Features Interactions Isoform Disease Linear motifs Fingerprint Network All partners

CSK21_HUMAN

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]

050100150200250300350
Transmembrane
Phase separation
ELM
Phosphorylation
PFAM
Coiled coil
Anchor
Disordered
Interacting regions
Sequence
LOADING 91%

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050100150200250300350
CSK21_HUMAN
LOADING 67%
050100150200250300350
CSK21_HUMAN
LOADING 67%
0100200300400500600700800
CSK21_HUMAN
LOADING 67%
050100150200250300350
CSK21_HUMAN
LOADING 67%
01002003004005006007008009001,000
CSK21_HUMAN
LOADING 67%
Download full PS network for entry.
050100150200250300350
Interacting regions
Canonical [CSK21_HUMAN]
Isoform [A0A2R8Y7T1] alignment
Isoform [A0A2R8Y797] alignment
Isoform [A0A2R8Y3W6] alignment
Isoform [A0A2R8Y5A0] alignment
Isoform [A0A2R8Y4H0] alignment
Isoform [A0A2R8Y4D6] alignment
Isoform [E7EU96] alignment
Isoform [A0A2R8YDY7] alignment
Isoform [A0A2R8YDP2] alignment
Isoform [A0A2R8YD58] alignment
Isoform [A0A2R8YCK2] alignment
Isoform [A0A2R8YCC9] alignment
Isoform [A0A2R8YFU2] alignment
Isoform [A0A2R8YEW1] alignment
Isoform [A0A2R8YF43] alignment
Isoform [A0A2R8YF47] alignment
Isoform [A0A2R8YEL7] alignment
Isoform [V9GY80] alignment
Isoform [V9GYA2] alignment
Isoform [V9GYW6] alignment
Isoform [P68400-2] alignment
Isoform [A0A087WY74] alignment
LOADING 28%

No data found.

No annotated instance was found. To search for linear motifs, use the ELM prediction server.

Molecular function

Biological process

Disease

No data found.

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