BRSK1

Identifiers

BRSK1, hSAD1, BR serine/threonine kinase 1

External IDs

MGI: 2685946 HomoloGene: 57169 GeneCards: BRSK1

2.7.11.26

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
Cellular component	• synapse • nucleoplasm • microtubule organizing center • cytoskeleton • cell junction • cytoplasm • synaptic vesicle • centrosome • nucleus
Biological process	• response to ionizing radiation • neuron projection morphogenesis • intracellular signal transduction • phosphorylation • G2 DNA damage checkpoint • 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
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_115806.1


NP_001003920.2 NP_001162044.1

Location (UCSC)

Chr 19: 55.28 – 55.31 Mb

Chr 7: 4.69 – 4.72 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

BR serine/threonine kinase 1 is an enzyme that in humans is encoded by the BRSK1 gene.^[3]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ "Entrez Gene: BR serine/threonine kinase 1". Retrieved 2011-10-18.

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.
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". The Biochemical Journal. 411 (2): 249–60. doi:10.1042/BJ20080067. PMID 18254724.
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.

Transferases: phosphorus-containing groups (EC 2.7)

2.7.1-2.7.4:
phosphotransferase/kinase
(PO₄)

2.7.1: OH acceptor	Hexo- Gluco- Fructo- Hepatic Galacto- Phosphofructo- 1 Liver Muscle Platelet 2 Riboflavin Shikimate Thymidine ADP-thymidine NAD⁺ Glycerol Pantothenate Mevalonate Pyruvate Deoxycytidine PFP Diacylglycerol Phosphoinositide 3 Class I PI 3 Class II PI 3 Sphingosine Glucose-1,6-bisphosphate synthase

2.7.2: COOH acceptor	Phosphoglycerate Aspartate kinase

2.7.3: N acceptor	Creatine

2.7.4: PO₄ acceptor	Phosphomevalonate Adenylate Nucleoside-diphosphate Uridylate Guanylate Thiamine-diphosphate

2.7.6: diphosphotransferase
(P₂O₇)

2.7.7: nucleotidyltransferase
(PO₄-nucleoside)

Polymerase

DNA polymerase	DNA-directed DNA polymerase I II III IV V RNA-directed DNA polymerase Reverse transcriptase Telomerase DNA nucleotidylexotransferase/Terminal deoxynucleotidyl transferase

RNA nucleotidyltransferase	RNA polymerase/DNA-directed RNA polymerase RNA polymerase I RNA polymerase II RNA polymerase III RNA polymerase IV Primase RNA-dependent RNA polymerase PNPase

Phosphorolytic
3' to 5' exoribonuclease

Nucleotidyltransferase

Guanylyltransferase

mRNA capping enzyme

Other

2.7.8: miscellaneous

Phosphatidyltransferases	CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase CDP-diacylglycerol—serine O-phosphatidyltransferase CDP-diacylglycerol—inositol 3-phosphatidyltransferase CDP-diacylglycerol—choline O-phosphatidyltransferase

Glycosyl-1-phosphotransferase	N-acetylglucosamine-1-phosphate transferase

2.7.10-2.7.13: protein kinase
(PO₄; protein acceptor)

2.7.10: protein-tyrosine	see tyrosine kinases

2.7.11: protein-serine/threonine	see serine/threonine-specific protein kinases

2.7.12: protein-dual-specificity	see serine/threonine-specific protein kinases

2.7.13: protein-histidine	Protein-histidine pros-kinase Protein-histidine tele-kinase Histidine kinase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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BRSK1

References

Further reading