CAMK2B

CAMK2B
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3BHH
Identifiers
Aliases	CAMK2B, CAM2, CAMK2, CAMKB, calcium/calmodulin dependent protein kinase II beta, MRD54, CaMKIIbeta
External IDs	OMIM: 607707; MGI: 88257; HomoloGene: 111050; GeneCards: CAMK2B; OMA:CAMK2B - orthologs
Gene location (Human)
Chr.	Chromosome 7 (human)
End	44,334,577 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	6,016,362 bp
RNA expression pattern
	Top expressed in
	cerebellar cortex; ; cerebellar hemisphere; ; right hemisphere of cerebellum; ; cerebellar vermis; ; lateral nuclear group of thalamus; ; paraflocculus of cerebellum; ; nucleus accumbens; ; parietal lobe; ; Brodmann area 9; ; right frontal lobe;
	Top expressed in
	dentate gyrus of hippocampal formation granule cell; ; CA3 field; ; superior frontal gyrus; ; primary visual cortex; ; entorhinal cortex; ; olfactory tubercle; ; perirhinal cortex; ; cerebellar cortex; ; hippocampus proper; ; nucleus accumbens;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	transferase activity; nucleotide binding; protein kinase activity; protein homodimerization activity; kinase activity; protein binding; actin binding; ATP binding; protein serine/threonine kinase activity; calmodulin-dependent protein kinase activity; calmodulin binding; identical protein binding;
Cellular component	endocytic vesicle membrane; cytosol; membrane; plasma membrane; nucleoplasm; microtubule organizing center; sarcoplasmic reticulum membrane; sarcoplasmic reticulum; cytoskeleton; cytoplasm; neuron projection; cell junction; synapse;
Biological process	cell differentiation; regulation of synapse structural plasticity; regulation of calcium ion transport; regulation of long-term neuronal synaptic plasticity; interferon-gamma-mediated signaling pathway; phosphorylation; nervous system development; MAPK cascade; multicellular organism development; positive regulation of synapse maturation; protein phosphorylation; positive regulation of neuron projection development; protein autophosphorylation; regulation of skeletal muscle adaptation; positive regulation of dendritic spine morphogenesis; regulation of dendritic spine development; signal transduction; peptidyl-serine phosphorylation; peptidyl-threonine phosphorylation; intracellular signal transduction; regulation of neuron migration; regulation of cellular response to heat;
	Sources:Amigo / QuickGO
Orthologs
	816
	12323
	ENSG00000058404
	ENSMUSG00000057897
	Q13554
	P28652
NM_001220; NM_001293170; NM_172078; NM_172079; NM_172080;
	NM_172081; NM_172082; NM_172083; NM_172084
	NM_001174053; NM_001174054; NM_007595
NP_001211; NP_001280099; NP_742075; NP_742076; NP_742077;
	NP_742078; NP_742079; NP_742080; NP_742081
	NP_001167524; NP_001167525; NP_031621
	Wikidata
View/Edit Human	View/Edit Mouse

Calcium/calmodulin-dependent protein kinase type II beta chain is an enzyme that in humans is encoded by the CAMK2B gene.

Function

The enzyme belongs to the serine/threonine protein kinase family and to the Ca²⁺/calmodulin-dependent protein kinase subfamily. Calcium signalling 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 beta chain. It is possible that distinct isoforms of this chain have different cellular localizations and interact differently with calmodulin. Eight transcript variants encoding eight distinct isoforms have been identified for this gene.^[5]

Interactions

CAMK2B has been shown to interact with Actinin alpha 4.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000058404 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000057897 – Ensembl, May 2017
^ "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.
^ "Entrez Gene: CAMK2B calcium/calmodulin-dependent protein kinase (CaM kinase) II beta".
^ Walikonis RS, Oguni A, Khorosheva EM, Jeng CJ, Asuncion FJ, Kennedy MB (Jan 2001). "Densin-180 forms a ternary complex with the (alpha)-subunit of Ca2+/calmodulin-dependent protein kinase II and (alpha)-actinin". J. Neurosci. 21 (2): 423–33. doi:10.1523/JNEUROSCI.21-02-00423.2001. PMC 6763799. PMID 11160423.

