EKS-HOS-00460
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-HOS-00460
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
CK1/CK1490.35.8E-1479269261
StatusReviewed
Ensembl ProteinENSP00000376146
UniProt AccessionP48730; A2I2P2; Q96KZ6; Q9BTN5;
Protein NameCasein kinase I isoform delta
Protein Synonyms/Alias CKI-delta; CKId; Tau-protein kinase CSNK1D;
Gene NameCSNK1D
Gene Synonyms/Alias CSNK1D; HCKID;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSG00000141551ENSP00000324464ENST00000314028
ENSG00000141551ENSP00000463757ENST00000580446
ENSG00000141551ENSP00000381531ENST00000398519
ENSG00000141551ENSP00000269361ENST00000269361
ENSG00000141551ENSP00000463906ENST00000580784
ENSG00000141551ENSP00000376146ENST00000392334
ENSG00000141551ENSP00000464551ENST00000581660
ENSG00000141551ENSP00000385769ENST00000403276
ENSG00000141551ENSP00000462144ENST00000585026
ENSG00000141551ENSP00000462079ENST00000584672
OrganismHomo sapiens
Functional DescriptionEssential serine/threonine-protein kinase that regulatesdiverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. May act as a negative regulator of circadian rhythmicity by phosphorylating PER1 and PER2, leading to retain PER1 in the cytoplasm. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA- binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. EIF6 phosphorylation promotes its nuclear export. Triggers down-regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate.
Protein Length409
Protein Sequence
(FASTA)
MELRVGNRYR LGRKIGSGSF GDIYLGTDIA AGEEVAIKLE CVKTKHPQLH IESKIYKMMQ 60
GGVGIPTIRW CGAEGDYNVM VMELLGPSLE DLFNFCSRKF SLKTVLLLAD QMISRIEYIH 120
SKNFIHRDVK PDNFLMGLGK KGNLVYIIDF GLAKKYRDAR THQHIPYREN KNLTGTARYA 180
SINTHLGIEQ SRRDDLESLG YVLMYFNLGS LPWQGLKAAT KRQKYERISE KKMSTPIEVL 240
CKGYPSEFAT YLNFCRSLRF DDKPDYSYLR QLFRNLFHRQ GFSYDYVFDW NMLKFGASRA 300
ADDAERERRD REERLRHSRN PATRGLPSTA SGRLRGTQEV APPTPLTPTS HTANTSPRPV 360
SGMERERKVS MRLHRGAPVN ISSSDLTGRQ DTSRMSTSQN SIPFEHHGK 409
Nucleotide Sequence
(FASTA)
ATGGAGCTGA GAGTCGGGAA CAGGTACCGG CTGGGCCGGA AGATCGGCAG CGGCTCCTTC 60
GGAGACATCT ATCTCGGTAC GGACATTGCT GCAGGAGAAG AGGTTGCCAT CAAGCTTGAA 120
TGTGTCAAAA CCAAACACCC TCAGCTCCAC ATTGAGAGCA AAATCTACAA GATGATGCAG 180
GGAGGAGTGG GCATCCCCAC CATCAGATGG TGCGGGGCAG AGGGGGACTA CAACGTCATG 240
GTGATGGAGC TGCTGGGGCC AAGCCTGGAG GACCTCTTCA ACTTCTGCTC CAGGAAATTC 300
AGCCTCAAAA CCGTCCTGCT GCTTGCTGAC CAAATGATCA GTCGCATCGA ATACATTCAT 360
TCAAAGAACT TCATCCACCG GGATGTGAAG CCAGACAACT TCCTCATGGG CCTGGGGAAG 420
AAGGGCAACC TGGTGTACAT CATCGACTTC GGGCTGGCCA AGAAGTACCG GGATGCACGC 480
ACCCACCAGC ACATCCCCTA TCGTGAGAAC AAGAACCTCA CGGGGACGGC GCGGTACGCC 540
TCCATCAACA CGCACCTTGG AATTGAACAA TCCCGAAGAG ATGACTTGGA GTCTCTGGGC 600
TACGTGCTAA TGTACTTCAA CCTGGGCTCT CTCCCCTGGC AGGGGCTGAA GGCTGCCACC 660
