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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Calcium/calmodulin-dependent protein kinase type II gamma chain''' is an [[enzyme]] that in humans is encoded by the ''CAMK2G'' [[gene]].<ref name="pmid8287681">{{cite journal | vauthors = Li X, Nghiem P, Schulman H, Francke U | title = 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 | journal = Cytogenet Cell Genet | volume = 66 | issue = 2 | pages = 113–6 | date = Feb 1994 | pmid = 8287681 | pmc = | doi = 10.1159/000133679 }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_CAMK2G_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ux0.
| PDB = {{PDB2|2ux0}}
| Name = Calcium/calmodulin-dependent protein kinase (CaM kinase) II gamma
| HGNCid = 1463
| Symbol = CAMK2G
| AltSymbols =; CAMK; CAMK-II; CAMKG; FLJ16043; MGC26678
| OMIM = 602123
| ECnumber =  2.7.11.17
| Homologene = 15596
| MGIid = 88259
| GeneAtlas_image1 = PBB_GE_CAMK2G_212669_at_tn.png
| GeneAtlas_image2 = PBB_GE_CAMK2G_212757_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004685 |text = calmodulin-dependent protein kinase activity}} {{GNF_GO|id=GO:0004723 |text = calcium-dependent protein serine/threonine phosphatase activity}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005954 |text = calcium- and calmodulin-dependent protein kinase complex}}
| Process = {{GNF_GO|id=GO:0000082 |text = G1/S transition of mitotic cell cycle}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006816 |text = calcium ion transport}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0030073 |text = insulin secretion}} {{GNF_GO|id=GO:0046777 |text = protein amino acid autophosphorylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 818
    | Hs_Ensembl = ENSG00000148660
    | Hs_RefseqProtein = NP_001213
    | Hs_RefseqmRNA = NM_001222
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 75242265
    | Hs_GenLoc_end = 75304349
    | Hs_Uniprot = Q13555
    | Mm_EntrezGene = 12325
    | Mm_Ensembl = ENSMUSG00000021820
    | Mm_RefseqmRNA = XM_980738
    | Mm_RefseqProtein = XP_985832
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 14
    | Mm_GenLoc_start = 19523427
    | Mm_GenLoc_end = 19582640
    | Mm_Uniprot = Q923T9
  }}
}}
'''Calcium/calmodulin-dependent protein kinase (CaM kinase) II gamma''', also known as '''CAMK2G''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref>{{cite web | title = Entrez Gene: CAMK2G calcium/calmodulin-dependent protein kinase (CaM kinase) II gamma| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=818| accessdate = }}</ref>
{{PBB_Summary
== Interactions ==
| section_title =
| summary_text = 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.<ref>{{cite web | title = Entrez Gene: CAMK2G calcium/calmodulin-dependent protein kinase (CaM kinase) II gamma| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=818| accessdate = }}</ref>
}}


==See also==
CAMK2G has been shown to [[Protein-protein interaction|interact]] with [[RRAD]].<ref name=pmid9115241>{{cite journal | vauthors = Moyers JS, Bilan PJ, Zhu J, Kahn CR | title = Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II | journal = J. Biol. Chem. | volume = 272 | issue = 18 | pages = 11832–9 | date = May 1997 | pmid = 9115241 | doi = 10.1074/jbc.272.18.11832 }}</ref>
[[Ca2+/calmodulin-dependent protein kinase]]


==References==
== See also ==
{{reflist|2}}
* [[Ca2+/calmodulin-dependent protein kinase]]
 
