The Full Wiki

More info on CAMK2G

CAMK2G: Wikis

Advertisements

Note: Many of our articles have direct quotes from sources you can cite, within the Wikipedia article! This article doesn't yet, but we're working on it! See more info or our list of citable articles.

Encyclopedia

From Wikipedia, the free encyclopedia

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

PDB rendering based on 2ux0.
Available structures
2ux0
Identifiers
Symbols CAMK2G; CAMK; CAMK-II; CAMKG; FLJ16043; MGC26678
External IDs OMIM602123 MGI88259 HomoloGene15596 GeneCards: CAMK2G Gene
EC number 2.7.11.17
RNA expression pattern
PBB GE CAMK2G 212669 at tn.png
PBB GE CAMK2G 212757 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 818 12325
Ensembl ENSG00000148660 ENSMUSG00000021820
UniProt Q13555 Q923T9
RefSeq (mRNA) NM_001222 XM_980738
RefSeq (protein) NP_001213 XP_985832
Location (UCSC) Chr 10:
75.24 - 75.3 Mb
Chr 14:
19.52 - 19.58 Mb
PubMed search [1] [2]

Calcium/calmodulin-dependent protein kinase type II gamma chain is an enzyme that in humans is encoded by the CAMK2G gene.[1]

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.[2]

Contents

See also

Ca2+/calmodulin-dependent protein kinase

Interactions

CAMK2G has been shown to interact with RRAD.[3]

References

  1. ^ Li X, Nghiem P, Schulman H, Francke U (Feb 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.  
  2. ^ "Entrez Gene: CAMK2G calcium/calmodulin-dependent protein kinase (CaM kinase) II gamma". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=818.  
  3. ^ Moyers, J S; Bilan P J, Zhu J, Kahn C R (May. 1997). "Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II". J. Biol. Chem. (UNITED STATES) 272 (18): 11832–9. ISSN 0021-9258. PMID 9115241.  

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. doi:10.1073/pnas.84.21.7518. 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. doi:10.1016/0092-8674(95)90311-9. 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. doi:10.1016/0016-5085(95)90594-4. 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. doi:10.1126/science.7690989. 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. doi:10.1074/jbc.270.9.4805. 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. doi:10.1073/pnas.92.5.1376. 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. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.  
  • 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. doi:10.1016/0167-4889(93)90023-I. 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. doi:10.1074/jbc.271.30.17957. 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. doi:10.1074/jbc.271.39.24231. PMID 8798667.  
  • Tombes RM, Krystal GW (1997). "Identification of novel human tumor cell-specific CaMK-II variants.". Biochim. Biophys. Acta 1355 (3): 281–92. doi:10.1016/S0167-4889(96)00141-3. 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. doi:10.1074/jbc.272.18.11832. PMID 9115241.  

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

Advertisements

Advertisements






Got something to say? Make a comment.
Your name
Your email address
Message