PCK1 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0071300Biological processcellular response to retinoic acid
GO_0018105Biological processpeptidyl-serine phosphorylation
GO_1904628Biological processcellular response to phorbol 13-acetate 12-myristate
GO_0071333Biological processcellular response to glucose stimulus
GO_0046327Biological processglycerol biosynthetic process from pyruvate
GO_1904640Biological processresponse to methionine
GO_0071549Biological processcellular response to dexamethasone stimulus
GO_0032869Biological processcellular response to insulin stimulus
GO_0043382Biological processpositive regulation of memory T cell differentiation
GO_0006107Biological processoxaloacetate metabolic process
GO_0032868Biological processresponse to insulin
GO_0051365Biological processcellular response to potassium ion starvation
GO_0046889Biological processpositive regulation of lipid biosynthetic process
GO_0071347Biological processcellular response to interleukin-1
GO_0046890Biological processregulation of lipid biosynthetic process
GO_0014823Biological processresponse to activity
GO_0032496Biological processresponse to lipopolysaccharide
GO_0042594Biological processresponse to starvation
GO_0097403Biological processcellular response to raffinose
GO_0071356Biological processcellular response to tumor necrosis factor
GO_0070741Biological processresponse to interleukin-6
GO_0046166Biological processglyceraldehyde-3-phosphate biosynthetic process
GO_0071475Biological processcellular hyperosmotic salinity response
GO_0071320Biological processcellular response to cAMP
GO_0071477Biological processcellular hypotonic salinity response
GO_0006094Biological processgluconeogenesis
GO_0071377Biological processcellular response to glucagon stimulus
GO_0072350Biological processtricarboxylic acid metabolic process
GO_0070365Biological processhepatocyte differentiation
GO_0071332Biological processcellular response to fructose stimulus
GO_0006006Biological processglucose metabolic process
GO_0042593Biological processglucose homeostasis
GO_0045944Biological processpositive regulation of transcription by RNA polymerase II
GO_0019543Biological processpropionate catabolic process
GO_0071456Biological processcellular response to hypoxia
GO_0070062Cellular componentextracellular exosome
GO_0005783Cellular componentendoplasmic reticulum
GO_0005829Cellular componentcytosol
GO_0005737Cellular componentcytoplasm
GO_0019003Molecular functionGDP binding
GO_0000287Molecular functionmagnesium ion binding
GO_0004613Molecular functionphosphoenolpyruvate carboxykinase (GTP) activity
GO_0030145Molecular functionmanganese ion binding
GO_0005525Molecular functionGTP binding
GO_0031406Molecular functioncarboxylic acid binding
GO_0106264Molecular functionprotein serine kinase activity (using GTP as donor)

IV. Literature review

[source]
Gene namePCK1
Protein namePhosphoenolpyruvate carboxykinase, cytosolic [GTP] (PEPCK-C) (EC 4.1.1.32) (Serine-protein kinase PCK1) (EC 2.7.11.-)
SynonymsPEPCK1
DescriptionFUNCTION: Cytosolic phosphoenolpyruvate carboxykinase that catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate (OAA) and acts as the rate-limiting enzyme in gluconeogenesis . Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle . At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle . At high glucose levels, it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate . Acts as a regulator of formation and maintenance of memory CD8(+) T-cells: up-regulated in these cells, where it generates phosphoenolpyruvate, via gluconeogenesis (By similarity). The resultant phosphoenolpyruvate flows to glycogen and pentose phosphate pathway, which is essential for memory CD8(+) T-cells homeostasis (By similarity). In addition to the phosphoenolpyruvate carboxykinase activity, also acts as a protein kinase when phosphorylated at Ser-90: phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes an atypical serine protein kinase activity using GTP as donor . The protein kinase activity regulates lipogenesis: upon phosphorylation at Ser-90, translocates to the endoplasmic reticulum and catalyzes phosphorylation of INSIG proteins (INSIG1 and INSIG2), thereby disrupting the interaction between INSIG proteins and SCAP and promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes . .

AccessionsP35558
ENST00000319441.6 [P35558-1]