AAGAGACAGA AATACGAAAG GATTAGCGAG AAGAAAATGT CCACCCCCAT CGAAGTGTTG 720
TGTAAAGGCT ACCCTTCCGA ATTTGCCACA TACCTGAATT TCTGCCGTTC CTTGCGTTTT 780
GACGACAAGC CTGACTACTC GTACCTGCGG CAGCTTTTCC GGAATCTGTT CCATCGCCAG 840
GGCTTCTCCT ATGACTACGT GTTCGACTGG AACATGCTCA AATTTGGTGC CAGCCGGGCC 900
GCCGATGACG CCGAGCGGGA GCGCAGGGAC CGAGAGGAGC GGCTGAGACA CTCGCGGAAC 960
CCGGCTACCC GCGGCCTCCC TTCCACAGCC TCCGGCCGCC TGCGGGGGAC GCAGGAAGTG 1020
GCTCCCCCCA CACCCCTCAC CCCTACCTCA CACACGGCTA ACACCTCCCC CCGGCCCGTC 1080
TCCGGCATGG AGAGAGAGCG GAAAGTGAGT ATGCGGCTGC ACCGCGGGGC CCCCGTCAAC 1140
ATCTCCTCGT CCGACCTCAC AGGCCGACAA GATACCTCTC GCATGTCCAC CTCACAGAAT 1200
AGCATTCCTT TCGAACACCA CGGCAAGTAG 1230
Domain Profile
S: 1     yrvvkkiGsGsfGdiylgknlasgeevaikleskkskapqlklesrvykilqggvgiPev  60
         yr+++kiGsGsfGdiylg+++a+geevaikle++k+k+pql++es++yk++qggvgiP++
Q: 9     YRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTI  68
         89**********************************************************
S: 61    ryfgkekkynvlvldllGpsledlfdlcerkfslktvllladqlisrieyvhskeliyrd  120
         r++g+e++ynv+v++llGpsledlf++c+rkfslktvllladq+isriey+hsk++i+rd
Q: 69    RWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRD  128
         ************************************************************
S: 121   ikPdnfllgigrkgkkvylidfGlakkyrdaktkkhipyreeksltGtaryasinthlgk  180
         +kPdnfl+g+g+kg+ vy+idfGlakkyrda+t++hipyre+k+ltGtaryasinthlg+
Q: 129   VKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGI  188
         ************************************************************
S: 181   eqsrrddleslgyvllyflrgslPWqglkaatkkqkyekisekklstsievlcegfPeef  240
         eqsrrddleslgyvl+yf+ gslPWqglkaatk+qkye+isekk+st+ievlc+g+P+ef
Q: 189   EQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEF  248
         ************************************************************
S: 241   atylkyvrklkfeekPdyeyl  261
         atyl+++r+l+f++kPdy+yl
Q: 249   ATYLNFCRSLRFDDKPDYSYL  269
         *******************97
Domain Sequence
(FASTA)
YRLGRKIGSG SFGDIYLGTD IAAGEEVAIK LECVKTKHPQ LHIESKIYKM MQGGVGIPTI 60
RWCGAEGDYN VMVMELLGPS LEDLFNFCSR KFSLKTVLLL ADQMISRIEY IHSKNFIHRD 120
VKPDNFLMGL GKKGNLVYII DFGLAKKYRD ARTHQHIPYR ENKNLTGTAR YASINTHLGI 180
EQSRRDDLES LGYVLMYFNL GSLPWQGLKA ATKRQKYERI SEKKMSTPIE VLCKGYPSEF 240
ATYLNFCRSL RFDDKPDYSY L 261
Keyword3D-structure; Alternative splicing; ATP-binding; Biological rhythms; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; Golgi apparatus; Kinase; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
