Ser85
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Home > Phosphorylation Site Page: > Ser85  -  EME1 (human)

Site Information
QPVRLLssEsEDEEE   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 453523

In vivo Characterization
Methods used to characterize site in vivo:
mass spectrometry ( 1 , 2 , 3 , 5 , 6 , 7 , 8 , 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 )
Disease tissue studied:
breast cancer ( 1 ) , cervical cancer ( 9 ) , cervical adenocarcinoma ( 9 ) , leukemia ( 5 ) , acute myelogenous leukemia ( 5 ) , lung cancer ( 2 ) , non-small cell lung cancer ( 2 )
Relevant cell line - cell type - tissue:

References 

1

Yi T, et al. (2014) Quantitative phosphoproteomic analysis reveals system-wide signaling pathways downstream of SDF-1/CXCR4 in breast cancer stem cells. Proc Natl Acad Sci U S A 111, E2182-90
24782546   Curated Info

2

Klammer M, et al. (2012) Phosphosignature predicts dasatinib response in non-small cell lung cancer. Mol Cell Proteomics 11, 651-68
22617229   Curated Info

3

Franz-Wachtel M, et al. (2012) Global detection of protein kinase D-dependent phosphorylation events in nocodazole-treated human cells. Mol Cell Proteomics 11, 160-70
22496350   Curated Info

4

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

5

Weber C, Schreiber TB, Daub H (2012) Dual phosphoproteomics and chemical proteomics analysis of erlotinib and gefitinib interference in acute myeloid leukemia cells. J Proteomics 75, 1343-56
22115753   Curated Info

6

Rigbolt KT, et al. (2011) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal 4, rs3
21406692   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

Christensen GL, et al. (2010) Quantitative phosphoproteomics dissection of seven-transmembrane receptor signaling using full and biased agonists. Mol Cell Proteomics 9, 1540-53
20363803   Curated Info

9

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

10

Pan C, Olsen JV, Daub H, Mann M (2009) Global effects of kinase inhibitors on signaling networks revealed by quantitative phosphoproteomics. Mol Cell Proteomics 8, 2796-808
19651622   Curated Info

11

Mayya V, et al. (2009) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal 2, ra46
19690332   Curated Info

12

Dephoure N, et al. (2008) A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A 105, 10762-7
18669648   Curated Info

13

Ruse CI, et al. (2008) Motif-specific sampling of phosphoproteomes. J Proteome Res 7, 2140-50
18452278   Curated Info

14

Olsen JV, et al. (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-48
17081983   Curated Info

15

Beausoleil SA, et al. (2004) Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A 101, 12130-5
15302935   Curated Info

16

MS This site is one of 509 sites observed by D. Stover et al using MS/FTMS of peptides from lysates of A431 cells grown either in vitro or as xenografts in BALB/c nu/nu mice. These sites were previously unpublished until now (July 27 2006). 66 sites were previously published in: Stover DR, et al. Differential phosphoprofiles of EGF and EGFR kinase inhibitor-treated human tumor cells and mouse xenografts Clin Proteomics 2004 Mar 01; 1(1): 69-80.
Curated Info