Ser565
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Home > Phosphorylation Site Page: > Ser565  -  PML (human)

Site Information
VIsssEDsDAENSSS   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 2479600

In vivo Characterization
Methods used to characterize site in vivo:
[32P] bio-synthetic labeling ( 13 ) , mass spectrometry ( 1 , 3 , 4 , 6 , 7 , 8 , 9 , 10 , 11 ) , mutation of modification site ( 13 , 14 ) , phospho-antibody ( 14 ) , western blotting ( 13 , 14 )
Disease tissue studied:
breast cancer ( 3 ) , colorectal cancer ( 14 ) , colorectal carcinoma ( 14 ) , leukemia ( 6 ) , acute myelogenous leukemia ( 6 ) , lung cancer ( 4 ) , non-small cell lung cancer ( 4 ) , melanoma skin cancer ( 1 )
Relevant cell line - cell type - tissue:

Upstream Regulation
Putative in vivo kinases:
CK2A1 (human) ( 14 )
Kinases, in vitro:
CK2A1 (human) ( 13 , 14 )
Treatments:
osmotic_stress ( 14 ) , TBB ( 14 ) , UV ( 14 )

Downstream Regulation
Effects of modification on PML:
protein degradation ( 14 )
Effects of modification on biological processes:
apoptosis, inhibited ( 14 ) , cell growth, altered ( 14 )

References 

1

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

2

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

3

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

4

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

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

7

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

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

Bennetzen MV, et al. (2010) Site-specific phosphorylation dynamics of the nuclear proteome during the DNA damage response. Mol Cell Proteomics 9, 1314-23
20164059   Curated Info

10

Schreiber TB, et al. (2010) An integrated phosphoproteomics work flow reveals extensive network regulation in early lysophosphatidic acid signaling. Mol Cell Proteomics 9, 1047-62
20071362   Curated Info

11

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

12

Percherancier Y, et al. (2009) Role of SUMO in RNF4-mediated promyelocytic leukemia protein (PML) degradation: sumoylation of PML and phospho-switch control of its SUMO binding domain dissected in living cells. J Biol Chem 284, 16595-608
19380586   Curated Info

13

Stehmeier P, Muller S (2009) Phospho-regulated SUMO interaction modules connect the SUMO system to CK2 signaling. Mol Cell 33, 400-9
19217413   Curated Info

14

Scaglioni PP, et al. (2006) A CK2-dependent mechanism for degradation of the PML tumor suppressor. Cell 126, 269-83
16873060   Curated Info