Curated Information

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Curated Information Page

PubMed Id: 6286669

This page summarizes selected information from the article 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.

Pierce MW, et al. (1982) The insulin-directed phosphorylation site on ATP-citrate lyase is identical with the site phosphorylated by the cAMP-dependent protein kinase in vitro. J Biol Chem 257, 10681-6 6286669

S454-p - ACLY (rat)

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Orthologous residues

ACLY (human): S455‑p, ACLY iso3 (human): S65‑p, ACLY (mouse): S455‑p, ACLY iso2 (mouse): S455‑p, ACLY iso3 (mouse): S455‑p, ACLY (rat): S454‑p

Characterization

Methods used to characterize site in vivo: [32P] bio-synthetic labeling, peptide sequencing, phosphopeptide mapping

Relevant cell lines - cell types - tissues: hepatocyte-liver

Cellular systems studied: primary cultured cells

Species studied: rat

Upstream Regulation

Treatments, proteins and their effect on site modification:

Treatments	Referenced Treatments	Manipulated Protein	Referenced Protein	Effect	Notes
insulin				increase

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