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Calcium/calmodulin-dependent protein kinase type II subunit alpha

December 01, 2023

Calcium/calmodulin-dependent protein kinase type II subunit alpha (CAMKIIα), a.k.a. Ca2+/calmodulin-dependent protein kinase II alpha, is one subunit of CamKII, a protein kinase (i.e., an enzyme which phosphorylates proteins) that in humans is encoded by the CAMK2A gene.[5][6]

CAMK2A
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCAMK2A, CAMKA, calcium/calmodulin dependent protein kinase II alpha, MRD53, CaMKIINalpha, MRT63, CaMKIIalpha
External IDsOMIM: 114078 MGI: 88256 HomoloGene: 56577 GeneCards: CAMK2A
Orthologs
SpeciesHumanMouse
Entrez

815

12322

Ensembl

ENSG00000070808

ENSMUSG00000024617

UniProt

Q9UQM7

P11798

RefSeq (mRNA)

NM_171825
NM_015981
NM_001363989
NM_001363990
NM_001369025

NM_001286809
NM_009792
NM_177407

RefSeq (protein)

NP_057065
NP_741960
NP_001350918
NP_001350919
NP_001355954

NP_001273738
NP_033922
NP_803126
NP_001390238
NP_001390241

Location (UCSC)Chr 5: 150.22 – 150.29 MbChr 18: 61.06 – 61.12 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function edit

The product of the CAMK2A gene is an enzyme that belongs to the serine/threonine-specific protein kinase family, as well as the Ca2+/calmodulin-dependent protein kinase II subfamily. Ca2+ signaling is crucial for several aspects of synaptic plasticity at glutamatergic synapses. This enzyme is composed of four different chains: alpha, beta, gamma, and delta. The alpha chain encoded by this gene is required for hippocampal long-term potentiation (LTP) and spatial learning.[citation needed] In addition to its calcium-calmodulin (CaM)-dependent activity, this protein can undergo autophosphorylation, resulting in CaM-independent activity. Two transcript variants encoding distinct isoforms have been identified for this gene.[7] According to a 2018 study by Bruno Reversade, the recessive mutation of CAMK2A in humans cause a syndrome of severe intellectual disability with growth retardation.[8]

Interactions edit

CAMK2A has been shown to interact with:

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000070808 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024617 - 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.
  5. ^ Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, et al. (February 1999). "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 6 (1): 63–70. doi:10.1093/dnares/6.1.63. PMID 10231032.
  6. ^ Lin CR, Kapiloff MS, Durgerian S, Tatemoto K, Russo AF, Hanson P, et al. (August 1987). "Molecular cloning of a brain-specific calcium/calmodulin-dependent protein kinase". Proceedings of the National Academy of Sciences of the United States of America. 84 (16): 5962–6. Bibcode:1987PNAS...84.5962L. doi:10.1073/pnas.84.16.5962. PMC 298983. PMID 3475713.
  7. ^ "Entrez Gene: CAMK2A calcium/calmodulin-dependent protein kinase (CaM kinase) II alpha".
  8. ^ Chia PH, Zhong FL, Niwa S, Bonnard C, Utami KH, Zeng R, et al. (May 2018). "A homozygous loss-of-function CAMK2A mutation causes growth delay, frequent seizures and severe intellectual disability". eLife. 7. doi:10.7554/eLife.32451. PMC 5963920. PMID 29784083.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  9. ^ Walikonis RS, Oguni A, Khorosheva EM, Jeng CJ, Asuncion FJ, Kennedy MB (January 2001). "Densin-180 forms a ternary complex with the (alpha)-subunit of Ca2+/calmodulin-dependent protein kinase II and (alpha)-actinin". The Journal of Neuroscience. 21 (2): 423–33. doi:10.1523/JNEUROSCI.21-02-00423.2001. PMC 6763799. PMID 11160423.
  10. ^ Dhavan R, Greer PL, Morabito MA, Orlando LR, Tsai LH (September 2002). "The cyclin-dependent kinase 5 activators p35 and p39 interact with the alpha-subunit of Ca2+/calmodulin-dependent protein kinase II and alpha-actinin-1 in a calcium-dependent manner". The Journal of Neuroscience. 22 (18): 7879–91. doi:10.1523/JNEUROSCI.22-18-07879.2002. PMC 6758084. PMID 12223541.
  11. ^ Gardoni F, Mauceri D, Fiorentini C, Bellone C, Missale C, Cattabeni F, Di Luca M (November 2003). "CaMKII-dependent phosphorylation regulates SAP97/NR2A interaction". The Journal of Biological Chemistry. 278 (45): 44745–52. doi:10.1074/jbc.M303576200. PMID 12933808. S2CID 19885326.

