CLK4 - Dual specificity protein kinase CLK4 - human protein (Function)
 
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CLK4 »  Dual specificity protein kinase CLK4   [ EC 2.7.12.1 ]
 
Protein also known as:  CDC-like kinase 4.
Gene name:  CLK4
Entry whose protein(s) existence is based on evidence at protein level
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GENE REF ISO

Function

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Overview 
Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates SRSF1 and SRSF3. Required for the regulation of alternative splicing of MAPT/TAU. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells.  
2
  • CuratedUniProtKB
GO molecular function 
ATP bindingdefinition[GO:0005524]  
  • IEAUniProtKB KW
Protein serine/threonine kinase activitydefinition[GO:0004674]  
  • ISSOrtholog Curator
Protein serine/threonine/tyrosine kinase activitydefinition[GO:0004712]  
  • IEAEC 2 GO
Protein tyrosine kinase activitydefinition[GO:0004713] silver  
  • IEAOrtholog Compara
GO biological process 
Protein autophosphorylationdefinition[GO:0046777] silver  
  • IEAOrtholog Compara
Regulation of RNA splicingdefinition[GO:0043484]  
1
  • IMPUniProtKB
Enzymatic activity 
This protein acts as an enzyme. It is known to catalyze the following reaction
EC 2.7.12.1: ATP + a protein ADP + a phosphoprotein.  
  • CuratedUniProtKB
It is regulated in the following manner
TG003 inhibits its kinase activity and affects the regulation of alternative splicing mediated by phosphorylation of SR proteins (By similarity).  
  • CuratedUniProtKB
 

Keywords

Molecular function 
Kinase  definition   [KW-0418]
Serine/threonine-protein kinase  definition   [KW-0723]
Transferase  definition   [KW-0808]
Tyrosine-protein kinase  definition   [KW-0829]
Technical term 
Reference proteome  definition   [KW-1185]
 

Further external links

Other
GenomeRNAi: 57396
PRO: PR:Q9HAZ1
Chemistry
GuidetoPHARMACOLOGY: 1993