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Protein

Casein kinase I isoform delta

Gene

CSNK1D

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential serine/threonine-protein kinase that regulates diverse 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. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phospohorylation. Controls PER1 and PER2 nuclear transport and degradation. 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.17 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.
ATP + [tau protein] = ADP + [tau protein] phosphate.

Enzyme regulationi

Exhibits substrate-dependent heparin activation. Drug-mediated inhibition leads to a delay of the oscillations with the magnitude of this effect dependent upon the timing of drug administration. Inhibited by phosphorylation. Repressed by 3-[(2,4,6-trimethoxyphenyl)methylidenyl]-indolin-2-one (IC261), N-(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamide (CKI-7), 4-[4-(2,3-dihydro-benzo[1,4]dioxin-6-yl)-5-pyridin-2-yl-1H-imidazol-2-yl]benzamide (D4476), 3,4-diaryl-isoxazoles and -imidazoles, and 4-(3-cyclohexyl-5-(4-fluoro-phenyl)-3H-imidazol-4-yl) pyrimidin-2-ylamine (PF670462, PF670).10 Publications

Kineticsi

Maximal velocity nearly identical for the reactions with alpha-casein and PER2 peptide.

  1. KM=36.5 µM for alpha-casein1 Publication
  2. KM=635.8 µM for PER2 peptide1 Publication
  3. KM=180.6 µM for ATP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei38 – 381ATPPROSITE-ProRule annotation
    Active sitei128 – 1281Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 239ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    GO - Biological processi

    • circadian regulation of gene expression Source: UniProtKB
    • DNA repair Source: ProtInc
    • endocytosis Source: GO_Central
    • G2/M transition of mitotic cell cycle Source: Reactome
    • Golgi organization Source: SYSCILIA_CCNET
    • microtubule nucleation Source: SYSCILIA_CCNET
    • mitotic cell cycle Source: Reactome
    • nonmotile primary cilium assembly Source: SYSCILIA_CCNET
    • organelle organization Source: Reactome
    • peptidyl-serine phosphorylation Source: GO_Central
    • positive regulation of canonical Wnt signaling pathway Source: BHF-UCL
    • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    • positive regulation of protein phosphorylation Source: BHF-UCL
    • protein localization to centrosome Source: SYSCILIA_CCNET
    • protein localization to cilium Source: SYSCILIA_CCNET
    • protein localization to Golgi apparatus Source: SYSCILIA_CCNET
    • protein phosphorylation Source: UniProtKB
    • regulation of cell shape Source: GO_Central
    • regulation of circadian rhythm Source: UniProtKB
    • signal transduction Source: ProtInc
    • spindle assembly Source: UniProtKB
    • Wnt signaling pathway Source: GO_Central
    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Biological rhythms, Wnt signaling pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_24941. Circadian Clock.
    REACT_267965. Anchoring of the basal body to the plasma membrane.
    SignaLinkiP48730.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Casein kinase I isoform delta (EC:2.7.11.1)
    Short name:
    CKI-delta
    Short name:
    CKId
    Alternative name(s):
    Tau-protein kinase CSNK1D (EC:2.7.11.26)
    Gene namesi
    Name:CSNK1D
    Synonyms:HCKID
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:2452. CSNK1D.

    Subcellular locationi

    GO - Cellular componenti

    • centrosome Source: UniProtKB
    • cytoplasm Source: GO_Central
    • cytosol Source: Reactome
    • Golgi apparatus Source: UniProtKB
    • nucleus Source: UniProtKB
    • perinuclear region of cytoplasm Source: UniProtKB
    • plasma membrane Source: UniProtKB
    • spindle Source: UniProtKB
    • spindle microtubule Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Advanced sleep phase syndrome, familial, 2 (FASPS2)2 Publications

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA disorder characterized by very early sleep onset and offset. Individuals are 'morning larks' with a 4 hours advance of the sleep, temperature and melatonin rhythms.

