Ser106
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Home > Phosphorylation Site Page: > Ser106  -  CAPZA1 (human)

Site Information
DHLRkEAsDPQPEEA   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 27445584

In vivo Characterization
Methods used to characterize site in vivo:
mass spectrometry ( 1 , 2 , 3 , 5 ) , mass spectrometry (in vitro) ( 1 ) , mutation of modification site ( 1 )
Disease tissue studied:
HER2 positive breast cancer ( 2 ) , luminal A breast cancer ( 2 ) , luminal B breast cancer ( 2 ) , breast cancer, triple negative ( 2 ) , prostate cancer ( 1 )
Relevant cell line - cell type - tissue:

Upstream Regulation
Putative in vivo kinases:
Pim1 (human) ( 1 )
Kinases, in vitro:
Pim1 (human) ( 1 )
Treatments:
AZD1208 ( 1 ) , SGI-1776 ( 1 )

Downstream Regulation
Effects of modification on biological processes:
cell adhesion, induced ( 1 ) , cell motility, induced ( 1 ) , cytoskeletal reorganization ( 1 )

References 

1

Santio NM, et al. (2020) PIM1 accelerates prostate cancer cell motility by phosphorylating actin capping proteins. Cell Commun Signal 18, 121
32771000   Curated Info

2

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

3

Sharma K, et al. (2014) Ultradeep human phosphoproteome reveals a distinct regulatory nature of Tyr and Ser/Thr-based signaling. Cell Rep 8, 1583-94
25159151   Curated Info

4

Shiromizu T, et al. (2013) Identification of missing proteins in the neXtProt database and unregistered phosphopeptides in the PhosphoSitePlus database as part of the Chromosome-centric Human Proteome Project. J Proteome Res 12, 2414-21
23312004   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