Further reading edit

  • Soderling TR (June 2000). "CaM-kinases: modulators of synaptic plasticity". Current Opinion in Neurobiology. 10 (3): 375–80. doi:10.1016/S0959-4388(00)00090-8. PMID 10851169. S2CID 31122499.
  • Hook SS, Means AR (2001). "Ca(2+)/CaM-dependent kinases: from activation to function". Annual Review of Pharmacology and Toxicology. 41 (1): 471–505. doi:10.1146/annurev.pharmtox.41.1.471. PMID 11264466.
  • Yamamoto H (March 2002). "[Molecular mechanisms of the intracellular localizations of Ca2+/calmodulin-dependent protein kinase II isoforms, and their physiological functions]". Tanpakushitsu Kakusan Koso. Protein, Nucleic Acid, Enzyme. 47 (3): 241–7. PMID 11889801.
  • Countaway JL, Nairn AC, Davis RJ (January 1992). "Mechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase". The Journal of Biological Chemistry. 267 (2): 1129–40. doi:10.1016/S0021-9258(18)48406-2. PMID 1309762.
  • Wegner M, Cao Z, Rosenfeld MG (April 1992). "Calcium-regulated phosphorylation within the leucine zipper of C/EBP beta". Science. 256 (5055): 370–3. Bibcode:1992Sci...256..370W. doi:10.1126/science.256.5055.370. PMID 1314426. S2CID 34818876.
  • Omary MB, Baxter GT, Chou CF, Riopel CL, Lin WY, Strulovici B (May 1992). "PKC epsilon-related kinase associates with and phosphorylates cytokeratin 8 and 18". The Journal of Cell Biology. 117 (3): 583–93. doi:10.1083/jcb.117.3.583. PMC 2289443. PMID 1374067.
  • Bredt DS, Ferris CD, Snyder SH (June 1992). "Nitric oxide synthase regulatory sites. Phosphorylation by cyclic AMP-dependent protein kinase, protein kinase C, and calcium/calmodulin protein kinase; identification of flavin and calmodulin binding sites". The Journal of Biological Chemistry. 267 (16): 10976–81. doi:10.1016/S0021-9258(19)49862-1. PMID 1375933.
  • Tokui T, Yamauchi T, Yano T, Nishi Y, Kusagawa M, Yatani R, Inagaki M (June 1990). "Ca2(+)-calmodulin-dependent protein kinase II phosphorylates various types of non-epithelial intermediate filament proteins". Biochemical and Biophysical Research Communications. 169 (3): 896–904. doi:10.1016/0006-291X(90)91977-Z. PMID 2114109.
  • Inagaki M, Gonda Y, Nishizawa K, Kitamura S, Sato C, Ando S, et al. (March 1990). "Phosphorylation sites linked to glial filament disassembly in vitro locate in a non-alpha-helical head domain". The Journal of Biological Chemistry. 265 (8): 4722–9. doi:10.1016/S0021-9258(19)39622-X. PMID 2155236.
  • Ohta Y, Ohba T, Miyamoto E (July 1990). "Ca2+/calmodulin-dependent protein kinase II: localization in the interphase nucleus and the mitotic apparatus of mammalian cells". Proceedings of the National Academy of Sciences of the United States of America. 87 (14): 5341–5. Bibcode:1990PNAS...87.5341O. doi:10.1073/pnas.87.14.5341. PMC 54319. PMID 2164678.
