Relation Results

Summary

Name CLK4
Full Name Dual specificity protein kinase CLK4
Synonyms CDC-like kinase 4
Primary ID Q9HAZ1
Links - -
Type protein
Relations 4
Function Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of ...
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Type: Score: Layout: SPV 
0.20.2730.20.358CLK4NR5A1ABL1MITFSRSF1

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▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ CLK4up-regulates activity img/direct-activation.png phosphorylation NR5A1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-274117 Ser203 EYPEPYAsPPQPGLP Homo sapiens HEK-293 Cell
pmid sentence
Immunoblotting analyses showed that the phosphorylation status of NR5A1 at Ser203 was attenuated by the CLK1/4 inhibitor.
Publications: 1 Organism: Homo Sapiens
+ CLK4down-regulates img/direct_inhibition.png phosphorylation ABL1 0.273
Identifier Residue Sequence Organism Cell Line
SIGNOR-181052 Thr735 DTEWRSVtLPRDLQS Homo sapiens
pmid sentence
Here, we identify clk1, clk4, mst1, mst2 and ttk (also known as mps1) as novel thr735 kinases in vitro / phosphorylation of thr735 in c-abl is critical for binding to 14-3-3
Publications: 1 Organism: Homo Sapiens
+ CLK4down-regulates quantity by destabilization img/direct_inhibition.png phosphorylation MITF 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-274116 Tyr360 ILKASVDyIRKLQRE Homo sapiens KYSE-150 Cell
pmid sentence
Mechanistically, wild type CLK4 (WT-CLK4) but not kinase-dead CLK4-K189R mutant phosphorylated MITF at Y360. This modification promoted its interaction with E3 ligase COP1 and its K63-linked ubiquitination at K308/K372, leading to sequestosome 1 recognition and autophagic degradation. 
Publications: 1 Organism: Homo Sapiens
+ CLK4up-regulates activity img/direct-activation.png phosphorylation SRSF1 0.358
Identifier Residue Sequence Organism Cell Line
SIGNOR-273860 in vitro
pmid sentence
In vitro, Clk/Sty efficiently phosphorylated the SR family member ASF/SF2 on serine residues located within its serine/arginine-rich region (the RS domain). Overexpression of the active Clk/Sty kinase caused a redistribution of SR proteins within the nucleus. These results suggest that Clk/Sty kinase directly regulates the activity and compartmentalization of SR splicing factors.
Publications: 1 Organism: In Vitro
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