Developer site: The content shown here is test data.

MyEClinic
MyEClinic
Health Dictionary AI Health Chat Find an Online Doctor
A serene Zen garden with raked sand and smooth stones, symbolising clarity and calm

Health Dictionary

Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

Back to skin conditions

CAMK2B

Introduction

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

Function

Function

The product of this gene 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.[1]

Interactions

Interactions

CAMK2B has been shown to interact with Actinin alpha 4.[2]

References

References

  1. ↑ “Entrez Gene: CAMK2B calcium/calmodulin-dependent protein kinase (CaM kinase) II beta”.
  2. ↑ 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. PMID 11160423.
Further reading

Further reading

  • 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. 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. 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. 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.
  • 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. 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. 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.
  • 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.
  • 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