CAMK2D

Calcium/calmodulin-dependent protein kinase II delta
Rendering based on PDB 2VN9​.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2VN9​, 2W2C​, 2WEL​, 3GP2​
Identifiers
Symbols	CAMK2D ; CAMKD
External IDs	OMIM: 607708 MGI: 1341265 HomoloGene: 55561 ChEMBL: 2801 GeneCards: CAMK2D Gene
EC number	2.7.11.17
Gene ontology Molecular function • protein serine/threonine kinase activity • calmodulin-dependent protein kinase activity • protein binding • calmodulin binding • ATP binding • sodium channel inhibitor activity • titin binding • protein homodimerization activity • ion channel binding • nitric-oxide synthase binding Cellular component • nucleus • nucleoplasm • cytoplasm • cytosol • plasma membrane • intercalated disc • membrane • T-tubule • endocytic vesicle membrane • neuromuscular junction • sarcoplasmic reticulum membrane • calcium channel complex • neuronal cell body • axon initial segment • perinuclear region of cytoplasm Biological process • G1/S transition of mitotic cell cycle • regulation of cell growth • response to hypoxia • regulation of the force of heart contraction • regulation of membrane depolarization • regulation of transcription from RNA polymerase II promoter • protein phosphorylation • calcium ion transport • synaptic transmission • regulation of heart contraction • regulation of G2/M transition of mitotic cell cycle • positive regulation of cardiac muscle hypertrophy • regulation of cell communication by electrical coupling • positive regulation of cardiac muscle cell apoptotic process • regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum • regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion • positive regulation of smooth muscle cell migration • peptidyl-serine phosphorylation • peptidyl-threonine phosphorylation • cytokine-mediated signaling pathway • cellular potassium ion homeostasis • endoplasmic reticulum calcium ion homeostasis • cellular response to heat • positive regulation of Rac protein signal transduction • protein autophosphorylation • positive regulation of smooth muscle cell proliferation • protein oligomerization • relaxation of cardiac muscle • regulation of ryanodine-sensitive calcium-release channel activity • interferon-gamma-mediated signaling pathway • regulation of cellular localization • cell growth involved in cardiac muscle cell development • positive regulation of ERK1 and ERK2 cascade • cellular response to calcium ion • cardiac muscle cell contraction • regulation of heart rate by cardiac conduction • regulation of cardiac muscle cell action potential • regulation of cardiac muscle cell action potential involved in regulation of contraction • regulation of cellular response to heat • regulation of histone deacetylase activity • regulation of cell communication by electrical coupling involved in cardiac conduction • regulation of relaxation of cardiac muscle • negative regulation of sodium ion transmembrane transport • regulation of generation of L-type calcium current • negative regulation of sodium ion transmembrane transporter activity Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	817	108058
Ensembl	ENSG00000145349	ENSMUSG00000053819
UniProt	Q13557	Q6PHZ2
RefSeq (mRNA)	NM_001221	NM_001025438
RefSeq (protein)	NP_001212	NP_001020609
Location (UCSC)	Chr 4: 113.45 – 113.76 Mb	Chr 3: 126.6 – 126.85 Mb
PubMed search

Calcium/calmodulin-dependent protein kinase type II delta chain is an enzyme that in humans is encoded by the CAMK2D gene.^[1]

The product of this gene belongs to the serine/threonine protein kinase family and to the Ca²⁺/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 delta chain. Four alternatively spliced transcript variants that encode three different isoforms have been characterized to date. Distinct isoforms of this chain have different expression patterns.^[1]

References

1. "Entrez Gene: CAMK2D calcium/calmodulin-dependent protein kinase (CaM kinase) II delta".

Further reading

• Hook SS, Means AR (2001). "Ca²⁺/CaM-dependent kinases: from activation to function". Annu. Rev. Pharmacol. Toxicol. 41 (1): 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.
• 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. PMC 413673. PMID 8404858.
• 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.
• Möhlig M, Wolter S, Mayer P; et al. (1997). "Insulinoma cells contain an isoform of Ca²⁺/calmodulin-dependent protein kinase II delta associated with insulin secretion vesicles". Endocrinology 138 (6): 2577–84. doi:10.1210/en.138.6.2577. PMID 9165051.
• Bauch A, Campbell KS, Reth M (1998). "Interaction of the CD5 cytoplasmic domain with the Ca²⁺/calmodulin-dependent kinase IIdelta". Eur. J. Immunol. 28 (7): 2167–77. doi:10.1002/(SICI)1521-4141(199807)28:07<2167::AID-IMMU2167>3.0.CO;2-L. PMID 9692886.
• "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. 1999. doi:10.1101/gr.8.11.1097. PMID 9847074.
• Hoch B, Meyer R, Hetzer R; et al. (1999). "Identification and expression of delta-isoforms of the multifunctional Ca²⁺/calmodulin-dependent protein kinase in failing and nonfailing human myocardium". Circ. Res. 84 (6): 713–21. doi:10.1161/01.res.84.6.713. PMID 10189359.
• Tombes RM, Mikkelsen RB, Jarvis WD, Grant S (1999). "Downregulation of delta CaM kinase II in human tumor cells". Biochim. Biophys. Acta 1452 (1): 1–11. doi:10.1016/S0167-4889(99)00113-5. PMID 10525155.
• Rochlitz H, Voigt A, Lankat-Buttgereit B; et al. (2000). "Cloning and quantitative determination of the human Ca²⁺/calmodulin-dependent protein kinase II (CaMK II) isoforms in human beta cells". Diabetologia 43 (4): 465–73. doi:10.1007/s001250051330. PMID 10819240.
• Inagaki N, Nishizawa M, Arimura N; et al. (2000). "Activation of Ca²⁺/calmodulin-dependent protein kinase II within post-synaptic dendritic spines of cultured hippocampal neurons". J. Biol. Chem. 275 (35): 27165–71. doi:10.1074/jbc.M003751200. PMID 10852918.
• Nair JS, DaFonseca CJ, Tjernberg A; et al. (2002). "Requirement of Ca²⁺ and CaMKII for Stat1 Ser-727 phosphorylation in response to IFN-gamma". Proc. Natl. Acad. Sci. U.S.A. 99 (9): 5971–6. doi:10.1073/pnas.052159099. PMC 122886. PMID 11972023.
• Mishra-Gorur K, Singer HA, Castellot JJ (2002). "The S18 ribosomal protein is a putative substrate for Ca²⁺/calmodulin-activated protein kinase II". J. Biol. Chem. 277 (37): 33537–40. doi:10.1074/jbc.C200342200. PMID 12145273.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Gaertner TR, Kolodziej SJ, Wang D; et al. (2004). "Comparative analyses of the three-dimensional structures and enzymatic properties of alpha, beta, gamma and delta isoforms of Ca²⁺-calmodulin-dependent protein kinase II". J. Biol. Chem. 279 (13): 12484–94. doi:10.1074/jbc.M313597200. PMID 14722083.
• Ballif BA, Villén J, Beausoleil SA; et al. (2005). "Phosphoproteomic analysis of the developing mouse brain". Mol. Cell Proteomics 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.