background:
SLK is a member of the serine/threonine kinase subfamily, Ste20. This subfamily is comprised of several mammalian kinases which exhibit sequence similarity to the Saccharomyces cerevisiae serine/threonine kinase Ste20, a protein involved in relaying signals from G protein-coupled receptors to cytosolic MAP kinase cascades. Members of this subfamily include KHS, GLK, YSK1, HPK1, Krs-1, Krs-2, GC kinase, HGK and SLK. SLK is a ubiquitously expressed protein that localizes to the cytoplasm and contains an N-terminal protein kinase domain, a central coiled-coil domain and a SLCterminal ATH domain. SLK is activated through cleavage by caspase-3. SLK indirectly associates with microtubules and plays an important role in cellular stress, cell motility, cell death and cytoskeletal dynamics.
Function:
SLK is a serine/threonine protein kinase that is involved in cytoskeletal reorganization and apoptosis. SLK is a microtubule-associated protein inducing actin stress fiber disassembly, it also mediates apoptosis and it is ubiquitously expressed; highest expression is found in heart and in skeletal muscle. There are two named isoforms.
Subcellular Location:
Cytoplasmic
Tissue Specificity:
Ubiquitously expressed. Highest expression is found in heart and in skeletal muscle.
Post-translational modifications:
Proteolytically cleaved by caspase-3.
Autophosphorylated. Phosphorylated upon DNA damage, probably by ATM or ATR.
Similarity:
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.
Contains 1 protein kinase domain.
Contains 1 UVR domain.
Database links:
UniProtKB/Swiss-Prot: Q9H2G2.1
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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