What is CLK3(2EU9)?

Dual specificity protein kinase CLK3 is an agitator that in bodies is encoded by the CLK3 gene.
The CLK3 gene encodes a serine/threonine blazon protein kinase with a non-conserved N-terminal domain. A continued and abbreviate isoform (phclk3 and pclk3/152) aftereffect from another splicing and coexist in altered tissues. Isoform phclk3/152 lacks the kinase domain.
CLK3 a CMGC kinase of the CLK family. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May play a role in acclimation RNA splicing. Three alternatively spliced isoforms accept been described. Isoform 2 is abbreviate and lacks the kinase domain. May be produced at actual low levels due to a abortive stop codon in the mRNA, arch to nonsense-mediated mRNA decay. Note: This description may cover advice from UniProtKB.
The CLK (CDC-like kinase) ancestors kinases are an evolutionarily conserved accumulation of bifold specificity kinases, able of phosphorylating protein substrates on serine, threonine, and tyrosine residues. The CLK ancestors kinases are begin in assorted species, including yeast, Drosophila, Arabidopsis, tobacco, mouse, rat, and human. A analytical role for the CLK ancestors kinases in development has been appropriate by plan on the Drosophila CLK homologue, DOA. Flies cogent low levels of the aberrant DOA protein appearance apparent neurologic abnormalities, and homozygosity for the DOA absent allele is embryonically lethal.
Recent plan on the murine CLK1 protein has amorphous to afford ablaze on added physiological roles of the CLK ancestors of kinases. Adjustment of mRNA splicing is now accustomed as a activating process, and one in which the CLK ancestors of kinases may accept an important function. CLK1 has been appear to bind to and phosphorylate serine/arginine-rich mRNA splicing factors on physiologically accordant sites in vitro. Moreover, Colwill et al.demonstrated that overexpression of CLK1 in COS beef leads to the subcellular redistribution of serine/ arginine-rich proteins, and to alterations in mRNA splicing in vivo. Collectively, these abstracts acerb advance a role for the CLK ancestors kinases in the adjustment of mRNA splicing in vivo.
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