== References ==
==Further reading==
{{reflist}}
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Hook SS, Means AR | title = Ca(2+)/CaM-dependent kinases: from activation to function. | journal = Annu. Rev. Pharmacol. Toxicol. | volume = 41 | issue =  | pages = 471–505 | year = 2001 | pmid = 11264466 | doi = 10.1146/annurev.pharmtox.41.1.471 }}
| citations =
* {{cite journal | vauthors = Yamamoto H | title = [Molecular mechanisms of the intracellular localizations of Ca2+/calmodulin-dependent protein kinase II isoforms, and their physiological functions] | journal = Tanpakushitsu Kakusan Koso | volume = 47 | issue = 3 | pages = 241–7 | year = 2002 | pmid = 11889801 | doi =  }}
*{{cite journal | author=Hook SS, Means AR |title=Ca(2+)/CaM-dependent kinases: from activation to function. |journal=Annu. Rev. Pharmacol. Toxicol. |volume=41 |issue=  |pages= 471-505 |year= 2001 |pmid= 11264466 |doi= 10.1146/annurev.pharmtox.41.1.471 }}
* {{cite journal | vauthors = Countaway JL, Nairn AC, Davis RJ | title = Mechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase. | journal = J. Biol. Chem. | volume = 267 | issue = 2 | pages = 1129–40 | year = 1992 | pmid = 1309762 | doi =  }}
*{{cite journal | author=Yamamoto H |title=[Molecular mechanisms of the intracellular localizations of Ca2+/calmodulin-dependent protein kinase II isoforms, and their physiological functions] |journal=Tanpakushitsu Kakusan Koso |volume=47 |issue= 3 |pages= 241-7 |year= 2002 |pmid= 11889801 |doi=  }}
* {{cite journal | vauthors = Ikebe M, Reardon S | title = Phosphorylation of smooth myosin light chain kinase by smooth muscle Ca2+/calmodulin-dependent multifunctional protein kinase. | journal = J. Biol. Chem. | volume = 265 | issue = 16 | pages = 8975–8 | year = 1990 | pmid = 2160950 | doi =  }}
*{{cite journal | author=Countaway JL, Nairn AC, Davis RJ |title=Mechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase. |journal=J. Biol. Chem. |volume=267 |issue= 2 |pages= 1129-40 |year= 1992 |pmid= 1309762 |doi=  }}
* {{cite journal | vauthors = Czernik AJ, Pang DT, Greengard P | title = Amino acid sequences surrounding the cAMP-dependent and calcium/calmodulin-dependent phosphorylation sites in rat and bovine synapsin I. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 84 | issue = 21 | pages = 7518–22 | year = 1987 | pmid = 3118371 | pmc = 299327 | doi = 10.1073/pnas.84.21.7518 }}
*{{cite journal | author=Ikebe M, Reardon S |title=Phosphorylation of smooth myosin light chain kinase by smooth muscle Ca2+/calmodulin-dependent multifunctional protein kinase. |journal=J. Biol. Chem. |volume=265 |issue= 16 |pages= 8975-8 |year= 1990 |pmid= 2160950 |doi=  }}
* {{cite journal | vauthors = Vulliet PR, Woodgett JR, Cohen P | title = Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase. | journal = J. Biol. Chem. | volume = 259 | issue = 22 | pages = 13680–3 | year = 1984 | pmid = 6150037 | doi =  }}
*{{cite journal | author=Czernik AJ, Pang DT, Greengard P |title=Amino acid sequences surrounding the cAMP-dependent and calcium/calmodulin-dependent phosphorylation sites in rat and bovine synapsin I. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 21 |pages= 7518-22 |year= 1987 |pmid= 3118371 |doi= }}
* {{cite journal | vauthors = Wen Z, Zhong Z, Darnell JE | title = Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation. | journal = Cell | volume = 82 | issue = 2 | pages = 241–50 | year = 1995 | pmid = 7543024 | doi = 10.1016/0092-8674(95)90311-9 }}
*{{cite journal | author=Vulliet PR, Woodgett JR, Cohen P |title=Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase. |journal=J. Biol. Chem. |volume=259 |issue= 22 |pages= 13680-3 |year= 1984 |pmid= 6150037 |doi=  }}
* {{cite journal | vauthors = Kwiatkowski AP, McGill JM | title = Human biliary epithelial cell line Mz-ChA-1 expresses new isoforms of calmodulin-dependent protein kinase II. | journal = Gastroenterology | volume = 109 | issue = 4 | pages = 1316–23 | year = 1995 | pmid = 7557101 | doi = 10.1016/0016-5085(95)90594-4 }}
