Ser152
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Home > Phosphorylation Site Page: > Ser152  -  REEP1 (mouse)

Site Information
SERLRsFsMQDLTTI   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 454487

In vivo Characterization
Methods used to characterize site in vivo:
mass spectrometry ( 2 , 3 , 5 , 6 , 7 , 8 , 9 , 10 , 11 , 12 , 13 , 14 )
Relevant cell line - cell type - tissue:
'fat, brown' ( 10 ) , brain ( 6 , 7 , 10 , 11 , 12 , 14 ) , heart ( 5 , 10 ) , HL-1 (myocyte) [Akt1 (mouse), knockdown, stable lentiviral expression of Akt1 shRNA] ( 3 ) , HL-1 (myocyte) [Akt2 (mouse), knockdown, stable lentiviral expression of Akt2 shRNA] ( 3 ) , HL-1 (myocyte) ( 3 ) , kidney ( 10 ) , liver ( 13 ) , lung ( 10 ) , MEF (fibroblast) [p53 (mouse), homozygous knockout] ( 8 ) , MEF (fibroblast) [TSC2 (mouse), homozygous knockout] ( 9 ) , neuron:postsynaptic density-'brain, hippocampus, CA1 region' ( 2 ) , spleen ( 10 ) , testis ( 10 )

Upstream Regulation
Regulatory protein:
TSC2 (mouse) ( 8 )
Treatments:
Torin1 ( 8 )

References 

1

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

2

Li J, et al. (2016) Long-term potentiation modulates synaptic phosphorylation networks and reshapes the structure of the postsynaptic interactome. Sci Signal 9, rs8
27507650   Curated Info

3

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

4

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

5

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

6

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

7

Goswami T, et al. (2012) Comparative phosphoproteomic analysis of neonatal and adult murine brain. Proteomics 12, 2185-9
22807455   Curated Info

8

Hsu PP, et al. (2011) The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signaling. Science 332, 1317-22
21659604   Curated Info

9

Yu Y, et al. (2011) Phosphoproteomic analysis identifies Grb10 as an mTORC1 substrate that negatively regulates insulin signaling. Science 332, 1322-6
21659605   Curated Info

10

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

11

Possemato A (2010) CST Curation Set: 9877; Year: 2010; Biosample/Treatment: tissue, brain/untreated; Disease: -; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: RXXp[ST] Antibodies Used to Purify Peptides prior to LCMS: Phospho-Akt Substrate (RXRXXS/T) (110B7) Rabbit mAb Cat#: 9614, PTMScan(R) Phospho-Akt Substrate Motif (RXXS*/T*) Immunoaffinity Beads Cat#: 1978
Curated Info

12

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

13

Villén J, Beausoleil SA, Gerber SA, Gygi SP (2007) Large-scale phosphorylation analysis of mouse liver. Proc Natl Acad Sci U S A 104, 1488-93
17242355   Curated Info

14

Ballif BA, et al. (2004) Phosphoproteomic analysis of the developing mouse brain. Mol Cell Proteomics 3, 1093-101
15345747   Curated Info