CAMK2G

Protein-coding gene in the species Homo sapiens
CAMK2G
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2UX0, 2V7O

Identifiers
AliasesCAMK2G, CAMK, CAMK-II, CAMKG, calcium/calmodulin dependent protein kinase II gamma
External IDsOMIM: 602123; MGI: 88259; HomoloGene: 15596; GeneCards: CAMK2G; OMA:CAMK2G - orthologs
Gene location (Human)
Chromosome 10 (human)
Chr.Chromosome 10 (human)[1]
Chromosome 10 (human)
Genomic location for CAMK2G
Genomic location for CAMK2G
Band10q22.2Start73,812,501 bp[1]
End73,874,591 bp[1]
Gene location (Mouse)
Chromosome 14 (mouse)
Chr.Chromosome 14 (mouse)[2]
Chromosome 14 (mouse)
Genomic location for CAMK2G
Genomic location for CAMK2G
Band14|14 A3Start20,734,875 bp[2]
End20,794,088 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • frontal pole

  • postcentral gyrus

  • right frontal lobe

  • popliteal artery

  • tibial arteries

  • Brodmann area 10

  • muscle layer of sigmoid colon

  • right coronary artery

  • lateral nuclear group of thalamus

  • primary visual cortex
Top expressed in
  • zygote

  • primary visual cortex

  • superior frontal gyrus

  • dentate gyrus of hippocampal formation granule cell

  • secondary oocyte

  • central gray substance of midbrain

  • muscle of thigh

  • triceps brachii muscle

  • primary motor cortex

  • pontine nuclei
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • nucleotide binding
  • protein kinase activity
  • protein homodimerization activity
  • kinase activity
  • protein binding
  • calcium-dependent protein serine/threonine phosphatase activity
  • 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
  • sarcoplasmic reticulum
  • sarcoplasmic reticulum membrane
  • cytoplasm
  • postsynaptic density
  • neuron projection
Biological process
  • regulation of calcium ion transport
  • phosphorylation
  • interferon-gamma-mediated signaling pathway
  • G1 phase
  • regulation of relaxation of cardiac muscle
  • insulin secretion
  • MAPK cascade
  • multicellular organism development
  • protein phosphorylation
  • protein complex oligomerization
  • regulation of cellular response to heat
  • protein autophosphorylation
  • regulation of skeletal muscle adaptation
  • calcium ion transport
  • protein dephosphorylation
  • nervous system development
  • peptidyl-serine phosphorylation
  • peptidyl-threonine phosphorylation
  • cell differentiation
  • intracellular signal transduction
  • regulation of molecular function
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

818

12325

Ensembl

ENSG00000148660

ENSMUSG00000021820

UniProt

Q13555

Q923T9

RefSeq (mRNA)
NM_001204492
NM_001222
NM_172169
NM_172170
NM_172171

NM_172172
NM_172173
NM_001320898

NM_001039138
NM_001039139
NM_178597
NM_001360186

RefSeq (protein)
NP_001191421
NP_001213
NP_001307827
NP_751909
NP_751910

NP_751911
NP_751913
NP_001354443
NP_001354445
NP_001354446
NP_001354447
NP_001354448
NP_001354449
NP_001354450
NP_001354451
NP_001354452
NP_001354453
NP_001354454
NP_001354455
NP_001354456
NP_001354457
NP_001354458
NP_001354459
NP_001354460
NP_001354461
NP_001354462
NP_001354463
NP_001354464
NP_001354465
NP_001354466
NP_001354467
NP_001354468
NP_001354469
NP_001354470
NP_001354471
NP_001354472
NP_001354473
NP_001354474
NP_001354475
NP_001354476
NP_001354477

NP_001034227
NP_001034228
NP_848712
NP_001347115

Location (UCSC)Chr 10: 73.81 – 73.87 MbChr 14: 20.73 – 20.79 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Calcium/calmodulin-dependent protein kinase type II gamma chain is an enzyme that in humans is encoded by the CAMK2G gene.[5]

Function

The product of this gene belongs to the Serine/Threonine protein kinase family, and to the Ca(2+)/calmodulin-dependent protein kinase subfamily. Calcium signaling 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 gamma chain. Six alternatively spliced variants that encode six different isoforms have been characterized to date. Additional alternative splice variants that encode different isoforms have been described, but their full-length nature has not been determined.[6]

Interactions

CAMK2G has been shown to interact with RRAD.[7]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000148660 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000021820 – 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. ^ Li X, Nghiem P, Schulman H, Francke U (Feb 1994). "Localization of the CAMKG gene encoding gamma isoforms of multifunctional calcium/calmodulin-dependent protein kinase (CaM kinase) to human chromosome 10 band q22 and mouse chromosome 14". Cytogenet Cell Genet. 66 (2): 113–6. doi:10.1159/000133679. PMID 8287681. S2CID 46836396.
  6. ^ "Entrez Gene: CAMK2G calcium/calmodulin-dependent protein kinase (CaM kinase) II gamma".
  7. ^ Moyers JS, Bilan PJ, Zhu J, Kahn CR (May 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.

