Thr306
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Home > Phosphorylation Site Page: > Thr306  -  CAMK2A (human)

Site Information
LkGAILttMLAtRNF   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 449596

In vivo Characterization
Methods used to characterize site in vivo:
mass spectrometry ( 3 , 5 ) , mutation of modification site ( 2 , 7 ) , phospho-antibody ( 2 ) , western blotting ( 2 )
Disease tissue studied:
lung cancer ( 3 )
Relevant cell line - cell type - tissue:
293 (epithelial) ( 2 , 7 ) , A549 (pulmonary) ( 3 ) , HCT116 (intestinal) ( 5 ) , MV4-11 (macrophage) ( 5 ) , neuron-'brain, hippocampus' ( 7 )

Upstream Regulation
Kinases, in vitro:
CAMK2A (human) ( 6 )

Downstream Regulation
Effects of modification on CAMK2A:
intracellular localization ( 7 ) , molecular association, regulation ( 2 )
Inhibit interaction with:
NMDAR2B (human) ( 2 )

References 

1

Shiromizu T, et al. (2013) Identification of missing proteins in the neXtProt database and unregistered phosphopeptides in the PhosphoSitePlus database as part of the Chromosome-centric Human Proteome Project. J Proteome Res 12, 2414-21
23312004   Curated Info

2

O'Leary H, et al. (2011) Nucleotides and Phosphorylation Bi-directionally Modulate Ca2+/Calmodulin-dependent Protein Kinase II (CaMKII) Binding to the N-Methyl-D-aspartate (NMDA) Receptor Subunit GluN2B. J Biol Chem 286, 31272-81
21768120   Curated Info

3

Yu G, et al. (2011) Phosphoproteome profile of human lung cancer cell line A549. Mol Biosyst 7, 472-9
21060948   Curated Info

4

Coultrap SJ, et al. (2010) CaMKII autonomy is substrate-dependent and further stimulated by Ca2+/calmodulin. J Biol Chem 285, 17930-7
20353941   Curated Info

5

Oppermann FS, et al. (2009) Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics 8, 1751-64
19369195   Curated Info

6

Robison AJ, Winder DG, Colbran RJ, Bartlett RK (2007) Oxidation of calmodulin alters activation and regulation of CaMKII. Biochem Biophys Res Commun 356, 97-101
17343827   Curated Info

7

Bayer KU, et al. (2006) Transition from reversible to persistent binding of CaMKII to postsynaptic sites and NR2B. J Neurosci 26, 1164-74
16436603   Curated Info