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RPS6KA2

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From Wikipedia, the free encyclopedia

Enzyme found in humans

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;OMA:RPS6KA2 - orthologs

Gene location (Human)

Chr.	Chromosome 6 (human)^[1]

Band	6q27	Start	166,409,364bp^[1]
Band	6q27	End	166,906,451bp^[1]

Gene location (Mouse)

Chr.	Chromosome 17 (mouse)^[2]

Band	17 A1\|17 4.7 cM	Start	7,437,514bp^[2]
Band	17 A1\|17 4.7 cM	End	7,570,714bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

inferior olivary nucleus

lower lobe of lung

internal globus pallidus

dorsal motor nucleus of vagus nerve

inferior ganglion of vagus nerve

C1 segment

optic nerve

right lung

corpus callosum

superior vestibular nucleus

Top expressed in

granulocyte

muscle of thigh

neural layer of retina

tail of embryo

superior frontal gyrus

dentate gyrus of hippocampal formation granule cell

primary visual cortex

genital tubercle

lens

ventricular zone

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

Species

Human

Mouse

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 Mb

Chr 17: 7.44 – 7.57 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Ribosomal protein S6 kinase alpha-2 is anenzyme that in humans is encoded by theRPS6KA2gene.^[5]^[6]

This gene encodes a member of the RSK (ribosomal S6 kinase) family ofserine andthreonine kinases. This kinase contains 2 non-identical kinase catalytic domains and phosphorylates various substrates, including members of themitogen-activated kinase (MAPK) signalling pathway. The activity of this protein has been implicated in controlling cell growth anddifferentiation. Alternate transcriptional splice variants, encoding differentisoforms, have been characterized.^[6]

Interactions

[edit]

RPS6KA2 has been shown tointeract withMAPK3^[7]^[8] andMAPK1.^[7]^[8]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000071242 –Ensembl, May 2017
^^a ^b ^cGRCm38: 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.
^^a ^b"Entrez Gene: RPS6KA2 ribosomal protein S6 kinase, 90kDa, polypeptide 2".
^^a ^bRoux 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.
^^a ^bZhao 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.

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.

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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