PASK
Domain
The protein kinase domain mediates binding to phosphatidylinositol.
Function
Serine/threonine-protein kinase involved in energy homeostasis and protein translation. Phosphorylates EEF1A1, GYS1, PDX1 and RPS6. Probably plays a role under changing environmental conditions (oxygen, glucose, nutrition), rather than under standard conditions. Acts as a sensor involved in energy homeostasis: regulates glycogen synthase synthesis by mediating phosphorylation of GYS1, leading to GYS1 inactivation. May be involved in glucose-stimulated insulin production in pancreas and regulation of glucagon secretion by glucose in alpha cells; however such data require additional evidences. May play a role in regulation of protein translation by phosphorylating EEF1A1, leading to increase translation efficiency. May also participate in respiratory regulation.
Post-translational modifications
Autophosphorylated on Thr-1161 and Thr-1165. Autophosphorylation is activated by phospholipids.
Sequence Similarities
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.
Tissue Specificity
Ubiquitously expressed, with slightly higher expression in brain, prostate and testis. Reduced expression was found in placenta. Present in germ cells of testis and in the midpiece of sperm tails (at protein level).
Cellular localization
- Cytoplasm
- Nucleus
- Localizes in the nucleus of testis germ cells and in the midpiece of sperm tails.
Alternative names
KIAA0135, PASK, PAS domain-containing serine/threonine-protein kinase, PAS-kinase, PASKIN, hPASK