CAMK2D

From Wikipedia, the free encyclopedia

Calcium/calmodulin-dependent protein kinase (CaM kinase) II delta

Identifiers

CAMK2D; CAMKD; MGC44911

External IDs

OMIM: 607708 MGI: 1341265 HomoloGene: 55561

Gene ontology
Molecular Function:	• nucleotide binding • protein serine/threonine kinase activity • calmodulin-dependent protein kinase activity • calmodulin binding • ATP binding • transferase activity
Cellular Component:	• calcium- and calmodulin-dependent protein kinase complex
Biological Process:	• G1/S transition of mitotic cell cycle • regulation of cell growth • protein amino acid phosphorylation • calcium ion transport • protein amino acid autophosphorylation

Orthologs

Human

Mouse

n/a

Refseq

NM_001221 (mRNA)
NP_001212 (protein)

NM_001025438 (mRNA)
NP_001020609 (protein)

Location

Chr 4: 114.59 - 114.9 Mb

Chr 3: 126.59 - 126.84 Mb

Pubmed search

[1]

[2]

Calcium/calmodulin-dependent protein kinase (CaM kinase) II delta, also known as CAMK2D, is a human 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 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]

[edit] References

^ ^a ^b Entrez Gene: CAMK2D calcium/calmodulin-dependent protein kinase (CaM kinase) II delta.

[edit] 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.
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.
Tombes RM, Krystal GW (1997). "Identification of novel human tumor cell-specific CaMK-II variants.". Biochim. Biophys. Acta 1355 (3): 281–92. 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. 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. 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. PMID 9692886.
"Toward a complete human genome sequence." (1999). Genome Res. 8 (11): 1097–108. 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. 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. 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. 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. 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. 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.