Ser180
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Home > Phosphorylation Site Page: > Ser180  -  PRPS1 (human)

Site Information
GGAkRVTsIADrLNV   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 18014261

In vivo Characterization
Methods used to characterize site in vivo:
immunoprecipitation ( 1 ) , mass spectrometry ( 1 , 3 , 4 , 5 ) , mutation of modification site ( 1 ) , phospho-antibody ( 1 ) , western blotting ( 1 )
Disease tissue studied:
brain cancer ( 1 ) , glioblastoma ( 1 ) , glioma ( 1 ) , breast cancer ( 1 ) , cervical cancer ( 5 ) , cervical adenocarcinoma ( 5 ) , liver cancer ( 1 ) , hepatocellular carcinoma ( 1 ) , lung cancer ( 1 ) , non-small cell lung cancer ( 1 ) , non-small cell lung adenocarcinoma ( 1 ) , pancreatic cancer ( 1 ) , pancreatic carcinoma ( 1 )
Relevant cell line - cell type - tissue:

Upstream Regulation
Putative in vivo kinases:
AMPKA1 (human) ( 1 )
Kinases, in vitro:
AMPKA1 (human) ( 1 )
Treatments:
compound_C ( 1 ) , hypoxia ( 1 )

Downstream Regulation
Effects of modification on PRPS1:
activity, inhibited ( 1 ) , protein conformation ( 1 )
Effects of modification on biological processes:
cell growth, inhibited ( 1 )

References 

1

Qian X, et al. (2018) Conversion of PRPS Hexamer to Monomer by AMPK-Mediated Phosphorylation Inhibits Nucleotide Synthesis in Response to Energy Stress. Cancer Discov 8, 94-107
29074724   Curated Info

2

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

3

Santamaria A, et al. (2011) The Plk1-dependent phosphoproteome of the early mitotic spindle. Mol Cell Proteomics 10, M110.004457
20860994   Curated Info

4

Zhao X, et al. (2011) Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes. Mol Cell Proteomics 10, M110.000299
20833797   Curated Info

5

Olsen JV, et al. (2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal 3, ra3
20068231   Curated Info