RPS6KA1

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Ribosomal protein S6 kinase, 90kDa, polypeptide 1
Rendering based on PDB 2WNT.
Available structures PDB 2WNT, 2Z7Q, 2Z7R, 2Z7S
Identifiers
Symbols	RPS6KA1; HU-1; MAPKAPK1A; RSK; RSK1
External IDs	OMIM: 601684 MGI: 104558 HomoloGene: 55703 GeneCards: RPS6KA1 Gene
EC number	2.7.11.1
Gene Ontology Molecular function • nucleotide binding • magnesium ion binding • protein serine/threonine kinase activity • protein binding • ATP binding • kinase activity • caspase inhibitor activity Cellular component • nucleoplasm • nucleoplasm • cytosol Biological process • toll-like receptor signaling pathway • MyD88-dependent toll-like receptor signaling pathway • MyD88-dependent toll-like receptor signaling pathway • MyD88-independent toll-like receptor signaling pathway • MyD88-independent toll-like receptor signaling pathway • signal transduction • intracellular protein kinase cascade • synaptic transmission • axon guidance • Toll signaling pathway • phosphorylation • toll-like receptor 1 signaling pathway • toll-like receptor 2 signaling pathway • toll-like receptor 3 signaling pathway • toll-like receptor 4 signaling pathway • negative regulation of caspase activity • innate immune response • nerve growth factor receptor signaling pathway • stress-activated MAPK cascade Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6195	20111
Ensembl	ENSG00000117676	ENSMUSG00000003644
UniProt	Q15418	Q3TIM6
RefSeq (mRNA)	NM_001006665.1	NM_009097.4
RefSeq (protein)	NP_001006666.1	NP_033123.2
Location (UCSC)	Chr 1: 26.86 – 26.9 Mb	Chr 4: 133.4 – 133.44 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]

Interactions

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

See also

• Ribosomal s6 kinase

References

1. ^ Moller DE, Xia CH, Tang W, Zhu AX, Jakubowski M (Apr 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". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6195. 
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. doi:10.1074/jbc.M208475200. ISSN 0021-9258. PMID 12618428. 
4. ^ Roux, Philippe P; Richards Stephanie A, Blenis John (Jul. 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. doi:10.1128/MCB.23.14.4796-4804.2003. ISSN 0270-7306. PMC 162206. PMID 12832467. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=162206. 
5. ^ Eblen, Scott T; Kumar N Vinay, Shah Kavita, Henderson Michelle J, Watts Colin K W, Shokat Kevan M, Weber Michael J (Apr. 2003). "Identification of novel ERK2 substrates through use of an engineered kinase and ATP analogs". J. Biol. Chem. (United States) 278 (17): 14926–35. doi:10.1074/jbc.M300485200. ISSN 0021-9258. PMID 12594221. 
6. ^ Smith, J A; Poteet-Smith C E, Malarkey K, Sturgill T W (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". J. Biol. Chem. (UNITED STATES) 274 (5): 2893–8. doi:10.1074/jbc.274.5.2893. ISSN 0021-9258. PMID 9915826. 
7. ^ Schouten, G J; Vertegaal A C, Whiteside S T, Israël A, Toebes M, Dorsman J C, van der Eb A J, Zantema A (Jun. 1997). "IkappaB alpha is a target for the mitogen-activated 90 kDa ribosomal S6 kinase". EMBO J. (ENGLAND) 16 (11): 3133–44. doi:10.1093/emboj/16.11.3133. ISSN 0261-4189. PMC 1169932. PMID 9214631. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1169932. 
8. ^ Suzuki, T; Matsuda S, Tsuzuku J K, Yoshida Y, Yamamoto T (Feb. 2001). "A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob". Genes Cells (England) 6 (2): 131–8. doi:10.1046/j.1365-2443.2001.00406.x. ISSN 1356-9597. PMID 11260258. 
9. ^ Roux, Philippe P; Ballif Bryan A, Anjum Rana, Gygi Steven P, Blenis John (Sep. 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. doi:10.1073/pnas.0405659101. ISSN 0027-8424. PMC 518784. PMID 15342917. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=518784. 
10. ^ Rolfe, Mark; McLeod Laura E, Pratt Phillip F, Proud Christopher G (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)". Biochem. J. (England) 388 (Pt 3): 973–84. doi:10.1042/BJ20041888. PMC 1183479. PMID 15757502. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1183479. 

