Ser68
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Home > Phosphorylation Site Page: > Ser68  -  AHCYL1 (mouse)

Site Information
RSLSRsIsQsstDsy   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 467244

In vivo Characterization
Methods used to characterize site in vivo:
[32P] bio-synthetic labeling ( 4 ) , immunoprecipitation ( 1 , 3 ) , mass spectrometry (in vitro) ( 3 ) , mutation of modification site ( 1 , 4 ) , phospho-antibody ( 2 ) , western blotting ( 1 , 2 )
Relevant cell line - cell type - tissue:
'brain, cerebellum' ( 2 ) , COS (fibroblast) ( 1 , 3 , 4 ) , HeLa (cervical) ( 4 ) , SF9 ( 4 )

Upstream Regulation
Kinases, in vitro:
CK1A (human) ( 3 ) , PRKD1 (human) ( 3 )
Phosphatases, in vitro:
PPP1CA (human) ( 3 )

Downstream Regulation
Effects of modification on AHCYL1:
molecular association, regulation ( 1 , 3 , 4 ) , phosphorylation ( 3 )
Induce interaction with:
IP3R1 (human) ( 4 ) , PIP4K2A (human) ( 1 ) , PIP5K1A (mouse) ( 1 ) , PPP1CA (human) ( 3 )

References 

1

Ando H, et al. (2015) IRBIT Interacts with the Catalytic Core of Phosphatidylinositol Phosphate Kinase Type Iα and IIα through Conserved Catalytic Aspartate Residues. PLoS One 10, e0141569
26509711   Curated Info

2

Ando H, Mizutani A, Mikoshiba K (2009) An IRBIT homologue lacks binding activity to inositol 1,4,5-trisphosphate receptor due to the unique N-terminal appendage. J Neurochem 109, 539-50
19220705   Curated Info

3

Devogelaere B, et al. (2007) Protein phosphatase-1 is a novel regulator of the interaction between IRBIT and the inositol 1,4,5-trisphosphate receptor. Biochem J 407, 303-11
17635105   Curated Info

4

Ando H, et al. (2006) IRBIT suppresses IP3 receptor activity by competing with IP3 for the common binding site on the IP3 receptor. Mol Cell 22, 795-806
16793548   Curated Info