CSNK1D
entrez
1453
canonical
uniprot
P48730
canonical
ensembl
ENSG00000141551
resolver
ensp
ENSP00000324464
resolver
ensp
ENSP00000376146
resolver
ensp
ENSP00000381531
resolver
ensp
ENSP00000673968
resolver
enst
ENST00000398519
resolver
genesymbol
CSNK1D
resolver
genesymbol_syn
HCKID
resolver
hgnc
HGNC:2452
resolver
uniprot
A2I2P2
resolver
uniprot
H7BYT1
resolver
uniprot
Q96KZ6
resolver
uniprot
Q9BTN5
resolver
uniprot_entry
H7BYT1_HUMAN
resolver
uniprot_entry
KC1D_HUMAN
resolver
uniprot_sec
A2I2P2
resolver
uniprot_sec
Q96KZ6
resolver
uniprot_sec
Q9BTN5
resolver
activity_regulation
ACTIVITY REGULATION: 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). {ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:16027726, ECO:0000269|PubMed:19043076, ECO:0000269|PubMed:19591487, ECO:0000269|PubMed:20407760, ECO:0000269|PubMed:20696890, ECO:0000269|PubMed:21084295, ECO:0000269|PubMed:21258417, ECO:0000269|PubMed:21422228, ECO:0000269|PubMed:9632646}.
uniprot
proteins
amino_acid_sequence
MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRAADDAERERRDREERLRHSRNPATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPVSGMERERKVSMRLHRGAPVNISSSDLTGRQDTSRMSTSQIPGRVASSGLQSVVHR
uniprot
proteins
disease_involvement
DISEASE: Advanced sleep phase syndrome, familial, 2 (FASPS2) [MIM:615224]: An autosomal dominant 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. {ECO:0000269|PubMed:15800623, ECO:0000269|PubMed:23636092}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
ec_number
2.7.11.26
uniprot
proteins
function
FUNCTION: 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 phosphorylation. 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. Phosphorylates NEDD9/HEF1 (By similarity). 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. {ECO:0000250|UniProtKB:Q9DC28, ECO:0000269|PubMed:10606744, ECO:0000269|PubMed:12270943, ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:16027726, ECO:0000269|PubMed:17562708, ECO:0000269|PubMed:17962809, ECO:0000269|PubMed:19043076, ECO:0000269|PubMed:20041275, ECO:0000269|PubMed:20048001, ECO:0000269|PubMed:20407760, ECO:0000269|PubMed:20637175, ECO:0000269|PubMed:20696890, ECO:0000269|PubMed:20699359, ECO:0000269|PubMed:21084295, ECO:0000269|PubMed:21422228, ECO:0000269|PubMed:23636092}.
uniprot
proteins
mass_dalton
47330
uniprot
proteins
mutagenesis
MUTAGEN 38; /note="K->M: Impaired kinase activity and abnormal subcellular localization with exclusive accumulation to the nucleus."; /evidence="ECO:0000269|PubMed:11161704"; MUTAGEN 176; /note="T->I: Impaired kinase activity and abnormal subcellular localization with exclusive accumulation to the nucleus."; /evidence="ECO:0000269|PubMed:11161704
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated on serine and threonine residues; this autophosphorylation represses activity. Reactivated by phosphatase-mediated dephosphorylation. May be dephosphorylated by PP1.
uniprot
proteins
protein_family
CK1 Ser/Thr protein kinase family
uniprot
proteins
protein_family
Casein kinase I subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
10606744
uniprot
proteins
pubmed
10826492
uniprot
proteins
pubmed
11161704
uniprot
proteins
pubmed
11165242
uniprot
proteins
pubmed
12270714
uniprot
proteins
pubmed
12270943
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14761950
uniprot
proteins
pubmed
15070676
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15800623
uniprot
proteins
pubmed
16027726
uniprot
proteins
pubmed
16618118
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17562708
uniprot
proteins
pubmed
17962809
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19043076
uniprot
proteins
pubmed
19339517
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19591487
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20041275
uniprot
proteins
pubmed
20048001
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20407760
uniprot
proteins
pubmed
20637175
uniprot
proteins
pubmed
20696890
uniprot
proteins
pubmed
20699359
uniprot
proteins
pubmed
21084295
uniprot
proteins
pubmed
21145983
uniprot
proteins
pubmed
21258417
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21422228
uniprot
proteins
pubmed
22168824
uniprot
proteins
pubmed
23106386
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23636092
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
29222110
uniprot
proteins
pubmed
29789297
uniprot
proteins
pubmed
34718754
uniprot
proteins
pubmed
8786104
uniprot
proteins
pubmed
9632646
uniprot
proteins
pubmed
9761932
uniprot
proteins
sequence_length
415
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm, perinuclear region. Cell membrane. Cytoplasm, cytoskeleton, spindle. Golgi apparatus. Note=Localized at mitotic spindle microtubules, and at the centrosomes and interphase in interphase cells. Recruited to the spindle apparatus and the centrosomes in response to DNA-damage. Correct subcellular localization requires kinase activity.
uniprot
proteins