  • Lee RH, Brown BM, Lolley RN (September 1990). "Protein kinase A phosphorylates retinal phosducin on serine 73 in situ". The Journal of Biological Chemistry. 265 (26): 15860–6. doi:10.1016/S0021-9258(18)55478-8. PMID 2394752.
  • Ku NO, Omary MB (October 1994). "Identification of the major physiologic phosphorylation site of human keratin 18: potential kinases and a role in filament reorganization". The Journal of Cell Biology. 127 (1): 161–71. doi:10.1083/jcb.127.1.161. PMC 2120194. PMID 7523419.
  • Drewes G, Trinczek B, Illenberger S, Biernat J, Schmitt-Ulms G, Meyer HE, et al. (March 1995). "Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262". The Journal of Biological Chemistry. 270 (13): 7679–88. doi:10.1074/jbc.270.13.7679. PMID 7706316. S2CID 2039456.
  • Tsujimura K, Tanaka J, Ando S, Matsuoka Y, Kusubata M, Sugiura H, et al. (August 1994). "Identification of phosphorylation sites on glial fibrillary acidic protein for cdc2 kinase and Ca(2+)-calmodulin-dependent protein kinase II". Journal of Biochemistry. 116 (2): 426–34. doi:10.1093/oxfordjournals.jbchem.a124542. PMID 7822264.
  • Toyofuku T, Curotto Kurzydlowski K, Narayanan N, MacLennan DH (October 1994). "Identification of Ser38 as the site in cardiac sarcoplasmic reticulum Ca(2+)-ATPase that is phosphorylated by Ca2+/calmodulin-dependent protein kinase". The Journal of Biological Chemistry. 269 (42): 26492–6. doi:10.1016/S0021-9258(18)47221-3. PMID 7929371.
  • Rivera VM, Miranti CK, Misra RP, Ginty DD, Chen RH, Blenis J, Greenberg ME (October 1993). "A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity". Molecular and Cellular Biology. 13 (10): 6260–73. doi:10.1128/mcb.13.10.6260. PMC 364685. PMID 8413226.
  • Omkumar RV, Kiely MJ, Rosenstein AJ, Min KT, Kennedy MB (December 1996). "Identification of a phosphorylation site for calcium/calmodulindependent protein kinase II in the NR2B subunit of the N-methyl-D-aspartate receptor". The Journal of Biological Chemistry. 271 (49): 31670–8. doi:10.1074/jbc.271.49.31670. PMID 8940188. S2CID 8332020.
  • Rotenberg A, Mayford M, Hawkins RD, Kandel ER, Muller RU (December 1996). "Mice expressing activated CaMKII lack low frequency LTP and do not form stable place cells in the CA1 region of the hippocampus". Cell. 87 (7): 1351–61. doi:10.1016/S0092-8674(00)81829-2. PMID 8980240. S2CID 16704390.
  • Paudel HK (January 1997). "The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase". The Journal of Biological Chemistry. 272 (3): 1777–85. doi:10.1016/S0021-9258(19)67481-8. PMID 8999860.

