CAMK1

From Wikipedia, the free encyclopedia

Calcium/calmodulin-dependent protein kinase I

PDB rendering based on 1a06.

Available structures: 1a06

Identifiers

Symbol(s)

CAMK1; CAMKI; MGC120317; MGC120318

External IDs

OMIM: 604998 MGI: 1098535 HomoloGene: 74503

Gene ontology
Molecular Function:	• nucleotide binding • protein serine/threonine kinase activity • calmodulin-dependent protein kinase activity • calmodulin binding • ATP binding • transferase activity
Cellular Component:	• nucleus
Biological Process:	• protein amino acid phosphorylation • nucleocytoplasmic transport • signal transduction • multicellular organismal development • nervous system development • cell differentiation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003656 (mRNA)
NP_003647 (protein)

NM_133926 (mRNA)
NP_598687 (protein)

Location

Chr 3: 9.77 - 9.79 Mb

Chr 6: 113.3 - 113.31 Mb

Pubmed search

[1]

[2]

Calcium/calmodulin-dependent protein kinase I, also known as CAMK1, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: CAMK1 calcium/calmodulin-dependent protein kinase I.

[edit] 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. 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. PMID 7559563.
Haribabu B, Hook SS, Selbert MA, et al. (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. PMID 7641687.
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. 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. 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. 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. 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. 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. 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. 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. PMID 10571231.
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. doi:10.1038/35040593. 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. doi:10.1073/pnas.260501497. 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. 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. 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. doi:10.1073/pnas.242603899. 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.