RPS6KA2

From Wikipedia, the free encyclopedia

Ribosomal protein S6 kinase, 90kDa, polypeptide 2

Identifiers

RPS6KA2; HU-2; RSK; MAPKAPK1C; RSK3; S6K-alpha; S6K-alpha2; p90-RSK3; pp90RSK3

External IDs

OMIM: 601685 MGI: 1342290 HomoloGene: 36318

Gene ontology
Molecular Function:	• nucleotide binding • magnesium ion binding • protein serine/threonine kinase activity • ATP binding • transferase activity
Cellular Component:	• nucleus
Biological Process:	• protein amino acid phosphorylation • protein kinase cascade

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_001006932 (mRNA)
NP_001006933 (protein)

XM_489703 (mRNA)
XP_489703 (protein)

Location

Chr 6: 166.74 - 167.2 Mb

n/a

Pubmed search

[1]

[2]

Ribosomal protein S6 kinase, 90kDa, polypeptide 2, also known as RPS6KA2, is a human gene.^[1]

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. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.^[1]

[edit] References

^ ^a ^b Entrez Gene: RPS6KA2 ribosomal protein S6 kinase, 90kDa, polypeptide 2.

[edit] Further reading

Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317–20. 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. PMID 7623830.
Moller DE, Xia CH, Tang W, et al. (1994). "Human rsk isoforms: cloning and characterization of tissue-specific expression.". Am. J. Physiol. 266 (2 Pt 1): C351–9. PMID 8141249.
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. 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. PMID 8688081.
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. 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. 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. 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. 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. 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. 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. 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. PMID 10501965.
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. 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. 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. 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. 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. PMID 11698596.