RPS6KB2

RPS6KB2
Identifiers
Aliases	RPS6KB2, KLS, P70-beta, P70-beta-1, P70-beta-2, S6K-beta2, S6K2, SRK, STK14B, p70(S6K)-beta, p70S6Kb, ribosomal protein S6 kinase B2, S6KB, S6KI(2), S6Kbeta
External IDs	OMIM: 608939; MGI: 1927343; HomoloGene: 68374; GeneCards: RPS6KB2; OMA:RPS6KB2 - orthologs
Gene location (Human)
Chr.	Chromosome 11 (human)
End	67,435,401 bp
RNA expression pattern
	Top expressed in
	skin of leg; ; skin of abdomen; ; granulocyte; ; body of stomach; ; apex of heart; ; right lobe of liver; ; right hemisphere of cerebellum; ; anterior pituitary; ; muscle of thigh; ; mucosa of transverse colon;
	n/a
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity; protein kinase activity; nucleotide binding; peptide binding; kinase activity; protein serine/threonine kinase activity; ATP binding; ribosomal protein S6 kinase activity;
Cellular component	cytoplasm; nucleoplasm; nucleus;
Biological process	intracellular signal transduction; protein biosynthesis; phosphorylation; protein phosphorylation; positive regulation of translational initiation; signal transduction; protein kinase B signaling; TOR signaling;
	Sources:Amigo / QuickGO
Orthologs
	6199
	58988
	ENSG00000175634
	ENSMUSG00000024830
	Q9UBS0
	Q9Z1M4
	NM_001007071; NM_003952
	NM_021485
	NP_003943
	NP_067460.1
	Wikidata
View/Edit Human	View/Edit Mouse

Ribosomal protein S6 kinase beta-2 is an enzyme that in humans is encoded by the RPS6KB2 gene.^[4]^[5]^[6]

This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine/threonine kinases. This kinase contains two nonidentical kinase catalytic domains and phosphorylates the S6 ribosomal protein and eucaryotic translation initiation factor 4B (eIF4B). Phosphorylation of S6 leads to an increase in protein synthesis and cell proliferation.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000175634 – 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.
^ Saitoh M, ten Dijke P, Miyazono K, Ichijo H (Jan 1999). "Cloning and characterization of p70(S6K beta) defines a novel family of p70 S6 kinases". Biochem Biophys Res Commun. 253 (2): 470–476. doi:10.1006/bbrc.1998.9784. PMID 9878560.
^ Gout I, Minami T, Hara K, Tsujishita Y, Filonenko V, Waterfield MD, Yonezawa K (Dec 1998). "Molecular cloning and characterization of a novel p70 S6 kinase, p70 S6 kinase beta containing a proline-rich region". J Biol Chem. 273 (46): 30061–30064. doi:10.1074/jbc.273.46.30061. PMID 9804755.
^ ^a ^b "Entrez Gene: RPS6KB2 ribosomal protein S6 kinase, 70kDa, polypeptide 2".