    See also OMIM:615224
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti44 – 441T → A in FASPS2; strongly reduces kinase activity. 2 Publications
    VAR_029075
    Natural varianti46 – 461H → R in FASPS2; strongly reduces kinase activity. 1 Publication
    VAR_069801

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi38 – 381K → M: Impaired kinase activity and abnormal subcellular localization with exclusive accumulation to the nucleus. 1 Publication
    Mutagenesisi176 – 1761T → I: Impaired kinase activity and abnormal subcellular localization with exclusive accumulation to the nucleus. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi615224. phenotype.
    Orphaneti164736. Familial advanced sleep-phase syndrome.
    PharmGKBiPA26952.

    Polymorphism and mutation databases

    BioMutaiCSNK1D.
    DMDMi27923980.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 415415Casein kinase I isoform deltaPRO_0000192833Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei331 – 3311Phosphoserine1 Publication
    Modified residuei370 – 3701PhosphoserineBy similarity
    Modified residuei382 – 3821PhosphoserineBy similarity
    Modified residuei383 – 3831Phosphoserine1 Publication
    Modified residuei384 – 3841Phosphoserine1 Publication
    Modified residuei411 – 4111Phosphoserine1 Publication

    Post-translational modificationi

    Autophosphorylated on serine and threonine residues; this autophosphorylation represses activity. Reactivated by phosphatase-mediated dephosphorylation. May be dephosphorylated by PP1.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP48730.
    PaxDbiP48730.
    PRIDEiP48730.

    PTM databases

    PhosphoSiteiP48730.

    Expressioni

    Tissue specificityi

    Expressed in all tissues examined, including brain, heart, lung, liver, pancreas, kidney, placenta and skeletal muscle. However, kinase activity is not uniform, with highest kinase activity in splenocytes. In blood, highly expressed in hemopoietic cells and mature granulocytes. Also found in monocytes and lymphocytes.2 Publications

    Developmental stagei

    Highly present in extravillous trophoblast cells, which are present at the placenta implantation site and invade the decidua and decidual vessels.1 Publication

    Gene expression databases

    BgeeiP48730.
    CleanExiHS_CSNK1D.
    ExpressionAtlasiP48730. baseline and differential.
    GenevisibleiP48730. HS.

    Organism-specific databases

    HPAiCAB015410.

    Interactioni

    Subunit structurei

    Binds to DNMT1 and MAP1A (By similarity). Monomer. Component of the circadian core oscillator, which includes the CRY proteins, CLOCK, or NPAS2, ARTNL/BMAL1 or ARTNL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Interacts directly with PER1 and PER2 which may lead to their degradation. Interacts with MAPT/TAU, SNAPIN, DBNDD2, AIB1/NCOA3 and ESR1. AKAP9/AKAP450 binding promotes centrosomal subcellular location. Binds to tubulins in mitotic cells upon DNA damage.By similarity9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Dvl2Q608382EBI-751621,EBI-641940From a different organism.
    DVL3Q929974EBI-751621,EBI-739789
    LURAP1Q96LR24EBI-751621,EBI-741355
    MDM2Q009876EBI-751621,EBI-389668
    TRIM9Q9C0263EBI-751621,EBI-720828
    ZDHHC17Q8IUH53EBI-9087876,EBI-524753

    Protein-protein interaction databases

    BioGridi107837. 43 interactions.
    DIPiDIP-39735N.
    IntActiP48730. 19 interactions.
    MINTiMINT-1454355.
    STRINGi9606.ENSP00000324464.

