In earlier experiments, we could demonstrate that the serum and glucocorticoid inducible kinase SGK1 is a powerful regulator of Orai1, the pore forming unit of Ca²⁺ release-activated calcium (CRAC) channels and STIM1, the Orai1 activating endoplasmic reticulum (ER) calcium sensor. Overexpression of constitutively active ^S422DSGK1 but not of inactive ^K127NSGK1 significantly enhanced the Orai1 protein abundance in the cell membrane, the CRAC current (I_CRAC) and the store-operated Ca²⁺ entry (SOCE) following depletion of ER Ca²⁺ stores. The effect was partially explained by the ubiquitin ligase Nedd4-2 (neuronal precursor cells expressed developmentally downregulated), which ubiquitinates Orai1 thus preparing the channel protein for degradation. SGK1 phosphorylates Nedd4-2 thus fostering binding to the 14-3-3 protein and prevention of interaction with Orai1. The SGK1 dependent regulation could, however, not be fully explained by inhibition of Nedd4-2. SGK1 is known to regulate the transcription factor NFkB. The present study thus explored whether SGK1 influences Orai1 and/or STIM1 transcription. Transfection of human embryonic kidney HEK293 cells with constitutively active ^S422DSGK1 but not transfection with inactive ^K127NSGK1 enhanced the transcript levels of both Orai1 and STIM1. Transfection of HEK293 cells with the NFkB subunit p65 similarly increased Orai1 and STIM1 transcript levels. Conversely, silencing of NFkB downregulated the transcription of both STIM1 and Orai1. Finally, treatment of HEK293 cells with the NFkB inhibitor Wogonin (24 hours 100 mM) decreased the transcript levels of both, Orai1 and STIM1. The present observations reveal a powerful genomic regulation of Orai1/STIM1 by SGK1 dependent NFkB signalling.