External links edit


 

This article on a gene on human chromosome 5 is a stub. You can help Wikipedia by expanding it.

December 01, 2023
calcium, calmodulin, dependent, protein, kinase, type, subunit, alpha, camkiiα, calmodulin, dependent, protein, kinase, alpha, subunit, camkii, protein, kinase, enzyme, which, phosphorylates, proteins, that, humans, encoded, camk2a, gene, camk2aavailable, stru. Calcium calmodulin dependent protein kinase type II subunit alpha CAMKIIa a k a Ca2 calmodulin dependent protein kinase II alpha is one subunit of CamKII a protein kinase i e an enzyme which phosphorylates proteins that in humans is encoded by the CAMK2A gene 5 6 CAMK2AAvailable structuresPDBOrtholog search PDBe RCSBList of PDB id codes2VZ6 3SOA 5IG3IdentifiersAliasesCAMK2A CAMKA calcium calmodulin dependent protein kinase II alpha MRD53 CaMKIINalpha MRT63 CaMKIIalphaExternal IDsOMIM 114078 MGI 88256 HomoloGene 56577 GeneCards CAMK2AGene location Human Chr Chromosome 5 human 1 Band5q32Start150 219 491 bp 1 End150 290 093 bp 1 Gene location Mouse Chr Chromosome 18 mouse 2 Band18 E1 18 34 41 cMStart61 058 690 bp 2 End61 121 224 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inamygdalaprefrontal cortexRegion I of hippocampus properBrodmann area 9cingulate gyrusfrontal poleorbitofrontal cortexBrodmann area 46Brodmann area 10nucleus accumbensTop expressed insuperior frontal gyrusolfactory tuberclepiriform cortexsubiculumprimary motor cortexnucleus accumbensentorhinal cortexRegion I of hippocampus propertriceps brachii musclemedial geniculate nucleusMore reference expression dataBioGPSn aGene ontologyMolecular functiontransferase activity nucleotide binding protein kinase activity protein homodimerization activity kinase activity protein binding glutamate receptor binding ATP binding metal ion binding protein serine threonine kinase activity calmodulin binding calmodulin dependent protein kinase activity calcium dependent protein serine threonine kinase activity identical protein bindingCellular componentendocytic vesicle membrane cytosol membrane plasma membrane synapse nucleoplasm cell junction presynaptic membrane nucleus cytoplasm mitochondrion postsynaptic density neuron projection calcium and calmodulin dependent protein kinase complex dendrite cell projection dendritic spine postsynaptic membrane Schaffer collateral CA1 synapseBiological processphosphorylation interferon gamma mediated signaling pathway G1 phase angiotensin activated signaling pathway positive regulation of cardiac muscle cell apoptotic process regulation of neurotransmitter secretion regulation of mitochondrial membrane permeability involved in apoptotic process MAPK cascade response to ischemia positive regulation of NF kappaB transcription factor activity regulation of cellular response to heat regulation of neuronal synaptic plasticity protein autophosphorylation calcium ion transport positive regulation of calcium ion transport dendrite morphogenesis Wnt signaling pathway calcium modulating pathway nervous system development peptidyl serine phosphorylation peptidyl threonine phosphorylation cell differentiation intracellular signal transduction protein phosphorylation G1 S transition of mitotic cell cycle dendritic spine development regulation of synaptic vesicle docking peptidyl threonine autophosphorylation regulation of neuron migrationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez81512322EnsemblENSG00000070808ENSMUSG00000024617UniProtQ9UQM7P11798RefSeq mRNA NM 171825NM 015981NM 001363989NM 001363990NM 001369025NM 001286809NM 009792NM 177407RefSeq protein NP 057065NP 741960NP 001350918NP 001350919NP 001355954NP 001273738NP 033922NP 803126NP 001390238NP 001390241Location UCSC Chr 5 150 22 150 29 MbChr 18 61 06 61 12 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 Interactions 3 References 4 Further reading 5 External linksFunction editThe product of the CAMK2A gene is an enzyme that belongs to the serine threonine specific protein kinase family as well as the Ca2 calmodulin dependent protein kinase II subfamily Ca2 signaling is crucial for several aspects of synaptic plasticity at glutamatergic synapses This enzyme is composed of four different