Curated Information
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Curated Information Page
PubMed Id: 10087064 
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.
Makhinson M, Chotiner JK, Watson JB, O'Dell TJ (1999) Adenylyl cyclase activation modulates activity-dependent changes in synaptic strength and Ca2+/calmodulin-dependent kinase II autophosphorylation. J Neurosci 19, 2500-10 10087064
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T286-p - CAMK2A (mouse)
Orthologous residues
CAMK2A (human): T286‑p, CAMK2A iso2 (human): T286‑p, CAMK2A (mouse): T286‑p, CAMK2A iso2 (mouse): , CAMK2A (rat): T286‑p
Characterization
 Methods used to characterize site in vivo phospho-antibody
 Relevant cell lines - cell types - tissues:  'brain, hippocampus'
 Cellular systems studied:  tissue
 Species studied:  mouse
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CAMK2A (mouse) pharmacological activator of upstream enzyme, antisense inhibition of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
Ca(2+) increase
electrical stimulation increase
forskolin increase
calyculin A increase
APV no change compared to control
isoproterenol no change compared to control


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