Ser126
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Home > Phosphorylation Site Page: > Ser126  -  PXN (mouse)

Site Information
sFPNKQksAEPsPtV   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 450227

In vivo Characterization
Methods used to characterize site in vivo:
[32P] bio-synthetic labeling ( 12 ) , electrophoretic mobility shift ( 12 ) , mass spectrometry ( 1 , 2 , 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 ) , mutation of modification site ( 11 , 12 ) , phospho-antibody ( 11 , 12 ) , western blotting ( 12 )
Disease tissue studied:
anthrax infection ( 7 )
Relevant cell line - cell type - tissue:
'3T3-L1, differentiated' (adipocyte) ( 3 ) , 32Dcl3 (myeloid) [FLT3 (mouse), transfection, chimera with human FLT3-ITD mutant (corresponding to wild type P36888 ( 10 ) , 32Dcl3 (myeloid) ( 10 ) , 3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout] ( 12 ) , BAC1 (macrophage) ( 11 ) , heart ( 4 ) , J774 (macrophage) ( 11 ) , kidney ( 8 ) , liver ( 1 , 2 ) , lung ( 8 ) , macrophage-bone marrow ( 9 ) , macrophage-bone marrow [DUSP1 (mouse), homozygous knockout] ( 9 ) , macrophage-peritoneum ( 11 ) , macrophage-peritoneum [MPRIP (mouse), homozygous knockout] ( 5 ) , MEF (fibroblast) ( 6 ) , MEF (fibroblast) [TSC2 (mouse), homozygous knockout] ( 6 ) , RAW 264 (macrophage) ( 11 ) , spleen ( 7 , 8 )

Upstream Regulation
Regulatory protein:
FLT3 (mouse) ( 10 )
Putative in vivo kinases:
GSK3A (mouse) ( 11 )
Phosphatases, in vitro:
PPP2CA (mouse) ( 12 )
Treatments:
4-HT ( 12 ) , GSK-3_inhibitor_I ( 11 ) , inhibitor_IX ( 11 ) , insulin ( 3 ) , lithium ( 11 ) , LPS ( 9 , 11 ) , LY294002 ( 3 , 12 ) , M-CSF ( 11 ) , MK-2206 ( 3 ) , okadaic_acid ( 12 ) , PD98059 ( 11 , 12 ) , PDGF ( 12 ) , phorbol_ester ( 11 ) , PP2 ( 11 ) , siRNA ( 11 ) , U0126 ( 11 , 12 )

Downstream Regulation
Effects of modification on biological processes:
cell motility, altered ( 11 ) , cytoskeletal reorganization ( 11 )

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

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

3

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

4

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

5

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

6

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

7

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

8

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

9

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

10

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

11

Cai X, Li M, Vrana J, Schaller MD (2006) Glycogen synthase kinase 3- and extracellular signal-regulated kinase-dependent phosphorylation of paxillin regulates cytoskeletal rearrangement. Mol Cell Biol 26, 2857-68
16537926   Curated Info

12

Woodrow MA, et al. (2003) Ras-induced serine phosphorylation of the focal adhesion protein paxillin is mediated by the Raf-->MEK-->ERK pathway. Exp Cell Res 287, 325-38
12837288   Curated Info