Ser132
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Home > Phosphorylation Site Page: > Ser132  -  HDGF (mouse)

Site Information
kKGsAEGssDEEGKL   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 452718

In vivo Characterization
Methods used to characterize site in vivo:
mass spectrometry ( 1 , 2 , 4 , 5 , 6 , 7 , 8 , 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 ) , mass spectrometry (in vitro) ( 17 )
Disease tissue studied:
anthrax infection ( 21 ) , leukemia ( 15 ) , acute myelogenous leukemia ( 15 ) , lymphoma ( 30 ) , B cell lymphoma ( 30 ) , melanoma skin cancer ( 26 )
Relevant cell line - cell type - tissue:
'3T3-L1, differentiated' (adipocyte) ( 4 , 10 ) , 32Dcl3 (myeloid) ( 23 ) , 32Dcl3 (myeloid) [FLT3 (mouse), transfection, chimera with human FLT3-ITD mutant (corresponding to wild type P36888 ~aa 525-695 ETILLNS...IFEYCC)] ( 23 ) , 3T3 (fibroblast) ( 27 ) , BaF3 ('B lymphocyte, precursor') [JAK3 (human), transfection] ( 1 ) , blood ( 15 ) , brain ( 16 , 25 ) , C2C12 (myoblast) ( 17 , 24 ) , heart ( 11 ) , HL-1 (myocyte) ( 7 ) , 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 ) , liver ( 2 , 9 , 14 , 29 ) , liver [leptin (mouse), homozygous knockout] ( 14 ) , macrophage-peritoneum ( 13 ) , macrophage-peritoneum [MPRIP (mouse), homozygous knockout] ( 13 ) , MC3T3-E1 (preosteoblast) ( 5 ) , MEF (fibroblast) ( 12 , 19 ) , MEF (fibroblast) [p53 (mouse), homozygous knockout] ( 18 ) , MEF (fibroblast) [Raptor (mouse), knockdown] ( 12 ) , MEF (fibroblast) [RICTOR (mouse), knockdown] ( 12 ) , MEF (fibroblast) [TSC2 (mouse), homozygous knockout] ( 19 ) , mpkCCD (renal) ( 22 ) , P19 (testicular) ( 28 ) , RAW 264.7 (macrophage) ( 6 ) , skin [mGluR1 (mouse), transgenic, TG mutant mice] ( 26 ) , spleen ( 21 ) , stromal ( 8 ) , T lymphocyte-spleen ( 20 ) , WEHI-231 (B lymphocyte) ( 30 )

Upstream Regulation
Regulatory protein:
RICTOR (mouse) ( 12 )
Treatments:
ischemia ( 8 ) , NAG-thiazoline ( 27 ) , okadaic_acid ( 27 ) , PUGNAc ( 27 )

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
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

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

14

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

15

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

16

Goswami T, et al. (2012) Comparative phosphoproteomic analysis of neonatal and adult murine brain. Proteomics 12, 2185-9
22807455   Curated Info

17

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

18

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

19

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

20

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

21

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

22

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

23

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

24

Kim BG, et al. (2009) 'Two-stage double-technique hybrid (TSDTH)' identification strategy for the analysis of BMP2-induced transdifferentiation of premyoblast C2C12 cells to osteoblast. J Proteome Res 8, 4441-54
19655815   Curated Info

25

Zhou J (2009) CST Curation Set: 7384; Year: 2009; Biosample/Treatment: tissue, brain/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: QXp[ST]
Curated Info

26

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

27

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

28

Smith JC, et al. (2007) A differential phosphoproteomic analysis of retinoic acid-treated P19 cells. J Proteome Res 6, 3174-86
17622165   Curated Info

29

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

30

Shu H, et al. (2004) Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line. Mol Cell Proteomics 3, 279-86
14729942   Curated Info