Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Curated Information Page
PubMed Id: 22608923 
Min SH, et al. (2012) Negative regulation of the stability and tumor suppressor function of fbw7 by the pin1 prolyl isomerase. Mol Cell 46, 771-83 22608923
This page summarizes selected information from the record 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.
Download Sites

T205-p - FBXW7 (human)
Orthologous residues
FBXW7 (human): T205‑p, FBXW7 iso2 (human): T125‑p, FBXW7 (mouse): T127‑p, FBXW7 iso3 (mouse): T208‑p
 Methods used to characterize site in vivo immunoprecipitation, mutation of modification site
 Disease tissue studied:  colorectal cancer, colorectal carcinoma
 Relevant cell lines - cell types - tissues:  293T (epithelial), HCT116 (intestinal)
 Cellular systems studied:  cell lines
 Species studied:  human
Downstream Regulation
 Effect of modification (function):  molecular association, regulation, protein degradation, ubiquitination
 Effect of modification (process):  carcinogenesis, induced, cell growth, induced
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
PIN1 (human) Induces pull-down assay
 Comments:  Pin1 disrupts FBXW7 dimerization.

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.