Available structures
PDBOrtholog search: PDBe RCSB
AliasesRPS6KA1, HU-1, MAPKAPK1A, RSK, RSK1, p90Rsk, ribosomal protein S6 kinase A1, MAPKAPK1
External IDsOMIM: 601684 MGI: 104558 HomoloGene: 55703 GeneCards: RPS6KA1
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 1: 26.53 – 26.58 MbChr 4: 133.57 – 133.62 Mb
PubMed search[3][4]
View/Edit HumanView/Edit Mouse

Ribosomal protein S6 kinase alpha-1 is an enzyme that in humans is encoded by the RPS6KA1 gene.[5]


This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine/threonine kinases. This kinase contains 2 nonidentical 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. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[6]


RPS6KA1 has been shown to interact with:

See also


  1. ^ a b c ENSG00000281877 GRCh38: Ensembl release 89: ENSG00000117676, ENSG00000281877Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000003644Ensembl, 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. ^ Moller DE, Xia CH, Tang W, Zhu AX, Jakubowski M (Feb 1994). "Human rsk isoforms: cloning and characterization of tissue-specific expression". The American Journal of Physiology. 266 (2 Pt 1): C351–9. doi:10.1152/ajpcell.1994.266.2.C351. PMID 8141249.
  6. ^ "Entrez Gene: RPS6KA1 ribosomal protein S6 kinase, 90kDa, polypeptide 1".
  7. ^ Schouten GJ, Vertegaal AC, Whiteside ST, Israël A, Toebes M, Dorsman JC, van der Eb AJ, Zantema A (Jun 1997). "IkappaB alpha is a target for the mitogen-activated 90 kDa ribosomal S6 kinase". The EMBO Journal. 16 (11): 3133–44. doi:10.1093/emboj/16.11.3133. PMC 1169932. PMID 9214631.
  8. ^ Roux PP, Richards SA, Blenis J (Jul 2003). "Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity". Molecular and Cellular Biology. 23 (14): 4796–804. doi:10.1128/mcb.23.14.4796-4804.2003. PMC 162206. PMID 12832467.
  9. ^ Eblen ST, Kumar NV, Shah K, Henderson MJ, Watts CK, Shokat KM, Weber MJ (Apr 2003). "Identification of novel ERK2 substrates through use of an engineered kinase and ATP analogs". The Journal of Biological Chemistry. 278 (17): 14926–35. doi:10.1074/jbc.M300485200. PMID 12594221.
  10. ^ Smith JA, Poteet-Smith CE, Malarkey K, Sturgill TW (Jan 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. doi:10.1074/jbc.274.5.2893. PMID 9915826.
  11. ^ Suzuki T, Matsuda S, Tsuzuku JK, Yoshida Y, Yamamoto T (Feb 2001). "A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob". Genes to Cells. 6 (2): 131–8. doi:10.1046/j.1365-2443.2001.00406.x. PMID 11260258.
  12. ^ Roux PP, Ballif BA, Anjum R, Gygi SP, Blenis J (Sep 2004). "Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase". Proceedings of the National Academy of Sciences of the United States of America. 101 (37): 13489–94. Bibcode:2004PNAS..10113489R. doi:10.1073/pnas.0405659101. PMC 518784. PMID 15342917.
  13. ^ Rolfe M, McLeod LE, Pratt PF, Proud CG (Jun 2005). "Activation of protein synthesis in cardiomyocytes by the hypertrophic agent phenylephrine requires the activation of ERK and involves phosphorylation of tuberous sclerosis complex 2 (TSC2)". The Biochemical Journal. 388 (Pt 3): 973–84. doi:10.1042/BJ20041888. PMC 1183479. PMID 15757502.
  14. ^ Cavet ME, Lehoux S, Berk BC (May 2003). "14-3-3beta is a p90 ribosomal S6 kinase (RSK) isoform 1-binding protein that negatively regulates RSK kinase activity". The Journal of Biological Chemistry. 278 (20): 18376–83. doi:10.1074/jbc.M208475200. PMID 12618428.

Further reading