Ser235
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage PhosphoSitePlus® v6.7.7
Powered by Cell Signaling Technology
Home > Phosphorylation Site Page: > Ser235  -  AQP0 (human)

Site Information
KsIsERLsVLKGAKP   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 450116

In vivo Characterization
Methods used to characterize site in vivo:
mass spectrometry ( 3 , 5 , 6 ) , mass spectrometry (in vitro) ( 4 ) , mutation of modification site ( 1 , 2 )
Relevant cell line - cell type - tissue:
lens ( 3 , 5 , 6 ) , oocyte ( 2 ) , Pichia pastoris (yeast cell) ( 1 )

Downstream Regulation
Effects of modification on AQP0:
activity, induced ( 1 ) , molecular association, regulation ( 1 , 2 , 4 ) , protein conformation ( 2 )
Inhibit interaction with:
Calmodulin (cow) ( 4 ) , Calmodulin (human) ( 1 , 2 )

References 

1

Kreida S, et al. (2023) The role of phosphorylation in calmodulin-mediated gating of human AQP0. Biochem J
38032258   Curated Info

2

Fields JB, et al. (2017) Calmodulin Gates Aquaporin 0 Permeability through a Positively Charged Cytoplasmic Loop. J Biol Chem 292, 185-195
27660387   Curated Info

3

Gutierrez DB, et al. (2016) Spatial distributions of phosphorylated membrane proteins aquaporin 0 and MP20 across young and aged human lenses. Exp Eye Res 149, 59-65
27339748   Curated Info

4

Rose KM, et al. (2008) Aquaporin 0-calmodulin interaction and the effect of aquaporin 0 phosphorylation. Biochemistry 47, 339-47
18081321   Curated Info

5

Ball LE, Garland DL, Crouch RK, Schey KL (2004) Post-translational modifications of aquaporin 0 (AQP0) in the normal human lens: spatial and temporal occurrence. Biochemistry 43, 9856-65
15274640   Curated Info

6

Schey KL, Little M, Fowler JG, Crouch RK (2000) Characterization of human lens major intrinsic protein structure. Invest Ophthalmol Vis Sci 41, 175-82
10634618   Curated Info