Biology:CAMK2G

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

Calcium/calmodulin-dependent protein kinase type II gamma chain is an enzyme that in humans is encoded by the CAMK2G gene.

Function

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.

Interactions

CAMK2G has been shown to interact with RRAD.

See also

• Ca2+/calmodulin-dependent protein kinase

Further reading

• "Ca(2+)/CaM-dependent kinases: from activation to function.". Annu. Rev. Pharmacol. Toxicol. 41: 471–505. 2001. doi:10.1146/annurev.pharmtox.41.1.471. PMID 11264466. 
• "[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. 2002. PMID 11889801. 
• "Mechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase.". J. Biol. Chem. 267 (2): 1129–40. 1992. doi:10.1016/S0021-9258(18)48406-2. PMID 1309762. 
• "Phosphorylation of smooth myosin light chain kinase by smooth muscle Ca2+/calmodulin-dependent multifunctional protein kinase.". J. Biol. Chem. 265 (16): 8975–8. 1990. doi:10.1016/S0021-9258(19)38796-4. PMID 2160950. 
• "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. 1987. doi:10.1073/pnas.84.21.7518. PMID 3118371. Bibcode: 1987PNAS...84.7518C. 
• "Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase.". J. Biol. Chem. 259 (22): 13680–3. 1984. doi:10.1016/S0021-9258(18)89798-8. PMID 6150037. 
• "Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation.". Cell 82 (2): 241–50. 1995. doi:10.1016/0092-8674(95)90311-9. PMID 7543024. 
• "Human biliary epithelial cell line Mz-ChA-1 expresses new isoforms of calmodulin-dependent protein kinase II.". Gastroenterology 109 (4): 1316–23. 1995. doi:10.1016/0016-5085(95)90594-4. PMID 7557101. 
• "A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma.". Science 261 (5129): 1744–6. 1993. doi:10.1126/science.7690989. PMID 7690989. Bibcode: 1993Sci...261.1744S. 
• "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. 1995. doi:10.1074/jbc.270.9.4805. PMID 7876254. 
• "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. 1995. doi:10.1073/pnas.92.5.1376. PMID 7877986. Bibcode: 1995PNAS...92.1376Y. 
• "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• "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. 1993. doi:10.1016/0167-4889(93)90023-I. PMID 8380342. 
• "Multiple and cooperative phosphorylation events regulate the CREM activator function". EMBO J. 12 (10): 3903–11. 1993. doi:10.1002/j.1460-2075.1993.tb06068.x. PMID 8404858. 
• "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. 1993. doi:10.1016/S0021-9258(18)53345-7. PMID 8449910. 
• "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. 1996. doi:10.1074/jbc.271.30.17957. PMID 8663317. 
• "Phosphorylation and inhibition of type III adenylyl cyclase by calmodulin-dependent protein kinase II in vivo". J. Biol. Chem. 271 (39): 24231–5. 1996. doi:10.1074/jbc.271.39.24231. PMID 8798667. 
• "Identification of novel human tumor cell-specific CaMK-II variants". Biochim. Biophys. Acta 1355 (3): 281–92. 1997. doi:10.1016/S0167-4889(96)00141-3. PMID 9060999. 
• "Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II". J. Biol. Chem. 272 (18): 11832–9. 1997. doi:10.1074/jbc.272.18.11832. PMID 9115241. 

External links

• Human CAMK2G genome location and CAMK2G gene details page in the UCSC Genome Browser.
• Overview of all the structural information available in the PDB for UniProt: Q13555 (Calcium/calmodulin-dependent protein kinase type II subunit gamma) at the PDBe-KB.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.