Ser412
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage PhosphoSitePlus® v6.5.9.3
Powered by Cell Signaling Technology
Home > Phosphorylation Site Page: > Ser412  -  TAK1 (mouse)

Site Information
NGQPRRRsIQDLtVT   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 455196

In vivo Characterization
Methods used to characterize site in vivo:
amino acid analysis ( 1 ) , mass spectrometry ( 2 , 3 , 4 , 5 , 6 , 7 , 8 , 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 ) , mutation of modification site ( 36 ) , phospho-antibody ( 36 ) , western blotting ( 36 )
Disease tissue studied:
anthrax infection ( 22 ) , leukemia ( 16 ) , acute myelogenous leukemia ( 16 ) , neuroblastoma ( 20 ) , melanoma skin cancer ( 31 )
Relevant cell line - cell type - tissue:
'3T3-L1, differentiated' (adipocyte) ( 4 , 6 , 11 ) , 'brain, cerebellum' ( 32 ) , 'brain, cerebral cortex' ( 32 , 34 ) , 'brain, embryonic' ( 33 ) , 'brain, hippocampus, dentate gyrus' ( 32 ) , 'brain, midbrain' ( 32 ) , 'fat, brown' ( 23 ) , 32Dcl3 (myeloid) [FLT3 (mouse), transfection, chimera with human FLT3-ITD mutant (corresponding to wild type P36888 ( 29 ) , 32Dcl3 (myeloid) ( 29 ) , BaF3 ('B lymphocyte, precursor') [JAK3 (human), transfection] ( 2 ) , blood ( 16 ) , brain ( 17 , 23 , 25 ) , fibroblast-lung ( 26 , 27 ) , heart ( 12 , 23 ) , HL-1 (myocyte) [Akt1 (mouse), knockdown, stable lentiviral expression of Akt1 shRNA] ( 8 ) , HL-1 (myocyte) [Akt2 (mouse), knockdown, stable lentiviral expression of Akt2 shRNA] ( 8 ) , HL-1 (myocyte) ( 8 ) , kidney ( 23 ) , liver ( 3 , 10 , 15 , 23 , 35 ) , liver [leptin (mouse), homozygous knockout] ( 15 ) , lung ( 23 ) , macrophage-bone marrow ( 24 ) , macrophage-bone marrow [DUSP1 (mouse), homozygous knockout] ( 24 ) , macrophage-peritoneum ( 14 ) , MC3T3-E1 (preosteoblast) ( 5 ) , MEF (fibroblast) ( 13 , 14 , 19 ) , MEF (fibroblast) [p53 (mouse), homozygous knockout] ( 18 ) , MEF (fibroblast) [Raptor (mouse), knockdown] ( 13 ) , MEF (fibroblast) [RICTOR (mouse), knockdown] ( 13 ) , MEF (fibroblast) [TSC2 (mouse), homozygous knockout] ( 19 ) , mpkCCD (renal) ( 28 ) , N1E-115 (neuron) ( 20 ) , pancreas ( 23 ) , RAW 264 (macrophage) ( 36 ) , RAW 264.7 (macrophage) ( 7 ) , RAW 267.4 (macrophage) ( 30 ) , skin [mGluR1 (mouse), transgenic, TG mutant mice] ( 31 ) , spleen ( 22 , 23 ) , T lymphocyte-spleen ( 21 ) , testis ( 23 )

Upstream Regulation
Regulatory protein:
MPRIP (mouse) ( 14 )
Treatments:
PGE2a ( 36 ) , PTH(1-34) ( 5 ) , RANKL ( 36 )

Downstream Regulation
Effects of modification on TAK1:
phosphorylation ( 36 )
Effects of modification on biological processes:
cell differentiation, altered ( 36 ) , transcription, altered ( 36 )

References 

1

Watson CJF, et al. (2020) TAK1 signaling activity links the mast cell cytokine response and degranulation in allergic inflammation. J Leukoc Biol
32108376   Curated Info

2

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

3

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

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

Parker BL, et al. (2015) Targeted phosphoproteomics of insulin signaling using data-independent acquisition mass spectrometry. Sci Signal 8, rs6
26060331   Curated Info

7

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

8

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

9

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

10

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

11

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

12

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

13

Robitaille AM, et al. (2013) Quantitative phosphoproteomics reveal mTORC1 activates de novo pyrimidine synthesis. Science 339, 1320-3
23429704   Curated Info

14

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

15

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

16

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

17

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

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

21

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

22

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

23

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

24

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

25

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

26

Guo A (2010) CST Curation Set: 9811; Year: 2010; Biosample/Treatment: cell line, mouse lung fibroblasts/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: RXXp[ST]
Curated Info

27

Guo A (2010) CST Curation Set: 9812; Year: 2010; Biosample/Treatment: cell line, mouse lung fibroblasts/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: RXXp[ST]
Curated Info

28

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

29

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

30

Trost M, et al. (2009) The phagosomal proteome in interferon-gamma-activated macrophages. Immunity 30, 143-54
19144319   Curated Info

31

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

32

Trinidad JC, et al. (2008) Quantitative analysis of synaptic phosphorylation and protein expression. Mol Cell Proteomics 7, 684-96
18056256   Curated Info

33

Possemato A (2008) CST Curation Set: 3825; Year: 2008; Biosample/Treatment: tissue, brain/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: (K/R)XpSX(K/R) Antibodies Used to Purify Peptides prior to LCMS: Phospho-(Ser) PKC Substrate Antibody Cat#: 2261, PTMScan(R) Phospho-PKC Substrate Motif (K/RXpSXK/R) Immunoaffinity Beads Cat#: 1985
Curated Info

34

Munton RP, et al. (2007) Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations. Mol Cell Proteomics 6, 283-93
17114649   Curated Info

35

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

36

Kobayashi Y, et al. (2005) Prostaglandin E2 enhances osteoclastic differentiation of precursor cells through protein kinase A-dependent phosphorylation of TAK1. J Biol Chem 280, 11395-403
15647289   Curated Info