RPS6KA3

RPS6KA3
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4D9T, 4D9U, 4JG6, 4JG7, 4JG8, 4NUS, 4NW5, 4NW6, 5D9K, 5D9L
Identifiers
Aliases	RPS6KA3, CLS, HU-3, ISPK-1, MAPKAPK1B, MRX19, RSK, RSK2, S6K-alpha3, p90-RSK2, pp90RSK2, ribosomal protein S6 kinase A3
External IDs	OMIM: 300075 MGI: 104557 HomoloGene: 37940 GeneCards: RPS6KA3
Gene location (Human)
Chr.	X chromosome (human)[1]
End	20,267,519 bp[1]
Gene location (Mouse)
Chr.	X chromosome (mouse)[2]
End	159,368,244 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• transferase activity; • protein kinase activity; • nucleotide binding; • metal ion binding; • cysteine-type endopeptidase inhibitor activity involved in apoptotic process; • GO:0001948 protein binding; • ATP binding; • protein kinase binding; • magnesium ion binding; • kinase activity; • protein serine/threonine kinase activity; • ribosomal protein S6 kinase activity;
Cellular component	• cytoplasm; • cytosol; • nucleoplasm; • cell nucleus;
Biological process	• skeletal system development; • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; • regulation of translation in response to stress; • GO:0007243 intracellular signal transduction; • phosphorylation; • negative regulation of apoptotic process; • protein phosphorylation; • central nervous system development; • positive regulation of cell growth; • response to lipopolysaccharide; • positive regulation of cell differentiation; • cell cycle; • regulation of DNA-templated transcription in response to stress; • signal transduction; • positive regulation of transcription from RNA polymerase II promoter; • toll-like receptor signaling pathway; • apoptotic process; • peptidyl-serine phosphorylation;
	Sources:Amigo / QuickGO
Orthologs
	6197
	110651
	ENSG00000177189
	ENSMUSG00000031309
	P51812
	P18654
	NM_004586
	NM_148945; NM_001346675
	NP_004577
	NP_001333604; NP_683747
	Wikidata
View/Edit Human	View/Edit Mouse

protein S6 kinase, 90kDa, polypeptide 3, also s RPS6KA3, is an enzyme that in humans is encoded by the RPS6KA3 gene.[5][6]

Function

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.[5]

Clinical significance

Mutations in this gene have been associated with Coffin–Lowry syndrome (CLS).[7]

Interactions

RPS6KA3 has been shown to interact with CREB-binding protein,[8] MAPK1[9][10] and PEA15.[11]

References

GRCh38: Ensembl release 89: ENSG00000177189 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000031309 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Entrez Gene: RPS6KA3 ribosomal protein S6 kinase, 90kDa, polypeptide 3".
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. doi:10.1152/ajpcell.1994.266.2.C351. PMID 8141249.
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. doi:10.1038/sj.ejhg.5200738. PMID 11896450.
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. doi:10.1128/MCB.21.20.7089-7096.2001. PMC 99884. PMID 11564891.
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. doi:10.1074/jbc.271.47.29773. PMID 8939914.
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. doi:10.1074/jbc.274.5.2893. PMID 9915826.
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. doi:10.1074/jbc.M303988200. PMID 12796492.

