Ser123
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Home > Phosphorylation Site Page: > Ser123  -  PPP1R2 (mouse)

Site Information
RtREQEssGEEDNDL   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 449053

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 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 , 39 , 40 )
Disease tissue studied:
anthrax infection ( 18 ) , leukemia ( 14 ) , acute myelogenous leukemia ( 14 ) , melanoma skin cancer ( 36 )
Relevant cell line - cell type - tissue:
'3T3-L1, differentiated' (adipocyte) ( 3 , 9 ) , 'brain, embryonic' ( 27 , 28 , 32 , 35 ) , 'fat, brown' ( 19 ) , 'stem, embryonic' ( 23 , 24 , 25 ) , blood ( 14 ) , brain ( 15 , 19 , 21 , 26 , 33 , 34 , 40 ) , heart ( 10 , 19 , 30 , 31 ) , Hepa 1-6 (epithelial) ( 37 ) , HL-1 (myocyte) [Akt1 (mouse), knockdown, stable lentiviral expression of Akt1 shRNA] ( 6 ) , HL-1 (myocyte) [Akt2 (mouse), knockdown, stable lentiviral expression of Akt2 shRNA] ( 6 ) , HL-1 (myocyte) ( 6 ) , kidney ( 19 ) , liver ( 1 , 8 , 13 , 19 , 29 , 39 ) , liver [leptin (mouse), homozygous knockout] ( 13 ) , lung ( 19 ) , macrophage-bone marrow ( 20 ) , macrophage-bone marrow [DUSP1 (mouse), homozygous knockout] ( 20 ) , macrophage-peritoneum [MPRIP (mouse), homozygous knockout] ( 12 ) , MC3T3-E1 (preosteoblast) ( 4 ) , MEF (fibroblast) ( 11 , 17 ) , MEF (fibroblast) [p53 (mouse), homozygous knockout] ( 16 ) , MEF (fibroblast) [Raptor (mouse), knockdown] ( 11 ) , MEF (fibroblast) [RICTOR (mouse), knockdown] ( 11 ) , MEF (fibroblast) [TSC2 (mouse), homozygous knockout] ( 17 ) , mpkCCD (renal) ( 22 ) , P19 (testicular) ( 38 ) , pancreas ( 19 ) , RAW 264.7 (macrophage) ( 5 ) , skin [mGluR1 (mouse), transgenic, TG mutant mice] ( 36 ) , spleen ( 18 , 19 ) , stromal ( 7 ) , testis ( 19 )

Upstream Regulation
Regulatory protein:
TSC2 (mouse) ( 16 )
Treatments:
insulin ( 9 ) , LY294002 ( 9 ) , retinoic_acid ( 38 )

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

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

7

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

8

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

9

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

10

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

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

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

16

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

17

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

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

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

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

Tucker M (2009) CST Curation Set: 8081; Year: 2009; Biosample/Treatment: cell line, embryonic stem cells (mouse)(PTEN)/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: pY Antibodies Used to Purify Peptides prior to LCMS: Phospho-Tyrosine Mouse mAb (P-Tyr-100) Cat#: 9411, PTMScan(R) Phospho-Tyr Motif (Y*) Immunoaffinity Beads Cat#: 1991
Curated Info

24

Tucker M (2009) CST Curation Set: 8072; Year: 2009; Biosample/Treatment: cell line, embryonic stem cells (mouse)(PTEN)/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: p[STY] Antibodies Used to Purify Peptides prior to LCMS: Phospho-Tyrosine (P-Tyr-1000) Rabbit mAb Cat#: 8954, Phospho-Tyrosine Rabbit mAb (p-Tyr-1000) Immunoaffinity Beads Cat#: 8876
Curated Info

25

Li H, et al. (2009) SysPTM: a systematic resource for proteomic research on post-translational modifications. Mol Cell Proteomics 8, 1839-49
19366988   Curated Info

26

Zhou J (2009) CST Curation Set: 7431; Year: 2009; Biosample/Treatment: tissue, brain/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: pSP
Curated Info

27

Zhou J (2009) CST Curation Set: 7428; Year: 2009; Biosample/Treatment: tissue, brain/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: pSP
Curated Info

28

Zhou J (2009) CST Curation Set: 7429; Year: 2009; Biosample/Treatment: tissue, brain/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: pSP
Curated Info

29

Zhou J (2009) CST Curation Set: 7387; Year: 2009; Biosample/Treatment: tissue, liver/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: QXp[ST]
Curated Info

30

Zhou J (2009) CST Curation Set: 7385; Year: 2009; Biosample/Treatment: tissue, heart/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: QXp[ST]
Curated Info

31

Zhou J (2009) CST Curation Set: 7386; Year: 2009; Biosample/Treatment: tissue, heart/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: QXp[ST]
Curated Info

32

Zhou J (2009) CST Curation Set: 7381; Year: 2009; Biosample/Treatment: tissue, brain/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: QXp[ST]
Curated Info

33

Zhou J (2009) CST Curation Set: 7383; Year: 2009; Biosample/Treatment: tissue, brain/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: QXp[ST]
Curated Info

34

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

35

Zhou J (2009) CST Curation Set: 7382; Year: 2009; Biosample/Treatment: tissue, brain/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: QXp[ST]
Curated Info

36

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

37

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

38

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

39

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

40

Ballif BA, et al. (2004) Phosphoproteomic analysis of the developing mouse brain. Mol Cell Proteomics 3, 1093-101
15345747   Curated Info