Ser57

Site Information
LEDGRTLsDYNIQkE SwissProt Entrez-Gene
Blast this site against: NCBI SwissProt PDB
Site Group ID: 12667103

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) ( 5 ) , brain ( 7 , 9 , 10 ) , HL-1 (myocyte) [Akt1 (mouse), knockdown, stable lentiviral expression of Akt1 shRNA] ( 3 ) , HL-1 (myocyte) [Akt2 (mouse), knockdown, stable lentiviral expression of Akt2 shRNA] ( 3 ) , HL-1 (myocyte) ( 3 ) , kidney ( 9 ) , liver ( 1 , 4 , 12 ) , lung ( 9 ) , macrophage-peritoneum ( 6 ) , MEF (fibroblast) [p53 (mouse), homozygous knockout] ( 8 ) , spermatozoa ( 11 )

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) ( 5 ) , brain ( 7 , 9 , 10 ) , HL-1 (myocyte) [Akt1 (mouse), knockdown, stable lentiviral expression of Akt1 shRNA] ( 3 ) , HL-1 (myocyte) [Akt2 (mouse), knockdown, stable lentiviral expression of Akt2 shRNA] ( 3 ) , HL-1 (myocyte) ( 3 ) , kidney ( 9 ) , liver ( 1 , 4 , 12 ) , lung ( 9 ) , macrophage-peritoneum ( 6 ) , MEF (fibroblast) [p53 (mouse), homozygous knockout] ( 8 ) , spermatozoa ( 11 )

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	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
4	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
5	Humphrey SJ, et al. (2013) Dynamic Adipocyte Phosphoproteome Reveals that Akt Directly Regulates mTORC2. Cell Metab 17, 1009-20 23684622 Curated Info
6	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
7	Trinidad JC, et al. (2012) Global identification and characterization of both O-GlcNAcylation and phosphorylation at the murine synapse. Mol Cell Proteomics 11, 215-29 22645316 Curated Info
8	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
9	Huttlin EL, et al. (2010) A tissue-specific atlas of mouse protein phosphorylation and expression. Cell 143, 1174-89 21183079 Curated Info
10	Wiśniewski JR, et al. (2010) Brain phosphoproteome obtained by a FASP-based method reveals plasma membrane protein topology. J Proteome Res 9, 3280-9 20415495 Curated Info
11	Platt MD, Salicioni AM, Hunt DF, Visconti PE (2009) Use of differential isotopic labeling and mass spectrometry to analyze capacitation-associated changes in the phosphorylation status of mouse sperm proteins. J Proteome Res 8, 1431-40 19186949 Curated Info
12	Villén J, Beausoleil SA, Gerber SA, Gygi SP (2007) Large-scale phosphorylation analysis of mouse liver. Proc Natl Acad Sci U S A 104, 1488-93 17242355 Curated Info