Ser201
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage PhosphoSitePlus® v6.7.1.1
Powered by Cell Signaling Technology
Home > Phosphorylation Site Page: > Ser201  -  SF2 (mouse)

Site Information
VDGPRsPsyGRsRsR   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 465633

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 )
Disease tissue studied:
anthrax infection ( 14 )
Relevant cell line - cell type - tissue:
'3T3-L1, differentiated' (adipocyte) ( 3 , 7 ) , 'brain, forebrain' ( 22 ) , 'fat, brown' ( 15 ) , 32Dcl3 (myeloid) [FLT3 (mouse), transfection, chimera with human FLT3-ITD mutant (corresponding to wild type P36888 ( 18 ) , 32Dcl3 (myeloid) ( 18 ) , 3T3 (fibroblast) ( 21 ) , brain ( 15 ) , C2C12 (myoblast) ( 11 ) , C3H10T1/2 (fibroblast) [FGFR2 (mouse), FGFR2 K668E] ( 20 ) , heart ( 8 , 15 ) , kidney ( 15 ) , liver ( 1 , 6 , 10 , 15 , 19 ) , liver [leptin (mouse), homozygous knockout] ( 10 ) , lung ( 15 ) , macrophage-bone marrow ( 16 ) , macrophage-bone marrow [DUSP1 (mouse), homozygous knockout] ( 16 ) , macrophage-peritoneum ( 9 ) , macrophage-peritoneum [MPRIP (mouse), homozygous knockout] ( 9 ) , MC3T3-E1 (preosteoblast) ( 4 ) , MEF (fibroblast) [p53 (mouse), homozygous knockout] ( 12 ) , MEF (fibroblast) [TSC2 (mouse), homozygous knockout] ( 13 ) , mpkCCD (renal) ( 17 ) , pancreas ( 15 ) , RAW 264.7 (macrophage) ( 5 ) , spleen ( 14 , 15 ) , testis ( 15 )

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

Pinto SM, et al. (2015) Quantitative phosphoproteomic analysis of IL-33-mediated signaling. Proteomics 15, 532-44
25367039   Curated Info

6

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

7

Humphrey SJ, et al. (2013) Dynamic Adipocyte Phosphoproteome Reveals that Akt Directly Regulates mTORC2. Cell Metab 17, 1009-20
23684622   Curated Info

8

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

9

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

10

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

11

Knight JD, et al. (2012) A novel whole-cell lysate kinase assay identifies substrates of the p38 MAPK in differentiating myoblasts. Skelet Muscle 2, 5
22394512   Curated Info

12

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

13

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

14

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

15

Huttlin EL, et al. (2010) A tissue-specific atlas of mouse protein phosphorylation and expression. Cell 143, 1174-89
21183079   Curated Info

16

Weintz G, et al. (2010) The phosphoproteome of toll-like receptor-activated macrophages. Mol Syst Biol 6, 371
20531401   Curated Info

17

Rinschen MM, et al. (2010) Quantitative phosphoproteomic analysis reveals vasopressin V2-receptor-dependent signaling pathways in renal collecting duct cells. Proc Natl Acad Sci U S A 107, 3882-7
20139300   Curated Info

18

Choudhary C, et al. (2009) Mislocalized activation of oncogenic RTKs switches downstream signaling outcomes. Mol Cell 36, 326-39
19854140   Curated Info

19

Zhou J (2009) CST Curation Set: 7425; Year: 2009; Biosample/Treatment: tissue, liver/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: HXXp[ST]
Curated Info

20

Li Y (2008) CST Curation Set: 5593; Year: 2008; Biosample/Treatment: cell line, 10T1/2FGFRK668E/FGF; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: PXpSP, pSPX(K/R) Antibodies Used to Purify Peptides prior to LCMS: Phospho-MAPK/CDK Substrates (PXSP or SPXR/K) (34B2) Rabbit mAb Cat#: 2325, PTMScan(R) Phospho-MAPK/CDK Substrate Motif (PXS*P, S*PXK/R) Immunoaffinity Beads Cat#: 1982
Curated Info

21

Wang Z, Gucek M, Hart GW (2008) Cross-talk between GlcNAcylation and phosphorylation: site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc. Proc Natl Acad Sci U S A 105, 13793-8
18779572   Curated Info

22

Collins MO, et al. (2008) Phosphoproteomic analysis of the mouse brain cytosol reveals a predominance of protein phosphorylation in regions of intrinsic sequence disorder. Mol Cell Proteomics 7, 1331-48
18388127   Curated Info