Ser369
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage PhosphoSitePlus®
Powered by Cell Signaling Technology
Home > Phosphorylation Site Page: > Ser369  -  RSK2 (mouse)

Site Information
TAKtPKDsPGIPPsA   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 448064

In vivo Characterization
Methods used to characterize site in vivo:
[32P] bio-synthetic labeling ( 21 ) , mass spectrometry ( 1 , 2 , 4 , 5 , 6 , 7 , 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 ) , mutation of modification site ( 20 , 21 ) , phospho-antibody ( 19 , 20 , 21 ) , western blotting ( 19 , 20 )
Disease tissue studied:
neuroblastoma ( 14 ) , melanoma skin cancer ( 17 )
Relevant cell line - cell type - tissue:
'3T3-L1, differentiated' (adipocyte) ( 5 , 9 ) , 32Dcl3 (myeloid) ( 16 ) , 32Dcl3 (myeloid) [FLT3 (mouse), transfection, chimera with human FLT3-ITD mutant (corresponding to wild type P36888 ~aa 525-695 ETILLNS...IFEYCC)] ( 16 ) , 3T3 (fibroblast) ( 19 ) , BaF3 ('B lymphocyte, precursor') [JAK3 (human), transfection] ( 1 ) , COS (fibroblast) ( 20 , 21 ) , dendritic cell ( 19 ) , dendritic cell [MAPKAPK2 (mouse), homozygous knockout] ( 19 ) , dendritic cell [MSK1 (mouse), homozygous knockout] ( 19 ) , heart ( 10 ) , Hepa 1-6 (epithelial) ( 18 ) , HL-1 (myocyte) ( 7 ) , HL-1 (myocyte) [Akt1 (mouse), knockdown, stable lentiviral expression of Akt1 shRNA] ( 7 ) , HL-1 (myocyte) [Akt2 (mouse), knockdown, stable lentiviral expression of Akt2 shRNA] ( 7 ) , liver ( 2 ) , macrophage-bone marrow ( 15 ) , macrophage-bone marrow [DUSP1 (mouse), homozygous knockout] ( 15 ) , macrophage-peritoneum ( 11 ) , macrophage-peritoneum [MPRIP (mouse), homozygous knockout] ( 11 ) , MC3T3-E1 (preosteoblast) ( 4 ) , MEF (fibroblast) [p53 (mouse), homozygous knockout] ( 12 ) , MEF (fibroblast) [TSC2 (mouse), homozygous knockout] ( 13 ) , N1E-115 (neuron) ( 14 ) , RAW 264.7 (macrophage) ( 6 ) , skin [mGluR1 (mouse), transgenic, TG mutant mice] ( 17 )

Upstream Regulation
Regulatory protein:
FLT3 (mouse) ( 16 )
Kinases, in vitro:
PDK1 (mouse) ( 21 )
Treatments:
BIRB-0796 ( 19 ) , EGF ( 20 , 21 ) , insulin ( 9 ) , LPS ( 19 ) , PD184352 ( 19 ) , SB203580 ( 19 )

Downstream Regulation
Effects of modification on RSK2:
enzymatic activity, induced ( 20 , 21 )

References 

1

Degryse S, et al. (2017) Mutant JAK3 phosphoproteomic profiling predicts synergism between JAK3 inhibitors and MEK/BCL2 inhibitors for the treatment of T-cell acute lymphoblastic leukemia. Leukemia
28852199   Curated Info

2

Robles MS, Humphrey SJ, Mann M (2017) Phosphorylation Is a Central Mechanism for Circadian Control of Metabolism and Physiology. Cell Metab 25, 118-127
27818261   Curated Info

3

Sacco F, et al. (2016) Glucose-regulated and drug-perturbed phosphoproteome reveals molecular mechanisms controlling insulin secretion. Nat Commun 7, 13250
27841257   Curated Info

4

Williams GR, et al. (2016) Exploring G protein-coupled receptor signaling networks using SILAC-based phosphoproteomics. Methods 92, 36-50
26160508   Curated Info

5

Parker BL, et al. (2015) Targeted phosphoproteomics of insulin signaling using data-independent acquisition mass spectrometry. Sci Signal 8, rs6
26060331   Curated Info

6

Pinto SM, et al. (2015) Quantitative phosphoproteomic analysis of IL-33-mediated signaling. Proteomics 15, 532-44
25367039   Curated Info

7

Reinartz M, Raupach A, Kaisers W, Gödecke A (2014) AKT1 and AKT2 induce distinct phosphorylation patterns in HL-1 cardiac myocytes. J Proteome Res 13, 4232-45
25162660   Curated Info

8

Mertins P, et al. (2014) Ischemia in tumors induces early and sustained phosphorylation changes in stress kinase pathways but does not affect global protein levels. Mol Cell Proteomics 13, 1690-704
24719451   Curated Info

9

Humphrey SJ, et al. (2013) Dynamic Adipocyte Phosphoproteome Reveals that Akt Directly Regulates mTORC2. Cell Metab 17, 1009-20
23684622   Curated Info

10

Lundby A, et al. (2013) In vivo phosphoproteomics analysis reveals the cardiac targets of β-adrenergic receptor signaling. Sci Signal 6, rs11
23737553   Curated Info

11

Wu X, et al. (2012) Investigation of receptor interacting protein (RIP3)-dependent protein phosphorylation by quantitative phosphoproteomics. Mol Cell Proteomics 11, 1640-51
22942356   Curated Info

12

Hsu PP, et al. (2011) The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signaling. Science 332, 1317-22
21659604   Curated Info

13

Yu Y, et al. (2011) Phosphoproteomic analysis identifies Grb10 as an mTORC1 substrate that negatively regulates insulin signaling. Science 332, 1322-6
21659605   Curated Info

14

Wang Y, et al. (2011) Spatial phosphoprotein profiling reveals a compartmentalized extracellular signal-regulated kinase switch governing neurite growth and retraction. J Biol Chem 286, 18190-201
21454597   Curated Info

15

Weintz G, et al. (2010) The phosphoproteome of toll-like receptor-activated macrophages. Mol Syst Biol 6, 371
20531401   Curated Info

16

Choudhary C, et al. (2009) Mislocalized activation of oncogenic RTKs switches downstream signaling outcomes. Mol Cell 36, 326-39
19854140   Curated Info

17

Zanivan S, et al. (2008) Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry. J Proteome Res 7, 5314-26
19367708   Curated Info

18

Pan C, Gnad F, Olsen JV, Mann M (2008) Quantitative phosphoproteome analysis of a mouse liver cell line reveals specificity of phosphatase inhibitors. Proteomics 8, 4534-46
18846507   Curated Info

19

Zaru R, et al. (2007) The MAPK-activated kinase Rsk controls an acute Toll-like receptor signaling response in dendritic cells and is activated through two distinct pathways. Nat Immunol 8, 1227-35
17906627   Curated Info

20

Frödin M, Jensen CJ, Merienne K, Gammeltoft S (2000) A phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1. EMBO J 19, 2924-34
10856237   Curated Info

21

Jensen CJ, et al. (1999) 90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1. J Biol Chem 274, 27168-76
10480933   Curated Info