Alternative titles; symbols
HGNC Approved Gene Symbol: STK17A
Cytogenetic location: 7p13 Genomic coordinates (GRCh38) : 7:43,583,108-43,627,379 (from NCBI)
Apoptosis, or programmed cell death, is a highly regulated process that is crucial in development. Deregulation of apoptosis is responsible for a wide range of diseases such as autoimmune and neurodegenerative disorders. By sequence homology searches using the catalytic domains of 2 serine/threonine kinases important in the regulation of apoptosis, DAP kinase (600954) and ZIP kinase (603289), Sanjo et al. (1998) cloned 2 novel members of the ser/thr protein kinase family, which they termed DRAK1 and DRAK2 (604727), but which were later designated STK17A and STK17B, respectively. The full-length STK17A cDNA encodes a deduced 414-amino acid protein with a molecular mass of 46.56 kD. The putative kinase domain is located at the N terminus and contains all 11 subdomains conserved among ser/thr kinases. STK17A and STK17B share 59.7% amino acid identity. Northern blot analysis revealed that STK17A is expressed as a 1.9-kb transcript predominantly in placenta, but also in heart, lung, skeletal muscle, kidney, and pancreas. An in vitro assay demonstrated that STK17A is capable of autophosphorylation and of phosphorylating myosin light chain as an exogenous substrate, and that the noncatalytic C terminus is crucial for full kinase activity. Immunofluorescence studies showed that both STK17A and STK17B are localized in the nucleus. NIH 3T3 cells transfected with STK17A expression plasmid displayed the morphologic changes typical of cells undergoing apoptosis, but not when transfected with STK17A with an inactivated kinase domain or a truncated noncatalytic C-terminal region. A colony formation assay showed that the apoptosis-inducing activity of STK17A requires the intact structure of the entire gene and that STK17A and STK17B share similar levels of apoptosis-inducing activity.
Sanjo, H., Kawai, T., Akira, S. DRAKs, novel serine/threonine kinases related to death-associated protein kinase that trigger apoptosis. J. Biol. Chem. 273: 29066-29071, 1998. [PubMed: 9786912] [Full Text: https://doi.org/10.1074/jbc.273.44.29066]