Ser54
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Home > Phosphorylation Site Page: > Ser54  -  phosducin (rat)

Site Information
KEILRQMsSPQSRDD   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 454888

In vivo Characterization
Methods used to characterize site in vivo:
immunoprecipitation ( 4 ) , mass spectrometry (in vitro) ( 1 , 2 , 3 ) , phospho-antibody ( 4 )
Relevant cell line - cell type - tissue:
retina ( 4 )

Upstream Regulation
Kinases, in vitro:
CAMK2A (mouse) ( 5 ) , PKACA (human) ( 3 )
Treatments:
light ( 4 )

Downstream Regulation
Effects of modification on phosducin:
molecular association, regulation ( 1 , 2 , 3 , 5 ) , protein conformation ( 2 , 3 ) , protein stabilization ( 1 )
Induce interaction with:
14-3-3 zeta (human) ( 1 , 2 , 3 , 5 )
Inhibit interaction with:
G-beta 1 (human) ( 5 ) , G-gamma 2 (human) ( 5 )

References 

1

Kacirova M, et al. (2017) Structural Basis for the 14-3-3 Protein-Dependent Inhibition of Phosducin Function. Biophys J 112, 1339-1349
28402877   Curated Info

2

Kacirova M, et al. (2015) Structural Characterization of Phosducin and Its Complex with the 14-3-3 Protein. J Biol Chem 290, 16246-60
25971962   Curated Info

3

Rezabkova L, et al. (2012) Structural modulation of phosducin by phosphorylation and 14-3-3 protein binding. Biophys J 103, 1960-9
23199924   Curated Info

4

Song H, Belcastro M, Young EJ, Sokolov M (2007) Compartment-specific phosphorylation of phosducin in rods underlies adaptation to various levels of illumination. J Biol Chem 282, 23613-21
17569665   Curated Info

5

Thulin CD, et al. (2001) Modulation of the G protein regulator phosducin by Ca2+/calmodulin-dependent protein kinase II phosphorylation and 14-3-3 protein binding. J Biol Chem 276, 23805-15
11331285   Curated Info