CAMK2G

From Wikipedia, the free encyclopedia

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

PDB rendering based on 2ux0.

Available structures: 2ux0

Identifiers

Symbol(s)

CAMK2G; CAMK; CAMK-II; CAMKG; FLJ16043; MGC26678

External IDs

OMIM: 602123 MGI: 88259 HomoloGene: 15596

EC number

2.7.11.17

Gene ontology
Molecular Function:	• nucleotide binding • protein serine/threonine kinase activity • calmodulin-dependent protein kinase activity • calcium-dependent protein serine/threonine phosphatase activity • calmodulin binding • ATP binding • transferase activity
Cellular Component:	• cellular_component • calcium- and calmodulin-dependent protein kinase complex
Biological Process:	• G1/S transition of mitotic cell cycle • protein amino acid phosphorylation • calcium ion transport • signal transduction • insulin secretion • protein amino acid autophosphorylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001222 (mRNA)
NP_001213 (protein)

XM_980738 (mRNA)
XP_985832 (protein)

Location

Chr 10: 75.24 - 75.3 Mb

Chr 14: 19.52 - 19.58 Mb

Pubmed search

[1]

[2]

Calcium/calmodulin-dependent protein kinase (CaM kinase) II gamma, also known as CAMK2G, is a human gene.

The product of this gene belongs to the Serine/Threonine protein kinase family, and to the Ca(2+)/calmodulin-dependent protein kinase subfamily. Calcium signaling is crucial for several aspects of plasticity at glutamatergic synapses. In mammalian cells the enzyme is composed of four different chains: alpha, beta, gamma, and delta. The product of this gene is a gamma chain. Six alternatively spliced variants that encode six different isoforms have been characterized to date. Additional alternative splice variants that encode different isoforms have been described, but their full-length nature has not been determined.^[1]

[edit] References

^ Entrez Gene: CAMK2G calcium/calmodulin-dependent protein kinase (CaM kinase) II gamma.

[edit] Further reading

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.
Ikebe M, Reardon S (1990). "Phosphorylation of smooth myosin light chain kinase by smooth muscle Ca2+/calmodulin-dependent multifunctional protein kinase.". J. Biol. Chem. 265 (16): 8975-8. PMID 2160950.
Czernik AJ, Pang DT, Greengard P (1987). "Amino acid sequences surrounding the cAMP-dependent and calcium/calmodulin-dependent phosphorylation sites in rat and bovine synapsin I.". Proc. Natl. Acad. Sci. U.S.A. 84 (21): 7518-22. PMID 3118371.
Vulliet PR, Woodgett JR, Cohen P (1984). "Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase.". J. Biol. Chem. 259 (22): 13680-3. PMID 6150037.
Wen Z, Zhong Z, Darnell JE (1995). "Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation.". Cell 82 (2): 241-50. PMID 7543024.
Kwiatkowski AP, McGill JM (1995). "Human biliary epithelial cell line Mz-ChA-1 expresses new isoforms of calmodulin-dependent protein kinase II.". Gastroenterology 109 (4): 1316-23. PMID 7557101.
Shuai K, Stark GR, Kerr IM, Darnell JE (1993). "A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma.". Science 261 (5129): 1744-6. PMID 7690989.
Zhu J, Reynet C, Caldwell JS, Kahn CR (1995). "Characterization of Rad, a new member of Ras/GTPase superfamily, and its regulation by a unique GTPase-activating protein (GAP)-like activity.". J. Biol. Chem. 270 (9): 4805-12. PMID 7876254.
Yakel JL, Vissavajjhala P, Derkach VA, et al. (1995). "Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate receptors.". Proc. Natl. Acad. Sci. U.S.A. 92 (5): 1376-80. PMID 7877986.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171-4. PMID 8125298.
Li X, Nghiem P, Schulman H, Francke U (1994). "Localization of the CAMKG gene encoding gamma isoforms of multifunctional calcium/calmodulin-dependent protein kinase (CaM kinase) to human chromosome 10 band q22 and mouse chromosome 14.". Cytogenet. Cell Genet. 66 (2): 113-6. PMID 8287681.
Suko J, Maurer-Fogy I, Plank B, et al. (1993). "Phosphorylation of serine 2843 in ryanodine receptor-calcium release channel of skeletal muscle by cAMP-, cGMP- and CaM-dependent protein kinase.". Biochim. Biophys. Acta 1175 (2): 193-206. PMID 8380342.
de Groot RP, den Hertog J, Vandenheede JR, et al. (1993). "Multiple and cooperative phosphorylation events regulate the CREM activator function.". EMBO J. 12 (10): 3903-11. PMID 8404858.
Nghiem P, Saati SM, Martens CL, et al. (1993). "Cloning and analysis of two new isoforms of multifunctional Ca2+/calmodulin-dependent protein kinase. Expression in multiple human tissues.". J. Biol. Chem. 268 (8): 5471-9. PMID 8449910.
Shimomura A, Ogawa Y, Kitani T, et al. (1996). "Calmodulin-dependent protein kinase II potentiates transcriptional activation through activating transcription factor 1 but not cAMP response element-binding protein.". J. Biol. Chem. 271 (30): 17957-60. PMID 8663317.
Wei J, Wayman G, Storm DR (1996). "Phosphorylation and inhibition of type III adenylyl cyclase by calmodulin-dependent protein kinase II in vivo.". J. Biol. Chem. 271 (39): 24231-5. PMID 8798667.
Tombes RM, Krystal GW (1997). "Identification of novel human tumor cell-specific CaMK-II variants.". Biochim. Biophys. Acta 1355 (3): 281-92. PMID 9060999.
Moyers JS, Bilan PJ, Zhu J, Kahn CR (1997). "Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II.". J. Biol. Chem. 272 (18): 11832-9. PMID 9115241.