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: 8376365 
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.
Beretta L, Dobránsky T, Sobel A (1993) Multiple phosphorylation of stathmin. Identification of four sites phosphorylated in intact cells and in vitro by cyclic AMP-dependent protein kinase and p34cdc2. J Biol Chem 268, 20076-84 8376365
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

S16-p - STMN1 (mouse) ▲
Orthologous residues
STMN1 (human): S16‑p, STMN1 (mouse): S16‑p, STMN1 (rat): S16‑p, STMN1 (chicken): S16‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, peptide sequencing
 Cellular systems studied:  cell lines, tissue
 Species studied:  mouse, rat
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE PKACa (human)
 Comments:  PKC did not phosphorylate stathmin in vitro.Mouse brain
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
forskolin, phorbol ester increase
NGF increase

S25-p - STMN1 (mouse) ▲
Orthologous residues
STMN1 (human): S25‑p, STMN1 (mouse): S25‑p, STMN1 (rat): S25‑p, STMN1 (chicken): G25‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, peptide sequencing
 Cellular systems studied:  cell lines, tissue
 Species studied:  mouse, rat
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
forskolin, phorbol ester increase
NGF increase

S38-p - STMN1 (mouse) ▲
Orthologous residues
STMN1 (human): S38‑p, STMN1 (mouse): S38‑p, STMN1 (rat): S38‑p, STMN1 (chicken): S38‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, peptide sequencing
 Cellular systems studied:  cell lines, tissue
 Species studied:  mouse, rat
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
forskolin, phorbol ester increase
NGF increase

S63-p - STMN1 (mouse) ▲
Orthologous residues
STMN1 (human): S63‑p, STMN1 (mouse): S63‑p, STMN1 (rat): S63‑p, STMN1 (chicken): S63‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, peptide sequencing
 Cellular systems studied:  cell lines, tissue
 Species studied:  mouse, rat
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE PKACa (human)
 Comments:  PKC did not phosphorylate stathmin in vitro.Mouse brain
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
forskolin, phorbol ester 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.