CAMK1

Protein-coding gene in the species Homo sapiens
CAMK1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4FG7, 4FG8, 4FG9, 4FGB

Identifiers
AliasesCAMK1, CAMKI, calcium/calmodulin dependent protein kinase I, CaMKI-alpha, CaM kinase I alpha
External IDsOMIM: 604998 MGI: 1098535 HomoloGene: 117458 GeneCards: CAMK1
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for CAMK1
Genomic location for CAMK1
Band3p25.3Start9,757,347 bp[1]
End9,769,992 bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for CAMK1
Genomic location for CAMK1
Band6 E3|6 52.75 cMStart113,311,085 bp[2]
End113,320,945 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • nucleus accumbens

  • prefrontal cortex

  • caudate nucleus

  • monocyte

  • amygdala

  • left uterine tube

  • putamen

  • cingulate gyrus

  • left coronary artery

  • Brodmann area 9
Top expressed in
  • superior frontal gyrus

  • external carotid artery

  • dorsomedial hypothalamic nucleus

  • internal carotid artery

  • arcuate nucleus

  • myocardium of ventricle

  • ventromedial nucleus

  • calvaria

  • lateral hypothalamus

  • mammillary body
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • nucleotide binding
  • protein kinase activity
  • kinase activity
  • protein serine/threonine kinase activity
  • protein binding
  • catalytic activity
  • ATP binding
  • calmodulin-dependent protein kinase activity
  • calmodulin binding
Cellular component
  • cytoplasm
  • nucleus
  • intracellular anatomical structure
  • postsynaptic density
  • glutamatergic synapse
  • cytosol
Biological process
  • cell differentiation
  • positive regulation of synapse structural plasticity
  • positive regulation of muscle cell differentiation
  • regulation of muscle cell differentiation
  • phosphorylation
  • positive regulation of syncytium formation by plasma membrane fusion
  • regulation of histone H3-K9 acetylation
  • negative regulation of protein binding
  • positive regulation of dendritic spine development
  • nervous system development
  • positive regulation of peptidyl-serine phosphorylation
  • positive regulation of protein serine/threonine kinase activity
  • positive regulation of protein acetylation
  • regulation of protein localization
  • positive regulation of protein export from nucleus
  • multicellular organism development
  • protein phosphorylation
  • nucleocytoplasmic transport
  • positive regulation of neuron projection development
  • cell cycle
  • metabolism
  • regulation of protein binding
  • positive regulation of transcription by RNA polymerase II
  • signal transduction
  • peptidyl-threonine phosphorylation
  • intracellular signal transduction
  • regulation of synapse organization
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

8536

52163

Ensembl

ENSG00000134072

ENSMUSG00000030272

UniProt

Q14012

Q91YS8

RefSeq (mRNA)

NM_003656

NM_133926

RefSeq (protein)

NP_003647
NP_003647.1

NP_598687

Location (UCSC)Chr 3: 9.76 – 9.77 MbChr 6: 113.31 – 113.32 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Calcium/calmodulin-dependent protein kinase type 1 is an enzyme that in humans is encoded by the CAMK1 gene.[5][6]

Calcium/calmodulin-dependent protein kinase I is expressed in many tissues and is a component of a calmodulin-dependent protein kinase cascade. Calcium/calmodulin directly activates calcium/calmodulin-dependent protein kinase I by binding to the enzyme and indirectly promotes the phosphorylation and synergistic activation of the enzyme by calcium/calmodulin-dependent protein kinase I kinase.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000134072 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030272 – 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. ^ Haribabu B, Hook SS, Selbert MA, Goldstein EG, Tomhave ED, Edelman AM, Snyderman R, Means AR (Sep 1995). "Human calcium-calmodulin dependent protein kinase I: cDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase I kinase". EMBO J. 14 (15): 3679–86. doi:10.1002/j.1460-2075.1995.tb00037.x. PMC 394442. PMID 7641687.
  6. ^ a b "Entrez Gene: CAMK1 calcium/calmodulin-dependent protein kinase I".

