Overview
| Uniprot ID | P19784 |
|---|
| Protein Name | Casein kinase II subunit alpha' |
|---|
| Gene Name | CSNK2A2 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 103 |
IKLIDTVKDPVSKTP |
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:30898438). Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection (PubMed:11704824, PubMed:16193064, PubMed:30898438). 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:12631575, PubMed:19387551, PubMed:19387552). 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, RAD9A, RAD51 and HTATSF1, promoting their recruitment to DNA damage sites (PubMed:20545769, PubMed:21482717, PubMed:22325354, PubMed:26811421, PubMed:30898438, PubMed:35597237). Can also negatively regulate apoptosis (PubMed:19387551, PubMed:19387552). Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3 (PubMed:12631575, PubMed:19387551, PubMed:19387552). Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8 (PubMed:12631575, PubMed:19387551, PubMed:19387552). Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV (PubMed:12631575, PubMed:19387551, PubMed:19387552). Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB (PubMed:12631575, PubMed:19387551, PubMed:19387552). Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function (PubMed:19387550). 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: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:19387551, PubMed:19387552). May phosphorylate histone H2A on 'Ser-1' (PubMed:38334665)
Protein Sequence
10
MPGPAAGSRA
20
RVYAEVNSLR
30
SREYWDYEAH
40
VPSWGNQDDY
50
QLVRKLGRGK
60
YSEVFEAINI
70
TNNERVVVKI
80
LKPVKKKKIK
90
REVKILENLR
100
GGTNIIKLID
110
TVKDPVSKTP
120
ALVFEYINNT
130
DFKQLYQILT
140
DFDIRFYMYE
150
LLKALDYCHS
160
KGIMHRDVKP
170
HNVMIDHQQK
180
KLRLIDWGLA
190
EFYHPAQEYN
200
VRVASRYFKG
210
PELLVDYQMY
220
DYSLDMWSLG
230
CMLASMIFRR
240
EPFFHGQDNY
250
DQLVRIAKVL
260
GTEELYGYLK
270
KYHIDLDPHF
280
NDILGQHSRK
290
RWENFIHSEN
300
RHLVSPEALD
310
LLDKLLRYDH
320
QQRLTAKEAM
330
EHPYFYPVVK
340
EQSQPCADNA
350
VLSSGLTAAR
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0001669 |
acrosomal vesicle |
| Cellular Component |
GO:0000785 |
chromatin |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0005956 |
protein kinase CK2 complex |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0106310 |
protein serine kinase activity |
| Molecular Function |
GO:0004674 |
protein serine/threonine kinase activity |
| Biological Process |
GO:0006915 |
apoptotic process |
| Biological Process |
GO:0021987 |
cerebral cortex development |
| Biological Process |
GO:0006974 |
DNA damage response |
| Biological Process |
GO:0006351 |
DNA-templated transcription |
| Biological Process |
GO:0006302 |
double-strand break repair |
| Biological Process |
GO:0031507 |
heterochromatin formation |
| Biological Process |
GO:0097421 |
liver regeneration |
| Biological Process |
GO:2001234 |
negative regulation of apoptotic signaling pathway |
| Biological Process |
GO:0032435 |
negative regulation of proteasomal ubiquitin-dependent protein catabolic process |
| Biological Process |
GO:0045893 |
positive regulation of DNA-templated transcription |
| Biological Process |
GO:1903955 |
positive regulation of protein targeting to mitochondrion |
| Biological Process |
GO:1905818 |
regulation of chromosome separation |
| Biological Process |
GO:1901524 |
regulation of mitophagy |
| Biological Process |
GO:0007283 |
spermatogenesis |
| Biological Process |
GO:0016055 |
Wnt signaling pathway |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.