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: 16177823 
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.
Hu Y, et al. (2005) Akt phosphorylates acinus and inhibits its proteolytic cleavage, preventing chromatin condensation. EMBO J 24, 3543-54 16177823
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
Download Sites

S1180-p - acinus (rat) ▲
Orthologous residues
acinus (human): S1180‑p, acinus (mouse): S1179‑p, acinus iso5 (mouse): S393‑p, acinus (rat): S1180‑p
Characterization
 Methods used to characterize site in vivo:  mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  293 (epithelial), PC-12 (chromaffin)
 Cellular systems studied:  cell lines
 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 (rat) transfection of inactive enzyme, pharmacological inhibitor of upstream enzyme, microscopy-colocalization, antisense inhibition of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
EGF increase
LY294002 EGF inhibit treatment-induced increase
NGF increase
wortmannin NGF inhibit treatment-induced increase
PD98059 NGF no effect upon treatment-induced increase
LY294002 NGF inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  protein stabilization
 Comments:  S1180 phosphorylation prevents proteolytic degradation of acinus and blocks chromatin condensation in vivo and in vitro

S1329-p - acinus (rat) ▲
Orthologous residues
acinus (human): S1331‑p, acinus (mouse): S1328‑p, acinus iso5 (mouse): S542‑p, acinus (rat): S1329‑p
Characterization
 Methods used to characterize site in vivo:  mutation of modification site
 Relevant cell lines - cell types - tissues:  PC-12 (chromaffin)
 Cellular systems studied:  cell lines
 Species studied:  rat
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE Akt1 (human)

S473-p - Akt1 (rat) ▲
Orthologous residues
Akt1 (human): S473‑p, Akt1 (mouse): S473‑p, Akt1 (rat): S473‑p, Akt1 (fruit fly): S586‑p, Akt1 (cow): S473‑p
Characterization
 Methods used to characterize site in vivo:  phospho-antibody
 Relevant cell lines - cell types - tissues:  PC-12 (chromaffin)
 Cellular systems studied:  cell lines
 Species studied:  rat
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
EGF increase
LY294002 EGF inhibit treatment-induced increase
NGF increase
wortmannin NGF inhibit treatment-induced increase
PD98059 NGF no effect upon treatment-induced increase
LY294002 NGF inhibit treatment-induced 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.