    Structurei

    Secondary structure

    1
    415
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53Combined sources
    Turni6 – 83Combined sources
    Beta strandi9 – 168Combined sources
    Beta strandi21 – 288Combined sources
    Turni29 – 324Combined sources
    Beta strandi33 – 419Combined sources
    Beta strandi44 – 463Combined sources
    Helixi49 – 5911Combined sources
    Beta strandi68 – 747Combined sources
    Beta strandi77 – 837Combined sources
    Helixi89 – 957Combined sources
    Turni96 – 983Combined sources
    Helixi102 – 12120Combined sources
    Helixi131 – 1333Combined sources
    Beta strandi134 – 1363Combined sources
    Helixi139 – 1413Combined sources
    Beta strandi145 – 1473Combined sources
    Beta strandi154 – 1574Combined sources
    Turni159 – 1613Combined sources
    Helixi177 – 1793Combined sources
    Helixi182 – 1854Combined sources
    Helixi192 – 20817Combined sources
    Turni212 – 2154Combined sources
    Helixi223 – 23412Combined sources
    Helixi237 – 2404Combined sources
    Turni241 – 2433Combined sources
    Helixi247 – 25711Combined sources
    Helixi266 – 27914Combined sources
    Turni289 – 2924Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UYSX-ray2.30A/B/C/D1-294[»]
    3UYTX-ray2.00A/B/C/D1-294[»]
    3UZPX-ray1.94A/B1-294[»]
    4HGTX-ray1.80A/B1-294[»]
    4HNFX-ray2.07A/B1-294[»]
    4KB8X-ray1.95A/B/C/D3-317[»]
    4KBAX-ray1.98A/B/C/D3-317[»]
    4KBCX-ray1.98A/B1-317[»]
    4KBKX-ray2.10A/B/C/D3-317[»]
    4TW9X-ray2.40A/B1-295[»]
    4TWCX-ray1.70A/B1-295[»]
    ProteinModelPortaliP48730.
    SMRiP48730. Positions 3-294.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 277269Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni278 – 36487Centrosomal localization signal (CLS)Add
    BLAST
    Regioni317 – 34226AutoinhibitoryBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00760000119040.
    HOGENOMiHOG000182055.
    HOVERGENiHBG000176.
    InParanoidiP48730.
    KOiK08959.
    PhylomeDBiP48730.
    TreeFamiTF300544.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P48730-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MELRVGNRYR LGRKIGSGSF GDIYLGTDIA AGEEVAIKLE CVKTKHPQLH
    60 70 80 90 100
    IESKIYKMMQ GGVGIPTIRW CGAEGDYNVM VMELLGPSLE DLFNFCSRKF
    110 120 130 140 150
    SLKTVLLLAD QMISRIEYIH SKNFIHRDVK PDNFLMGLGK KGNLVYIIDF
    160 170 180 190 200
    GLAKKYRDAR THQHIPYREN KNLTGTARYA SINTHLGIEQ SRRDDLESLG
    210 220 230 240 250
    YVLMYFNLGS LPWQGLKAAT KRQKYERISE KKMSTPIEVL CKGYPSEFAT
    260 270 280 290 300
    YLNFCRSLRF DDKPDYSYLR QLFRNLFHRQ GFSYDYVFDW NMLKFGASRA
    310 320 330 340 350
    ADDAERERRD REERLRHSRN PATRGLPSTA SGRLRGTQEV APPTPLTPTS
    360 370 380 390 400
    HTANTSPRPV SGMERERKVS MRLHRGAPVN ISSSDLTGRQ DTSRMSTSQI
    410
    PGRVASSGLQ SVVHR
    Length:415
    Mass (Da):47,330
    Last modified:January 27, 2003 - v2
    Checksum:iB97F1717A52466D2
    GO
    Isoform 2 (identifier: P48730-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         400-415: IPGRVASSGLQSVVHR → NSIPFEHHGK

    Show »
    Length:409
    Mass (Da):46,832
    Checksum:i970B55B1AF6B56DD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti330 – 3301A → D in AAC50807 (PubMed:8786104).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti44 – 441T → A in FASPS2; strongly reduces kinase activity. 2 Publications
    VAR_029075
    Natural varianti46 – 461H → R in FASPS2; strongly reduces kinase activity. 1 Publication
    VAR_069801
    Natural varianti97 – 971S → C in breast cancer samples; infiltrating ductal carcinoma; somatic mutation. 2 Publications
    VAR_036451
    Natural varianti401 – 4011P → A.1 Publication
    Corresponds to variant rs56124628 [ dbSNP | Ensembl ].
    VAR_042081

