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Available structures
PDB Ortholog search: PDBe RCSB
Aliases RPS6KA3, CLS, HU-3, ISPK-1, MAPKAPK1B, MRX19, RSK, RSK2, S6K-alpha3, p90-RSK2, pp90RSK2, ribosomal protein S6 kinase A3
External IDs MGI: 104557 HomoloGene: 37940 GeneCards: RPS6KA3
RNA expression pattern
PBB GE RPS6KA3 203843 at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr X: 20.15 – 20.27 Mb Chr X: 159.21 – 159.37 Mb
PubMed search [1] [2]
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Ribosomal protein S6 kinase, 90kDa, polypeptide 3, also known as RPS6KA3, is an enzyme that in humans is encoded by the RPS6KA3 gene.[3][4]


This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine/threonine kinases. This kinase contains 2 non-identical kinase catalytic domains and phosphorylates various substrates, including members of the mitogen-activated kinase (MAPK) signalling pathway. The activity of this protein has been implicated in controlling cell growth and differentiation.[3]

Clinical significance[edit]

Mutations in this gene have been associated with Coffin–Lowry syndrome (CLS).[5]


RPS6KA3 has been shown to interact with CREB-binding protein,[6] MAPK1[7][8] and PEA15.[9]


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ a b "Entrez Gene: RPS6KA3 ribosomal protein S6 kinase, 90kDa, polypeptide 3". 
  4. ^ Moller DE, Xia CH, Tang W, Zhu AX, Jakubowski M (February 1994). "Human rsk isoforms: cloning and characterization of tissue-specific expression". The American Journal of Physiology. 266 (2 Pt 1): C351–9. PMID 8141249. 
  5. ^ Jacquot S, Zeniou M, Touraine R, Hanauer A (January 2002). "X-linked Coffin-Lowry syndrome (CLS, MIM 303600, RPS6KA3 gene, protein product known under various names: pp90(rsk2), RSK2, ISPK, MAPKAP1)". European Journal of Human Genetics. 10 (1): 2–5. PMID 11896450. doi:10.1038/sj.ejhg.5200738. 
  6. ^ Merienne K, Pannetier S, Harel-Bellan A, Sassone-Corsi P (October 2001). "Mitogen-regulated RSK2-CBP interaction controls their kinase and acetylase activities". Molecular and Cellular Biology. 21 (20): 7089–96. PMC 99884Freely accessible. PMID 11564891. doi:10.1128/MCB.21.20.7089-7096.2001. 
  7. ^ Zhao Y, Bjorbaek C, Moller DE (November 1996). "Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases". The Journal of Biological Chemistry. 271 (47): 29773–9. PMID 8939914. doi:10.1074/jbc.271.47.29773. 
  8. ^ Smith JA, Poteet-Smith CE, Malarkey K, Sturgill TW (January 1999). "Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo". The Journal of Biological Chemistry. 274 (5): 2893–8. PMID 9915826. doi:10.1074/jbc.274.5.2893. 
  9. ^ Vaidyanathan H, Ramos JW (August 2003). "RSK2 activity is regulated by its interaction with PEA-15". The Journal of Biological Chemistry. 278 (34): 32367–72. PMID 12796492. doi:10.1074/jbc.M303988200. 

Further reading[edit]

External links[edit]