CSNK2A1
entrez
1457
canonical
uniprot
P68400
canonical
ensembl
ENSG00000101266
resolver
ensp
ENSP00000217244
resolver
ensp
ENSP00000339247
resolver
ensp
ENSP00000495248
resolver
ensp
ENSP00000495998
resolver
ensp
ENSP00000496569
resolver
genesymbol
CSNK2A1
resolver
genesymbol_syn
CK2A1
resolver
hgnc
HGNC:2457
resolver
uniprot
B4DYS6
resolver
uniprot
D3DVV8
resolver
uniprot
P19138
resolver
uniprot
P20426
resolver
uniprot
Q14013
resolver
uniprot
Q5U065
resolver
uniprot_entry
CSK21_HUMAN
resolver
uniprot_sec
B4DYS6
resolver
uniprot_sec
D3DVV8
resolver
uniprot_sec
P19138
resolver
uniprot_sec
P20426
resolver
uniprot_sec
Q14013
resolver
uniprot_sec
Q5U065
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.
uniprot
proteins
amino_acid_sequence
MSGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKDQARMGSSSMPGGSTPVSSANMMSGISSVPTPSPLGPLAGSPVIAAANPLGMPVPAAAGAQQ
uniprot
proteins
disease_involvement
DISEASE: Okur-Chung neurodevelopmental syndrome (OCNDS) [MIM:617062]: An autosomal dominant neurodevelopmental disorder characterized by developmental delay, intellectual disability, behavioral problems, hypotonia, speech problems, microcephaly, pachygyria and variable dysmorphic features. {ECO:0000269|PubMed:27048600}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 (PubMed:11239457, PubMed:11704824, PubMed:16193064, PubMed:18411307, PubMed:18583988, PubMed:18678890, PubMed:19188443, PubMed:20545769, PubMed:20625391, PubMed:22017874, PubMed:22406621, PubMed:24962073, PubMed:30898438, PubMed:31439799). Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection (PubMed:12631575, PubMed:19387551, PubMed:19387552). May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response (PubMed:12631575, PubMed:19387551, PubMed:19387552). 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 (PubMed:11704824, PubMed:19188443). Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation (PubMed:11239457). 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 (PubMed:18411307, PubMed:18583988, PubMed:18678890, PubMed:20545769, PubMed:21482717, PubMed:22325354, PubMed:26811421, PubMed:28512243, PubMed:30898438, PubMed:35597237). Can also negatively regulate apoptosis (PubMed:16193064, PubMed:22184066). Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3 (PubMed:16193064). Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8 (PubMed:16193064). Phosphorylates YY1, protecting YY1 from cleavage by CASP7 during apoptosis (PubMed:22184066). Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV (PubMed:12631575, PubMed:19387550, PubMed:19387551, PubMed:19387552, PubMed:23123191). Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, ATF4, SRF, MAX, JUN, FOS, MYC and MYB (PubMed:12631575, PubMed:19387550, PubMed:19387551, PubMed:19387552, PubMed:23123191). Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function (PubMed:19387550). Mediates sequential phosphorylation of FNIP1, promoting its gradual interaction with Hsp90, leading to activate both kinase and non-kinase client proteins of Hsp90 (PubMed:30699359). Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1 (PubMed:19387549). Acts as an ectokinase that phosphorylates several extracellular proteins (PubMed:12631575, PubMed:19387550, PubMed:19387551, PubMed:19387552). During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV (PubMed:12631575, PubMed:19387550, PubMed:19387551, PubMed:19387552). Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation (PubMed:20625391, PubMed:22406621). 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 CCAR2 at 'Thr-454' in gastric carcinoma tissue (PubMed:24962073). Phosphorylates FMR1, promoting FMR1-dependent formation of a membraneless compartment (PubMed:30765518, PubMed:31439799). May phosphorylate histone H2A on 'Ser-1' (PubMed:38334665). {ECO:0000250|UniProtKB:P19139, ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:11704824, ECO:0000269|PubMed:16193064, ECO:0000269|PubMed:18411307, ECO:0000269|PubMed:18583988, ECO:0000269|PubMed:18678890, ECO:0000269|PubMed:19188443, ECO:0000269|PubMed:20545769, ECO:0000269|PubMed:20625391, ECO:0000269|PubMed:21482717, ECO:0000269|PubMed:22017874, ECO:0000269|PubMed:22184066, ECO:0000269|PubMed:22325354, ECO:0000269|PubMed:22406621, ECO:0000269|PubMed:23123191, ECO:0000269|PubMed:24962073, ECO:0000269|PubMed:26811421, ECO:0000269|PubMed:28512243, ECO:0000269|PubMed:30699359, ECO:0000269|PubMed:30765518, ECO:0000269|PubMed:30898438, ECO:0000269|PubMed:31439799, ECO:0000269|PubMed:35597237, ECO:0000269|PubMed:38334665, ECO:0000303|PubMed:12631575, ECO:0000303|PubMed:19387549, ECO:0000303|PubMed:19387550, ECO:0000303|PubMed:19387551, ECO:0000303|PubMed:19387552}.
uniprot
proteins
mass_dalton
45144
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. {ECO:0000269|PubMed:7592773}.
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
11092945
uniprot
proteins
pubmed
11239457
uniprot
proteins
pubmed
11574463
uniprot
proteins
pubmed
11704824
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
12393879
uniprot
proteins
pubmed
12631575
uniprot
proteins
pubmed
12860116
uniprot
proteins
pubmed
14646071
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15684395
uniprot
proteins
pubmed
16193064
uniprot
proteins
pubmed
18411307
uniprot
proteins
pubmed
18583988
uniprot
proteins
pubmed
18678890
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19188443
uniprot
proteins
pubmed
19387549
uniprot
proteins
pubmed
19387550
uniprot
proteins
pubmed
19387551
uniprot
proteins
pubmed
19387552
uniprot
proteins
pubmed
19387553
uniprot
proteins
pubmed
19923321
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20545769
uniprot
proteins
pubmed
20625391
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21482717
uniprot
proteins
pubmed
2174700
uniprot
proteins
pubmed
22017874
uniprot
proteins
pubmed
22184066
uniprot
proteins
pubmed
22325354
uniprot
proteins
pubmed
22406621
uniprot
proteins
pubmed
23123191
uniprot
proteins
pubmed
24962073
uniprot
proteins
pubmed
26811421
uniprot
proteins
pubmed
27048600
uniprot
proteins
pubmed
2752008
uniprot
proteins
pubmed
28512243
uniprot
proteins
pubmed
30699359
uniprot
proteins
pubmed
30765518
uniprot
proteins
pubmed
30898438
uniprot
proteins
pubmed
31439799
uniprot
proteins
pubmed
35597237
uniprot
proteins
pubmed
38334665
uniprot
proteins
pubmed
7592773
uniprot
proteins
pubmed
8420794
uniprot
proteins
sequence_length
391
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23123191, ECO:0000269|PubMed:24962073}.
uniprot
proteins