Ser1040
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Home > Phosphorylation Site Page: > Ser1040  -  SSFA2 (human)

Site Information
LRAVRMPsPFRSSAL   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 4769725

In vivo Characterization
Methods used to characterize site in vivo:
mass spectrometry ( 1 , 2 , 4 , 6 , 7 , 8 )
Disease tissue studied:
breast cancer ( 1 ) , breast ductal carcinoma ( 1 ) , breast cancer, triple negative ( 1 ) , cervical cancer ( 8 ) , cervical adenocarcinoma ( 8 )
Relevant cell line - cell type - tissue:
breast ( 1 ) , HeLa (cervical) ( 4 , 7 ) , HeLa S3 (cervical) ( 6 , 8 ) , liver ( 2 )

Upstream Regulation
Treatments:
ischemia ( 1 ) , nocodazole ( 8 )

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

Bian Y, et al. (2014) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics 96, 253-62
24275569   Curated Info

3

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

4

Zhou H, et al. (2013) Toward a comprehensive characterization of a human cancer cell phosphoproteome. J Proteome Res 12, 260-71
23186163   Curated Info

5

Beli P, et al. (2012) Proteomic Investigations Reveal a Role for RNA Processing Factor THRAP3 in the DNA Damage Response. Mol Cell 46, 212-25
22424773   Curated Info

6

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

7

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

8

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