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PASK (PAS domain containing serine/threonine kinase)

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The Function of PASK

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 to respiratory regulation.

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Protein names

Recommended name:

PAS domain-containing serine/threonine-protein kinase

Alternative name(s):

PAS-kinase
PASKIN
hPASK

PASK SNPs

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  1. RS17382723 (PASK) ??

Top Gene-Substance Interactions

PASK Interacts with These Diseases

Disease Score

Substances That Increase PASK

Substances Interaction Organism Category

Substances That Decrease PASK

Substances Interaction Organism Category

Conditions with Increased Gene Activity

Condition Change (log2fold) Comparison Species Experimental variables Experiment name

Conditions with Decreased Gene Activity

Condition Change (log2fold) Comparison Species Experimental variables Experiment name

Technical

The following transcription factors affect gene expression:

  • FOXO4
  • Pbx1a
  • MEF-2A
  • GATA-1
  • YY1

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).

Enzyme Regulation:

Protein kinase activity is inhibited by the first PAS domain: binding of an unidentified ligand desinhibits the protein kinase activity. May be activated by autophosphorylation on Thr-1161 and Thr-1165 (PubMed:11459942). The activating role of autophosphorylation at Thr-1161 is unclear: according to a report, autophosphorylation at Thr-1161 does not play a major role in activation (PubMed:20943661). Autophosphorylation is enhanced upon phosphatidylinositol monophosphate (phosphatidylinositol 4-phosphate) binding and inhibited upon phosphatidylinositol bi- and tri-phosphate binding. In contrast, phosphorylation of target proteins is inhibited upon all phosphatidylinositol-binding (phosphatidylinositol mono- bi- and tri-phosphate).

Molecular Function:

  • Atp Binding
  • Phosphatidylinositol Binding
  • Protein Serine/Threonine Kinase Activity

Biological Processes:

  • Negative Regulation Of Glycogen Biosynthetic Process
  • Positive Regulation Of Translation
  • Protein Autophosphorylation
  • Protein Phosphorylation
  • Regulation Of Energy Homeostasis
  • Regulation Of Glucagon Secretion
  • Regulation Of Glucose Metabolic Process
  • Regulation Of Respiratory Gaseous Exchange
*synonyms

Synonyms/Aliases/Alternative Names of the Gene:

hypothetical protein| mTERF domain-containing protein 2| A306_14772| AS27_13268| AS28_11896| CG3105 gene product from transcript CG3105-RA| CG3105-PA| D623_10035080| Dmel_CG3105| H920_16057| I79_005309| M91_12489| M959_06186| MDA_GLEAN10026158| N301_12685| N303_11049| N306_08730| N308_03792| N312_08957| N322_08017| N324_09453| N325_10493| N327_08443| N328_09118| N329_09644| N333_09654| N334_12242| N339_09160| N340_03506| N341_10656| PAL_GLEAN10006472| PANDA_012296| pas| PAS domain-containing serine/threonine-protein kinase| paskin| PAS kinase| PAS-kinase| Pask-PA| per-arnt-sim (PAS) domain kinase| STK37| UY3_14259| Y1Q_020773| Y956_12574| pask

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