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: 12151336 
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.
Li F, et al. (2002) p21-activated kinase 1 interacts with and phosphorylates histone H3 in breast cancer cells. EMBO Rep 3, 767-73 12151336
Download Sites

S11-p - H3 (human)
Orthologous residues
H3 (human): S11‑p, H3 (mouse): S11‑p, H3 iso2 (mouse): S11‑p, H3 iso3 (mouse): S11‑p, H3 (rat): S11‑p, H3 iso3 (rat): S11‑p, H3 (pig): S11‑p, H3 (chicken): S11‑p, H3 (cow): S11‑p
Characterization
 Methods used to characterize site in vivo phospho-antibody, western blotting
 Disease tissue studied:  breast cancer
 Relevant cell lines - cell types - tissues:  MCF-7 (breast cell)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PAK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PAK1 (human) co-immunoprecipitation, phospho-antibody, transfection of constitutively active enzyme, microscopy-colocalization


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.