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Mapping of phosphorylation sites on Sgk3 by LC-MS/MS

ABSTRACT: The phosphorylation profile of Sgk3 protein expressed either in Sf9 insect cells or HEK 293T human cells was assessed by mass spectrometry.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Dorothea Anrather

LAB HEAD: Thomas A. Leonard

PROVIDER: PXD026281 | Pride | 2022-02-17

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20180208_QexHF2_RSLC2_Pokorny_Leonard_MFPL_insol_Sgk3_GluC.raw	Raw
	201802_insect.zip	Other
	20180711_QExHFX3_RSLC4_Pokorny_Leonard_MFPL_insol_Sgk3_GluC.raw	Raw
	201807_human.zip	Other
	MaxQuant_1.6.0.16.zip	Other

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Publications

In vitro reconstitution of Sgk3 activation by phosphatidylinositol 3-phosphate.

Pokorny Daniel D Truebestein Linda L Fleming Kaelin D KD Burke John E JE Leonard Thomas A TA

The Journal of biological chemistry 20210625 2

Serum- and glucocorticoid-regulated kinase 3 (Sgk3) is a serine/threonine protein kinase activated by the phospholipid phosphatidylinositol 3-phosphate (PI3P) downstream of growth factor signaling via class I phosphatidylinositol 3-kinase (PI3K) signaling and by class III PI3K/Vps34-mediated PI3P production on endosomes. Upregulation of Sgk3 activity has recently been linked to a number of human cancers; however, the precise mechanism of activation of Sgk3 is unknown. Here, we use a wide range o ...[more]

PMID: 34181950

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