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Site Information |
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sNVsstGsIDMVDsP SwissProt Entrez-Gene |
Blast this site against: NCBI SwissProt PDB |
Site Group ID: 454127 |
In vivo Characterization | |
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References | |
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Ferrer I, et al. (2022) Dysregulated Brain Protein Phosphorylation Linked to Increased Human Tau Expression in the hTau Transgenic Mouse Model. Int J Mol Sci 23
35742871 Curated Info |
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Tugaeva KV, Tsvetkov PO, Sluchanko NN (2017) Bacterial co-expression of human Tau protein with protein kinase A and 14-3-3 for studies of 14-3-3/phospho-Tau interaction. PLoS One 12, e0178933
28575131 Curated Info |
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Hanger DP, et al. (2007) Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis. J Biol Chem 282, 23645-54
17562708 Curated Info |
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Sato S, Cerny RL, Buescher JL, Ikezu T (2006) Tau-tubulin kinase 1 (TTBK1), a neuron-specific tau kinase candidate, is involved in tau phosphorylation and aggregation. J Neurochem 98, 1573-84
16923168 Curated Info |
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Yamamoto H, et al. (2005) Phosphorylation of tau at serine 416 by Ca2+/calmodulin-dependent protein kinase II in neuronal soma in brain. J Neurochem 94, 1438-47
16000144 Curated Info |
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Schneider A, et al. (1999) Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. Biochemistry 38, 3549-58
10090741 Curated Info |
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Hanger DP, et al. (1998) New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry. J Neurochem 71, 2465-76
9832145 Curated Info |