PASK

This gene encodes a member of the serine/threonine kinase family that contains two PAS domains. Expression of this gene is regulated by glucose, and the encoded protein plays a role in the regulation of insulin gene expression. Downregulation of this gene may play a role in type 2 diabetes. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Nov 2011]

Full Name

PAS Domain Containing Serine/Threonine Kinase

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.

Biological Process

Energy homeostasisISS:UniProtKB
Intracellular signal transductionManual Assertion Based On ExperimentIBA:GO_Central
Negative regulation of glycogen biosynthetic processManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of translationManual Assertion Based On ExperimentTAS:UniProtKB
Protein autophosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Protein phosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of glucagon secretionISS:UniProtKB
Regulation of respiratory gaseous exchangeISS:UniProtKB

Cellular Location

Cytoplasm
Nucleus
Localizes in the nucleus of testis germ cells and in the midpiece of sperm tails.

PTM

Autophosphorylated on Thr-1161 and Thr-1165. Autophosphorylation is activated by phospholipids.