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei400 – 41516IPGRV…SVVHR → NSIPFEHHGK in isoform 2. 2 PublicationsVSP_010253Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U29171 mRNA. Translation: AAC50807.1.
    U31285 mRNA. Translation: AAC50808.1.
    AB091044 mRNA. Translation: BAC10903.1.
    AK291758 mRNA. Translation: BAF84447.1.
    EF015900 Genomic DNA. Translation: ABM64211.1.
    BC003558 mRNA. Translation: AAH03558.1.
    BC015775 mRNA. Translation: AAH15775.1.
    CCDSiCCDS11805.1. [P48730-1]
    CCDS11806.1. [P48730-2]
    PIRiG01876.
    RefSeqiNP_001884.2. NM_001893.4. [P48730-1]
    NP_620693.1. NM_139062.2. [P48730-2]
    UniGeneiHs.631725.

    Genome annotation databases

    EnsembliENST00000314028; ENSP00000324464; ENSG00000141551.
    ENST00000392334; ENSP00000376146; ENSG00000141551. [P48730-2]
    GeneIDi1453.
    KEGGihsa:1453.
    UCSCiuc002kei.3. human. [P48730-2]
    uc002kej.3. human. [P48730-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U29171 mRNA. Translation: AAC50807.1.
    U31285 mRNA. Translation: AAC50808.1.
    AB091044 mRNA. Translation: BAC10903.1.
    AK291758 mRNA. Translation: BAF84447.1.
    EF015900 Genomic DNA. Translation: ABM64211.1.
    BC003558 mRNA. Translation: AAH03558.1.
    BC015775 mRNA. Translation: AAH15775.1.
    CCDSiCCDS11805.1. [P48730-1]
    CCDS11806.1. [P48730-2]
    PIRiG01876.
    RefSeqiNP_001884.2. NM_001893.4. [P48730-1]
    NP_620693.1. NM_139062.2. [P48730-2]
    UniGeneiHs.631725.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UYSX-ray2.30A/B/C/D1-294[»]
    3UYTX-ray2.00A/B/C/D1-294[»]
    3UZPX-ray1.94A/B1-294[»]
    4HGTX-ray1.80A/B1-294[»]
    4HNFX-ray2.07A/B1-294[»]
    4KB8X-ray1.95A/B/C/D3-317[»]
    4KBAX-ray1.98A/B/C/D3-317[»]
    4KBCX-ray1.98A/B1-317[»]
    4KBKX-ray2.10A/B/C/D3-317[»]
    4TW9X-ray2.40A/B1-295[»]
    4TWCX-ray1.70A/B1-295[»]
    ProteinModelPortaliP48730.
    SMRiP48730. Positions 3-294.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi107837. 43 interactions.
    DIPiDIP-39735N.
    IntActiP48730. 19 interactions.
    MINTiMINT-1454355.
    STRINGi9606.ENSP00000324464.

    Chemistry

    ChEMBLiCHEMBL3038494.
    GuidetoPHARMACOLOGYi1997.

    PTM databases

    PhosphoSiteiP48730.

    Polymorphism and mutation databases

    BioMutaiCSNK1D.
    DMDMi27923980.

    Proteomic databases

    MaxQBiP48730.
    PaxDbiP48730.
    PRIDEiP48730.