Sequence SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Bos taurus"; ?>Caenorhabditis elegans"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Ciona intestinalis"; ?>Ciona savignyi"; ?>Danio rerio"; ?>Dasypus novemcinctus"; ?>Dipodomys ordii"; ?>Drosophila melanogaster"; ?>Equus caballus"; ?>Erinaceus europaeus"; ?>Felis catus"; ?>Gadus morhua"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Gorilla gorilla"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Macropus eugenii"; ?>Meleagris gallopavo"; ?>Microcebus murinus"; ?>Monodelphis domestica"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Ochotona princeps"; ?>Oreochromis niloticus"; ?>Ornithorhynchus anatinus"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Petromyzon marinus"; ?>Pongo abelii"; ?>Procavia capensis"; ?>Pteropus vampyrus"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Sorex araneus"; ?>Taeniopygia guttata"; ?>Takifugu rubripes"; ?>Tarsius syrichta"; ?>Tetraodon nigroviridis"; ?>Tursiops truncatus"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>Saccharomyces cerevisiae"; ?>Schizosaccharomyces pombe"; ?>
EKS-AIM-00425
EKS-ANC-00440
EKS-BOT-00452
EKS-CAE-00380
EKS-CAJ-00457
EKS-CAF-00456
EKS-CAP-00485
EKS-CII-00257
EKS-CIS-00212
EKS-DAR-00859
EKS-DAN-00027
EKS-DIO-00094
EKS-DRM-00213
EKS-EQC-00445
EKS-ERE-00046
EKS-FEC-00433
EKS-GAM-00265
EKS-GAG-00380
EKS-GAA-00549
EKS-GOG-00445
EKS-ICT-00436
EKS-LAC-00465
EKS-LOA-00463
EKS-MAM-00450
EKS-MAE-00069
EKS-MEG-00371
EKS-MIM-00080
EKS-MOD-00443
EKS-MUM-00485
EKS-MUP-00448
EKS-MYL-00448
EKS-NOL-00412
EKS-OCP-00116
EKS-ORN-00572
EKS-ORA-00393
EKS-ORC-00427
EKS-ORL-00523
EKS-OTG-00455
EKS-PAT-00427
EKS-PES-00401
EKS-PEM-00248
EKS-POA-00440
EKS-PRC-00057
EKS-PTV-00160
EKS-RAN-00466
EKS-SAH-00423
EKS-SOA-00043
EKS-TAG-00516
EKS-TAR-00565
EKS-TAS-00063
EKS-TEN-00566
EKS-TUT-00161
EKS-XET-00604
EKS-XIM-00564
EKS-SAC-00093
EKS-SCP-00094
Gene Ontology
GO:0005813; C:centrosome
GO:0005829; C:cytosol
GO:0005794; C:Golgi apparatus
GO:0005634; C:nucleus
GO:0048471; C:perinuclear region of cytoplasm
GO:0005886; C:plasma membrane
GO:0005876; C:spindle microtubule
GO:0005524; F:ATP binding
GO:0004672; F:protein kinase activity
GO:0004674; F:protein serine/threonine kinase activity
GO:0050321; F:tau-protein kinase activity
GO:0032922; P:circadian regulation of gene expression
GO:0006281; P:DNA repair
GO:0000086; P:G2/M transition of mitotic cell cycle
GO:0090263; P:positive regulation of canonical Wnt receptor signaling pathway
GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process
GO:0001934; P:positive regulation of protein phosphorylation
GO:0042752; P:regulation of circadian rhythm
GO:0007165; P:signal transduction
GO:0051225; P:spindle assembly
GO:0016055; P:Wnt receptor signaling pathway
KEGG
hsa:1453;
InterPros
IPR011009; Kinase-like_dom.
IPR000719; Prot_kinase_cat_dom.
IPR017441; Protein_kinase_ATP_BS.
IPR008271; Ser/Thr_kinase_AS.
Pfam
PF00069; Pkinase; 1.
SMARTs
Prosites
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
Prints
Created Date20-Feb-2013