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.
Thiel G, Czernik AJ, Gorelick F, Nairn AC, Greengard P (1988). "Ca2+/calmodulin-dependent protein kinase II: identification of threonine-286 as the autophosphorylation site in the alpha subunit associated with the generation of Ca2+-independent activity". Proc. Natl. Acad. Sci. U.S.A. 85 (17): 6337–41. Bibcode:1988PNAS...85.6337T. doi:10.1073/pnas.85.17.6337. PMC 281965. PMID 2842767.
Schworer CM, Colbran RJ, Keefer JR, Soderling TR (1988). "Ca2+/calmodulin-dependent protein kinase II. Identification of a regulatory autophosphorylation site adjacent to the inhibitory and calmodulin-binding domains". J. Biol. Chem. 263 (27): 13486–9. doi:10.1016/S0021-9258(18)68264-X. PMID 3417668.
Penadés JR, Bernal D, Revert F, Johansson C, Fresquet VJ, Cervera J, Wieslander J, Quinones S, Saus J (1995). "Characterization and expression of multiple alternatively spliced transcripts of the Goodpasture antigen gene region. Goodpasture antibodies recognize recombinant proteins representing the autoantigen and one of its alternative forms". Eur. J. Biochem. 229 (3): 754–60. doi:10.1111/j.1432-1033.1995.tb20524.x. PMID 7758473.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Omkumar RV, Kiely MJ, Rosenstein AJ, Min KT, Kennedy MB (1997). "Identification of a phosphorylation site for calcium/calmodulindependent protein kinase II in the NR2B subunit of the N-methyl-D-aspartate receptor". J. Biol. Chem. 271 (49): 31670–8. doi:10.1074/jbc.271.49.31670. PMID 8940188.
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.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Chang BH, Mukherji S, Soderling TR (1998). "Characterization of a calmodulin kinase II inhibitor protein in brain". Proc. Natl. Acad. Sci. U.S.A. 95 (18): 10890–5. Bibcode:1998PNAS...9510890C. doi:10.1073/pnas.95.18.10890. PMC 27991. PMID 9724800.
Rochlitz H, Voigt A, Lankat-Buttgereit B, Göke B, Heimberg H, Nauck MA, Schiemann U, Schatz H, Pfeiffer AF (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.
Wang P, Wu YL, Zhou TH, Sun Y, Pei G (2000). "Identification of alternative splicing variants of the beta subunit of human Ca(2+)/calmodulin-dependent protein kinase II with different activities". FEBS Lett. 475 (2): 107–10. doi:10.1016/S0014-5793(00)01634-3. PMID 10858498. S2CID 39732332.
Novak G, Seeman P, Tallerico T (2001). "Schizophrenia: elevated mRNA for calcium-calmodulin-dependent protein kinase IIbeta in frontal cortex". Brain Res. Mol. Brain Res. 82 (1–2): 95–100. doi:10.1016/S0169-328X(00)00188-1. PMID 11042361.
Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Walikonis RS, Oguni A, Khorosheva EM, Jeng CJ, Asuncion FJ, Kennedy MB (2001). "Densin-180 forms a ternary complex with the (alpha)-subunit of Ca2+/calmodulin-dependent protein kinase II and (alpha)-actinin". J. Neurosci. 21 (2): 423–33. doi:10.1523/JNEUROSCI.21-02-00423.2001. PMC 6763799. PMID 11160423.
Liao GY, Wagner DA, Hsu MH, Leonard JP (2001). "Evidence for direct protein kinase-C mediated modulation of N-methyl-D-aspartate receptor current". Mol. Pharmacol. 59 (5): 960–4. doi:10.1124/mol.59.5.960. PMID 11306676.
Yue C, Sanborn BM (2001). "KN-93 inhibition of G protein signaling is independent of the ability of Ca2+/calmodulin-dependent protein kinase II to phosphorylate phospholipase Cbeta3 on 537-Ser". Mol. Cell. Endocrinol. 175 (1–2): 149–56. doi:10.1016/S0303-7207(01)00383-5. PMID 11325525. S2CID 338776.
Schell MJ, Erneux C, Irvine RF (2001). "Inositol 1,4,5-trisphosphate 3-kinase A associates with F-actin and dendritic spines via its N terminus". J. Biol. Chem. 276 (40): 37537–46. doi:10.1074/jbc.M104101200. PMID 11468283.
Li G, Laabich A, Liu LO, Xue J, Cooper NG (2002). "Molecular cloning and sequence analyses of calcium/calmodulin-dependent protein kinase II from fetal and adult human brain. Sequence analyses of human brain calcium/calmodulin-dependent protein kinase II". Mol. Biol. Rep. 28 (1): 35–41. doi:10.1023/A:1011951814898. PMID 11710563. S2CID 22670733.
Poggi A, Carosio R, Spaggiari GM, Fortis C, Tambussi G, Dell'Antonio G, Dal Cin E, Rubartelli A, Zocchi MR (2002). "NK cell activation by dendritic cells is dependent on LFA-1-mediated induction of calcium-calmodulin kinase II: inhibition by HIV-1 Tat C-terminal domain". J. Immunol. 168 (1): 95–101. doi:10.4049/jimmunol.168.1.95. PMID 11751951.

External links

Human CAMK2B genome location and CAMK2B gene details page in the UCSC Genome Browser.

This article on a gene on human chromosome 7 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000058404 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000057897 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: CAMK2B calcium/calmodulin-dependent protein kinase (CaM kinase) II beta".

[pmid11160423-6] Walikonis RS, Oguni A, Khorosheva EM, Jeng CJ, Asuncion FJ, Kennedy MB (Jan 2001). "Densin-180 forms a ternary complex with the (alpha)-subunit of Ca2+/calmodulin-dependent protein kinase II and (alpha)-actinin". J. Neurosci. 21 (2): 423–33. doi:10.1523/JNEUROSCI.21-02-00423.2001. PMC 6763799. PMID 11160423.

[1]

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Function

Interactions

References

Further reading

External links