*{{cite journal | author=Wen Z, Zhong Z, Darnell JE |title=Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation. |journal=Cell |volume=82 |issue= 2 |pages= 241-50 |year= 1995 |pmid= 7543024 |doi= }}
* {{cite journal | vauthors = Shuai K, Stark GR, Kerr IM, Darnell JE | title = A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma. | journal = Science | volume = 261 | issue = 5129 | pages = 1744–6 | year = 1993 | pmid = 7690989 | doi = 10.1126/science.7690989 }}
*{{cite journal | author=Kwiatkowski AP, McGill JM |title=Human biliary epithelial cell line Mz-ChA-1 expresses new isoforms of calmodulin-dependent protein kinase II. |journal=Gastroenterology |volume=109 |issue= 4 |pages= 1316-23 |year= 1995 |pmid= 7557101 |doi= }}
* {{cite journal | vauthors = Zhu J, Reynet C, Caldwell JS, Kahn CR | title = Characterization of Rad, a new member of Ras/GTPase superfamily, and its regulation by a unique GTPase-activating protein (GAP)-like activity. | journal = J. Biol. Chem. | volume = 270 | issue = 9 | pages = 4805–12 | year = 1995 | pmid = 7876254 | doi = 10.1074/jbc.270.9.4805 }}
*{{cite journal | author=Shuai K, Stark GR, Kerr IM, Darnell JE |title=A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma. |journal=Science |volume=261 |issue= 5129 |pages= 1744-6 |year= 1993 |pmid= 7690989 |doi= }}
* {{cite journal | vauthors = Yakel JL, Vissavajjhala P, Derkach VA, Brickey DA, Soderling TR | title = Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate receptors. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 5 | pages = 1376–80 | year = 1995 | pmid = 7877986 | pmc = 42522 | doi = 10.1073/pnas.92.5.1376 }}
*{{cite journal | author=Zhu J, Reynet C, Caldwell JS, Kahn CR |title=Characterization of Rad, a new member of Ras/GTPase superfamily, and its regulation by a unique GTPase-activating protein (GAP)-like activity. |journal=J. Biol. Chem. |volume=270 |issue= 9 |pages= 4805-12 |year= 1995 |pmid= 7876254 |doi= }}
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | year = 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Yakel JL, Vissavajjhala P, Derkach VA, ''et al.'' |title=Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate receptors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 5 |pages= 1376-80 |year= 1995 |pmid= 7877986 |doi= }}
* {{cite journal | vauthors = Suko J, Maurer-Fogy I, Plank B, Bertel O, Wyskovsky W, Hohenegger M, Hellmann G | title = Phosphorylation of serine 2843 in ryanodine receptor-calcium release channel of skeletal muscle by cAMP-, cGMP- and CaM-dependent protein kinase | journal = Biochim. Biophys. Acta | volume = 1175 | issue = 2 | pages = 193–206 | year = 1993 | pmid = 8380342 | doi = 10.1016/0167-4889(93)90023-I }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = de Groot RP, den Hertog J, Vandenheede JR, Goris J, Sassone-Corsi P | title = Multiple and cooperative phosphorylation events regulate the CREM activator function | journal = EMBO J. | volume = 12 | issue = 10 | pages = 3903–11 | year = 1993 | pmid = 8404858 | pmc = 413673 | doi =  }}
*{{cite journal | author=Li X, Nghiem P, Schulman H, Francke U |title=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. |journal=Cytogenet. Cell Genet. |volume=66 |issue= 2 |pages= 113-6 |year= 1994 |pmid= 8287681 |doi= }}
* {{cite journal | vauthors = Nghiem P, Saati SM, Martens CL, Gardner P, Schulman H | title = Cloning and analysis of two new isoforms of multifunctional Ca2+/calmodulin-dependent protein kinase. Expression in multiple human tissues | journal = J. Biol. Chem. | volume = 268 | issue = 8 | pages = 5471–9 | year = 1993 | pmid = 8449910 | doi =  }}
*{{cite journal | author=Suko J, Maurer-Fogy I, Plank B, ''et al.'' |title=Phosphorylation of serine 2843 in ryanodine receptor-calcium release channel of skeletal muscle by cAMP-, cGMP- and CaM-dependent protein kinase. |journal=Biochim. Biophys. Acta |volume=1175 |issue= 2 |pages= 193-206 |year= 1993 |pmid= 8380342 |doi=  }}
