CAMK2A

From Wikipedia, the free encyclopedia

Calcium/calmodulin-dependent protein kinase (CaM kinase) II alpha

PDB rendering based on 1hkx.

Available structures: 1hkx

Identifiers

Symbol(s)

CAMK2A; CAMKA; KIAA0968

External IDs

OMIM: 114078 MGI: 88256 HomoloGene: 56577

Gene ontology
Molecular Function:	• nucleotide binding • protein serine/threonine kinase activity • calmodulin binding • ATP binding • transferase activity
Cellular Component:	• calcium- and calmodulin-dependent protein kinase complex
Biological Process:	• protein amino acid phosphorylation • activation of NF-kappaB transcription factor

Orthologs

Human

Mouse

Refseq

NM_015981 (mRNA)
NP_057065 (protein)

NM_009792 (mRNA)
NP_033922 (protein)

Location

Chr 5: 149.58 - 149.65 Mb

Chr 18: 61.05 - 61.11 Mb

Pubmed search

[1]

[2]

Calcium/calmodulin-dependent protein kinase (CaM kinase) II alpha, also known as CAMK2A, is a human gene.

The product of this gene belongs to the Serine/Threonine protein kinases family, and to the Ca(2+)/calmodulin-dependent protein kinases subfamily. Calcium signaling is crucial for several aspects of plasticity at glutamatergic synapses. This enzyme is composed of four different chains: alpha, beta, gamma, and delta. The alpha chain encoded by this gene is required for hippocampal long-term potentiation (LTP) and spatial learning. In addition to its calcium-calmodulin (CaM)-dependent activity, this protein can undergo autophosphorylation, resulting in CaM-independent activity. Two transcript variants encoding distinct isoforms have been identified for this gene.^[1]

[edit] References

^ Entrez Gene: CAMK2A calcium/calmodulin-dependent protein kinase (CaM kinase) II alpha.

[edit] Further reading

Soderling TR (2000). "CaM-kinases: modulators of synaptic plasticity.". Curr. Opin. Neurobiol. 10 (3): 375–80. PMID 10851169.
Hook SS, Means AR (2001). "Ca(2+)/CaM-dependent kinases: from activation to function.". Annu. Rev. Pharmacol. Toxicol. 41: 471–505. doi:10.1146/annurev.pharmtox.41.1.471. PMID 11264466.
Yamamoto H (2002). "[Molecular mechanisms of the intracellular localizations of Ca2+/calmodulin-dependent protein kinase II isoforms, and their physiological functions]". Tanpakushitsu Kakusan Koso 47 (3): 241–7. PMID 11889801.
Countaway JL, Nairn AC, Davis RJ (1992). "Mechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase.". J. Biol. Chem. 267 (2): 1129–40. PMID 1309762.
Wegner M, Cao Z, Rosenfeld MG (1992). "Calcium-regulated phosphorylation within the leucine zipper of C/EBP beta.". Science 256 (5055): 370–3. PMID 1314426.
Omary MB, Baxter GT, Chou CF, et al. (1992). "PKC epsilon-related kinase associates with and phosphorylates cytokeratin 8 and 18.". J. Cell Biol. 117 (3): 583–93. PMID 1374067.
Bredt DS, Ferris CD, Snyder SH (1992). "Nitric oxide synthase regulatory sites. Phosphorylation by cyclic AMP-dependent protein kinase, protein kinase C, and calcium/calmodulin protein kinase; identification of flavin and calmodulin binding sites.". J. Biol. Chem. 267 (16): 10976–81. PMID 1375933.
Tokui T, Yamauchi T, Yano T, et al. (1990). "Ca2(+)-calmodulin-dependent protein kinase II phosphorylates various types of non-epithelial intermediate filament proteins.". Biochem. Biophys. Res. Commun. 169 (3): 896–904. PMID 2114109.
Inagaki M, Gonda Y, Nishizawa K, et al. (1990). "Phosphorylation sites linked to glial filament disassembly in vitro locate in a non-alpha-helical head domain.". J. Biol. Chem. 265 (8): 4722–9. PMID 2155236.
Ohta Y, Ohba T, Miyamoto E (1990). "Ca2+/calmodulin-dependent protein kinase II: localization in the interphase nucleus and the mitotic apparatus of mammalian cells.". Proc. Natl. Acad. Sci. U.S.A. 87 (14): 5341–5. PMID 2164678.
Lee RH, Brown BM, Lolley RN (1990). "Protein kinase A phosphorylates retinal phosducin on serine 73 in situ.". J. Biol. Chem. 265 (26): 15860–6. PMID 2394752.
Lin CR, Kapiloff MS, Durgerian S, et al. (1987). "Molecular cloning of a brain-specific calcium/calmodulin-dependent protein kinase.". Proc. Natl. Acad. Sci. U.S.A. 84 (16): 5962–6. PMID 3475713.
Ku NO, Omary MB (1994). "Identification of the major physiologic phosphorylation site of human keratin 18: potential kinases and a role in filament reorganization.". J. Cell Biol. 127 (1): 161–71. PMID 7523419.
Drewes G, Trinczek B, Illenberger S, et al. (1995). "Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262.". J. Biol. Chem. 270 (13): 7679–88. PMID 7706316.
Tsujimura K, Tanaka J, Ando S, et al. (1995). "Identification of phosphorylation sites on glial fibrillary acidic protein for cdc2 kinase and Ca(2+)-calmodulin-dependent protein kinase II.". J. Biochem. 116 (2): 426–34. PMID 7822264.
Toyofuku T, Curotto Kurzydlowski K, Narayanan N, MacLennan DH (1994). "Identification of Ser38 as the site in cardiac sarcoplasmic reticulum Ca(2+)-ATPase that is phosphorylated by Ca2+/calmodulin-dependent protein kinase.". J. Biol. Chem. 269 (42): 26492–6. PMID 7929371.
Rivera VM, Miranti CK, Misra RP, et al. (1993). "A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity.". Mol. Cell. Biol. 13 (10): 6260–73. PMID 8413226.
Omkumar RV, Kiely MJ, Rosenstein AJ, et al. (1997). "Identification of a phosphorylation site for calcium/calmodulindependent protein kinase II in the NR2B subunit of the N-methyl-D-aspartate receptor.". J. Biol. Chem. 271 (49): 31670–8. PMID 8940188.
Rotenberg A, Mayford M, Hawkins RD, et al. (1997). "Mice expressing activated CaMKII lack low frequency LTP and do not form stable place cells in the CA1 region of the hippocampus.". Cell 87 (7): 1351–61. PMID 8980240.
Paudel HK (1997). "The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase.". J. Biol. Chem. 272 (3): 1777–85. PMID 8999860.