Ser308
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Home > Phosphorylation Site Page: > Ser308  -  DAPK1 (mouse)

Site Information
ARKKWKQsVRLISLC   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 448142

In vivo Characterization
Methods used to characterize site in vivo:
electrophoretic mobility shift ( 7 ) , immunoprecipitation ( 6 ) , mass spectrometry ( 2 , 4 ) , mutation of modification site ( 1 , 8 , 9 ) , phospho-antibody ( 5 , 6 , 7 , 8 , 9 ) , western blotting ( 1 , 5 , 6 , 7 , 8 , 9 )
Relevant cell line - cell type - tissue:
'3T3-L1, differentiated' (adipocyte) ( 2 ) , 'brain, hippocampus' ( 1 ) , 'kidney, tubule, proximal' ( 6 ) , 'neuron, cortical' ( 5 ) , 293 (epithelial) ( 1 , 7 ) , HEK293T (epithelial) ( 6 , 9 ) , HeLa (cervical) ( 7 , 8 , 9 ) , liver ( 4 ) , liver [leptin (mouse), homozygous knockout] ( 4 ) , MEF (fibroblast) ( 6 , 9 )

Upstream Regulation
Regulatory protein:
UNC5B (mouse) ( 9 )
Putative in vivo kinases:
DAPK1 (mouse) ( 5 , 9 )
Kinases, in vitro:
DAPK1 (human) ( 9 )
Putative upstream phosphatases:
PPP2CA (human) ( 6 )
Phosphatases, in vitro:
PPP2CA (human) ( 6 )
Treatments:
calyculin_A ( 6 ) , ciclosporin ( 6 ) , deoxygenation ( 5 ) , geldanamycin ( 7 ) , glycine ( 5 ) , ionomycin ( 6 ) , netrin-1 ( 9 ) , NMDA ( 5 ) , okadaic_acid ( 6 ) , tunicamycin ( 6 )

Downstream Regulation
Effects of modification on DAPK1:
enzymatic activity, inhibited ( 5 , 6 , 7 , 8 , 9 ) , molecular association, regulation ( 1 , 7 , 8 ) , protein degradation ( 7 )
Effects of modification on biological processes:
apoptosis, altered ( 6 , 9 ) , apoptosis, induced ( 8 )
Inhibit interaction with:
CHIP (human) ( 7 ) , Calmodulin (human) ( 8 ) , MIB1 (human) ( 7 ) , NMDAR2B (human) ( 1 )

References 

1

Goodell DJ, et al. (2017) DAPK1 Mediates LTD by Making CaMKII/GluN2B Binding LTP Specific. Cell Rep 19, 2231-2243
28614711   Curated Info

2

Parker BL, et al. (2015) Targeted phosphoproteomics of insulin signaling using data-independent acquisition mass spectrometry. Sci Signal 8, rs6
26060331   Curated Info

3

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

4

Grimsrud PA, et al. (2012) A quantitative map of the liver mitochondrial phosphoproteome reveals posttranslational control of ketogenesis. Cell Metab 16, 672-83
23140645   Curated Info

5

Tu W, et al. (2010) DAPK1 interaction with NMDA receptor NR2B subunits mediates brain damage in stroke. Cell 140, 222-34
20141836   Curated Info

6

Gozuacik D, et al. (2008) DAP-kinase is a mediator of endoplasmic reticulum stress-induced caspase activation and autophagic cell death. Cell Death Differ 15, 1875-86
18806755   Curated Info

7

Zhang L, Nephew KP, Gallagher PJ (2007) Regulation of death-associated protein kinase. Stabilization by HSP90 heterocomplexes. J Biol Chem 282, 11795-804
17324930   Curated Info

8

Jin Y, Blue EK, Gallagher PJ (2006) Control of death-associated protein kinase (DAPK) activity by phosphorylation and proteasomal degradation. J Biol Chem 281, 39033-40
17056602   Curated Info

9

Llambi F, et al. (2005) The dependence receptor UNC5H2 mediates apoptosis through DAP-kinase. EMBO J 24, 1192-201
15729359   Curated Info