* {{cite journal | vauthors = Shimomura A, Ogawa Y, Kitani T, Fujisawa H, Hagiwara M | title = Calmodulin-dependent protein kinase II potentiates transcriptional activation through activating transcription factor 1 but not cAMP response element-binding protein | journal = J. Biol. Chem. | volume = 271 | issue = 30 | pages = 17957–60 | year = 1996 | pmid = 8663317 | doi = 10.1074/jbc.271.30.17957 }}
*{{cite journal | author=de Groot RP, den Hertog J, Vandenheede JR, ''et al.'' |title=Multiple and cooperative phosphorylation events regulate the CREM activator function. |journal=EMBO J. |volume=12 |issue= 10 |pages= 3903-11 |year= 1993 |pmid= 8404858 |doi=  }}
* {{cite journal | vauthors = Wei J, Wayman G, Storm DR | title = Phosphorylation and inhibition of type III adenylyl cyclase by calmodulin-dependent protein kinase II in vivo | journal = J. Biol. Chem. | volume = 271 | issue = 39 | pages = 24231–5 | year = 1996 | pmid = 8798667 | doi = 10.1074/jbc.271.39.24231 }}
*{{cite journal | author=Nghiem P, Saati SM, Martens CL, ''et al.'' |title=Cloning and analysis of two new isoforms of multifunctional Ca2+/calmodulin-dependent protein kinase. Expression in multiple human tissues. |journal=J. Biol. Chem. |volume=268 |issue= 8 |pages= 5471-9 |year= 1993 |pmid= 8449910 |doi= }}
* {{cite journal | vauthors = Tombes RM, Krystal GW | title = Identification of novel human tumor cell-specific CaMK-II variants | journal = Biochim. Biophys. Acta | volume = 1355 | issue = 3 | pages = 281–92 | year = 1997 | pmid = 9060999 | doi = 10.1016/S0167-4889(96)00141-3 }}
*{{cite journal | author=Shimomura A, Ogawa Y, Kitani T, ''et al.'' |title=Calmodulin-dependent protein kinase II potentiates transcriptional activation through activating transcription factor 1 but not cAMP response element-binding protein. |journal=J. Biol. Chem. |volume=271 |issue= 30 |pages= 17957-60 |year= 1996 |pmid= 8663317 |doi= }}
* {{cite journal | vauthors = Moyers JS, Bilan PJ, Zhu J, Kahn CR | title = Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II | journal = J. Biol. Chem. | volume = 272 | issue = 18 | pages = 11832–9 | year = 1997 | pmid = 9115241 | doi = 10.1074/jbc.272.18.11832 }}
*{{cite journal | author=Wei J, Wayman G, Storm DR |title=Phosphorylation and inhibition of type III adenylyl cyclase by calmodulin-dependent protein kinase II in vivo. |journal=J. Biol. Chem. |volume=271 |issue= 39 |pages= 24231-5 |year= 1996 |pmid= 8798667 |doi= }}
*{{cite journal | author=Tombes RM, Krystal GW |title=Identification of novel human tumor cell-specific CaMK-II variants. |journal=Biochim. Biophys. Acta |volume=1355 |issue= 3 |pages= 281-92 |year= 1997 |pmid= 9060999 |doi= }}
*{{cite journal  | author=Moyers JS, Bilan PJ, Zhu J, Kahn CR |title=Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II. |journal=J. Biol. Chem. |volume=272 |issue= 18 |pages= 11832-9 |year= 1997 |pmid= 9115241 |doi=  }}
}}
{{refend}}
{{refend}}
==External links==
* {{UCSC gene info|CAMK2G}}
{{PDB Gallery|geneid=818}}
{{Serine/threonine-specific protein kinases}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}


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[[Category:EC 2.7.11]]

Latest revision as of 01:25, 27 October 2017

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Identifiers
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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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RefSeq (mRNA)

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View/Edit Human

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

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.[2]

Interactions

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

See also

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. doi:10.1159/000133679. PMID 8287681.
  2. ↑ "Entrez Gene: CAMK2G calcium/calmodulin-dependent protein kinase (CaM kinase) II gamma".
  3. ↑ Moyers JS, Bilan PJ, Zhu J, Kahn CR (May 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.

Further reading

External links

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


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