    Protocols and materials databases

    DNASUi1453.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000314028; ENSP00000324464; ENSG00000141551.
    ENST00000392334; ENSP00000376146; ENSG00000141551. [P48730-2]
    GeneIDi1453.
    KEGGihsa:1453.
    UCSCiuc002kei.3. human. [P48730-2]
    uc002kej.3. human. [P48730-1]

    Organism-specific databases

    CTDi1453.
    GeneCardsiGC17M080203.
    HGNCiHGNC:2452. CSNK1D.
    HPAiCAB015410.
    MIMi600864. gene.
    615224. phenotype.
    neXtProtiNX_P48730.
    Orphaneti164736. Familial advanced sleep-phase syndrome.
    PharmGKBiPA26952.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00760000119040.
    HOGENOMiHOG000182055.
    HOVERGENiHBG000176.
    InParanoidiP48730.
    KOiK08959.
    PhylomeDBiP48730.
    TreeFamiTF300544.

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_24941. Circadian Clock.
    REACT_267965. Anchoring of the basal body to the plasma membrane.
    SignaLinkiP48730.

    Miscellaneous databases

    ChiTaRSiCSNK1D. human.
    GeneWikiiCSNK1D.
    GenomeRNAii1453.
    NextBioi5961.
    PROiP48730.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP48730.
    CleanExiHS_CSNK1D.
    ExpressionAtlasiP48730. baseline and differential.
    GenevisibleiP48730. HS.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequence analysis of the cDNA for the human casein kinase I delta (CSNK1D) gene and its chromosomal localization."
      Kusuda J., Hidari N., Hidari M., Hashimoto K.
      Genomics 32:140-143(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Involvement of casein kinase Iepsilon in cytokine-induced granulocytic differentiation."
      Okamura A., Iwata N., Nagata A., Tamekane A., Shimoyama M., Gomyo H., Yakushijin K., Urahama N., Hamaguchi M., Fukui C., Chihara K., Ito M., Matsui T.
      Blood 103:2997-3004(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Hematopoietic stem cell.
    3. NHLBI resequencing and genotyping service (RS&G)
      Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Placenta.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Placenta and Spleen.
    6. "Regulation of casein kinase I epsilon and casein kinase I delta by an in vivo futile phosphorylation cycle."
      Rivers A., Gietzen K.F., Vielhaber E., Virshup D.M.
      J. Biol. Chem. 273:15980-15984(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, AUTOPHOSPHORYLATION.
    7. "Protein kinase CK1 is a p53-threonine 18 kinase which requires prior phosphorylation of serine 15."
      Dumaz N., Milne D.M., Meek D.W.
      FEBS Lett. 463:312-316(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS TP53 KINASE.
    8. "Interaction of casein kinase 1 delta (CK1delta) with post-Golgi structures, microtubules and the spindle apparatus."
      Behrend L., Stoeter M., Kurth M., Rutter G., Heukeshoven J., Deppert W., Knippschild U.
      Eur. J. Cell Biol. 79:240-251(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TUBULINS, SUBCELLULAR LOCATION.
    9. "Catalytic activity of protein kinase CK1 delta (casein kinase 1delta) is essential for its normal subcellular localization."
      Milne D.M., Looby P., Meek D.W.
      Exp. Cell Res. 263:43-54(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-38 AND THR-176.
    10. "Human casein kinase Idelta phosphorylation of human circadian clock proteins period 1 and 2."
      Camacho F., Cilio M., Guo Y., Virshup D.M., Patel K., Khorkova O., Styren S., Morse B., Yao Z., Keesler G.A.
      FEBS Lett. 489:159-165(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PER1 AND PER2.
    11. "Casein kinase 1 regulates connexin-43 gap junction assembly."
      Cooper C.D., Lampe P.D.
      J. Biol. Chem. 277:44962-44968(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS CONNEXIN-43/GJA1 KINASE, INTERACTION WITH CONNEXIN-43/GJA1.
    12. "Centrosomal anchoring of the protein kinase CK1delta mediated by attachment to the large, coiled-coil scaffolding protein CG-NAP/AKAP450."
