Curated Information
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Curated Information Page
PubMed Id: 15809304 
Rangone H, et al. (2005) Phosphorylation of arfaptin 2 at Ser260 by Akt Inhibits PolyQ-huntingtin-induced toxicity by rescuing proteasome impairment. J Biol Chem 280, 22021-8 15809304
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, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
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S260-p - arfaptin 2 (human)
Orthologous residues
arfaptin 2 (human): S260‑p, arfaptin 2 (mouse): S260‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  'neuron, cortical'-brain, 293 (epithelial) [arfaptin 2 (human)], 293T (epithelial), NG108-15 (neuron) [arfaptin 2 (human)]
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human, rat
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (human) transfection of wild-type enzyme
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Comments:  phosphorylation of site by Akt1 has a neuroprotective effect in Huntington's disease.


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