CAMK2A

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CAMK2A
Protein CAMK2A PDB 1hkx.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCAMK2A, CAMKA, calcium/calmodulin dependent protein kinase II alpha, MRD53, CaMKIINalpha
External IDsMGI: 88256 HomoloGene: 56577 GeneCards: CAMK2A
Gene location (Human)
Chromosome 5 (human)
Chr.Chromosome 5 (human)[1]
Chromosome 5 (human)
Genomic location for CAMK2A
Genomic location for CAMK2A
Band5q32Start150,219,491 bp[1]
End150,290,291 bp[1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_171825
NM_015981
NM_001363989
NM_001363990

NM_001286809
NM_009792
NM_177407

RefSeq (protein)

NP_057065
NP_741960
NP_001350918
NP_001350919

NP_001273738
NP_033922
NP_803126

Location (UCSC)Chr 5: 150.22 – 150.29 MbChr 18: 60.93 – 60.99 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Calcium/calmodulin-dependent protein kinase type II alpha chain (CAMKIIα) is an enzyme that in humans is encoded by the CAMK2A gene.[5][6]

Function[edit]

The product of this gene belongs to the Serine/Threonine protein kinases family, and to the Ca2+/calmodulin-dependent protein kinase II subfamily. Calcium signaling is crucial for several aspects of 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(needs citation, perhaps Harvward et al. 2016). 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]

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:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Jul 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 Res. 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, Schulman H, Rosenfeld MG (Sep 1987). "Molecular cloning of a brain-specific calcium/calmodulin-dependent protein kinase". Proc Natl Acad Sci U S A. 84 (16): 5962–6. doi:10.1073/pnas.84.16.5962. PMC 298983Freely accessible. PMID 3475713. 
  7. ^ "Entrez Gene: CAMK2A calcium/calmodulin-dependent protein kinase (CaM kinase) II alpha". 
  8. ^ 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. 
  9. ^ Dhavan R, Greer PL, Morabito MA, Orlando LR, Tsai LH (Sep 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". J. Neurosci. 22 (18): 7879–91. PMID 12223541. 
  10. ^ Gardoni F, Mauceri D, Fiorentini C, Bellone C, Missale C, Cattabeni F, Di Luca M (Nov 2003). "CaMKII-dependent phosphorylation regulates SAP97/NR2A interaction". J. Biol. Chem. 278 (45): 44745–52. doi:10.1074/jbc.M303576200. PMID 12933808. 

Further reading[edit]

External links[edit]