Ser1045

Site Information
RSHtGDLsPNVQsRD SwissProt Entrez-Gene
Blast this site against: NCBI SwissProt PDB
Site Group ID: 3215688

In vivo Characterization
Methods used to characterize site in vivo:	mass spectrometry ( 1 , 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 , 21 , 22 , 23 )
Disease tissue studied:	anthrax infection ( 18 ) , leukemia ( 14 ) , acute myelogenous leukemia ( 14 ) , neuroblastoma ( 17 ) , melanoma skin cancer ( 22 )
Relevant cell line - cell type - tissue:	'3T3-L1, differentiated' (adipocyte) ( 3 , 5 , 10 ) , 32Dcl3 (myeloid) [FLT3 (mouse), transfection, chimera with human FLT3-ITD mutant (corresponding to wild type P36888 ( 21 ) , 32Dcl3 (myeloid) ( 21 ) , blood ( 14 ) , brain ( 15 ) , Hepa 1-6 (epithelial) ( 23 ) , 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 ) , liver ( 1 , 9 , 13 , 19 ) , liver [leptin (mouse), homozygous knockout] ( 13 ) , macrophage-bone marrow ( 20 ) , macrophage-bone marrow [DUSP1 (mouse), homozygous knockout] ( 20 ) , macrophage-peritoneum ( 12 ) , MC3T3-E1 (preosteoblast) ( 4 ) , MEF (fibroblast) [Raptor (mouse), knockdown] ( 11 ) , MEF (fibroblast) [RICTOR (mouse), knockdown] ( 11 ) , MEF (fibroblast) [TSC2 (mouse), homozygous knockout] ( 16 ) , MEF (fibroblast) ( 11 ) , N1E-115 (neuron) ( 17 ) , pancreas ( 19 ) , RAW 264.7 (macrophage) ( 6 ) , skin [mGluR1 (mouse), transgenic, TG mutant mice] ( 22 ) , spleen ( 18 ) , stromal ( 8 )

Upstream Regulation
Regulatory protein:	Raptor (mouse) ( 11 )
Treatments:	insulin ( 10 ) , ischemia ( 8 ) , LPS ( 20 )

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	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
4	Williams GR, et al. (2016) Exploring G protein-coupled receptor signaling networks using SILAC-based phosphoproteomics. Methods 92, 36-50 26160508 Curated Info
5	Parker BL, et al. (2015) Targeted phosphoproteomics of insulin signaling using data-independent acquisition mass spectrometry. Sci Signal 8, rs6 26060331 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	Robitaille AM, et al. (2013) Quantitative phosphoproteomics reveal mTORC1 activates de novo pyrimidine synthesis. Science 339, 1320-3 23429704 Curated Info
12	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
13	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
14	Trost M, et al. (2012) Posttranslational regulation of self-renewal capacity: insights from proteome and phosphoproteome analyses of stem cell leukemia. Blood 120, e17-27 22802335 Curated Info
15	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
16	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
17	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
18	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
19	Huttlin EL, et al. (2010) A tissue-specific atlas of mouse protein phosphorylation and expression. Cell 143, 1174-89 21183079 Curated Info
20	Weintz G, et al. (2010) The phosphoproteome of toll-like receptor-activated macrophages. Mol Syst Biol 6, 371 20531401 Curated Info
21	Choudhary C, et al. (2009) Mislocalized activation of oncogenic RTKs switches downstream signaling outcomes. Mol Cell 36, 326-39 19854140 Curated Info
22	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
23	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