Open Access Articles- Top Results for RPS6KA1


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External IDsOMIM601684 MGI104558 HomoloGene55703 IUPHAR: 1527 ChEMBL: 2553 GeneCards: RPS6KA1 Gene
EC number2.7.11.1
RNA expression pattern
File:PBB GE RPS6KA1 203379 at tn.png
More reference expression data
RefSeq (mRNA)NM_001006665NM_001285505
RefSeq (protein)NP_001006666NP_001272434
Location (UCSC)Chr 1:
26.53 – 26.58 Mb
Chr 4:
133.85 – 133.89 Mb
PubMed search[1][2]

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

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.[2]


RPS6KA1 has been shown to interact with YWHAB,[3] MAPK1,[4][5][6] IκBα,[7] TOB1[8] and TSC2.[9][10]

See also


  1. ^ Moller DE, Xia CH, Tang W, Zhu AX, Jakubowski M (April 1994). "Human rsk isoforms: cloning and characterization of tissue-specific expression". Am J Physiol 266 (2 Pt 1): C351–9. PMID 8141249. 
  2. ^ "Entrez Gene: RPS6KA1 ribosomal protein S6 kinase, 90kDa, polypeptide 1". 
  3. ^ Cavet, Megan E; Lehoux Stephanie; Berk Bradford C (May 2003). "14-3-3beta is a p90 ribosomal S6 kinase (RSK) isoform 1-binding protein that negatively regulates RSK kinase activity". J. Biol. Chem. (United States) 278 (20): 18376–83. ISSN 0021-9258. PMID 12618428. doi:10.1074/jbc.M208475200. 
  4. ^ Roux, Philippe P; Richards Stephanie A; Blenis John (July 2003). "Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity". Mol. Cell. Biol. (United States) 23 (14): 4796–804. ISSN 0270-7306. PMC 162206. PMID 12832467. doi:10.1128/MCB.23.14.4796-4804.2003. 
  5. ^ Eblen, Scott T; Kumar N Vinay; Shah Kavita; Henderson Michelle J; Watts Colin K W; Shokat Kevan M; Weber Michael J (April 2003). "Identification of novel ERK2 substrates through use of an engineered kinase and ATP analogs". J. Biol. Chem. (United States) 278 (17): 14926–35. ISSN 0021-9258. PMID 12594221. doi:10.1074/jbc.M300485200. 
  6. ^ Smith, J A; Poteet-Smith C E; Malarkey K; Sturgill T W (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". J. Biol. Chem. (UNITED STATES) 274 (5): 2893–8. ISSN 0021-9258. PMID 9915826. doi:10.1074/jbc.274.5.2893. 
  7. ^ Schouten, G J; Vertegaal A C, Whiteside S T, Israël A, Toebes M, Dorsman J C, van der Eb A J, Zantema A (June 1997). "IkappaB alpha is a target for the mitogen-activated 90 kDa ribosomal S6 kinase". EMBO J. (ENGLAND) 16 (11): 3133–44. ISSN 0261-4189. PMC 1169932. PMID 9214631. doi:10.1093/emboj/16.11.3133. 
  8. ^ Suzuki, T; Matsuda S; Tsuzuku J K; Yoshida Y; Yamamoto T (February 2001). "A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob". Genes Cells (England) 6 (2): 131–8. ISSN 1356-9597. PMID 11260258. doi:10.1046/j.1365-2443.2001.00406.x. 
  9. ^ Roux, Philippe P; Ballif Bryan A; Anjum Rana; Gygi Steven P; Blenis John (September 2004). "Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase". Proc. Natl. Acad. Sci. U.S.A. (United States) 101 (37): 13489–94. ISSN 0027-8424. PMC 518784. PMID 15342917. doi:10.1073/pnas.0405659101. 
  10. ^ Rolfe, Mark; McLeod Laura E; Pratt Phillip F; Proud Christopher G (June 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)". Biochem. J. (England) 388 (Pt 3): 973–84. PMC 1183479. PMID 15757502. doi:10.1042/BJ20041888. 

Further reading


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