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Contents

   



(Top)
 


1 Function  





2 Clinical significance  





3 Interactions  





4 References  





5 Further reading  





6 External links  














RPS6KA3






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RPS6KA3

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes

4D9T, 4D9U, 4JG6, 4JG7, 4JG8, 4NUS, 4NW5, 4NW6, 5D9K, 5D9L

Identifiers

Aliases

RPS6KA3, CLS, HU-3, ISPK-1, MAPKAPK1B, MRX19, RSK, RSK2, S6K-alpha3, p90-RSK2, pp90RSK2, ribosomal protein S6 kinase A3, XLID19

External IDs

OMIM: 300075; MGI: 104557; HomoloGene: 37940; GeneCards: RPS6KA3; OMA:RPS6KA3 - orthologs

Gene location (Human)

X chromosome (human)

Chr.

X chromosome (human)[1]

X chromosome (human)

Genomic location for RPS6KA3

Genomic location for RPS6KA3

Band

Xp22.12

Start

20,149,911 bp[1]

End

20,267,519 bp[1]

Gene location (Mouse)

X chromosome (mouse)

Chr.

X chromosome (mouse)[2]

X chromosome (mouse)

Genomic location for RPS6KA3

Genomic location for RPS6KA3

Band

X F4|X 73.27 cM

Start

157,993,303 bp[2]

End

158,151,240 bp[2]

Bgee

Mouse (ortholog)


  • mucosa of sigmoid colon

  • biceps brachii

  • triceps brachii muscle

  • islet of Langerhans

  • deltoid muscle

  • gastrocnemius muscle

  • glutes

  • quadriceps femoris muscle

  • Skeletal muscle tissue of biceps brachii

  • body of femur

  • left colon

  • white adipose tissue

  • lumbar spinal ganglion

  • Paneth cell

  • left lung lobe

  • genital tubercle

  • mandibular prominence

  • gastrula
  • More reference expression data

    BioGPS

    More reference expression data

    Molecular function

  • protein kinase activity
  • nucleotide binding
  • metal ion binding
  • cysteine-type endopeptidase inhibitor activity involved in apoptotic process
  • protein binding
  • ATP binding
  • protein kinase binding
  • magnesium ion binding
  • kinase activity
  • protein serine/threonine kinase activity
  • ribosomal protein S6 kinase activity
  • Cellular component

  • cytosol
  • nucleoplasm
  • nucleus
  • Biological process

  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process
  • regulation of translation in response to stress
  • intracellular signal transduction
  • phosphorylation
  • negative regulation of apoptotic process
  • protein phosphorylation
  • central nervous system development
  • positive regulation of cell growth
  • response to lipopolysaccharide
  • positive regulation of cell differentiation
  • cell cycle
  • regulation of DNA-templated transcription in response to stress
  • signal transduction
  • positive regulation of transcription by RNA polymerase II
  • toll-like receptor signaling pathway
  • apoptotic process
  • peptidyl-serine phosphorylation
  • Sources:Amigo / QuickGO

    Species

    Human

    Mouse

    Entrez

    Ensembl

    UniProt

    RefSeq (mRNA)

    NM_004586

    NM_148945
    NM_001346675

    RefSeq (protein)

    NP_004577

    NP_001333604
    NP_683747

    Location (UCSC)

    Chr X: 20.15 – 20.27 Mb

    Chr X: 157.99 – 158.15 Mb

    PubMed search

    [3]

    [4]

    Wikidata

    protein S6 kinase, 90kDa, polypeptide 3, also s RPS6KA3, is an enzyme that in humans is encoded by the RPS6KA3 gene.[5][6]

    Function[edit]

    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.[5]

    Clinical significance[edit]

    Mutations in this gene have been associated with Coffin–Lowry syndrome (CLS).[7]

    Interactions[edit]

    RPS6KA3 has been shown to interact with CREB-binding protein,[8] MAPK1[9][10] and PEA15.[11]

