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: 17358057 
Zöllner A, Pasquinelli MA, Bernhardt R, Beratan DN (2007) Protein phosphorylation and intermolecular electron transfer: a joint experimental and computational study of a hormone biosynthesis pathway. J Am Chem Soc 129, 4206-16 17358057
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

T129-p - adrenodoxin (cow)
Orthologous residues
adrenodoxin (human): T131‑p, adrenodoxin (mouse): T135‑p, adrenodoxin (rat): T135‑p, adrenodoxin (cow): T129‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CK2A1 (human)
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
CYP11A1 (cow) Induces 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.