Further reading

  • Hook SS, Means AR (2001). "Ca(2+)/CaM-dependent kinases: from activation to function". Annu. Rev. Pharmacol. Toxicol. 41: 471–505. doi:10.1146/annurev.pharmtox.41.1.471. PMID 11264466.
  • 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.
  • Countaway JL, Nairn AC, Davis RJ (1992). "Mechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase". J. Biol. Chem. 267 (2): 1129–40. doi:10.1016/S0021-9258(18)48406-2. PMID 1309762.
  • Ikebe M, Reardon S (1990). "Phosphorylation of smooth myosin light chain kinase by smooth muscle Ca2+/calmodulin-dependent multifunctional protein kinase". J. Biol. Chem. 265 (16): 8975–8. doi:10.1016/S0021-9258(19)38796-4. PMID 2160950.
  • Czernik AJ, Pang DT, Greengard P (1987). "Amino acid sequences surrounding the cAMP-dependent and calcium/calmodulin-dependent phosphorylation sites in rat and bovine synapsin I." Proc. Natl. Acad. Sci. U.S.A. 84 (21): 7518–22. Bibcode:1987PNAS...84.7518C. doi:10.1073/pnas.84.21.7518. PMC 299327. PMID 3118371.
  • Vulliet PR, Woodgett JR, Cohen P (1984). "Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase". J. Biol. Chem. 259 (22): 13680–3. doi:10.1016/S0021-9258(18)89798-8. PMID 6150037.
  • Wen Z, Zhong Z, Darnell JE (1995). "Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation". Cell. 82 (2): 241–50. doi:10.1016/0092-8674(95)90311-9. PMID 7543024. S2CID 6717533.
  • Kwiatkowski AP, McGill JM (1995). "Human biliary epithelial cell line Mz-ChA-1 expresses new isoforms of calmodulin-dependent protein kinase II". Gastroenterology. 109 (4): 1316–23. doi:10.1016/0016-5085(95)90594-4. PMID 7557101.
  • Shuai K, Stark GR, Kerr IM, Darnell JE (1993). "A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma". Science. 261 (5129): 1744–6. Bibcode:1993Sci...261.1744S. doi:10.1126/science.7690989. PMID 7690989.
  • Zhu J, Reynet C, Caldwell JS, Kahn CR (1995). "Characterization of Rad, a new member of Ras/GTPase superfamily, and its regulation by a unique GTPase-activating protein (GAP)-like activity". J. Biol. Chem. 270 (9): 4805–12. doi:10.1074/jbc.270.9.4805. PMID 7876254.
  • Yakel JL, Vissavajjhala P, Derkach VA, Brickey DA, Soderling TR (1995). "Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate receptors". Proc. Natl. Acad. Sci. U.S.A. 92 (5): 1376–80. Bibcode:1995PNAS...92.1376Y. doi:10.1073/pnas.92.5.1376. PMC 42522. PMID 7877986.
  • 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.
  • Suko J, Maurer-Fogy I, Plank B, Bertel O, Wyskovsky W, Hohenegger M, Hellmann G (1993). "Phosphorylation of serine 2843 in ryanodine receptor-calcium release channel of skeletal muscle by cAMP-, cGMP- and CaM-dependent protein kinase". Biochim. Biophys. Acta. 1175 (2): 193–206. doi:10.1016/0167-4889(93)90023-I. PMID 8380342.
  • de Groot RP, den Hertog J, Vandenheede JR, Goris J, Sassone-Corsi P (1993). "Multiple and cooperative phosphorylation events regulate the CREM activator function". EMBO J. 12 (10): 3903–11. doi:10.1002/j.1460-2075.1993.tb06068.x. PMC 413673. PMID 8404858.
  • Nghiem P, Saati SM, Martens CL, Gardner P, Schulman H (1993). "Cloning and analysis of two new isoforms of multifunctional Ca2+/calmodulin-dependent protein kinase. Expression in multiple human tissues". J. Biol. Chem. 268 (8): 5471–9. doi:10.1016/S0021-9258(18)53345-7. PMID 8449910.
  • Shimomura A, Ogawa Y, Kitani T, Fujisawa H, Hagiwara M (1996). "Calmodulin-dependent protein kinase II potentiates transcriptional activation through activating transcription factor 1 but not cAMP response element-binding protein". J. Biol. Chem. 271 (30): 17957–60. doi:10.1074/jbc.271.30.17957. PMID 8663317.
  • Wei J, Wayman G, Storm DR (1996). "Phosphorylation and inhibition of type III adenylyl cyclase by calmodulin-dependent protein kinase II in vivo". J. Biol. Chem. 271 (39): 24231–5. doi:10.1074/jbc.271.39.24231. PMID 8798667.
  • 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.

External links

  • Human CAMK2G genome location and CAMK2G gene details page in the UCSC Genome Browser.
  • Overview of all the structural information available in the PDB for UniProt: Q13555 (Calcium/calmodulin-dependent protein kinase type II subunit gamma) at the PDBe-KB.


  • v
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  • 2ux0: STRUCTURE OF THE OLIGOMERISATION DOMAIN OF CALCIUM-CALMODULIN DEPENDENT PROTEIN KINASE II GAMMA
    2ux0: STRUCTURE OF THE OLIGOMERISATION DOMAIN OF CALCIUM-CALMODULIN DEPENDENT PROTEIN KINASE II GAMMA
  • v
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  • e
Non-specific serine/threonine protein kinases (EC 2.7.11.1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
  • -
IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)
Cyclin-dependent kinase (EC 2.7.11.22)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
Tau-protein kinase (EC 2.7.11.26)
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)
  • -
Tropomyosin kinase (EC 2.7.11.28)
  • -
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)
  • -
Receptor protein serine/threonine kinase (EC 2.7.11.30)
MAP2K
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