Ser187
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Home > Phosphorylation Site Page: > Ser187  -  SMN (human)

Site Information
sDNIkPksAPWNsFL   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 9316349

In vivo Characterization
Methods used to characterize site in vivo:
mass spectrometry ( 1 , 2 , 3 , 5 ) , mass spectrometry (in vitro) ( 4 ) , mutation of modification site ( 4 )
Disease tissue studied:
breast cancer ( 2 ) , breast ductal carcinoma ( 2 ) , HER2 positive breast cancer ( 1 ) , luminal A breast cancer ( 1 ) , luminal B breast cancer ( 1 ) , breast cancer, triple negative ( 1 )
Relevant cell line - cell type - tissue:
breast ( 1 , 2 ) , COS7 (fibroblast) ( 4 ) , HeLa (cervical) ( 5 ) , Jurkat (T lymphocyte) ( 3 )

Upstream Regulation
Kinases, in vitro:
PKACA (human) ( 4 )
Treatments:
ischemia ( 2 )

Downstream Regulation
Effects of modification on SMN:
molecular association, regulation ( 4 )
Inhibit interaction with:
GEMIN8 (human) ( 4 ) , SIP1 (human) ( 4 )

References 

1

Mertins P, et al. (2016) Proteogenomics connects somatic mutations to signalling in breast cancer. Nature 534, 55-62
27251275   Curated Info

2

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

3

Mertins P, et al. (2013) Integrated proteomic analysis of post-translational modifications by serial enrichment. Nat Methods 10, 634-7
23749302   Curated Info

4

Wu CY, et al. (2011) Identification of the phosphorylation sites in the survival motor neuron protein by protein kinase A. Biochim Biophys Acta 1814, 1134-9
21609790   Curated Info

5

Kettenbach AN, et al. (2011) Quantitative phosphoproteomics identifies substrates and functional modules of aurora and polo-like kinase activities in mitotic cells. Sci Signal 4, rs5
21712546   Curated Info

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