Ser328
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Home > Phosphorylation Site Page: > Ser328  -  p47phox (human)

Site Information
QDAYRRNsVRFLQQR   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 449404

In vivo Characterization
Methods used to characterize site in vivo:
[32P] bio-synthetic labeling ( 17 , 18 ) , flow cytometry ( 1 ) , immunoprecipitation ( 11 ) , mutation of modification site ( 1 , 8 , 11 , 12 , 16 , 17 ) , peptide sequencing ( 18 ) , phospho-antibody ( 2 , 3 , 4 , 5 , 6 , 7 , 9 , 10 , 11 , 12 ) , phosphoamino acid analysis ( 18 ) , phosphopeptide mapping ( 17 , 18 ) , western blotting ( 2 , 3 , 4 , 5 , 6 , 7 , 9 , 10 , 11 , 12 )
Disease tissue studied:
leukemia ( 16 ) , chronic myelogenous leukemia ( 16 )
Relevant cell line - cell type - tissue:
B lymphocyte-blood ( 12 ) , B lymphocyte-spleen ( 17 ) , COS7 (fibroblast) ( 11 ) , EA.hy 926 (endothelial) ( 5 ) , K562 (erythroid) ( 16 ) , MEF (fibroblast) ( 1 ) , microvessel endothelial ( 8 ) , neutrophil ( 2 , 3 , 5 , 17 , 18 ) , neutrophil-blood ( 4 , 6 , 7 , 9 , 10 ) , SVEC (endothelial) ( 11 )

Upstream Regulation
Regulatory protein:
FPR1 (mouse) ( 7 )
Putative in vivo kinases:
Akt3 (human) ( 1 )
Kinases, in vitro:
Akt1 (human) ( 14 ) , PKACA (human) ( 17 ) , PKCA (human) ( 15 , 17 ) , PKCB iso2 (human) ( 15 ) , PKCD (human) ( 15 )
Treatments:
albumin ( 5 ) , anv-polysaccharides ( 6 ) , CL097 ( 10 ) , fibrinogen ( 2 ) , fMLP ( 2 , 3 , 10 , 18 ) , GM-CSF ( 5 ) , juglone ( 10 ) , LPS ( 4 ) , LY294002 ( 2 ) , pansorbin ( 12 ) , phorbol_ester ( 2 , 3 , 6 , 10 , 12 , 18 ) , thymoquinone ( 7 ) , TNF ( 10 ) , zymosan ( 9 )

Downstream Regulation
Effects of modification on p47phox:
enzymatic activity, induced ( 1 , 3 , 16 ) , intracellular localization ( 3 ) , molecular association, regulation ( 13 , 15 , 16 ) , phosphorylation ( 11 )
Effects of modification on biological processes:
cell growth, induced ( 1 ) , signaling pathway regulation ( 3 , 4 , 11 )
Induce interaction with:
ACTB (human) ( 13 ) , CYBA (human) ( 15 , 16 )

References 

1

Polytarchou C, et al. (2020) Akt3 induces oxidative stress and DNA damage by activating the NADPH oxidase via phosphorylation of p47. Proc Natl Acad Sci U S A 117, 28806-28815
33139577   Curated Info

2

Song Z, et al. (2020) Class I phosphoinositide 3-kinases control sustained NADPH oxidase activation in adherent neutrophils. Biochem Pharmacol 178, 114088
32531347   Curated Info

3

Chniguir A, et al. (2019) Eugenol prevents fMLF-induced superoxide anion production in human neutrophils by inhibiting ERK1/2 signaling pathway and p47phox phosphorylation. Sci Rep 9, 18540
31811262   Curated Info

4

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

5

Htwe SS, et al. (2018) Inter-α inhibitor proteins maintain neutrophils in a resting state by regulating shape and reducing ROS production. Blood Adv 2, 1923-1934
30093530   Curated Info

6

Boukemara H, et al. (2016) Anvillea garcinii extract inhibits the oxidative burst of primary human neutrophils. BMC Complement Altern Med 16, 433
27809835   Curated Info

7

Boudiaf K, et al. (2016) Thymoquinone strongly inhibits fMLF-induced neutrophil functions and exhibits anti-inflammatory properties in vivo. Biochem Pharmacol 104, 62-73
26774451   Curated Info

8

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

9

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

10

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

11

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

12

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

13

Tamura M, et al. (2006) Identification of an actin-binding site in p47phox an organizer protein of NADPH oxidase. FEBS Lett 580, 261-7
16375898   Curated Info

14

Chen Q, et al. (2003) Akt phosphorylates p47phox and mediates respiratory burst activity in human neutrophils. J Immunol 170, 5302-8
12734380   Curated Info

15

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

16

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

17

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

18

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