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RPS6KB2

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From Wikipedia, the free encyclopedia

Enzyme

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)^[1]

Band	11q13.2	Start	67,428,460bp^[1]
Band	11q13.2	End	67,435,401bp^[1]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

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

BioGPS


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

Species

Human

Mouse

Entrez


6199


58988

Ensembl


ENSG00000175634


ENSMUSG00000024830

UniProt


Q9UBS0


Q9Z1M4

RefSeq (mRNA)


NM_001007071 NM_003952


NM_021485

RefSeq (protein)


NP_003943


NP_067460.1

Location (UCSC)

Chr 11: 67.43 – 67.44 Mb

n/a

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

Ribosomal protein S6 kinase beta-2 is anenzyme that in humans is encoded by theRPS6KB2gene.^[4]^[5]^[6]

This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine/threoninekinases. This kinase contains two nonidentical kinase catalytic domains andphosphorylates 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

[edit]

^^a ^b ^cGRCh38: 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.

Kinases:Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated mTOR EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1
Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3 PDK4
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4
Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase Aurora C kinase
Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-
IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP
cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY
cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1
Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3
Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase
Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2
G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6
Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK1A CAMK1B CAMK1D CAMK1G CAMK2 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1
Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4
Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2
Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19
Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4
Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1
Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14
MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14
Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-
Tropomyosin kinase (EC 2.7.11.28)	-
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-
Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

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	EC1Oxidoreductases (list) EC2Transferases (list) EC3Hydrolases (list) EC4Lyases (list) EC5Isomerases (list) EC6Ligases (list) EC7Translocases (list)

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