Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
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
Download Sites

S454-p - ACLY (rat)
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


Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.