Omary MB, Baxter GT, Chou CF, Riopel CL, Lin WY, Strulovici B (May 1992). "PKC epsilon-related kinase associates with and phosphorylates cytokeratin 8 and 18". The Journal of Cell Biology. 117 (3): 583–93. doi:10.1083/jcb.117.3.583. PMC 2289443. PMID 1374067.
Ku NO, Omary MB (October 1994). "Identification of the major physiologic phosphorylation site of human keratin 18: potential kinases and a role in filament reorganization". The Journal of Cell Biology. 127 (1): 161–71. doi:10.1083/jcb.127.1.161. PMC 2120194. PMID 7523419.
Adams MD, Kerlavage AR, Fleischmann RD, Fuldner RA, Bult CJ, Lee NH, Kirkness EF, Weinstock KG, Gocayne JD, White O (September 1995). "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence" (PDF). Nature. 377 (6547 Suppl): 3–174. PMID 7566098.
Zhao Y, Bjørbaek C, Weremowicz S, Morton CC, Moller DE (August 1995). "RSK3 encodes a novel pp90rsk isoform with a unique N-terminal sequence: growth factor-stimulated kinase function and nuclear translocation". Molecular and Cellular Biology. 15 (8): 4353–63. doi:10.1128/MCB.15.8.4353. PMC 230675. PMID 7623830.
Bjørbaek C, Vik TA, Echwald SM, Yang PY, Vestergaard H, Wang JP, Webb GC, Richmond K, Hansen T, Erikson RL (January 1995). "Cloning of a human insulin-stimulated protein kinase (ISPK-1) gene and analysis of coding regions and mRNA levels of the ISPK-1 and the protein phosphatase-1 genes in muscle from NIDDM patients". Diabetes. 44 (1): 90–7. doi:10.2337/diabetes.44.1.90. PMID 7813820.
Donnelly AJ, Choo KH, Kozman HM, Gedeon AK, Danks DM, Mulley JC (July 1994). "Regional localisation of a non-specific X-linked mental retardation gene (MRX19) to Xp22". American Journal of Medical Genetics. 51 (4): 581–5. doi:10.1002/ajmg.1320510457. PMID 7943043.
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. doi:10.1152/ajpcell.1994.266.2.C351. PMID 8141249.
Xing J, Ginty DD, Greenberg ME (August 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.
Trivier E, De Cesare D, Jacquot S, Pannetier S, Zackai E, Young I, Mandel JL, Sassone-Corsi P, Hanauer A (December 1996). "Mutations in the kinase Rsk-2 associated with Coffin-Lowry syndrome". Nature. 384 (6609): 567–70. doi:10.1038/384567a0. PMID 8955270.
Paudel HK (November 1997). "Phosphorylation by neuronal cdc2-like protein kinase promotes dimerization of Tau protein in vitro". The Journal of Biological Chemistry. 272 (45): 28328–34. doi:10.1074/jbc.272.45.28328. PMID 9353289.
Joel PB, Smith J, Sturgill TW, Fisher TL, Blenis J, Lannigan DA (April 1998). "pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167". Molecular and Cellular Biology. 18 (4): 1978–84. doi:10.1128/mcb.18.4.1978. PMC 121427. PMID 9528769.
Zheng-Fischhöfer Q, Biernat J, Mandelkow EM, Illenberger S, Godemann R, Mandelkow E (March 1998). "Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation". European Journal of Biochemistry. 252 (3): 542–52. doi:10.1046/j.1432-1327.1998.2520542.x. PMID 9546672.
Deak M, Clifton AD, Lucocq LM, Alessi DR (August 1998). "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB". The EMBO Journal. 17 (15): 4426–41. doi:10.1093/emboj/17.15.4426. PMC 1170775. PMID 9687510.
Du K, Montminy M (December 1998). "CREB is a regulatory target for the protein kinase Akt/PKB". The Journal of Biological Chemistry. 273 (49): 32377–9. doi:10.1074/jbc.273.49.32377. PMID 9829964.
Hanger DP, Betts JC, Loviny TL, Blackstock WP, Anderton BH (December 1998). "New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry". Journal of Neurochemistry. 71 (6): 2465–76. doi:10.1046/j.1471-4159.1998.71062465.x. PMID 9832145.
Jacquot S, Merienne K, De Cesare D, Pannetier S, Mandel JL, Sassone-Corsi P, Hanauer A (December 1998). "Mutation analysis of the RSK2 gene in Coffin-Lowry patients: extensive allelic heterogeneity and a high rate of de novo mutations". American Journal of Human Genetics. 63 (6): 1631–40. doi:10.1086/302153. PMC 1377634. PMID 9837815.
Jacquot S, Merienne K, Pannetier S, Blumenfeld S, Schinzel A, Hanauer A (1999). "Germline mosaicism in Coffin-Lowry syndrome". European Journal of Human Genetics. 6 (6): 578–82. doi:10.1038/sj.ejhg.5200230. PMID 9887375.
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. doi:10.1074/jbc.274.5.2893. PMID 9915826.
Abidi F, Jacquot S, Lassiter C, Trivier E, Hanauer A, Schwartz CE (January 1999). "Novel mutations in Rsk-2, the gene for Coffin-Lowry syndrome (CLS)". European Journal of Human Genetics. 7 (1): 20–6. doi:10.1038/sj.ejhg.5200231. PMID 10094187.
Merienne K, Jacquot S, Pannetier S, Zeniou M, Bankier A, Gecz J, Mandel JL, Mulley J, Sassone-Corsi P, Hanauer A (May 1999). "A missense mutation in RPS6KA3 (RSK2) responsible for non-specific mental retardation". Nature Genetics. 22 (1): 13–4. doi:10.1038/8719. PMID 10319851.

External links

GeneReviews/NCBI/NIH/UW entry on Coffin–Lowry syndrome

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000177189 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000031309 - Ensembl, 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.

[entrez-5] "Entrez Gene: RPS6KA3 ribosomal protein S6 kinase, 90kDa, polypeptide 3".

[pmid8141249-6] 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. doi:10.1152/ajpcell.1994.266.2.C351. PMID 8141249.

[pmid11896450-7] 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. doi:10.1038/sj.ejhg.5200738. PMID 11896450.

[pmid11564891-8] 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. doi:10.1128/MCB.21.20.7089-7096.2001. PMC 99884. PMID 11564891.

[pmid8939914-9] 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. doi:10.1074/jbc.271.47.29773. PMID 8939914.

[pmid9915826-10] 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. doi:10.1074/jbc.274.5.2893. PMID 9915826.

[pmid12796492-11] 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. doi:10.1074/jbc.M303988200. PMID 12796492.

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)