Further reading

• Chen RH, Sarnecki C, Blenis J (1992). "Nuclear localization and regulation of erk- and rsk-encoded protein kinases.". Mol. Cell. Biol. 12 (3): 915–27. PMC 369523. PMID 1545823. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=369523. 
• Tratner I, Ofir R, Verma IM (1992). "Alteration of a cyclic AMP-dependent protein kinase phosphorylation site in the c-Fos protein augments its transforming potential.". Mol. Cell. Biol. 12 (3): 998–1006. PMC 369532. PMID 1545828. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=369532. 
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Chen RH, Abate C, Blenis J (1994). "Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase". Proc. Natl. Acad. Sci. U.S.A. 90 (23): 10952–6. doi:10.1073/pnas.90.23.10952. PMC 47899. PMID 8248197. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=47899. 
• Rivera VM, Miranti CK, Misra RP, et al. (1993). "A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity". Mol. Cell. Biol. 13 (10): 6260–73. PMC 364685. PMID 8413226. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=364685. 
• Chen ZJ, Parent L, Maniatis T (1996). "Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity". Cell 84 (6): 853–62. doi:10.1016/S0092-8674(00)81064-8. PMID 8601309. 
• Barge RM, de Koning JP, Pouwels K, et al. (1996). "Tryptophan 650 of human granulocyte colony-stimulating factor (G-CSF) receptor, implicated in the activation of JAK2, is also required for G-CSF-mediated activation of signaling complexes of the p21ras route". Blood 87 (6): 2148–53. PMID 8630373. 
• Wong EV, Schaefer AW, Landreth G, Lemmon V (1996). "Involvement of p90rsk in neurite outgrowth mediated by the cell adhesion molecule L1". J. Biol. Chem. 271 (30): 18217–23. doi:10.1074/jbc.271.30.18217. PMID 8663493. 
• Xing J, Ginty DD, Greenberg ME (1996). "Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase". Science 273 (5277): 959–63. doi:10.1126/science.273.5277.959. PMID 8688081. 
• Nakajima T, Fukamizu A, Takahashi J, et al. (1996). "The signal-dependent coactivator CBP is a nuclear target for pp90RSK". Cell 86 (3): 465–74. doi:10.1016/S0092-8674(00)80119-1. PMID 8756728. 
• Zhao Y, Bjorbaek C, Moller DE (1997). "Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases". J. Biol. Chem. 271 (47): 29773–9. doi:10.1074/jbc.271.47.29773. PMID 8939914. 
• Zaheer A, Lim R (1997). "Protein kinase A (PKA)- and protein kinase C-phosphorylated glia maturation factor promotes the catalytic activity of PKA". J. Biol. Chem. 272 (8): 5183–6. doi:10.1074/jbc.272.8.5183. PMID 9030586. 
• Schouten GJ, Vertegaal AC, Whiteside ST, et al. (1997). "IkappaB alpha is a target for the mitogen-activated 90 kDa ribosomal S6 kinase". EMBO J. 16 (11): 3133–44. doi:10.1093/emboj/16.11.3133. PMC 1169932. PMID 9214631. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1169932. 
• Li HL, Forman MS, Kurosaki T, Puré E (1997). "Syk is required for BCR-mediated activation of p90Rsk, but not p70S6k, via a mitogen-activated protein kinase-independent pathway in B cells". J. Biol. Chem. 272 (29): 18200–8. doi:10.1074/jbc.272.29.18200. PMID 9218456. 
• Chang YW, Traugh JA (1997). "Phosphorylation of elongation factor 1 and ribosomal protein S6 by multipotential S6 kinase and insulin stimulation of translational elongation". J. Biol. Chem. 272 (45): 28252–7. doi:10.1074/jbc.272.45.28252. PMID 9353277. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• del Peso L, González-García M, Page C, et al. (1997). "Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt". Science 278 (5338): 687–9. doi:10.1126/science.278.5338.687. PMID 9381178. 
• Dalby KN, Morrice N, Caudwell FB, et al. (1998). "Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK". J. Biol. Chem. 273 (3): 1496–505. doi:10.1074/jbc.273.3.1496. PMID 9430688. 
• Joel PB, Smith J, Sturgill TW, et al. (1998). "pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167". Mol. Cell. Biol. 18 (4): 1978–84. PMC 121427. PMID 9528769. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=121427.