CAMK2G

CAMK2G
Identifiers
Aliases	CAMK2G, CAMK, CAMK-II, CAMKG, calcium/calmodulin dependent protein kinase II gamma
External IDs	OMIM: 602123; MGI: 88259; HomoloGene: 15596; GeneCards: CAMK2G; OMA:CAMK2G - orthologs
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2UX0, 2V7O
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 2.7.11.17 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 10 (human) Band 10q22.2 Start 73,812,501 bp End 73,874,591 bp
Gene location (Mouse) Chr. Chromosome 14 (mouse) Band 14|14 A3 Start 20,734,875 bp End 20,794,088 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in frontal pole postcentral gyrus right frontal lobe popliteal artery tibial arteries Brodmann area 10 muscle layer of sigmoid colon right coronary artery lateral nuclear group of thalamus primary visual cortex Top expressed in zygote primary visual cortex superior frontal gyrus dentate gyrus of hippocampal formation granule cell secondary oocyte central gray substance of midbrain muscle of thigh triceps brachii muscle primary motor cortex pontine nuclei More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding protein kinase activity protein homodimerization activity kinase activity protein binding calcium-dependent protein serine/threonine phosphatase activity ATP binding protein serine/threonine kinase activity calmodulin-dependent protein kinase activity calmodulin binding identical protein binding Cellular component endocytic vesicle membrane cytosol membrane plasma membrane nucleoplasm sarcoplasmic reticulum sarcoplasmic reticulum membrane cytoplasm postsynaptic density neuron projection Biological process regulation of calcium ion transport phosphorylation interferon-gamma-mediated signaling pathway G1 phase regulation of relaxation of cardiac muscle insulin secretion MAPK cascade multicellular organism development protein phosphorylation protein complex oligomerization regulation of cellular response to heat protein autophosphorylation regulation of skeletal muscle adaptation calcium ion transport protein dephosphorylation nervous system development peptidyl-serine phosphorylation peptidyl-threonine phosphorylation cell differentiation intracellular signal transduction regulation of molecular function Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 818 12325 Ensembl ENSG00000148660 ENSMUSG00000021820 UniProt Q13555 Q923T9 RefSeq (mRNA) NM_001204492 NM_001222 NM_172169 NM_172170 NM_172171 NM_172172 NM_172173 NM_001320898 NM_001039138 NM_001039139 NM_178597 NM_001360186 RefSeq (protein) NP_001191421 NP_001213 NP_001307827 NP_751909 NP_751910 NP_751911 NP_751913 NP_001354443 NP_001354445 NP_001354446 NP_001354447 NP_001354448 NP_001354449 NP_001354450 NP_001354451 NP_001354452 NP_001354453 NP_001354454 NP_001354455 NP_001354456 NP_001354457 NP_001354458 NP_001354459 NP_001354460 NP_001354461 NP_001354462 NP_001354463 NP_001354464 NP_001354465 NP_001354466 NP_001354467 NP_001354468 NP_001354469 NP_001354470 NP_001354471 NP_001354472 NP_001354473 NP_001354474 NP_001354475 NP_001354476 NP_001354477 NP_001034227 NP_001034228 NP_848712 NP_001347115 Location (UCSC) Chr 10: 73.81 – 73.87 Mb Chr 14: 20.73 – 20.79 Mb PubMed search
Wikidata
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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

• 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. doi:10.1016/S0021-9258(18)48406-2. 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. doi:10.1016/S0021-9258(19)38796-4. 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. Bibcode:1987PNAS...84.7518C. doi:10.1073/pnas.84.21.7518. PMC 299327. 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. doi:10.1016/S0021-9258(18)89798-8. 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. S2CID 6717533.
• 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. Bibcode:1993Sci...261.1744S. 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, Brickey DA, Soderling TR (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. Bibcode:1995PNAS...92.1376Y. doi:10.1073/pnas.92.5.1376. PMC 42522. 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, Bertel O, Wyskovsky W, Hohenegger M, Hellmann G (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, Goris J, Sassone-Corsi P (1993). "Multiple and cooperative phosphorylation events regulate the CREM activator function". EMBO J. 12 (10): 3903–11. doi:10.1002/j.1460-2075.1993.tb06068.x. PMC 413673. PMID 8404858.
• Nghiem P, Saati SM, Martens CL, Gardner P, Schulman H (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. doi:10.1016/S0021-9258(18)53345-7. PMID 8449910.
• Shimomura A, Ogawa Y, Kitani T, Fujisawa H, Hagiwara M (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.

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.