Ser320
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Home > Phosphorylation Site Page: > Ser320  -  p47phox (human)

Site Information
QRsRKRLsQDAYRRN   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 451726

In vivo Characterization
Methods used to characterize site in vivo:
[32P] bio-synthetic labeling ( 11 , 12 ) , immunoprecipitation ( 6 ) , mass spectrometry ( 2 , 8 ) , mutation of modification site ( 3 , 6 , 7 , 10 , 11 ) , peptide sequencing ( 12 ) , phospho-antibody ( 1 , 4 , 5 , 6 , 7 ) , phosphoamino acid analysis ( 12 ) , phosphopeptide mapping ( 11 , 12 ) , western blotting ( 1 , 4 , 5 , 6 , 7 )
Disease tissue studied:
HER2 positive breast cancer ( 2 ) , luminal A breast cancer ( 2 ) , luminal B breast cancer ( 2 ) , breast cancer, triple negative ( 2 ) , leukemia ( 10 ) , chronic myelogenous leukemia ( 10 )
Relevant cell line - cell type - tissue:
B lymphocyte-blood ( 7 ) , B lymphocyte-spleen ( 11 ) , breast ( 2 ) , COS7 (fibroblast) ( 6 ) , K562 (erythroid) ( 10 ) , microvessel endothelial ( 3 ) , neutrophil ( 8 , 11 , 12 ) , neutrophil-blood ( 1 , 4 , 5 ) , SVEC (endothelial) ( 6 )

Upstream Regulation
Putative in vivo kinases:
IRAK4 (human) ( 8 )
Kinases, in vitro:
IRAK4 (human) ( 8 ) , PKACA (human) ( 11 ) , PKCA (human) ( 9 , 11 ) , PKCB iso2 (human) ( 9 ) , PKCD (human) ( 9 )
Treatments:
CL097 ( 5 ) , fMLP ( 12 ) , LPS ( 1 , 8 ) , pansorbin ( 7 ) , phorbol_ester ( 7 , 12 ) , zymosan ( 4 )

Downstream Regulation
Effects of modification on p47phox:
molecular association, regulation ( 9 )
Effects of modification on biological processes:
signaling pathway regulation ( 1 )
Induce interaction with:
CYBA (human) ( 9 )

References 

1

Liu M, et al. (2019) The Prolyl Isomerase Pin1 Controls Lipopolysaccharide-Induced Priming of NADPH Oxidase in Human Neutrophils. Front Immunol 10, 2567
31736979   Curated Info

2

Mertins P, et al. (2016) Proteogenomics connects somatic mutations to signalling in breast cancer. Nature 534, 55-62
27251275   Curated Info

3

Meijles DN, Fan LM, Howlin BJ, Li JM (2014) Molecular Insights of p47phox Phosphorylation Dynamics in the Regulation of NADPH Oxidase Activation and Superoxide Production. J Biol Chem 289, 22759-70
24970888   Curated Info

4

Makni-Maalej K, et al. (2013) Zymosan induces NADPH oxidase activation in human neutrophils by inducing the phosphorylation of p47phox and the activation of Rac2: involvement of protein tyrosine kinases, PI3Kinase, PKC, ERK1/2 and p38MAPkinase. Biochem Pharmacol 85, 92-100
23085266   Curated Info

5

Makni-Maalej K, et al. (2012) The TLR7/8 Agonist CL097 Primes N-Formyl-Methionyl-Leucyl-Phenylalanine-Stimulated NADPH Oxidase Activation in Human Neutrophils: Critical Role of p47phox Phosphorylation and the Proline Isomerase Pin1. J Immunol 189, 4657-65
23002436   Curated Info

6

Teng L, Fan LM, Meijles D, Li JM (2012) Divergent Effects of p47phox Phosphorylation at S303-4 or S379 on Tumor Necrosis Factor-α Signaling via TRAF4 and MAPK in Endothelial Cells. Arterioscler Thromb Vasc Biol 32, 1488-96
22460559   Curated Info

7

Belambri SA, et al. (2012) Phosphorylation of p47phox is required for receptor-mediated NADPH oxidase/NOX2 activation in Epstein-Barr virus-transformed human B lymphocytes. Am J Blood Res 2, 187-93
23119229   Curated Info

8

Pacquelet S, et al. (2007) Cross-talk between IRAK-4 and the NADPH oxidase. Biochem J 403, 451-61
17217339   Curated Info

9

Fontayne A, Dang PM, Gougerot-Pocidalo MA, El-Benna J (2002) Phosphorylation of p47phox sites by PKC alpha, beta II, delta, and zeta: effect on binding to p22phox and on NADPH oxidase activation. Biochemistry 41, 7743-50
12056906   Curated Info

10

Ago T, Nunoi H, Ito T, Sumimoto H (1999) Mechanism for phosphorylation-induced activation of the phagocyte NADPH oxidase protein p47(phox). Triple replacement of serines 303, 304, and 328 with aspartates disrupts the SH3 domain-mediated intramolecular interaction in p47(phox), thereby activating the oxidase. J Biol Chem 274, 33644-53
10559253   Curated Info

11

El Benna J, Faust RP, Johnson JL, Babior BM (1996) Phosphorylation of the respiratory burst oxidase subunit p47phox as determined by two-dimensional phosphopeptide mapping. Phosphorylation by protein kinase C, protein kinase A, and a mitogen-activated protein kinase. J Biol Chem 271, 6374-8
8626435   Curated Info

12

el Benna J, Faust LP, Babior BM (1994) The phosphorylation of the respiratory burst oxidase component p47phox during neutrophil activation. Phosphorylation of sites recognized by protein kinase C and by proline-directed kinases. J Biol Chem 269, 23431-6
8089108   Curated Info