RPS6KA2

Enzyme found in humans
RPS6KA2
Identifiers
AliasesRPS6KA2, HU-2, MAPKAPK1C, RSK, RSK3, S6K-alpha, S6K-alpha2, p90-RSK3, pp90RSK3, p90RSK2, ribosomal protein S6 kinase A2
External IDsOMIM: 601685 MGI: 1342290 HomoloGene: 100680 GeneCards: RPS6KA2
Gene location (Human)
Chromosome 6 (human)
Chr.Chromosome 6 (human)[1]
Chromosome 6 (human)
Genomic location for RPS6KA2
Genomic location for RPS6KA2
Band6q27Start166,409,364 bp[1]
End166,906,451 bp[1]
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)[2]
Chromosome 17 (mouse)
Genomic location for RPS6KA2
Genomic location for RPS6KA2
Band17 A1|17 4.7 cMStart7,437,514 bp[2]
End7,570,714 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • inferior olivary nucleus

  • lower lobe of lung

  • internal globus pallidus

  • inferior ganglion of vagus nerve

  • optic nerve

  • right lung

  • corpus callosum

  • superior vestibular nucleus

  • external globus pallidus

  • sural nerve
Top expressed in
  • superior frontal gyrus

  • lens

  • yolk sac

  • neural tube

  • lip

  • esophagus

  • ganglionic eminence

  • skeletal muscle tissue

  • pretectal area

  • spermatocyte
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • nucleotide binding
  • protein kinase activity
  • metal ion binding
  • 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
  • nucleus
Biological process
  • phosphorylation
  • negative regulation of cell cycle
  • protein phosphorylation
  • positive regulation of apoptotic process
  • negative regulation of cell population proliferation
  • signal transduction
  • intracellular signal transduction
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

6196

20112

Ensembl

ENSG00000071242

ENSMUSG00000023809

UniProt

Q15349

Q9WUT3

RefSeq (mRNA)

NM_001006932
NM_021135
NM_001318936
NM_001318937
NM_001318938

NM_011299

RefSeq (protein)

NP_001006933
NP_001305865
NP_001305866
NP_001305867
NP_066958

NP_035429

Location (UCSC)Chr 6: 166.41 – 166.91 MbChr 17: 7.44 – 7.57 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000071242 – Ensembl, May 2017
  2. ^ a b c 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.
  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.
  6. ^ a b "Entrez Gene: RPS6KA2 ribosomal protein S6 kinase, 90kDa, polypeptide 2".
  7. ^ a b Roux PP, 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. 23 (14). United States: 4796–804. doi:10.1128/MCB.23.14.4796-4804.2003. ISSN 0270-7306. PMC 162206. PMID 12832467.
  8. ^ a b Zhao Y, Bjorbaek C, Moller D E (Nov 1996). "Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases". J. Biol. Chem. 271 (47). UNITED STATES: 29773–9. doi:10.1074/jbc.271.47.29773. ISSN 0021-9258. PMID 8939914.

Further reading

  • 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. S2CID 20150481.
  • 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.
  • v
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Non-specific serine/threonine protein kinases (EC 2.7.11.1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
  • -
IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)
Cyclin-dependent kinase (EC 2.7.11.22)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
Tau-protein kinase (EC 2.7.11.26)
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)
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Tropomyosin kinase (EC 2.7.11.28)
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Low-density-lipoprotein receptor kinase (EC 2.7.11.29)
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Receptor protein serine/threonine kinase (EC 2.7.11.30)
MAP2K
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