CAMK2D

CAMK2D
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2VN9, 2W2C, 2WEL, 3GP2
Identifiers
Aliases	CAMK2D, CAMKD, calcium/calmodulin dependent protein kinase II delta
External IDs	OMIM: 607708; MGI: 1341265; HomoloGene: 55561; GeneCards: CAMK2D; OMA:CAMK2D - orthologs
Gene location (Human) Chr. Chromosome 4 (human) Band 4q26 Start 113,418,054 bp End 113,761,927 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 G1- G2 Start 126,389,951 bp End 126,639,975 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in myocardium of left ventricle lateral nuclear group of thalamus cardiac muscle tissue of right atrium middle temporal gyrus Brodmann area 23 right ventricle entorhinal cortex tibialis anterior muscle deltoid muscle endothelial cell Top expressed in anterior amygdaloid area neural layer of retina lobe of cerebellum cerebellar vermis lateral septal nucleus medial geniculate nucleus dorsomedial hypothalamic nucleus atrium lateral hypothalamus ventral tegmental area More reference expression data BioGPS n/a
Gene ontology Molecular function kinase activity ATP binding protein kinase activity titin binding transferase activity protein homodimerization activity protein binding nucleotide binding sodium channel inhibitor activity calmodulin-dependent protein kinase activity protein serine/threonine kinase activity transmembrane transporter binding calmodulin binding identical protein binding Cellular component endocytic vesicle membrane membrane sarcoplasmic reticulum membrane plasma membrane nucleoplasm sarcoplasmic reticulum sarcolemma neuron projection nucleus cytoplasm cytosol calcium channel complex Biological process regulation of heart contraction interferon-gamma-mediated signaling pathway regulation of transcription by RNA polymerase II regulation of membrane depolarization positive regulation of cardiac muscle hypertrophy protein phosphorylation cellular response to calcium ion regulation of cardiac muscle cell action potential involved in regulation of contraction regulation of histone deacetylase activity regulation of cellular localization negative regulation of sodium ion transmembrane transport phosphorylation regulation of the force of heart contraction regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion regulation of ryanodine-sensitive calcium-release channel activity negative regulation of sodium ion transmembrane transporter activity MAPK cascade protein complex oligomerization regulation of cell growth regulation of cellular response to heat regulation of cell communication by electrical coupling involved in cardiac conduction regulation of heart rate by cardiac conduction nervous system development cell differentiation 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 peptidyl-serine phosphorylation peptidyl-threonine phosphorylation endoplasmic reticulum calcium ion homeostasis protein autophosphorylation relaxation of cardiac muscle cardiac muscle cell contraction regulation of cardiac muscle cell action potential regulation of relaxation of cardiac muscle regulation of calcium ion transmembrane transport via high voltage-gated calcium channel Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 817 108058 Ensembl ENSG00000145349 ENSMUSG00000053819 UniProt Q13557 Q6PHZ2 RefSeq (mRNA) NM_001221 NM_172114 NM_172115 NM_172127 NM_172128 NM_172129 NM_001321566 NM_001321567 NM_001321568 NM_001321569 NM_001321570 NM_001321571 NM_001321572 NM_001321573 NM_001321574 NM_001321575 NM_001321576 NM_001321577 NM_001321578 NM_001321579 NM_001321580 NM_001321581 NM_001321582 NM_001321583 NM_001321584 NM_001321585 NM_001321586 NM_001321587 NM_001321588 NM_001321589 NM_001321590 NM_001321591 NM_001321592 NM_001396964 NM_001396965 NM_001396966 NM_001396967 NM_001399855 NM_001399856 NM_001399857 NM_001399858 NM_001399859 NM_001399860 NM_001399861 NM_001399862 NM_001399863 NM_001399864 NM_001399865 NM_001025438 NM_001025439 NM_001293663 NM_001293664 NM_001293665 NM_001293666 NM_023813 NM_001346635 NM_001346636 RefSeq (protein) NP_001212 NP_001308495 NP_001308496 NP_001308497 NP_001308498 NP_001308499 NP_001308500 NP_001308501 NP_001308502 NP_001308503 NP_001308504 NP_001308505 NP_001308506 NP_001308507 NP_001308508 NP_001308509 NP_001308510 NP_001308511 NP_001308512 NP_001308513 NP_001308514 NP_001308515 NP_001308516 NP_001308517 NP_001308518 NP_001308519 NP_001308520 NP_001308521 NP_742112 NP_742113 NP_742125 NP_742126 NP_742127 NP_001020609 NP_001020610 NP_001280592 NP_001280593 NP_001280594 NP_001280595 NP_001333564 NP_001333565 NP_076302 Location (UCSC) Chr 4: 113.42 – 113.76 Mb Chr 3: 126.39 – 126.64 Mb PubMed search
Wikidata
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Calcium/calmodulin-dependent protein kinase type II delta chain is an enzyme that in humans is encoded by the CAMK2D gene.

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.

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. 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.

External links

• Human CAMK2D genome location and CAMK2D gene details page in the UCSC Genome Browser.