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Contents

   



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1 References  





2 Further reading  





3 External links  














CAMK2D






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From Wikipedia, the free encyclopedia
 


CAMK2D
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCAMK2D, CAMKD, calcium/calmodulin dependent protein kinase II delta
External IDsOMIM: 607708; MGI: 1341265; HomoloGene: 55561; GeneCards: CAMK2D; OMA:CAMK2D - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)Chr 4: 113.42 – 113.76 MbChr 3: 126.39 – 126.64 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Calcium/calmodulin-dependent protein kinase type II delta chain is an enzyme that in humans is encoded by the CAMK2D gene.[5]

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 plasticityatglutamatergic 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.[5]

References

[edit]
  • ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ a b "Entrez Gene: CAMK2D calcium/calmodulin-dependent protein kinase (CaM kinase) II delta".
  • Further reading

    [edit]
  • 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. doi:10.1002/j.1460-2075.1993.tb06068.x. 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/endo.138.6.5168. 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.
  • Sanger Centre, The; Washington University Genome Sequencing Cente, The (1999). "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. 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. Bibcode:2002PNAS...99.5971N. 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. Bibcode:2002PNAS...9916899M. 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.
  • [edit]


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    This page was last edited on 13 October 2022, at 06:01 (UTC).

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