CAMKK1

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; OMA:CAMKK1 - orthologs
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 72,909,834 bp [2] End 72,932,899 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right frontal lobe pancreatic ductal cell Brodmann area 9 prefrontal cortex right hemisphere of cerebellum middle temporal gyrus primary visual cortex endothelial cell cingulate gyrus anterior cingulate cortex Top expressed in dentate gyrus of hippocampal formation granule cell primary visual cortex superior frontal gyrus hippocampus proper facial motor nucleus anterior horn of spinal cord central gray substance of midbrain lumbar subsegment of spinal cord primary motor cortex cerebellar cortex More reference expression data BioGPS n/a
Gene ontology Molecular function kinase activity transferase activity nucleotide binding protein kinase activity protein serine/threonine kinase activity protein binding ATP binding calmodulin-dependent protein kinase activity calmodulin binding Cellular component cytosol nucleus cytoplasm nucleoplasm Biological process protein phosphorylation phosphorylation peptidyl-serine phosphorylation peptidyl-threonine phosphorylation 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: 72.91 – 72.93 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2004CBio...14.1436J. 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.