CAMKK1

Calcium/calmodulin-dependent protein kinase kinase 1 is an enzyme that in humans is encoded by the CAMKK1 gene.[5][6]

CAMKK1
Identifiers
Aliases	CAMKK1, CAMKKA, calcium/calmodulin-dependent protein kinase kinase 1, calcium/calmodulin dependent protein kinase kinase 1
External IDs	OMIM: 611411 MGI: 1891766 HomoloGene: 10327 GeneCards: CAMKK1
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17p13.2 Start 3,860,315 bp[1] End 3,894,891 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 B4 Start 73,019,008 bp[2] End 73,042,073 bp[2]
Gene ontology Molecular function • kinase activity • transferase activity • nucleotide binding • protein kinase activity • protein serine/threonine kinase activity • GO:0001948 protein binding • ATP binding • calmodulin-dependent protein kinase activity • calmodulin binding Cellular component • cytosol • cell nucleus • cytoplasm • nucleoplasm Biological process • protein phosphorylation • phosphorylation • peptidyl-serine phosphorylation • peptidyl-threonine phosphorylation • GO:0007243 intracellular signal transduction • positive regulation of protein kinase activity Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	84254	55984
Ensembl	ENSG00000004660	ENSMUSG00000020785
UniProt	Q8N5S9	Q8VBY2
RefSeq (mRNA)	NM_032294 NM_172206 NM_172207	NM_018883 NM_001362841
RefSeq (protein)	NP_115670 NP_757343 NP_757344	NP_061371 NP_001349770
Location (UCSC)	Chr 17: 3.86 – 3.89 Mb	Chr 11: 73.02 – 73.04 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

The product of this gene belongs to the serine/threonine protein kinase family, and to the Ca(2+)/calmodulin-dependent protein kinase (CAMK) subfamily. This protein plays a role in the calcium/calmodulin-dependent (CaM) kinase cascade. Three transcript variants encoding two distinct isoforms have been identified for this gene.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000004660 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020785 - 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. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (Mar 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
6. "Entrez Gene: CAMKK1 calcium/calmodulin-dependent protein kinase kinase 1, alpha".

External links

• Human CAMKK1 genome location and CAMKK1 gene details page in the UCSC Genome Browser.

Further reading

• Selbert MA, Anderson KA, Huang QH, et al. (1995). "Phosphorylation and activation of Ca(2+)-calmodulin-dependent protein kinase IV by Ca(2+)-calmodulin-dependent protein kinase Ia kinase. Phosphorylation of threonine 196 is essential for activation". J. Biol. Chem. 270 (29): 17616–21. doi:10.1074/jbc.270.29.17616. PMID 7615569.
• Tokumitsu H, Enslen H, Soderling TR (1995). "Characterization of a Ca2+/calmodulin-dependent protein kinase cascade. Molecular cloning and expression of calcium/calmodulin-dependent protein kinase kinase". J. Biol. Chem. 270 (33): 19320–4. doi:10.1074/jbc.270.33.19320. PMID 7642608.
• Tokumitsu H, Soderling TR (1996). "Requirements for calcium and calmodulin in the calmodulin kinase activation cascade". J. Biol. Chem. 271 (10): 5617–22. doi:10.1074/jbc.271.10.5617. PMID 8621423.
• 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.
• 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.
• Lawson ND, Zain M, Zibello T, et al. (1999). "Modulation of a calcium/calmodulin-dependent protein kinase cascade by retinoic acid during neutrophil maturation". Exp. Hematol. 27 (11): 1682–90. doi:10.1016/S0301-472X(99)00108-3. PMID 10560916.
• Okuno S, Kitani T, Matsuzaki H, et al. (2000). "Studies on the phosphorylation of protein kinase B by Ca(2+)/calmodulin-dependent protein kinases". J. Biochem. 127 (6): 965–70. doi:10.1093/oxfordjournals.jbchem.a022712. PMID 10833263.
• Okuno S, Kitani T, Fujisawa H (2002). "Regulation of Ca(2+)/calmodulin-dependent protein kinase kinase alpha by cAMP-dependent protein kinase: I. Biochemical analysis". J. Biochem. 130 (4): 503–13. doi:10.1093/oxfordjournals.jbchem.a003013. PMID 11574070.
• 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. PMC 139241. PMID 12477932.
• Imai S, Okayama N, Shimizu M, Itoh M (2003). "Increased intracellular calcium activates serum and glucocorticoid-inducible kinase 1 (SGK1) through a calmodulin-calcium calmodulin dependent kinase kinase pathway in Chinese hamster ovary cells". Life Sci. 72 (20): 2199–209. doi:10.1016/S0024-3205(03)00092-4. PMID 12628440.
• Ishikawa Y, Tokumitsu H, Inuzuka H, et al. (2003). "Identification and characterization of novel components of a Ca2+/calmodulin-dependent protein kinase cascade in HeLa cells". FEBS Lett. 550 (1–3): 57–63. doi:10.1016/S0014-5793(03)00817-2. PMID 12935886. S2CID 22116744.
• Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.