Ser662
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Home > Phosphorylation Site Page: > Ser662  -  PKCD (mouse)

Site Information
QEAFHGFsFVNPKFE   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 447580

In vivo Characterization
Methods used to characterize site in vivo:
mass spectrometry ( 1 , 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 , 21 , 22 , 23 , 24 , 25 ) , mutation of modification site ( 26 ) , phospho-antibody ( 26 , 27 ) , phosphoamino acid analysis ( 28 ) , western blotting ( 26 , 28 )
Disease tissue studied:
bladder cancer ( 28 ) , leukemia ( 12 ) , acute myelogenous leukemia ( 12 ) , melanoma skin cancer ( 21 )
Relevant cell line - cell type - tissue:
'3T3-L1, differentiated' (adipocyte) ( 4 , 8 ) , 'brain, embryonic' ( 24 ) , 293 (epithelial) ( 27 , 28 ) , 32Dcl3 (myeloid) [FLT3 (mouse), transfection, chimera with human FLT3-ITD mutant (corresponding to wild type P36888 ( 18 ) , 32Dcl3 (myeloid) ( 18 ) , blood ( 12 ) , brain ( 13 , 14 , 15 , 17 , 19 , 25 ) , embryo ( 14 ) , heart ( 9 ) , Hepa 1-6 (epithelial) ( 22 ) , HL-1 (myocyte) [Akt1 (mouse), knockdown, stable lentiviral expression of Akt1 shRNA] ( 5 ) , HL-1 (myocyte) [Akt2 (mouse), knockdown, stable lentiviral expression of Akt2 shRNA] ( 5 ) , HL-1 (myocyte) ( 5 ) , kidney ( 15 ) , L929 (fibroblast) ( 26 ) , liver ( 1 , 7 , 11 , 14 ) , liver [leptin (mouse), homozygous knockout] ( 11 ) , lung ( 15 ) , macrophage-bone marrow ( 16 ) , macrophage-bone marrow [DUSP1 (mouse), homozygous knockout] ( 16 ) , macrophage-peritoneum [MPRIP (mouse), homozygous knockout] ( 10 ) , MC3T3-E1 (preosteoblast) ( 3 ) , RAW 267.4 (macrophage) ( 20 ) , skin [mGluR1 (mouse), transgenic, TG mutant mice] ( 21 ) , spleen ( 15 ) , stromal ( 6 ) , UMUC3 (bladder cell) ( 28 )

Upstream Regulation
Treatments:
cell_adhesion ( 28 ) , collagen_IV ( 27 ) , fibronectin ( 27 ) , H2O2 ( 26 ) , ischemia ( 6 ) , LY294002 ( 28 ) , serum ( 28 )

Downstream Regulation
Effects of modification on PKCD:
intracellular localization ( 26 )

References 

1

Robles MS, Humphrey SJ, Mann M (2017) Phosphorylation Is a Central Mechanism for Circadian Control of Metabolism and Physiology. Cell Metab 25, 118-127
27818261   Curated Info

2

Sacco F, et al. (2016) Glucose-regulated and drug-perturbed phosphoproteome reveals molecular mechanisms controlling insulin secretion. Nat Commun 7, 13250
27841257   Curated Info

3

Williams GR, et al. (2016) Exploring G protein-coupled receptor signaling networks using SILAC-based phosphoproteomics. Methods 92, 36-50
26160508   Curated Info

4

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

5

Reinartz M, Raupach A, Kaisers W, Gödecke A (2014) AKT1 and AKT2 induce distinct phosphorylation patterns in HL-1 cardiac myocytes. J Proteome Res 13, 4232-45
25162660   Curated Info

6

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

7

Wilson-Grady JT, Haas W, Gygi SP (2013) Quantitative comparison of the fasted and re-fed mouse liver phosphoproteomes using lower pH reductive dimethylation. Methods 61, 277-86
23567750   Curated Info

8

Humphrey SJ, et al. (2013) Dynamic Adipocyte Phosphoproteome Reveals that Akt Directly Regulates mTORC2. Cell Metab 17, 1009-20
23684622   Curated Info

9

Lundby A, et al. (2013) In vivo phosphoproteomics analysis reveals the cardiac targets of β-adrenergic receptor signaling. Sci Signal 6, rs11
23737553   Curated Info

