Ser153
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Home > Phosphorylation Site Page: > Ser153  -  p21Cip1 (human)

Site Information
sMTDFyHskRrLIFS   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 456134

In vivo Characterization
Methods used to characterize site in vivo:
2D analysis ( 2 ) , [32P] bio-synthetic labeling ( 3 ) , microscopy-colocalization with upstream kinase ( 2 ) , mutation of modification site ( 2 , 3 ) , phospho-antibody ( 2 )
Relevant cell line - cell type - tissue:

Upstream Regulation
Putative in vivo kinases:
DYRK1B (human) ( 3 ) , PKCA (human) ( 2 )
Kinases, in vitro:
DYRK1B (human) ( 3 ) , PKCA (human) ( 2 )
Treatments:
phorbol_ester ( 2 ) , SB203580 ( 3 )

Downstream Regulation
Effects of modification on p21Cip1:
intracellular localization ( 2 , 3 ) , molecular association, regulation ( 2 )
Inhibit interaction with:
Calmodulin (human) ( 2 )

References 

1

Mertins P, et al. (2014) Ischemia in tumors induces early and sustained phosphorylation changes in stress kinase pathways but does not affect global protein levels. Mol Cell Proteomics 13, 1690-704
24719451   Curated Info

2

Rodríguez-Vilarrupla A, et al. (2005) Binding of calmodulin to the carboxy-terminal region of p21 induces nuclear accumulation via inhibition of protein kinase C-mediated phosphorylation of Ser153. Mol Cell Biol 25, 7364-74
16055744   Curated Info

3

Mercer SE, et al. (2005) Mirk/Dyrk1B mediates survival during the differentiation of C2C12 myoblasts. J Biol Chem 280, 25788-801
15851482   Curated Info