CSK21_HUMAN
Evidence for PS localization
Functions
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, PubMed, PubMed, PubMed, PubMed, PubMed, PubMed). Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection (PubMed, PubMed, PubMed). May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response (PubMed, PubMed, PubMed). 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, PubMed). Also required for p53/TP53-mediated apoptosis, phosphorylating Ser-392 of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis (PubMed). Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3 (PubMed). Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8 (PubMed). Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. 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, PubMed, PubMed, PubMed, PubMed). Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function (PubMed). Mediates sequential phosphorylation of FNIP1, promoting its gradual interaction with Hsp90, leading to activate both kinase and non-kinase client proteins of Hsp90 (PubMed). Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1 (PubMed). Acts as an ectokinase that phosphorylates several extracellular proteins (PubMed, PubMed, PubMed, PubMed). During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV (PubMed, PubMed, PubMed, PubMed). Phosphorylates PML at Ser-565 and primes it for ubiquitin-mediated degradation (PubMed, PubMed). Plays an important role in the circadian clock function by phosphorylating ARNTL/BMAL1 at Ser-90 which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry . Phosphorylates CCAR2 at Thr-454 in gastric carcinoma tissue (PubMed). [View more on UniProt]
Protein features

Binary interactions with known binding regions
To display all evidence describing the interaction with a partner, click on the protein name left to the bars.

Network
Isoforms

Disease-causing germline mutations
No data found.
Linear motifs
No annotated instance was found. To search for linear motifs, use the ELM prediction server.
Fingerprint
Molecular function
Term | Name | % | Distance from the top of the tree | Annotated in CSK21_HUMAN |
---|---|---|---|---|
GO:0003723 | RNA binding | 43.3790 | 4 | no |
GO:0043168 | anion binding | 26.0274 | 4 | yes |
GO:0000166 | nucleotide binding | 24.2009 | 4 | yes |
GO:0017076 | purine nucleotide binding | 24.2009 | 5 | yes |
GO:0032555 | purine ribonucleotide binding | 23.7443 | 4 | yes |
GO:0035639 | purine ribonucleoside triphosphate binding | 23.2877 | 4 | yes |
GO:0030554 | adenyl nucleotide binding | 22.3744 | 6 | yes |
GO:0032559 | adenyl ribonucleotide binding | 21.9178 | 5 | yes |
GO:0005524 | ATP binding | 21.4612 | 5 | yes |
GO:0043169 | cation binding | 20.5479 | 4 | no |
GO:0046872 | metal ion binding | 20.5479 | 5 | no |
GO:0016301 | kinase activity | 11.8721 | 4 | yes |
GO:0016773 | phosphotransferase activity, alcohol group as acceptor | 11.4155 | 4 | yes |
GO:0004674 | protein serine/threonine kinase activity | 7.7626 | 4 | yes |
GO:0106310 | protein serine kinase activity | 7.3059 | 4 | yes |
GO:0051879 | Hsp90 protein binding | 3.1963 | 4 | yes |
Biological process
Term | Name | % | Distance from top the of the tree | Annotated in CSK21_HUMAN |
---|---|---|---|---|
GO:0048522 | positive regulation of cellular process | 55.7078 | 4 | yes |
GO:0060255 | regulation of macromolecule metabolic process | 54.7945 | 4 | yes |
GO:0080090 | regulation of primary metabolic process | 53.4247 | 4 | yes |
GO:0031323 | regulation of cellular metabolic process | 52.5114 | 4 | yes |
GO:0048523 | negative regulation of cellular process | 50.6849 | 4 | yes |
GO:0009893 | positive regulation of metabolic process | 44.2922 | 4 | yes |
GO:0009889 | regulation of biosynthetic process | 43.3790 | 4 | yes |
GO:0010556 | regulation of macromolecule biosynthetic process | 43.3790 | 5 | yes |
GO:0031326 | regulation of cellular biosynthetic process | 43.3790 | 5 | yes |
GO:0010646 | regulation of cell communication | 42.4658 | 4 | yes |
GO:0010604 | positive regulation of macromolecule metabolic process | 41.5525 | 5 | yes |
GO:0051246 | regulation of protein metabolic process | 41.0959 | 5 | yes |
GO:0010468 | regulation of gene expression | 40.1826 | 6 | yes |
GO:0009966 | regulation of signal transduction | 39.7260 | 4 | yes |
GO:0009892 | negative regulation of metabolic process | 38.3562 | 4 | yes |
GO:0051128 | regulation of cellular component organization | 37.8995 | 4 | yes |
GO:0010605 | negative regulation of macromolecule metabolic process | 36.9863 | 5 | yes |
GO:0022607 | cellular component assembly | 36.5297 | 4 | no |
GO:0031325 | positive regulation of cellular metabolic process | 36.0731 | 5 | no |
GO:0019219 | regulation of nucleobase-containing compound metabolic process | 33.3333 | 5 | no |
GO:0031324 | negative regulation of cellular metabolic process | 32.8767 | 5 | yes |
GO:0051247 | positive regulation of protein metabolic process | 29.6804 | 6 | yes |
GO:0006996 | organelle organization | 29.6804 | 4 | no |
GO:0048584 | positive regulation of response to stimulus | 29.2237 | 4 | yes |
GO:0009891 | positive regulation of biosynthetic process | 29.2237 | 5 | no |
Disease
No data found.
All partners
Uniprot ID | Details | Highest evidence | Localizing into PSD | HPA (protein expression in neurons) |
---|---|---|---|---|
1433B_HUMAN | [view entry] [view interactions] | High throughput | yes | yes |
1433S_HUMAN | [view entry] [view interactions] | High throughput | yes | yes |
A16L1_HUMAN | [view entry] [view interactions] | Low throughput | yes | yes |
A4_HUMAN | [view entry] [view interactions] | High throughput | yes | yes |
ABCE1_HUMAN | [view interactions] | High throughput | no | yes |
ABR_HUMAN | [view entry] [view interactions] | High throughput | yes | yes |
ABT1_HUMAN | [view interactions] | High throughput | no | no |
ACE_HUMAN | [view interactions] | Low throughput | no | no |
ACINU_HUMAN | [view interactions] | High throughput | no | yes |
ADNP_HUMAN | [view interactions] | High throughput | no | yes |
AIP_HUMAN | [view entry] [view interactions] | High throughput | yes | yes |
AIRIM_HUMAN | [view interactions] | Low throughput | no | yes |
AK17A_HUMAN | [view interactions] | High throughput | no | no |
AKA10_HUMAN | [view interactions] | High throughput | no | no |
AKAP8_HUMAN | [view interactions] | High throughput | no | yes |
AKIP_HUMAN | [view interactions] | High throughput | no | yes |
AKT1_HUMAN | [view entry] [view interactions] | Low throughput | yes | yes |
ALKB5_HUMAN | [view interactions] | High throughput | no | yes |
AMOL1_HUMAN | [view interactions] | High throughput | no | no |
AN32A_HUMAN | [view interactions] | Low throughput | no | yes |
AN32B_HUMAN | [view interactions] | High throughput | no | yes |
AN36A_HUMAN | [view interactions] | High throughput | no | no |
AN36B_HUMAN | [view interactions] | High throughput | no | no |
ANDR_HUMAN | [view interactions] | High throughput | no | no |
ANKS3_HUMAN | [view interactions] | High throughput | no | yes |