CAMK1

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

CAMK1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4FG7, 4FG8, 4FG9, 4FGB
Identifiers
Aliases	CAMK1, CAMKI, calcium/calmodulin dependent protein kinase I, CaMKI-alpha, CaM kinase I alpha
External IDs	OMIM: 604998; MGI: 1098535; HomoloGene: 117458; GeneCards: CAMK1; OMA:CAMK1 - orthologs
Gene location (Human) Chr. Chromosome 3 (human) Band 3p25.3 Start 9,757,347 bp End 9,769,992 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6 E3|6 52.75 cM Start 113,311,085 bp End 113,320,945 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right adrenal cortex left adrenal cortex right frontal lobe nucleus accumbens prefrontal cortex caudate nucleus monocyte amygdala left uterine tube putamen Top expressed in superior frontal gyrus stroma of bone marrow primary visual cortex external carotid artery dorsomedial hypothalamic nucleus internal carotid artery right kidney arcuate nucleus myocardium of ventricle dentate gyrus of hippocampal formation granule cell 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 Species Human Mouse 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 Mb Chr 6: 113.31 – 113.32 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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.

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

• Human CAMK1 genome location and CAMK1 gene details page in the UCSC Genome Browser.