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: 12783885 
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.
Haan S, et al. (2003) Tyrosine phosphorylation disrupts elongin interaction and accelerates SOCS3 degradation. J Biol Chem 278, 31972-9 12783885
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

Y204-p - SOCS3 (human)
Orthologous residues
SOCS3 (human): Y204‑p, SOCS3 (mouse): Y204‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  A431 (epithelial), B lymphocyte-spleen, COS (fibroblast), RAW 264 (macrophage)
 Cellular systems studied:  cell lines
 Species studied:  human, monkey, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Lck (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE JAK2 (human) transfection of wild-type enzyme, transfection of inactive enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
EGF increase
LPS increase
vanadate LPS augment treatment-induced increase
cycloheximide increase
vanadate cycloheximide augment treatment-induced increase
vanadate increase
Downstream Regulation
 Effect of modification (function):  molecular association, regulation, protein degradation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
TCEB1 (human) Disrupts in vitro

Y221-p - SOCS3 (human)
Orthologous residues
SOCS3 (human): Y221‑p, SOCS3 (mouse): Y221‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  A431 (epithelial), B lymphocyte-spleen, COS (fibroblast), RAW 264 (macrophage)
 Cellular systems studied:  cell lines
 Species studied:  human, monkey, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Lck (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE JAK2 (human) transfection of wild-type enzyme, transfection of inactive enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
EGF increase
LPS increase
vanadate LPS augment treatment-induced increase
cycloheximide increase
vanadate cycloheximide augment treatment-induced increase
vanadate increase
Downstream Regulation
 Effect of modification (function):  molecular association, regulation, protein degradation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
TCEB1 (human) Disrupts in vitro


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.