Ser160

Site Information
KKNAkISsLLEEQFQ SwissProt Entrez-Gene
Blast this site against: NCBI SwissProt PDB
Site Group ID: 3193378

In vivo Characterization
Methods used to characterize site in vivo:	mass spectrometry ( 1 , 2 , 4 , 6 , 7 , 8 , 9 , 10 )
Relevant cell line - cell type - tissue:	'3T3-L1, differentiated' (adipocyte) ( 6 ) , BaF3 ('B lymphocyte, precursor') [JAK3 (human), transfection] ( 1 ) , 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 ) , liver ( 2 , 8 ) , liver [leptin (mouse), homozygous knockout] ( 8 ) , macrophage-peritoneum [MPRIP (mouse), homozygous knockout] ( 7 ) , MEF (fibroblast) [p53 (mouse), homozygous knockout] ( 10 ) , PC-12 (chromaffin) [TrkA (rat), transfection] ( 9 ) , PC-12 (chromaffin) ( 9 )

In vivo Characterization

Methods used to characterize site in vivo:

mass spectrometry ( 1 , 2 , 4 , 6 , 7 , 8 , 9 , 10 )

Relevant cell line - cell type - tissue:

'3T3-L1, differentiated' (adipocyte) ( 6 ) , BaF3 ('B lymphocyte, precursor') [JAK3 (human), transfection] ( 1 ) , 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 ) , liver ( 2 , 8 ) , liver [leptin (mouse), homozygous knockout] ( 8 ) , macrophage-peritoneum [MPRIP (mouse), homozygous knockout] ( 7 ) , MEF (fibroblast) [p53 (mouse), homozygous knockout] ( 10 ) , PC-12 (chromaffin) [TrkA (rat), transfection] ( 9 ) , PC-12 (chromaffin) ( 9 )

Upstream Regulation
Treatments:	PDGF ( 9 )

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 32 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	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	Humphrey SJ, et al. (2013) Dynamic Adipocyte Phosphoproteome Reveals that Akt Directly Regulates mTORC2. Cell Metab 17, 1009-20 23684622 Curated Info
7	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
8	Grimsrud PA, et al. (2012) A quantitative map of the liver mitochondrial phosphoproteome reveals posttranslational control of ketogenesis. Cell Metab 16, 672-83 23140645 Curated Info
9	Biarc J, Chalkley RJ, Burlingame AL, Bradshaw RA (2012) The induction of serine/threonine protein phosphorylations by a PDGFR/TrkA chimera in stably transfected PC12 cells. Mol Cell Proteomics 11, 15-30 22027198 Curated Info
10	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