BRSK1

BRSK1
Identifiers
Aliases	BRSK1, hSAD1, BR serine/threonine kinase 1, SAD-B
External IDs	OMIM: 609235; MGI: 2685946; HomoloGene: 57169; GeneCards: BRSK1; OMA:BRSK1 - orthologs
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 2.7.11.1 ↗ ↗ ↗ ↗ 2.7.11.26 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 19 (human) Band 19q13.42 Start 55,282,072 bp End 55,312,562 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7|7 A1 Start 4,693,603 bp End 4,718,996 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right frontal lobe Brodmann area 9 right hemisphere of cerebellum prefrontal cortex cingulate gyrus anterior cingulate cortex ganglionic eminence amygdala hypothalamus putamen Top expressed in primary visual cortex superior frontal gyrus dentate gyrus of hippocampal formation granule cell prefrontal cortex central gray substance of midbrain cerebellar cortex nucleus of stria terminalis hippocampus proper cingulate gyrus piriform cortex More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity nucleotide binding protein kinase activity metal ion binding kinase activity protein kinase binding magnesium ion binding protein serine/threonine kinase activity ATP binding tau-protein kinase activity gamma-tubulin binding tau protein binding Cellular component synapse nucleoplasm microtubule organizing center cytoskeleton cell junction cytoplasm synaptic vesicle centrosome nucleus presynaptic active zone distal axon Biological process response to ionizing radiation neuron projection morphogenesis intracellular signal transduction phosphorylation nervous system development cell cycle response to UV cellular response to DNA damage stimulus centrosome duplication establishment of cell polarity neurotransmitter secretion axonogenesis neuron differentiation protein phosphorylation mitotic G2 DNA damage checkpoint signaling associative learning regulation of neuron projection development regulation of synaptic plasticity regulation of axonogenesis microtubule cytoskeleton organization involved in establishment of planar polarity synaptic vesicle cycle regulation of synaptic vesicle clustering Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 84446 381979 Ensembl ENSG00000160469 ENSMUSG00000035390 UniProt Q8TDC3 Q5RJI5 RefSeq (mRNA) NM_032430 NM_001003920 NM_001168572 RefSeq (protein) NP_115806 NP_001003920 NP_001162044 Location (UCSC) Chr 19: 55.28 – 55.31 Mb Chr 7: 4.69 – 4.72 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

BR serine/threonine kinase 1 is an enzyme that in humans is encoded by the BRSK1 gene.

External links

• Human BRSK1 genome location and BRSK1 gene details page in the UCSC Genome Browser.

Further reading

• Lizcano JM, Göransson O, Toth R, Deak M, Morrice NA, Boudeau J, Hawley SA, Udd L, Mäkelä TP, Hardie DG, Alessi DR (Feb 2004). "LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1". The EMBO Journal. 23 (4): 833–43. doi:10.1038/sj.emboj.7600110. PMC 381014. PMID 14976552.
• Lu R, Niida H, Nakanishi M (Jul 2004). "Human SAD1 kinase is involved in UV-induced DNA damage checkpoint function". The Journal of Biological Chemistry. 279 (30): 31164–70. doi:10.1074/jbc.M404728200. PMID 15150265.
• Al-Hakim AK, Göransson O, Deak M, Toth R, Campbell DG, Morrice NA, Prescott AR, Alessi DR (Dec 2005). "14-3-3 cooperates with LKB1 to regulate the activity and localization of QSK and SIK". Journal of Cell Science. 118 (Pt 23): 5661–73. doi:10.1242/jcs.02670. PMID 16306228.
• Inoue E, Mochida S, Takagi H, Higa S, Deguchi-Tawarada M, Takao-Rikitsu E, Inoue M, Yao I, Takeuchi K, Kitajima I, Setou M, Ohtsuka T, Takai Y (Apr 2006). "SAD: a presynaptic kinase associated with synaptic vesicles and the active zone cytomatrix that regulates neurotransmitter release". Neuron. 50 (2): 261–75. doi:10.1016/j.neuron.2006.03.018. PMID 16630837. S2CID 15232412.
• Al-Hakim AK, Zagorska A, Chapman L, Deak M, Peggie M, Alessi DR (Apr 2008). "Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains" (PDF). The Biochemical Journal. 411 (2): 249–60. doi:10.1042/BJ20080067. PMID 18254724. S2CID 13038944.
• Bright NJ, Carling D, Thornton C (May 2008). "Investigating the regulation of brain-specific kinases 1 and 2 by phosphorylation". The Journal of Biological Chemistry. 283 (22): 14946–54. doi:10.1074/jbc.M710381200. PMC 3258900. PMID 18339622.
• Fogarty S, Hardie DG (Jan 2009). "C-terminal phosphorylation of LKB1 is not required for regulation of AMP-activated protein kinase, BRSK1, BRSK2, or cell cycle arrest". The Journal of Biological Chemistry. 284 (1): 77–84. doi:10.1074/jbc.M806152200. PMC 2610510. PMID 18854318.
• Stolk L, Zhai G, van Meurs JB, Verbiest MM, Visser JA, Estrada K, Rivadeneira F, Williams FM, Cherkas L, Deloukas P, Soranzo N, de Keyzer JJ, Pop VJ, Lips P, Lebrun CE, van der Schouw YT, Grobbee DE, Witteman J, Hofman A, Pols HA, Laven JS, Spector TD, Uitterlinden AG (Jun 2009). "Loci at chromosomes 13, 19 and 20 influence age at natural menopause". Nature Genetics. 41 (6): 645–7. doi:10.1038/ng.387. PMC 3000545. PMID 19448619.
• He C, Kraft P, Chen C, Buring JE, Paré G, Hankinson SE, Chanock SJ, Ridker PM, Hunter DJ, Chasman DI (Jun 2009). "Genome-wide association studies identify loci associated with age at menarche and age at natural menopause". Nature Genetics. 41 (6): 724–8. doi:10.1038/ng.385. PMC 2888798. PMID 19448621.
• Alvarado-Kristensson M, Rodríguez MJ, Silió V, Valpuesta JM, Carrera AC (Sep 2009). "SADB phosphorylation of gamma-tubulin regulates centrosome duplication". Nature Cell Biology. 11 (9): 1081–92. doi:10.1038/ncb1921. PMID 19648910. S2CID 41209616.