      Sillibourne J.E., Milne D.M., Takahashi M., Ono Y., Meek D.W.
      J. Mol. Biol. 322:785-797(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AKAP9/AKAP450, SUBCELLULAR LOCATION.
    13. "Casein kinase 1 delta phosphorylates tau and disrupts its binding to microtubules."
      Li G., Yin H., Kuret J.
      J. Biol. Chem. 279:15938-15945(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS MAPT/TAU KINASE, ENZYME REGULATION, INTERACTION WITH MAPT/TAU.
    14. "Inhibition of casein kinase I delta alters mitotic spindle formation and induces apoptosis in trophoblast cells."
      Stoeter M., Bamberger A.-M., Aslan B., Kurth M., Speidel D., Loening T., Frank H.-G., Kaufmann P., Loehler J., Henne-Bruns D., Deppert W., Knippschild U.
      Oncogene 24:7964-7975(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MITOTIC SPINDLE FORMATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, ENZYME REGULATION.
    15. "Dysbindin structural homologue CK1BP is an isoform-selective binding partner of human casein kinase-1."
      Yin H., Laguna K.A., Li G., Kuret J.
      Biochemistry 45:5297-5308(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, INTERACTION WITH DBNDD2.
    16. "Phosphorylation at Ser244 by CK1 determines nuclear localization and substrate targeting of PKD2."
      von Blume J., Knippschild U., Dequiedt F., Giamas G., Beck A., Auer A., Van Lint J., Adler G., Seufferlein T.
      EMBO J. 26:4619-4633(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS PKD2 KINASE.
    17. "Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis."
      Hanger D.P., Byers H.L., Wray S., Leung K.-Y., Saxton M.J., Seereeram A., Reynolds C.H., Ward M.A., Anderton B.H.
      J. Biol. Chem. 282:23645-23654(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS MAPT/TAU KINASE.
    18. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331 AND SER-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "3,4-Diaryl-isoxazoles and -imidazoles as potent dual inhibitors of p38alpha mitogen activated protein kinase and casein kinase 1delta."
      Peifer C., Abadleh M., Bischof J., Hauser D., Schattel V., Hirner H., Knippschild U., Laufer S.
      J. Med. Chem. 52:7618-7630(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Casein kinase I delta/epsilon phosphorylates topoisomerase IIalpha at serine-1106 and modulates DNA cleavage activity."
      Grozav A.G., Chikamori K., Kozuki T., Grabowski D.R., Bukowski R.M., Willard B., Kinter M., Andersen A.H., Ganapathi R., Ganapathi M.K.
      Nucleic Acids Res. 37:382-392(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS TOP2A KINASE, ENZYME REGULATION.
    24. "CK1delta modulates the transcriptional activity of ERalpha via AIB1 in an estrogen-dependent manner and regulates ERalpha-AIB1 interactions."
      Giamas G., Castellano L., Feng Q., Knippschild U., Jacob J., Thomas R.S., Coombes R.C., Smith C.L., Jiao L.R., Stebbing J.
      Nucleic Acids Res. 37:3110-3123(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AIB1/NCOA3 AND ESR1 KINASE, INTERACTION WITH AIB1/NCOA3 AND ESR1.
    25. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    26. "Casein kinase 1delta activates human recombinant deoxycytidine kinase by Ser-74 phosphorylation, but is not involved in the in vivo regulation of its activity."
      Smal C., Vertommen D., Amsailale R., Arts A., Degand H., Morsomme P., Rider M.H., Neste E.V., Bontemps F.
      Arch. Biochem. Biophys. 502:44-52(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS DCK KINASE.
    27. "Isoform specific phosphorylation of p53 by protein kinase CK1."
      Venerando A., Marin O., Cozza G., Bustos V.H., Sarno S., Pinna L.A.
      Cell. Mol. Life Sci. 67:1105-1118(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS P53/TP53 KINASE, GENE FAMILY.
    28. "A coordinated phosphorylation by Lats and CK1 regulates YAP stability through SCF(beta-TRCP)."
