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: 11784863 
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.
Crosio C, et al. (2002) Mitotic phosphorylation of histone H3: spatio-temporal regulation by mammalian Aurora kinases. Mol Cell Biol 22, 874-85 11784863
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 mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  293 (epithelial), 3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout], HeLa (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE AurA (human)
KINASE AurC (human)
KINASE AurB (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE AurA (human) transfection of wild-type enzyme, co-immunoprecipitation, transfection of inactive enzyme
KINASE AurB (human) transfection of wild-type enzyme, co-immunoprecipitation, transfection of inactive enzyme
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Effect of modification (process):  cell cycle regulation


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.