chains alpha beta gamma and delta The alpha chain encoded by this gene is required for hippocampal long term potentiation LTP and spatial learning citation needed In addition to its calcium calmodulin CaM dependent activity this protein can undergo autophosphorylation resulting in CaM independent activity Two transcript variants encoding distinct isoforms have been identified for this gene 7 According to a 2018 study by Bruno Reversade the recessive mutation of CAMK2A in humans cause a syndrome of severe intellectual disability with growth retardation 8 Interactions editCAMK2A has been shown to interact with Actinin alpha 4 9 CDK5R1 10 and DLG1 11 References edit a b c GRCh38 Ensembl release 89 ENSG00000070808 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000024617 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 Nagase T Ishikawa K Suyama M Kikuno R Hirosawa M Miyajima N et al February 1999 Prediction of the coding sequences of unidentified human genes XIII The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro DNA Research 6 1 63 70 doi 10 1093 dnares 6 1 63 PMID 10231032 Lin CR Kapiloff MS Durgerian S Tatemoto K Russo AF Hanson P et al August 1987 Molecular cloning of a brain specific calcium calmodulin dependent protein kinase Proceedings of the National Academy of Sciences of the United States of America 84 16 5962 6 Bibcode 1987PNAS 84 5962L doi 10 1073 pnas 84 16 5962 PMC 298983 PMID 3475713 Entrez Gene CAMK2A calcium calmodulin dependent protein kinase CaM kinase II alpha Chia PH Zhong FL Niwa S Bonnard C Utami KH Zeng R et al May 2018 A homozygous loss of function CAMK2A mutation causes growth delay frequent seizures and severe intellectual disability eLife 7 doi 10 7554 eLife 32451 PMC 5963920 PMID 29784083 a href Template Cite journal html title Template Cite journal cite journal a CS1 maint unflagged free DOI link Walikonis RS Oguni A Khorosheva EM Jeng CJ Asuncion FJ Kennedy MB January 2001 Densin 180 forms a ternary complex with the alpha subunit of Ca2 calmodulin dependent protein kinase II and alpha actinin The Journal of Neuroscience 21 2 423 33 doi 10 1523 JNEUROSCI 21 02 00423 2001 PMC 6763799 PMID 11160423 Dhavan R Greer PL Morabito MA Orlando LR Tsai LH September 2002 The cyclin dependent kinase 5 activators p35 and p39 interact with the alpha subunit of Ca2 calmodulin dependent protein kinase II and alpha actinin 1 in a calcium dependent manner The Journal of Neuroscience 22 18 7879 91 doi 10 1523 JNEUROSCI 22 18 07879 2002 PMC 6758084 PMID 12223541 Gardoni F Mauceri D Fiorentini C Bellone C Missale C Cattabeni F Di Luca M November 2003 CaMKII dependent phosphorylation regulates SAP97 NR2A interaction The Journal of Biological Chemistry 278 45 44745 52 doi 10 1074 jbc M303576200 PMID 12933808 S2CID 19885326 Further reading editSoderling TR June 2000 CaM kinases modulators of synaptic plasticity Current Opinion in Neurobiology 10 3 375 80 doi 10 1016 S0959 4388 00 00090 8 PMID 10851169 S2CID 31122499 Hook SS Means AR 2001 Ca 2 CaM dependent kinases from activation to function Annual Review of Pharmacology and Toxicology 41 1 471 505 doi 10 1146 annurev pharmtox 41 1 471 PMID 11264466 Yamamoto H March 2002 Molecular mechanisms of the intracellular localizations of Ca2 calmodulin dependent protein kinase II isoforms and their physiological functions Tanpakushitsu Kakusan Koso Protein Nucleic Acid Enzyme 47 3 241 7 PMID 11889801 Countaway JL Nairn AC Davis RJ January 1992 Mechanism of desensitization of the epidermal growth factor receptor protein tyrosine kinase The Journal of Biological Chemistry 267 2 1129 40 doi 10 1016 S0021 9258 18 48406 2 PMID 1309762 Wegner M Cao Z Rosenfeld MG April 1992 Calcium regulated phosphorylation within the leucine zipper of C EBP beta Science 256 5055 370 3 Bibcode 1992Sci 256 370W doi 10 1126 science 256 5055 370 PMID 1314426 S2CID 34818876 Omary MB Baxter GT Chou CF Riopel CL Lin WY Strulovici B May 1992 PKC epsilon related kinase associates with and phosphorylates cytokeratin 8 and 18 The Journal of Cell Biology 117 3 583 93 doi 10 1083 jcb 117 3 583 PMC 2289443 PMID 1374067 Bredt DS Ferris CD Snyder SH June 1992 Nitric oxide synthase regulatory sites Phosphorylation