RPS6KA2

RPS6KA2
Identifiers
Aliases	RPS6KA2, HU-2, MAPKAPK1C, RSK, RSK3, S6K-alpha, S6K-alpha2, p90-RSK3, pp90RSK3, p90RSK2, ribosomal protein S6 kinase A2
External IDs	OMIM: 601685 MGI: 1342290 HomoloGene: 100680 GeneCards: RPS6KA2
Gene location (Human)
Chr.	Chromosome 6 (human)[1]
End	166,906,451 bp[1]
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)[2]
End	7,303,315 bp[2]
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• transferase activity; • nucleotide binding; • protein kinase activity; • metal ion binding; • GO:0001948 protein binding; • protein serine/threonine/tyrosine kinase activity; • ATP 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	• phosphorylation; • negative regulation of cell cycle; • protein phosphorylation; • positive regulation of apoptotic process; • negative regulation of cell proliferation; • signal transduction; • GO:0007243 intracellular signal transduction;
	Sources:Amigo / QuickGO
Orthologs
	6196
	20112
	ENSG00000071242
	ENSMUSG00000023809
	Q15349
	Q9WUT3
	NM_001006932; NM_021135; NM_001318936; NM_001318937; NM_001318938
	NM_011299
	NP_001006933; NP_001305865; NP_001305866; NP_001305867; NP_066958
	NP_035429
	Wikidata
View/Edit Human	View/Edit Mouse

Ribosomal protein S6 kinase alpha-2 is an enzyme that in humans is encoded by the RPS6KA2 gene.[5][6]

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

Interactions

RPS6KA2 has been shown to interact with MAPK3[7][8] and MAPK1.[7][8]

References

GRCh38: Ensembl release 89: ENSG00000071242 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000023809 - 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.
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. doi:10.1152/ajpcell.1994.266.2.C351. PMID 8141249.
"Entrez Gene: RPS6KA2 ribosomal protein S6 kinase, 90kDa, polypeptide 2".
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.
Zhao, Y; Bjorbaek C; Moller D E (Nov 1996). "Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases". J. Biol. Chem. UNITED STATES. 271 (47): 29773–9. doi:10.1074/jbc.271.47.29773. ISSN 0021-9258. PMID 8939914.

Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
Zhao Y, Bjørbaek C, Weremowicz S, et al. (1995). "RSK3 encodes a novel pp90rsk isoform with a unique N-terminal sequence: growth factor-stimulated kinase function and nuclear translocation". Mol. Cell. Biol. 15 (8): 4353–63. doi:10.1128/MCB.15.8.4353. PMC 230675. PMID 7623830.
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. Bibcode:1996Sci...273..959X. doi:10.1126/science.273.5277.959. PMID 8688081. S2CID 22226803.
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.
Fukunaga R, Hunter T (1997). "MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates". EMBO J. 16 (8): 1921–33. doi:10.1093/emboj/16.8.1921. PMC 1169795. PMID 9155018.
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. Bibcode:1997Sci...278..687D. doi:10.1126/science.278.5338.687. PMID 9381178.
Deak M, Clifton AD, Lucocq LM, Alessi DR (1998). "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB". EMBO J. 17 (15): 4426–41. doi:10.1093/emboj/17.15.4426. PMC 1170775. PMID 9687510.
Du K, Montminy M (1999). "CREB is a regulatory target for the protein kinase Akt/PKB". J. Biol. Chem. 273 (49): 32377–9. doi:10.1074/jbc.273.49.32377. PMID 9829964.
Smith JA, Poteet-Smith CE, Malarkey K, Sturgill TW (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. 274 (5): 2893–8. doi:10.1074/jbc.274.5.2893. PMID 9915826.
Jensen CJ, Buch MB, Krag TO, et al. (1999). "90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1". J. Biol. Chem. 274 (38): 27168–76. doi:10.1074/jbc.274.38.27168. PMID 10480933.
Schimenti JC (2000). "ORFless, intronless, and mutant transcription units in the mouse t complex responder (Tcr) locus". Mamm. Genome. 10 (10): 969–76. doi:10.1007/s003359901142. PMID 10501965. S2CID 23157540.
Scheid MP, Schubert KM, Duronio V (1999). "Regulation of bad phosphorylation and association with Bcl-x(L) by the MAPK/Erk kinase". J. Biol. Chem. 274 (43): 31108–13. doi:10.1074/jbc.274.43.31108. PMID 10521512.
Tan Y, Demeter MR, Ruan H, Comb MJ (2000). "BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival". J. Biol. Chem. 275 (33): 25865–9. doi:10.1074/jbc.M004199200. PMID 10837486.
Lizcano JM, Morrice N, Cohen P (2001). "Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155". Biochem. J. 349 (Pt 2): 547–57. doi:10.1042/0264-6021:3490547. PMC 1221178. PMID 10880354.
Datta SR, Katsov A, Hu L, et al. (2000). "14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation". Mol. Cell. 6 (1): 41–51. doi:10.1016/S1097-2765(00)00006-X. PMID 10949026.
Gudi T, Casteel DE, Vinson C, et al. (2001). "NO activation of fos promoter elements requires nuclear translocation of G-kinase I and CREB phosphorylation but is independent of MAP kinase activation". Oncogene. 19 (54): 6324–33. doi:10.1038/sj.onc.1204007. PMID 11175347.
Willard FS, Crouch MF (2001). "MEK, ERK, and p90RSK are present on mitotic tubulin in Swiss 3T3 cells: a role for the MAP kinase pathway in regulating mitotic exit". Cell. Signal. 13 (9): 653–64. doi:10.1016/S0898-6568(01)00185-1. PMID 11495723.
Schinelli S, Zanassi P, Paolillo M, et al. (2001). "Stimulation of endothelin B receptors in astrocytes induces cAMP response element-binding protein phosphorylation and c-fos expression via multiple mitogen-activated protein kinase signaling pathways". J. Neurosci. 21 (22): 8842–53. doi:10.1523/JNEUROSCI.21-22-08842.2001. PMC 6762276. PMID 11698596.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000071242 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000023809 - 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.

[pmid8141249-5] 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. doi:10.1152/ajpcell.1994.266.2.C351. PMID 8141249.

[entrez-6] "Entrez Gene: RPS6KA2 ribosomal protein S6 kinase, 90kDa, polypeptide 2".

[pmid12832467-7] 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.

[pmid8939914-8] Zhao, Y; Bjorbaek C; Moller D E (Nov 1996). "Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases". J. Biol. Chem. UNITED STATES. 271 (47): 29773–9. doi:10.1074/jbc.271.47.29773. ISSN 0021-9258. PMID 8939914.

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)

RPS6KA2

Interactions

References

Further reading