CLK2 report

I. Expression across cell types

Insufficient scRNA-seq data for expression of CLK2 at single-cell level.

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of CLK2 at tissue level.

III. Associated gene sets

GO_0043484Biological processregulation of RNA splicing
GO_0018108Biological processpeptidyl-tyrosine phosphorylation
GO_0006468Biological processprotein phosphorylation
GO_0046777Biological processprotein autophosphorylation
GO_0045721Biological processnegative regulation of gluconeogenesis
GO_0010212Biological processresponse to ionizing radiation
GO_0016607Cellular componentnuclear speck
GO_0016604Cellular componentnuclear body
GO_0005654Cellular componentnucleoplasm
GO_0005634Cellular componentnucleus
GO_0004713Molecular functionprotein tyrosine kinase activity
GO_0004674Molecular functionprotein serine/threonine kinase activity
GO_0004712Molecular functionprotein serine/threonine/tyrosine kinase activity
GO_0005515Molecular functionprotein binding
GO_0042802Molecular functionidentical protein binding
GO_0106310Molecular functionprotein serine kinase activity
GO_0005524Molecular functionATP binding

IV. Literature review

[source]
Gene nameCLK2
Protein nameDual specificity protein kinase CLK2 (EC 2.7.12.1) (CDC-like kinase 2)
dual-specificity kinase (EC 2.7.12.1)
SynonymshCG_15308
DescriptionFUNCTION: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Acts as a suppressor of hepatic gluconeogenesis and glucose output by repressing PPARGC1A transcriptional activity on gluconeogenic genes via its phosphorylation. Phosphorylates PPP2R5B thereby stimulating the assembly of PP2A phosphatase with the PPP2R5B-AKT1 complex leading to dephosphorylation of AKT1. Phosphorylates: PTPN1, SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Phosphorylates PAGE4 at several serine and threonine residues and this phosphorylation attenuates the ability of PAGE4 to potentiate the transcriptional activator activity of JUN . .

AccessionsENST00000368361.9 [P49760-1]
ENST00000572269.5 [P49760-3]
Q9BRG8
ENST00000355560.4
ENST00000576584.1
B7Z8N6
P49760
B1AVT0
A8K7I0
ENST00000361168.9 [P49760-3]
ENST00000574445.5 [P49760-1]