by cyclic AMP dependent protein kinase protein kinase C and calcium calmodulin protein kinase identification of flavin and calmodulin binding sites The Journal of Biological Chemistry 267 16 10976 81 doi 10 1016 S0021 9258 19 49862 1 PMID 1375933 Tokui T Yamauchi T Yano T Nishi Y Kusagawa M Yatani R Inagaki M June 1990 Ca2 calmodulin dependent protein kinase II phosphorylates various types of non epithelial intermediate filament proteins Biochemical and Biophysical Research Communications 169 3 896 904 doi 10 1016 0006 291X 90 91977 Z PMID 2114109 Inagaki M Gonda Y Nishizawa K Kitamura S Sato C Ando S et al March 1990 Phosphorylation sites linked to glial filament disassembly in vitro locate in a non alpha helical head domain The Journal of Biological Chemistry 265 8 4722 9 doi 10 1016 S0021 9258 19 39622 X PMID 2155236 Ohta Y Ohba T Miyamoto E July 1990 Ca2 calmodulin dependent protein kinase II localization in the interphase nucleus and the mitotic apparatus of mammalian cells Proceedings of the National Academy of Sciences of the United States of America 87 14 5341 5 Bibcode 1990PNAS 87 5341O doi 10 1073 pnas 87 14 5341 PMC 54319 PMID 2164678 Lee RH Brown BM Lolley RN September 1990 Protein kinase A phosphorylates retinal phosducin on serine 73 in situ The Journal of Biological Chemistry 265 26 15860 6 doi 10 1016 S0021 9258 18 55478 8 PMID 2394752 Ku NO Omary MB October 1994 Identification of the major physiologic phosphorylation site of human keratin 18 potential kinases and a role in filament reorganization The Journal of Cell Biology 127 1 161 71 doi 10 1083 jcb 127 1 161 PMC 2120194 PMID 7523419 Drewes G Trinczek B Illenberger S Biernat J Schmitt Ulms G Meyer HE et al March 1995 Microtubule associated protein microtubule affinity regulating kinase p110mark A novel protein kinase that regulates tau microtubule interactions and dynamic instability by phosphorylation at the Alzheimer specific site serine 262 The Journal of Biological Chemistry 270 13 7679 88 doi 10 1074 jbc 270 13 7679 PMID 7706316 S2CID 2039456 Tsujimura K Tanaka J Ando S Matsuoka Y Kusubata M Sugiura H et al August 1994 Identification of phosphorylation sites on glial fibrillary acidic protein for cdc2 kinase and Ca 2 calmodulin dependent protein kinase II Journal of Biochemistry 116 2 426 34 doi 10 1093 oxfordjournals jbchem a124542 PMID 7822264 Toyofuku T Curotto Kurzydlowski K Narayanan N MacLennan DH October 1994 Identification of Ser38 as the site in cardiac sarcoplasmic reticulum Ca 2 ATPase that is phosphorylated by Ca2 calmodulin dependent protein kinase The Journal of Biological Chemistry 269 42 26492 6 doi 10 1016 S0021 9258 18 47221 3 PMID 7929371 Rivera VM Miranti CK Misra RP Ginty DD Chen RH Blenis J Greenberg ME October 1993 A growth factor induced kinase phosphorylates the serum response factor at a site that regulates its DNA binding activity Molecular and Cellular Biology 13 10 6260 73 doi 10 1128 mcb 13 10 6260 PMC 364685 PMID 8413226 Omkumar RV Kiely MJ Rosenstein AJ Min KT Kennedy MB December 1996 Identification of a phosphorylation site for calcium calmodulindependent protein kinase II in the NR2B subunit of the N methyl D aspartate receptor The Journal of Biological Chemistry 271 49 31670 8 doi 10 1074 jbc 271 49 31670 PMID 8940188 S2CID 8332020 Rotenberg A Mayford M Hawkins RD Kandel ER Muller RU December 1996 Mice expressing activated CaMKII lack low frequency LTP and do not form stable place cells in the CA1 region of the hippocampus Cell 87 7 1351 61 doi 10 1016 S0092 8674 00 81829 2 PMID 8980240 S2CID 16704390 Paudel HK January 1997 The regulatory Ser262 of microtubule associated protein tau is phosphorylated by phosphorylase kinase The Journal of Biological Chemistry 272 3 1777 85 doi 10 1016 S0021 9258 19 67481 8 PMID 8999860 External links editHuman CAMK2A genome location and CAMK2A gene details page in the UCSC Genome Browser Portal nbsp Biology nbsp This article on a gene on human chromosome 5 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Calcium calmodulin dependent protein kinase type II subunit alpha amp oldid 1171091120, wikipedia, wiki, book, books, library,

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