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: 11971983 
Nicolas G, et al. (2002) Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain. Mol Cell Biol 22, 3527-36 11971983
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

Y1176-p - SPTAN1 (rat)
Orthologous residues
SPTAN1 (human): Y1176‑p, SPTAN1 iso2 (human): Y1176‑p, SPTAN1 iso3 (human): Y1156‑p, SPTAN1 (mouse): Y1176‑p, SPTAN1 iso2 (mouse): Y1156‑p, SPTAN1 iso3 (mouse): Y1156‑p, SPTAN1 (rat): Y1176‑p
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  COS (fibroblast), RCCD1 (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  monkey, rat
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Lck (human)
KINASE Src (rat)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
vanadate 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.