Csnk2a1
entrez
12995
canonical
uniprot
Q60737
canonical
ensembl
ENSMUSG00000074698
resolver
ensp
ENSMUSP00000096829
resolver
ensp
ENSMUSP00000232069
resolver
ensp
ENSMUSP00000232071
resolver
ensp
ENSMUSP00000232072
resolver
ensp
ENSMUSP00000325469
resolver
ensp
ENSMUSP00000325471
resolver
enst
ENSMUST00000099224
resolver
genesymbol
Csnk2a1
resolver
genesymbol_syn
Ckiia
resolver
uniprot
Q8R0X4
resolver
uniprot_entry
CSK21_MOUSE
resolver
uniprot_sec
Q8R0X4
resolver
activity_regulation
ACTIVITY REGULATION: Constitutively active protein kinase whose activity is not directly affected by phosphorylation. Seems to be regulated by level of expression and localization (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MSGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKDQARMSSTSMAGGSTPVSSANMMSGISSVPTPSPLGPLAGSPVIAAANSLGIPVPAAAGAQQ
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (By similarity). Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection (By similarity). May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response (By similarity). During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage (By similarity). Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation (By similarity). Phosphorylates a number of DNA repair proteins in response to DNA damage, such as MDC1, MRE11, RAD9A, RAD51 and HTATSF1, promoting their recruitment to DNA damage sites (By similarity). Can also negatively regulate apoptosis (PubMed:18467326). Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3 (PubMed:18467326). Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8 (PubMed:18467326). Phosphorylates YY1, protecting YY1 from cleavage by CASP7 during apoptosis (By similarity). Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV (By similarity). Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, ATF4, SRF, MAX, JUN, FOS, MYC and MYB (By similarity). Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function (By similarity). Mediates sequential phosphorylation of FNIP1, promoting its gradual interaction with Hsp90, leading to activate both kinase and non-kinase client proteins of Hsp90 (By similarity). Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1 (PubMed:10806215). Acts as an ectokinase that phosphorylates several extracellular proteins (By similarity). Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation (By similarity). Plays an important role in the circadian clock function by phosphorylating BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry (By similarity). Phosphorylates FMR1, promoting FMR1-dependent formation of a membraneless compartment (By similarity). May phosphorylate histone H2A on 'Ser-1' (By similarity). {ECO:0000250|UniProtKB:P19139, ECO:0000250|UniProtKB:P68400, ECO:0000269|PubMed:10806215, ECO:0000269|PubMed:18467326}.
uniprot
proteins
mass_dalton
45134
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Thr-344, Thr-360, Ser-362 and Ser-370 by CDK1 in prophase and metaphase and dephosphorylated during anaphase. Phosphorylation does not directly affect casein kinase 2 activity, but may contribute to its regulation by forming binding sites for interacting proteins and/or targeting it to different compartments (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
CK2 subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Ser/Thr protein kinase family
uniprot
proteins
pubmed
10806215
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17954558
uniprot
proteins
pubmed
18467326
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19923321
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
7846532
uniprot
proteins
sequence_length
391
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P68400}.
uniprot
proteins