Ser43

Site Information
PPSVRtLsGEEEAEs SwissProt Entrez-Gene
Blast this site against: NCBI SwissProt PDB
Site Group ID: 4775732

In vivo Characterization
Methods used to characterize site in vivo:	mass spectrometry ( 1 , 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 , 11 , 12 )
Relevant cell line - cell type - tissue:	'3T3-L1, differentiated' (adipocyte) ( 3 ) , 'fat, brown' ( 12 ) , brain ( 12 ) , heart ( 7 , 12 ) , HL-1 (myocyte) [Akt1 (mouse), knockdown, stable lentiviral expression of Akt1 shRNA] ( 4 ) , HL-1 (myocyte) [Akt2 (mouse), knockdown, stable lentiviral expression of Akt2 shRNA] ( 4 ) , HL-1 (myocyte) ( 4 ) , kidney ( 12 ) , liver ( 1 , 6 ) , lung ( 12 ) , macrophage-peritoneum ( 8 ) , MEF (fibroblast) [p53 (mouse), homozygous knockout] ( 9 ) , MEF (fibroblast) ( 10 ) , pancreas ( 12 ) , spleen ( 12 ) , stromal ( 5 ) , T lymphocyte-spleen ( 11 ) , testis ( 12 )

In vivo Characterization

Methods used to characterize site in vivo:

mass spectrometry ( 1 , 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 , 11 , 12 )

Relevant cell line - cell type - tissue:

'3T3-L1, differentiated' (adipocyte) ( 3 ) , 'fat, brown' ( 12 ) , brain ( 12 ) , heart ( 7 , 12 ) , HL-1 (myocyte) [Akt1 (mouse), knockdown, stable lentiviral expression of Akt1 shRNA] ( 4 ) , HL-1 (myocyte) [Akt2 (mouse), knockdown, stable lentiviral expression of Akt2 shRNA] ( 4 ) , HL-1 (myocyte) ( 4 ) , kidney ( 12 ) , liver ( 1 , 6 ) , lung ( 12 ) , macrophage-peritoneum ( 8 ) , MEF (fibroblast) [p53 (mouse), homozygous knockout] ( 9 ) , MEF (fibroblast) ( 10 ) , pancreas ( 12 ) , spleen ( 12 ) , stromal ( 5 ) , T lymphocyte-spleen ( 11 ) , testis ( 12 )

References
1	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
2	Sacco F, et al. (2016) Glucose-regulated and drug-perturbed phosphoproteome reveals molecular mechanisms controlling insulin secretion. Nat Commun 7, 13250 27841257 Curated Info
3	Parker BL, et al. (2015) Targeted phosphoproteomics of insulin signaling using data-independent acquisition mass spectrometry. Sci Signal 8, rs6 26060331 Curated Info
4	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
5	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
6	Wilson-Grady JT, Haas W, Gygi SP (2013) Quantitative comparison of the fasted and re-fed mouse liver phosphoproteomes using lower pH reductive dimethylation. Methods 61, 277-86 23567750 Curated Info
7	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
8	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
9	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
10	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
11	Navarro MN, et al. (2011) Phosphoproteomic analysis reveals an intrinsic pathway for the regulation of histone deacetylase 7 that controls the function of cytotoxic T lymphocytes. Nat Immunol 12, 352-61 21399638 Curated Info
12	Huttlin EL, et al. (2010) A tissue-specific atlas of mouse protein phosphorylation and expression. Cell 143, 1174-89 21183079 Curated Info