Thr250

Site Information
AAEAGIAtPGtEDsD SwissProt Entrez-Gene
Blast this site against: NCBI SwissProt PDB
Site Group ID: 454277

In vivo Characterization
Methods used to characterize site in vivo:	mass spectrometry ( 1 , 3 , 4 , 5 , 7 , 8 , 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 )
Relevant cell line - cell type - tissue:	'3T3-L1, differentiated' (adipocyte) ( 8 ) , 'fat, brown' ( 16 ) , brain ( 11 , 12 , 16 , 17 , 19 ) , heart ( 9 , 16 ) , HL-1 (myocyte) [Akt1 (mouse), knockdown, stable lentiviral expression of Akt1 shRNA] ( 5 ) , HL-1 (myocyte) [Akt2 (mouse), knockdown, stable lentiviral expression of Akt2 shRNA] ( 5 ) , HL-1 (myocyte) ( 5 ) , kidney ( 16 ) , liver ( 1 , 7 , 18 ) , lung ( 16 ) , macrophage-peritoneum [MPRIP (mouse), homozygous knockout] ( 10 ) , MEF (fibroblast) [p53 (mouse), homozygous knockout] ( 13 ) , MEF (fibroblast) [TSC2 (mouse), homozygous knockout] ( 14 ) , neuron:postsynaptic density-'brain, hippocampus, CA1 region' ( 3 ) , pancreas ( 16 ) , RAW 264.7 (macrophage) ( 4 ) , spleen ( 16 ) , T lymphocyte-spleen ( 15 ) , testis ( 16 )

In vivo Characterization

Methods used to characterize site in vivo:

mass spectrometry ( 1 , 3 , 4 , 5 , 7 , 8 , 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 )

Relevant cell line - cell type - tissue:

'3T3-L1, differentiated' (adipocyte) ( 8 ) , 'fat, brown' ( 16 ) , brain ( 11 , 12 , 16 , 17 , 19 ) , heart ( 9 , 16 ) , HL-1 (myocyte) [Akt1 (mouse), knockdown, stable lentiviral expression of Akt1 shRNA] ( 5 ) , HL-1 (myocyte) [Akt2 (mouse), knockdown, stable lentiviral expression of Akt2 shRNA] ( 5 ) , HL-1 (myocyte) ( 5 ) , kidney ( 16 ) , liver ( 1 , 7 , 18 ) , lung ( 16 ) , macrophage-peritoneum [MPRIP (mouse), homozygous knockout] ( 10 ) , MEF (fibroblast) [p53 (mouse), homozygous knockout] ( 13 ) , MEF (fibroblast) [TSC2 (mouse), homozygous knockout] ( 14 ) , neuron:postsynaptic density-'brain, hippocampus, CA1 region' ( 3 ) , pancreas ( 16 ) , RAW 264.7 (macrophage) ( 4 ) , spleen ( 16 ) , T lymphocyte-spleen ( 15 ) , testis ( 16 )

Upstream Regulation
Regulatory protein:	ADRB1 (mouse) ( 9 )
Treatments:	long-term_potentiation ( 3 ) , refeeding ( 7 )

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	Li J, et al. (2016) Long-term potentiation modulates synaptic phosphorylation networks and reshapes the structure of the postsynaptic interactome. Sci Signal 9, rs8 27507650 Curated Info
4	Pinto SM, et al. (2015) Quantitative phosphoproteomic analysis of IL-33-mediated signaling. Proteomics 15, 532-44 25367039 Curated Info
5	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
6	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
7	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
8	Humphrey SJ, et al. (2013) Dynamic Adipocyte Phosphoproteome Reveals that Akt Directly Regulates mTORC2. Cell Metab 17, 1009-20 23684622 Curated Info
9	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
10	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
11	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
12	Goswami T, et al. (2012) Comparative phosphoproteomic analysis of neonatal and adult murine brain. Proteomics 12, 2185-9 22807455 Curated Info
13	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
14	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
15	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
16	Huttlin EL, et al. (2010) A tissue-specific atlas of mouse protein phosphorylation and expression. Cell 143, 1174-89 21183079 Curated Info
17	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
18	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
19	Ballif BA, et al. (2004) Phosphoproteomic analysis of the developing mouse brain. Mol Cell Proteomics 3, 1093-101 15345747 Curated Info