10

Wu X, et al. (2012) Investigation of receptor interacting protein (RIP3)-dependent protein phosphorylation by quantitative phosphoproteomics. Mol Cell Proteomics 11, 1640-51
22942356   Curated Info

11

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

12

Trost M, et al. (2012) Posttranslational regulation of self-renewal capacity: insights from proteome and phosphoproteome analyses of stem cell leukemia. Blood 120, e17-27
22802335   Curated Info

13

Trinidad JC, et al. (2012) Global identification and characterization of both O-GlcNAcylation and phosphorylation at the murine synapse. Mol Cell Proteomics 11, 215-29
22645316   Curated Info

14

Stokes MP, et al. (2012) PTMScan Direct: Identification and Quantification of Peptides from Critical Signaling Proteins by Immunoaffinity Enrichment Coupled with LC-MS/MS. Mol Cell Proteomics 11, 187-201
22322096   Curated Info

15

Huttlin EL, et al. (2010) A tissue-specific atlas of mouse protein phosphorylation and expression. Cell 143, 1174-89
21183079   Curated Info

16

Weintz G, et al. (2010) The phosphoproteome of toll-like receptor-activated macrophages. Mol Syst Biol 6, 371
20531401   Curated Info

17

Wiśniewski JR, et al. (2010) Brain phosphoproteome obtained by a FASP-based method reveals plasma membrane protein topology. J Proteome Res 9, 3280-9
20415495   Curated Info

18

Choudhary C, et al. (2009) Mislocalized activation of oncogenic RTKs switches downstream signaling outcomes. Mol Cell 36, 326-39
19854140   Curated Info

19

Zhou J (2009) CST Curation Set: 7414; Year: 2009; Biosample/Treatment: tissue, brain/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: HXXp[ST]
Curated Info

20

Trost M, et al. (2009) The phagosomal proteome in interferon-gamma-activated macrophages. Immunity 30, 143-54
19144319   Curated Info

21

Zanivan S, et al. (2008) Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry. J Proteome Res 7, 5314-26
19367708   Curated Info

22

Pan C, Gnad F, Olsen JV, Mann M (2008) Quantitative phosphoproteome analysis of a mouse liver cell line reveals specificity of phosphatase inhibitors. Proteomics 8, 4534-46
18846507   Curated Info

23

Guo A (2007) CST Curation Set: 3502; Year: 2007; Biosample/Treatment: cell line, E5/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: (F/Y)p[ST] Antibodies Used to Purify Peptides prior to LCMS: Phospho-(Ser/Thr) PDK1 Docking Motif (18A2) Mouse mAb Cat#: 9634, PTMScan(R) Phospho-PDK1 Docking Motif (F/YS*/T*F/Y) Immunoaffinity Beads Cat#: 1992
Curated Info

24

Guo A (2007) CST Curation Set: 3120; Year: 2007; Biosample/Treatment: tissue, brain/-; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: (F/Y)p[ST] Antibodies Used to Purify Peptides prior to LCMS: Phospho-(Ser/Thr) PDK1 Docking Motif (18A2) Mouse mAb Cat#: 9634, PTMScan(R) Phospho-PDK1 Docking Motif (F/YS*/T*F/Y) Immunoaffinity Beads Cat#: 1992
Curated Info

25

Guo A (2007) CST Curation Set: 3121; Year: 2007; Biosample/Treatment: tissue, brain/-; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: (F/Y)p[ST] Antibodies Used to Purify Peptides prior to LCMS: Phospho-(Ser/Thr) PDK1 Docking Motif (18A2) Mouse mAb Cat#: 9634, PTMScan(R) Phospho-PDK1 Docking Motif (F/YS*/T*F/Y) Immunoaffinity Beads Cat#: 1992
Curated Info

26

Lee YJ, et al. (2005) HSP25 inhibits protein kinase C delta-mediated cell death through direct interaction. J Biol Chem 280, 18108-19
15731106   Curated Info

27

Ivaska J, Bosca L, Parker PJ (2003) PKCepsilon is a permissive link in integrin-dependent IFN-gamma signalling that facilitates JAK phosphorylation of STAT1. Nat Cell Biol 5, 363-9
12640464   Curated Info

28

Parekh DB, et al. (2000) Beta1-integrin and PTEN control the phosphorylation of protein kinase C. Biochem J 352 Pt 2, 425-33
11085936   Curated Info