Curated Information
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Home > Curated Information Page > PubMed Id: 28334491
Chiki A, et al. (2017) Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6. Angew Chem Int Ed Engl 56, 5202-5207 28334491
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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T3-p - Huntingtin (human)
Modsite: _____MAtLEkLMkA SwissProt Entrez-Gene
Orthologous residues
Huntingtin (human): T3‑p, Huntingtin (mouse): T3‑p, Huntingtin (rat):
Downstream Regulation
Effect of modification (function):  protein conformation, protein stabilization
Comments:  inhibits aggregation

K6-ac - Huntingtin (human)
Modsite: __MAtLEkLMkAFEs SwissProt Entrez-Gene
Orthologous residues
Huntingtin (human): K6‑ac, Huntingtin (mouse): K6‑ac, Huntingtin (rat):
Downstream Regulation
Effect of modification (function):  protein conformation, protein stabilization
Comments:  reverses inhibitory effect of T3 phosphorylation on aggregation

K9-ac - Huntingtin (human)
Modsite: AtLEkLMkAFEsLks SwissProt Entrez-Gene
Orthologous residues
Huntingtin (human): K9‑ac, Huntingtin (mouse): K9‑ac, Huntingtin (rat): K2‑ac

K15-ac - Huntingtin (human)
Modsite: MkAFEsLksFQQQQQ SwissProt Entrez-Gene
Orthologous residues
Huntingtin (human): K15‑ac, Huntingtin (mouse): K15‑ac, Huntingtin (rat): K8‑ac