Calcium/calmodulin-dependent protein kinase type II subunit alpha

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

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. 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

CAMK2A has been shown to interact with:

References

  1. GRCh38: Ensembl release 89: ENSG00000070808 - Ensembl, May 2017
  2. 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.
  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


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