Further reading

  • Bredt DS, Ferris CD, Snyder SH (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". J. Biol. Chem. 267 (16): 10976–81. doi:10.1016/S0021-9258(19)49862-1. PMID 1375933.
  • Yokokura H, Picciotto MR, Nairn AC, Hidaka H (1995). "The regulatory region of calcium/calmodulin-dependent protein kinase I contains closely associated autoinhibitory and calmodulin-binding domains". J. Biol. Chem. 270 (40): 23851–9. doi:10.1074/jbc.270.40.23851. PMID 7559563.
  • Liu F, Thompson MA, Wagner S, et al. (1993). "Activating transcription factor-1 can mediate Ca(2+)- and cAMP-inducible transcriptional activation". J. Biol. Chem. 268 (9): 6714–20. doi:10.1016/S0021-9258(18)53308-1. PMID 8384217.
  • Chin D, Winkler KE, Means AR (1998). "Characterization of substrate phosphorylation and use of calmodulin mutants to address implications from the enzyme crystal structure of calmodulin-dependent protein kinase I". J. Biol. Chem. 272 (50): 31235–40. doi:10.1074/jbc.272.50.31235. PMID 9395448.
  • Hsu LS, Tsou AP, Chi CW, et al. (1998). "Cloning, expression and chromosomal localization of human Ca2+/calmodulin-dependent protein kinase kinase". J. Biomed. Sci. 5 (2): 141–9. doi:10.1007/bf02258368. PMID 9662074.
  • Matsushita M, Nairn AC (1998). "Characterization of the mechanism of regulation of Ca2+/ calmodulin-dependent protein kinase I by calmodulin and by Ca2+/calmodulin-dependent protein kinase kinase". J. Biol. Chem. 273 (34): 21473–81. doi:10.1074/jbc.273.34.21473. PMID 9705275.
  • Anderson KA, Means RL, Huang QH, et al. (1998). "Components of a calmodulin-dependent protein kinase cascade. Molecular cloning, functional characterization and cellular localization of Ca2+/calmodulin-dependent protein kinase kinase beta". J. Biol. Chem. 273 (48): 31880–9. doi:10.1074/jbc.273.48.31880. PMID 9822657.
  • Matsushita M, Nairn AC (1999). "Inhibition of the Ca2+/calmodulin-dependent protein kinase I cascade by cAMP-dependent protein kinase". J. Biol. Chem. 274 (15): 10086–93. doi:10.1074/jbc.274.15.10086. PMID 10187789.
  • Hayashi Y, Nishio M, Naito Y, et al. (1999). "Regulation of neuronal nitric-oxide synthase by calmodulin kinases". J. Biol. Chem. 274 (29): 20597–602. doi:10.1074/jbc.274.29.20597. PMID 10400690.
  • Hosaka M, Hammer RE, Südhof TC (1999). "A phospho-switch controls the dynamic association of synapsins with synaptic vesicles". Neuron. 24 (2): 377–87. doi:10.1016/S0896-6273(00)80851-X. PMID 10571231. S2CID 14103027.
  • Komeima K, Hayashi Y, Naito Y, Watanabe Y (2000). "Inhibition of neuronal nitric-oxide synthase by calcium/ calmodulin-dependent protein kinase IIalpha through Ser847 phosphorylation in NG108-15 neuronal cells". J. Biol. Chem. 275 (36): 28139–43. doi:10.1074/jbc.M003198200. PMID 10874031.
  • McKinsey TA, Zhang CL, Lu J, Olson EN (2000). "Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation". Nature. 408 (6808): 106–11. Bibcode:2000Natur.408..106M. doi:10.1038/35040593. PMC 4459600. PMID 11081517.
  • McKinsey TA, Zhang CL, Olson EN (2001). "Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5". Proc. Natl. Acad. Sci. U.S.A. 97 (26): 14400–5. Bibcode:2000PNAS...9714400M. doi:10.1073/pnas.260501497. PMC 18930. PMID 11114197.
  • Hsu LS, Chen GD, Lee LS, et al. (2001). "Human Ca2+/calmodulin-dependent protein kinase kinase beta gene encodes multiple isoforms that display distinct kinase activity". J. Biol. Chem. 276 (33): 31113–23. doi:10.1074/jbc.M011720200. PMID 11395482.
  • Condon JC, Pezzi V, Drummond BM, et al. (2002). "Calmodulin-dependent kinase I regulates adrenal cell expression of aldosterone synthase". Endocrinology. 143 (9): 3651–7. doi:10.1210/en.2001-211359. PMID 12193581.
  • Sakurada K, Kato H, Nagumo H, et al. (2003). "Synapsin I is phosphorylated at Ser603 by p21-activated kinases (PAKs) in vitro and in PC12 cells stimulated with bradykinin". J. Biol. Chem. 277 (47): 45473–9. doi:10.1074/jbc.M206673200. PMID 12237306.
  • Clapperton JA, Martin SR, Smerdon SJ, et al. (2003). "Structure of the complex of calmodulin with the target sequence of calmodulin-dependent protein kinase I: studies of the kinase activation mechanism". Biochemistry. 41 (50): 14669–79. doi:10.1021/bi026660t. PMID 12475216.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Izmailova E, Bertley FM, Huang Q, et al. (2003). "HIV-1 Tat reprograms immature dendritic cells to express chemoattractants for activated T cells and macrophages". Nat. Med. 9 (2): 191–7. doi:10.1038/nm822. PMID 12539042. S2CID 26145639.

External links

  • v
  • t
  • e
  • 1a06: CALMODULIN-DEPENDENT PROTEIN KINASE FROM RAT
    1a06: CALMODULIN-DEPENDENT PROTEIN KINASE FROM RAT
  • v
  • t
  • 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
Portal:
  • icon Biology


Stub icon

This article on a gene on human chromosome 3 is a stub. You can help Wikipedia by expanding it.

  • v
  • t
  • e