Ser1907

Site Information
PRGsGtAsDDEFENL SwissProt Entrez-Gene
Blast this site against: NCBI SwissProt PDB
Site Group ID: 453804

In vivo Characterization
Methods used to characterize site in vivo:	mass spectrometry ( 1 , 2 , 4 , 5 , 6 , 7 , 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 )
Disease tissue studied:	anthrax infection ( 23 ) , neuroblastoma ( 21 ) , melanoma skin cancer ( 28 )
Relevant cell line - cell type - tissue:	'3T3-L1, differentiated' (adipocyte) ( 4 , 10 ) , 'brain, cerebellum' ( 13 ) , 'fat, brown' ( 24 ) , 32Dcl3 (myeloid) [FLT3 (mouse), transfection, chimera with human FLT3-ITD mutant (corresponding to wild type P36888 ( 27 ) , 32Dcl3 (myeloid) ( 27 ) , BaF3 ('B lymphocyte, precursor') [JAK3 (human), transfection] ( 1 ) , brain ( 16 , 17 , 24 , 26 ) , heart ( 11 , 24 ) , Hepa 1-6 (epithelial) ( 29 ) , 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 ) , HL-1 (myocyte) ( 7 ) , kidney ( 24 ) , liver ( 2 , 9 , 15 , 24 , 30 , 31 ) , liver [leptin (mouse), homozygous knockout] ( 15 ) , lung ( 24 ) , macrophage-bone marrow ( 25 ) , macrophage-bone marrow [DUSP1 (mouse), homozygous knockout] ( 25 ) , macrophage-peritoneum ( 14 ) , MC3T3-E1 (preosteoblast) ( 5 ) , MEF (fibroblast) [p53 (mouse), homozygous knockout] ( 19 ) , MEF (fibroblast) [Raptor (mouse), knockdown] ( 12 ) , MEF (fibroblast) [RICTOR (mouse), knockdown] ( 12 ) , MEF (fibroblast) [TSC2 (mouse), homozygous knockout] ( 20 ) , MEF (fibroblast) ( 12 ) , N1E-115 (neuron) ( 21 ) , pancreas ( 24 ) , PC-12 (chromaffin) [TrkA (rat), transfection] ( 18 ) , PC-12 (chromaffin) ( 18 ) , RAW 264.7 (macrophage) ( 6 ) , skin [mGluR1 (mouse), transgenic, TG mutant mice] ( 28 ) , spleen ( 23 , 24 ) , T lymphocyte-spleen ( 22 ) , testis ( 24 )

Upstream Regulation
Treatments:	PDGF ( 18 )

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	Minard AY, et al. (2016) mTORC1 Is a Major Regulatory Node in the FGF21 Signaling Network in Adipocytes. Cell Rep 17, 29-36 27681418 Curated Info
5	Williams GR, et al. (2016) Exploring G protein-coupled receptor signaling networks using SILAC-based phosphoproteomics. Methods 92, 36-50 26160508 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	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
10	Humphrey SJ, et al. (2013) Dynamic Adipocyte Phosphoproteome Reveals that Akt Directly Regulates mTORC2. Cell Metab 17, 1009-20 23684622 Curated Info
11	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
12	Robitaille AM, et al. (2013) Quantitative phosphoproteomics reveal mTORC1 activates de novo pyrimidine synthesis. Science 339, 1320-3 23429704 Curated Info
13	Schindler J, Ye J, Jensen ON, Nothwang HG (2013) Monitoring the native phosphorylation state of plasma membrane proteins from a single mouse cerebellum. J Neurosci Methods 213, 153-64 23246975 Curated Info
14	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
15	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
16	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
17	Goswami T, et al. (2012) Comparative phosphoproteomic analysis of neonatal and adult murine brain. Proteomics 12, 2185-9 22807455 Curated Info
18	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
19	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
20	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
21	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
22	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
23	Manes NP, et al. (2011) Discovery of mouse spleen signaling responses to anthrax using label-free quantitative phosphoproteomics via mass spectrometry. Mol Cell Proteomics 10, M110.000927 21189417 Curated Info
24	Huttlin EL, et al. (2010) A tissue-specific atlas of mouse protein phosphorylation and expression. Cell 143, 1174-89 21183079 Curated Info
25	Weintz G, et al. (2010) The phosphoproteome of toll-like receptor-activated macrophages. Mol Syst Biol 6, 371 20531401 Curated Info
26	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
27	Choudhary C, et al. (2009) Mislocalized activation of oncogenic RTKs switches downstream signaling outcomes. Mol Cell 36, 326-39 19854140 Curated Info
28	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
29	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
30	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
31	Dai J, et al. (2007) Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry. J Proteome Res 6, 250-62 17203969 Curated Info