Ser554
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Home > Phosphorylation Site Page: > Ser554  -  Tau (mouse)

Site Information
NVRSkIGstENLKHQ   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 447930

In vivo Characterization
Methods used to characterize site in vivo:
immunoassay ( 11 ) , mass spectrometry ( 5 , 8 , 12 , 13 , 16 ) , phospho-antibody ( 1 , 2 , 3 , 4 , 6 , 7 , 9 , 11 , 14 , 15 , 18 , 19 ) , western blotting ( 1 , 2 , 3 , 4 , 7 , 9 , 11 , 14 , 15 , 18 )
Disease tissue studied:
neuroblastoma ( 2 , 4 , 9 )
Relevant cell line - cell type - tissue:
'brain, cerebral cortex' ( 1 , 2 , 7 ) , 'brain, embryonic' ( 16 ) , 'brain, hippocampus' ( 2 , 18 ) , 'brain, striatum' ( 11 ) , 'neuron, cerebellar granule'-brain ( 19 ) , 'neuron, cortical'-brain ( 6 ) , brain ( 3 , 8 , 12 , 14 , 15 ) , C2C12 (myoblast) ( 13 ) , heart ( 5 ) , MEF (fibroblast) [LKB1 (mouse), homozygous knockout] ( 17 ) , Neuro-2a (neuron) ( 4 , 9 ) , neuron-'brain, hippocampus' ( 1 ) , SK-N-BE(2) (neural crest) ( 2 )

Upstream Regulation
Regulatory protein:
Akt1 (mouse) ( 15 ) , CAMKK2 (mouse) ( 10 ) , CHIP (mouse) ( 15 ) , NMNAT2 (human) ( 7 ) , PAR1 (mouse) ( 15 ) , SNCA (mouse) ( 11 )
Putative in vivo kinases:
GSK3B (mouse) ( 11 )
Kinases, in vitro:
MARK2 (human) ( 17 )
Treatments:
aroused animals ( 14 ) , berberine ( 4 ) , beta-amyloid_42 ( 10 ) , calyculin_A ( 4 , 9 ) , clozapine ( 1 ) , cold_water_stress ( 18 ) , ether ( 18 ) , food deprivation ( 18 ) , glycosuria ( 6 ) , hibernating ( 14 ) , hyperglycemia ( 6 ) , hypothermia prone ( 6 ) , lactacystin ( 17 ) , melatonin ( 9 ) , MG132 ( 17 ) , okadaic_acid ( 7 ) , summer-active ( 14 )

Downstream Regulation
Effects of modification on Tau:
intracellular localization ( 11 ) , molecular association, regulation ( 11 ) , protein conformation ( 11 ) , protein degradation ( 17 )
Induce interaction with:
SNCA (mouse) ( 11 )

Disease / Diagnostics Relevance
Relevant diseases:
diabetes mellitus ( 6 ) , Parkinson's disease ( 3 , 11 )

References 

1

Choi Y, et al. (2017) Clozapine Improves Memory Impairment and Reduces Aβ Level in the Tg-APPswe/PS1dE9 Mouse Model of Alzheimer's Disease. Mol Neurobiol 54, 450-460
26742522   Curated Info

2

Lasagna-Reeves CA, et al. (2016) Reduction of Nuak1 Decreases Tau and Reverses Phenotypes in a Tauopathy Mouse Model. Neuron 92, 407-418
27720485   Curated Info

3

Credle JJ, et al. (2015) GSK-3β dysregulation contributes to parkinson's-like pathophysiology with associated region-specific phosphorylation and accumulation of tau and α-synuclein. Cell Death Differ 22, 838-51
25394490   Curated Info

4

Liu X, et al. (2014) Berberine attenuates axonal transport impairment and axonopathy induced by calyculin a in n2a cells. PLoS One 9, e93974
24713870   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

Papon MA, et al. (2013) Deregulation of protein phosphatase 2A and hyperphosphorylation of τ protein following onset of diabetes in NOD mice. Diabetes 62, 609-17
22961084   Curated Info

7

Cheng XS, et al. (2013) Nmnat2 attenuates Tau phosphorylation through activation of PP2A. J Alzheimers Dis 36, 185-95
23579329   Curated Info

8

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

9

Xiong YF, et al. (2011) Melatonin reduces the impairment of axonal transport and axonopathy induced by calyculin A. J Pineal Res 50, 319-27
21244478   Curated Info

10

Thornton C, et al. (2011) AMP-activated protein kinase (AMPK) is a tau kinase, activated in response to amyloid β-peptide exposure. Biochem J 434, 503-12
21204788   Curated Info

11

Wills J, et al. (2011) Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease. PLoS One 6, e17953
21445308   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

Guo A (2009) CST Curation Set: 6165; Year: 2009; Biosample/Treatment: cell line, C2C12/control; 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

14

Su B, et al. (2008) Physiological regulation of tau phosphorylation during hibernation. J Neurochem 105, 2098-108
18284615   Curated Info

15

Dickey CA, et al. (2008) Akt and CHIP coregulate tau degradation through coordinated interactions. Proc Natl Acad Sci U S A 105, 3622-7
18292230   Curated Info

16

Possemato A (2008) CST Curation Set: 3824; Year: 2008; 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

17

Kojima Y, et al. (2007) Suppression of tubulin polymerization by the LKB1-microtubule-associated protein/microtubule affinity-regulating kinase signaling. J Biol Chem 282, 23532-40
17573348   Curated Info

18

Ikeda Y, Ishiguro K, Fujita SC (2007) Ether stress-induced Alzheimer-like tau phosphorylation in the normal mouse brain. FEBS Lett 581, 891-7
17289030   Curated Info

19

Cheng CM, et al. (2005) Tau is hyperphosphorylated in the insulin-like growth factor-I null brain. Endocrinology 146, 5086-91
16123158   Curated Info