Lee-Fruman KK, Kuo CJ, Lippincott J, et al. (1999). "Characterization of S6K2, a novel kinase homologous to S6K1". Oncogene. 18 (36): 5108–5114. doi:10.1038/sj.onc.1202894. PMID 10490847.
Koh H, Jee K, Lee B, et al. (1999). "Cloning and characterization of a nuclear S6 kinase, S6 kinase-related kinase (SRK); a novel nuclear target of Akt". Oncogene. 18 (36): 5115–5119. doi:10.1038/sj.onc.1202895. PMID 10490848.
Martin KA, Schalm SS, Richardson C, et al. (2001). "Regulation of ribosomal S6 kinase 2 by effectors of the phosphoinositide 3-kinase pathway". J. Biol. Chem. 276 (11): 7884–7891. doi:10.1074/jbc.M006969200. PMID 11108711.
Martin KA, Schalm SS, Romanelli A, et al. (2001). "Ribosomal S6 kinase 2 inhibition by a potent C-terminal repressor domain is relieved by mitogen-activated protein-extracellular signal-regulated kinase kinase-regulated phosphorylation". J. Biol. Chem. 276 (11): 7892–7898. doi:10.1074/jbc.M009972200. PMID 11108720.
Minami T, Hara K, Oshiro N, et al. (2002). "Distinct regulatory mechanism for p70 S6 kinase beta from that for p70 S6 kinase alpha". Genes Cells. 6 (11): 1003–1015. doi:10.1046/j.1365-2443.2001.00479.x. PMID 11733037. S2CID 24500851.
Pardo OE, Arcaro A, Salerno G, et al. (2002). "Novel cross talk between MEK and S6K2 in FGF-2 induced proliferation of SCLC cells". Oncogene. 20 (52): 7658–7667. doi:10.1038/sj.onc.1204994. PMID 11753643.
Park IH, Bachmann R, Shirazi H, Chen J (2002). "Regulation of ribosomal S6 kinase 2 by mammalian target of rapamycin". J. Biol. Chem. 277 (35): 31423–31429. doi:10.1074/jbc.M204080200. PMID 12087098.
Kanayasu-Toyoda T, Yamaguchi T, Oshizawa T, et al. (2002). "Role of the p70 S6 kinase cascade in neutrophilic differentiation and proliferation of HL-60 cells-a study of transferrin receptor-positive and -negative cells obtained from dimethyl sulfoxide- or retinoic acid-treated HL-60 cells". Arch. Biochem. Biophys. 405 (1): 21–31. doi:10.1016/S0003-9861(02)00330-2. PMID 12176053.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Valovka T, Verdier F, Cramer R, et al. (2003). "Protein kinase C phosphorylates ribosomal protein S6 kinase betaII and regulates its subcellular localization". Mol. Cell. Biol. 23 (3): 852–863. doi:10.1128/MCB.23.3.852-863.2003. PMC 140705. PMID 12529391.
Phin S, Kupferwasser D, Lam J, Lee-Fruman KK (2003). "Mutational analysis of ribosomal S6 kinase 2 shows differential regulation of its kinase activity from that of ribosomal S6 kinase 1". Biochem. J. 373 (Pt 2): 583–91. doi:10.1042/BJ20021794. PMC 1223513. PMID 12713446.
Kanayasu-Toyoda T, Yamaguchi T, Oshizawa T, et al. (2003). "The role of c-Myc on granulocyte colony-stimulating factor-dependent neutrophilic proliferation and differentiation of HL-60 cells". Biochem. Pharmacol. 66 (1): 133–140. doi:10.1016/S0006-2952(03)00247-8. PMID 12818373.
An WL, Cowburn RF, Li L, et al. (2003). "Up-regulation of phosphorylated/activated p70 S6 kinase and its relationship to neurofibrillary pathology in Alzheimer's disease". Am. J. Pathol. 163 (2): 591–607. doi:10.1016/S0002-9440(10)63687-5. PMC 1868198. PMID 12875979.
Shao J, Evers BM, Sheng H (2004). "Roles of phosphatidylinositol 3'-kinase and mammalian target of rapamycin/p70 ribosomal protein S6 kinase in K-Ras-mediated transformation of intestinal epithelial cells". Cancer Res. 64 (1): 229–235. doi:10.1158/0008-5472.CAN-03-1859. PMID 14729629.
Lekmine F, Sassano A, Uddin S, et al. (2004). "Interferon-gamma engages the p70 S6 kinase to regulate phosphorylation of the 40S S6 ribosomal protein". Exp. Cell Res. 295 (1): 173–182. doi:10.1016/j.yexcr.2003.12.021. PMID 15051500.
Raught B, Peiretti F, Gingras AC, et al. (2005). "Phosphorylation of eucaryotic translation initiation factor 4B Ser422 is modulated by S6 kinases". EMBO J. 23 (8): 1761–1769. doi:10.1038/sj.emboj.7600193. PMC 394247. PMID 15071500.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–2127. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000175634 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9878560-4] Saitoh M, ten Dijke P, Miyazono K, Ichijo H (Jan 1999). "Cloning and characterization of p70(S6K beta) defines a novel family of p70 S6 kinases". Biochem Biophys Res Commun. 253 (2): 470–476. doi:10.1006/bbrc.1998.9784. PMID 9878560.

[pmid9804755-5] Gout I, Minami T, Hara K, Tsujishita Y, Filonenko V, Waterfield MD, Yonezawa K (Dec 1998). "Molecular cloning and characterization of a novel p70 S6 kinase, p70 S6 kinase beta containing a proline-rich region". J Biol Chem. 273 (46): 30061–30064. doi:10.1074/jbc.273.46.30061. PMID 9804755.

[entrez-6] "Entrez Gene: RPS6KB2 ribosomal protein S6 kinase, 70kDa, polypeptide 2".

[1]

[2]

[3]

[4]

[5]

[6]

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme 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)

References

Further reading