Ser593
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Home > Phosphorylation Site Page: > Ser593  -  TNRC15 (human)

Site Information
MWGRVPFsPGPAPPP   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 3203298

In vivo Characterization
Methods used to characterize site in vivo:
labeling using "Shokat-modified" upstream kinase ( 14 ) , mass spectrometry ( 1 , 2 , 3 , 4 , 5 , 6 , 8 , 10 , 11 , 12 , 13 , 15 ) , mass spectrometry (in vitro) ( 14 )
Disease tissue studied:
breast cancer ( 5 ) , breast ductal carcinoma ( 5 ) , HER2 positive breast cancer ( 1 ) , luminal A breast cancer ( 1 ) , luminal B breast cancer ( 1 ) , breast cancer, triple negative ( 1 ) , cervical cancer ( 13 ) , cervical adenocarcinoma ( 13 ) , lung cancer ( 3 ) , non-small cell lung adenocarcinoma ( 3 ) , ovarian cancer ( 5 ) , melanoma skin cancer ( 2 )
Relevant cell line - cell type - tissue:

Upstream Regulation
Kinases, in vitro:
CDK2 (human) ( 14 )
Treatments:
ischemia ( 5 ) , nocodazole ( 13 ) , selumetinib ( 2 ) , vemurafenib ( 2 )

References 

1

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

2

Stuart SA, et al. (2015) A Phosphoproteomic Comparison of B-RAFV600E and MKK1/2 Inhibitors in Melanoma Cells. Mol Cell Proteomics 14, 1599-615
25850435   Curated Info

3

Tsai CF, et al. (2015) Large-scale determination of absolute phosphorylation stoichiometries in human cells by motif-targeting quantitative proteomics. Nat Commun 6, 6622
25814448   Curated Info

4

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

5

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

6

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

7

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

8

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

9

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

10

Grosstessner-Hain K, et al. (2011) Quantitative phospho-proteomics to investigate the polo-like kinase 1-dependent phospho-proteome. Mol Cell Proteomics 10, M111.008540
21857030   Curated Info

11

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

12

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

13

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

14

Chi Y, et al. (2008) Identification of CDK2 substrates in human cell lysates. Genome Biol 9, R149
18847512   Curated Info

15

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