000256|ARBA:ARBA00036761};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12802;
CC         Evidence={ECO:0000256|ARBA:ARBA00036761};
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:0000256|ARBA:ARBA00001416};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC         Evidence={ECO:0000256|ARBA:ARBA00001416};
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:0000256|ARBA:ARBA00036446};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53905;
CC         Evidence={ECO:0000256|ARBA:ARBA00036446};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; AB209463; BAD92700.1; -; mRNA.
DR   AlphaFoldDB; Q59FJ7; -.
DR   IntAct; Q59FJ7; 4.
DR   MINT; Q59FJ7; -.
DR   MaxQB; Q59FJ7; -.
DR   PeptideAtlas; Q59FJ7; -.
DR   ProteomicsDB; 62650; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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; 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   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   Kinase {ECO:0000313|EMBL:BAD92700.1};
KW   Transferase {ECO:0000313|EMBL:BAD92700.1};
KW   Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT   DOMAIN          1..169
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          193..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..292
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAD92700.1"
SQ   SEQUENCE   342 AA;  39607 MW;  486A69476457CACB CRC64;
     CREEISRIEY IHSKNFIHRD VKPDNFLMGL GKKGNLVYII DFGLAKKYRD ARTHQHIPYR
     ENKNLTGTAR YASINTHLGI EQSRRDDLES LGYVLMYFNL GSLPWQGLKA ATKRQKYERI
     SEKKMSTPIE VLCKGYPSEF ATYLNFCRSL RFDDKPDYSY LRQLFRNLFH RQGFSYDYVF
     DWNMLKFGAS RAADDAERER RDREERLRHS RNPATRGLPS TASGRLRGTQ EVAPPTPLTP
     TSHTANTSPR PVSGMERERK VSMRLHRGAP VNISSSDLTG RQDTSRMSTS QVGAELPGGR
     WASGYPVRVK SGLWFLQGFF FPFFPPFLRV FNLARVWRLG CR
//