PCK1 Proteins

Protein Information

Phosphoenolpyruvate Carboxykinase 1 (PCK1) is a main control point for the regulation of gluconeogenesis. During gluconeogenesis PCK1 acts as the rate-limiting enzyme. PCK1 regulates the formation and maintenance of memory CH8(+) T-cells via gluconeogenesis. PCK1 aids in controlling the levels of metabolic intermediates in the citric acid cycle by regulating cataplerosis and anaplerosis. When glucose levels are high, PCK1 catalyzes the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (PEP). When they are low it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate. When phosphorylated at Ser-90 by AKT1, PCK1 acts as a protein kinase by reducing the binding affinity to oxaloacetate and promotes an atypical serine protein kinase activity using GTP as the donor. This activity regulates lipogenesis by disrupting the interaction between INSIG proteins and SCAP and promoting nuclear translocation of SREBP proteins and transcription of lipogenesis-related genes. An important paralog of this gene is PCK2.

Synonyms

AI265463; GTP; HGNC:8724; MGC22652; PCK; PCK1; Pck-1; PE PEPCKC; PEP carboxykinase; Pepck; PEPCK1; PEPCKC; PEPCK-C; phosphoenolpyruvate carboxykinase (GTP); phosphoenolpyruvate carboxykinase 1; phosphoenolpyruvate carboxykinase 1 (soluble); phosphoenolpyruvate carboxykinase 1, cytosolic; phosphoenolpyruvate carboxykinase, cytosolic; phosphoenolpyruvate carboxykinase, cytosolic (GTP); phosphoenolpyruvate carboxykinase, cytosolic [GTP]; phosphoenolpyruvate carboxylase; phosphopyruvate carboxylase; RATPEPCK