NP_033922.1
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
NCBI Official Full Name
calcium/calmodulin-dependent protein kinase type II subunit alpha isoform 1
NCBI Official Synonym Full Names
calcium/calmodulin-dependent protein kinase II alpha
NCBI Protein Information
calcium/calmodulin-dependent protein kinase type II subunit alpha; CaMK II; alpha-CaMKII; caMK-II subunit alpha; caM kinase II subunit alpha
UniProt Protein Name
Calcium/calmodulin-dependent protein kinase type II subunit alpha
UniProt Synonym Gene Names
UniProt Entry Name
KCC2A_MOUSE
UniProt Comments for Camk2a
CAMK2A: a protein kinase of the CAMK2 family. A prominent kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release. Member of the NMDAR signaling complex in excitatory synapses that may regulate NMDAR-dependent potentiation of the AMPAR and synaptic plasticity. The holoenzyme is composed of four different chains: alpha, beta, gamma, and delta. The different chains assemble into homo- or heteromultimeric holoenzymes composed of 8 to 12 subunits. May interact with BAALC, MPDZ, SYN1 and synGAP. 2 isoforms of the human protein are produced by alternative splicing.
Protein type: Protein kinase, CAMK; Kinase, protein; Protein kinase, Ser/Thr (non-receptor); EC 2.7.11.17; CAMK group; CAMK2 family
Cellular Component: dendrite cytoplasm; mitochondrion; cell soma; membrane; axon; postsynaptic density; dendrite; cytoplasm; plasma membrane; synapse; cell junction; nucleus
Molecular Function: glutamate receptor binding; protein homodimerization activity; calmodulin-dependent protein kinase activity; nucleotide binding; GTPase activating protein binding; protein kinase activity; transferase activity; calmodulin binding; protein serine/threonine kinase activity; protein binding; transferase activity, transferring phosphorus-containing groups; kinase activity; ATP binding
Biological Process: peptidyl-serine phosphorylation; ionotropic glutamate receptor signaling pathway; calcium ion transport; protein amino acid autophosphorylation; regulation of neurotransmitter secretion; positive regulation of calcium ion transport; phosphorylation; protein amino acid phosphorylation; regulation of neuronal synaptic plasticity; G1/S transition of mitotic cell cycle; activation of NF-kappaB transcription factor
Product References and Citations for anti-Camk2a antibody
1. Hughes K. et al. (2001) J. Biol. Chem. 276: 36008-36013. 2. Barria A. et al. (1997) Science 276: 2042-2045. 3. Bennet M.K. and Kennedy M.B. (1987) Proc. Natl. Acad. Sci. U.S.A. 84: 1794-1798. 4. Broke L., Srinivasan M. and Schulman H. (1995) J. Neurosci. 15: 6797-6808. 5. Nghiem P., Saati S. M., Martens C. L., Gardner P. and Schulman H. (1993) J. Biol. Chem. 268: 5471-5479. 6. Edman C.F. and Schulman H. (1994) Biochem. Biophys. Acta 1221: 90-102. 7. Tombes R.M. and Krystal G.W., (1997) Biochem. Biophys. Acta 13555: 281-292. 8. Means A.R. (2000) Mol. Endocrinol. 14: 4-12. 9. Makhinson M. et al. (1999) J. Neurosci. 19: 2500-2510. 10. Strack S. and Colbran R.J. (1998) J. Biol. Chem. 273: 20689-20692. 11. Leonard S.A., Lim I.A., Hemsworth D.E., Horne M.C. and Hell J.W. (1999) Proc. Natl. Acad. Sci. U.S.A. 96: 3239-3244. 12. Shen K. and Meyer Y. (1999) Science 284: 162-167. 1. Feng, T., Szabo, E., Dziak, E. and Opas, M. (2010). Cytoskeletal disassembly and cell rounding promotes adipogenesis from ES cells. Stem Cell Rev. 6 (1), 74-85. doi: 10.1007/s12015-010-9115-8.
Research Articles on Camk2a
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Pathways associated with anti-Camk2a antibody
Diseases associated with anti-Camk2a antibody
Organs/Tissues associated with anti-Camk2a antibody
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