      Zhao B., Li L., Tumaneng K., Wang C.-Y., Guan K.-L.
      Genes Dev. 24:72-85(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS YAP1 KINASE.
    29. "Casein kinase 1 regulates human hypoxia-inducible factor HIF-1."
      Kalousi A., Mylonis I., Politou A.S., Chachami G., Paraskeva E., Simos G.
      J. Cell Sci. 123:2976-2986(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS HIF1A KINASE.
    30. Cited for: FUNCTION IN CIRCADIAN RHYTHMS, ENZYME REGULATION.
    31. "Chronic treatment with a selective inhibitor of casein kinase I delta/epsilon yields cumulative phase delays in circadian rhythms."
      Sprouse J., Reynolds L., Kleiman R., Tate B., Swanson T.A., Pickard G.E.
      Psychopharmacology 210:569-576(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIRCADIAN RHYTHMS, ENZYME REGULATION.
    32. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    33. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. "Opposing action of casein kinase 1 and calcineurin in nucleo-cytoplasmic shuttling of mammalian translation initiation factor eIF6."
      Biswas A., Mukherjee S., Das S., Shields D., Chow C.W., Maitra U.
      J. Biol. Chem. 286:3129-3138(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS EIF6 KINASE, ENZYME REGULATION.
    35. "Casein kinase 1 delta functions at the centrosome to mediate Wnt-3a-dependent neurite outgrowth."
      Greer Y.E., Rubin J.S.
      J. Cell Biol. 192:993-1004(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS DVL2 AND DVL3 KINASE, ENZYME REGULATION, SUBCELLULAR LOCATION.
    36. "IC261 induces cell cycle arrest and apoptosis of human cancer cells via CK1delta/epsilon and Wnt/beta-catenin independent inhibition of mitotic spindle formation."
      Cheong J.K., Nguyen T.H., Wang H., Tan P., Voorhoeve P.M., Lee S.H., Virshup D.M.
      Oncogene 30:2558-2569(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, AUTOPHOSPHORYLATION.
    37. Cited for: REVIEW ON CIRCADIAN RHYTHMS, GENE FAMILY.
    38. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    39. "Crystallographic studies of casein kinase I delta toward a structural understanding of auto-inhibition."
      Longenecker K.L., Roach P.J., Hurley T.D.
      Acta Crystallogr. D 54:473-475(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    40. "Structural basis for the interaction between casein kinase 1 delta and a potent and selective inhibitor."
      Long A., Zhao H., Huang X.
      J. Med. Chem. 55:956-960(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 1-294 IN COMPLEX WITH INHIBITOR.
    41. "Structural basis for the potent and selective inhibition of casein kinase 1 epsilon."
      Long A.M., Zhao H., Huang X.
      J. Med. Chem. 55:10307-10311(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 1-294 IN COMPLEX WITH INHIBITOR.
    42. "Functional consequences of a CKIdelta mutation causing familial advanced sleep phase syndrome."
      Xu Y., Padiath Q.S., Shapiro R.E., Jones C.R., Wu S.C., Saigoh N., Saigoh K., Ptacek L.J., Fu Y.H.
      Nature 434:640-644(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FASPS2 ALA-44.
    43. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-97.
    44. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-97 AND ALA-401.
    45. Cited for: VARIANTS FASPS2 ALA-44 AND ARG-46, CHARACTERIZATION OF VARIANTS FASPS2 ALA-44 AND ARG-46, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiKC1D_HUMAN
    AccessioniPrimary (citable) accession number: P48730
    Secondary accession number(s): A2I2P2, Q96KZ6, Q9BTN5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 27, 2003
    Last modified: July 22, 2015
    This is version 159 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    May be involved in Alzheimer disease by phosphorylating MAPT/TAU.1 Publication

    Caution

    Was shown to phosphorylate and activate DCK in vitro but probably not in vivo.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.