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Site Information |
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KGFRRAVsELDAKQA SwissProt Entrez-Gene |
Blast this site against: NCBI SwissProt PDB |
Site Group ID: 448542 |
In vivo Characterization | |
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Methods used to characterize site in vivo: | |
Disease tissue studied: | |
Relevant cell line - cell type - tissue: |
Upstream Regulation | |
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Phosphatases, in vitro: | |
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Downstream Regulation | |
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Effects of modification on TH: | |
Induce interaction with: |
References | |
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Won SY, et al. (2021) cAMP Response Element Binding-Protein- and Phosphorylation-Dependent Regulation of Tyrosine Hydroxylase by PAK4: Implications for Dopamine Replacement Therapy. Mol Cells 44, 493-499
34238765 Curated Info |
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Waløen K, et al. (2021) . Mol Pharmacol
34031189 Curated Info |
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Skjevik AA, et al. (2014) The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes. J Mol Biol 426, 150-68
24055376 Curated Info |
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Shiromizu T, et al. (2013) Identification of missing proteins in the neXtProt database and unregistered phosphopeptides in the PhosphoSitePlus database as part of the Chromosome-centric Human Proteome Project. J Proteome Res 12, 2414-21
23312004 Curated Info |
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DeNardo BD, et al. (2013) Quantitative phosphoproteomic analysis identifies activation of the RET and IGF-1R/IR signaling pathways in neuroblastoma. PLoS One 8, e82513
24349301 Curated Info |
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Kobori N, Moore AN, Dash PK (2006) GDNF abates serum deprivation-induced tyrosine hydroxylase Ser19 phosphorylation and activity. Brain Res 1086, 142-51
16626642 Curated Info |
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Kleppe R, Toska K, Haavik J (2001) Interaction of phosphorylated tyrosine hydroxylase with 14-3-3 proteins: evidence for a phosphoserine 40-dependent association. J Neurochem 77, 1097-107
11359875 Curated Info |
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Sutherland C, et al. (1993) Phosphorylation and activation of human tyrosine hydroxylase in vitro by mitogen-activated protein (MAP) kinase and MAP-kinase-activated kinases 1 and 2. Eur J Biochem 217, 715-22
7901013 Curated Info |
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Le Bourdellès B, et al. (1991) Phosphorylation of human recombinant tyrosine hydroxylase isoforms 1 and 2: an additional phosphorylated residue in isoform 2, generated through alternative splicing. J Biol Chem 266, 17124-30
1680128 Curated Info |