    References[edit]

  • ^ "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.
  • ^ a b "Entrez Gene: RPS6KA3 ribosomal protein S6 kinase, 90kDa, polypeptide 3".
  • ^ Moller DE, Xia CH, Tang W, Zhu AX, Jakubowski M (February 1994). "Human rsk isoforms: cloning and characterization of tissue-specific expression". The American Journal of Physiology. 266 (2 Pt 1): C351–9. doi:10.1152/ajpcell.1994.266.2.C351. PMID 8141249.
  • ^ Jacquot S, Zeniou M, Touraine R, Hanauer A (January 2002). "X-linked Coffin-Lowry syndrome (CLS, MIM 303600, RPS6KA3 gene, protein product known under various names: pp90(rsk2), RSK2, ISPK, MAPKAP1)". European Journal of Human Genetics. 10 (1): 2–5. doi:10.1038/sj.ejhg.5200738. PMID 11896450.
  • ^ Merienne K, Pannetier S, Harel-Bellan A, Sassone-Corsi P (October 2001). "Mitogen-regulated RSK2-CBP interaction controls their kinase and acetylase activities". Molecular and Cellular Biology. 21 (20): 7089–96. doi:10.1128/MCB.21.20.7089-7096.2001. PMC 99884. PMID 11564891.
  • ^ Zhao Y, Bjorbaek C, Moller DE (November 1996). "Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases". The Journal of Biological Chemistry. 271 (47): 29773–9. doi:10.1074/jbc.271.47.29773. PMID 8939914.
  • ^ Smith JA, Poteet-Smith CE, Malarkey K, Sturgill TW (January 1999). "Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo". The Journal of Biological Chemistry. 274 (5): 2893–8. doi:10.1074/jbc.274.5.2893. PMID 9915826.
  • ^ Vaidyanathan H, Ramos JW (August 2003). "RSK2 activity is regulated by its interaction with PEA-15". The Journal of Biological Chemistry. 278 (34): 32367–72. doi:10.1074/jbc.M303988200. PMID 12796492.
  • Further reading[edit]

  • Ku NO, Omary MB (October 1994). "Identification of the major physiologic phosphorylation site of human keratin 18: potential kinases and a role in filament reorganization". The Journal of Cell Biology. 127 (1): 161–71. doi:10.1083/jcb.127.1.161. PMC 2120194. PMID 7523419.
  • Adams MD, Kerlavage AR, Fleischmann RD, Fuldner RA, Bult CJ, Lee NH, Kirkness EF, Weinstock KG, Gocayne JD, White O (September 1995). "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence" (PDF). Nature. 377 (6547 Suppl): 3–174. PMID 7566098.
  • Zhao Y, Bjørbaek C, Weremowicz S, Morton CC, Moller DE (August 1995). "RSK3 encodes a novel pp90rsk isoform with a unique N-terminal sequence: growth factor-stimulated kinase function and nuclear translocation". Molecular and Cellular Biology. 15 (8): 4353–63. doi:10.1128/MCB.15.8.4353. PMC 230675. PMID 7623830.
  • Bjørbaek C, Vik TA, Echwald SM, Yang PY, Vestergaard H, Wang JP, Webb GC, Richmond K, Hansen T, Erikson RL (January 1995). "Cloning of a human insulin-stimulated protein kinase (ISPK-1) gene and analysis of coding regions and mRNA levels of the ISPK-1 and the protein phosphatase-1 genes in muscle from NIDDM patients". Diabetes. 44 (1): 90–7. doi:10.2337/diabetes.44.1.90. PMID 7813820.
  • Donnelly AJ, Choo KH, Kozman HM, Gedeon AK, Danks DM, Mulley JC (July 1994). "Regional localisation of a non-specific X-linked mental retardation gene (MRX19) to Xp22". American Journal of Medical Genetics. 51 (4): 581–5. doi:10.1002/ajmg.1320510457. PMID 7943043.
  • Moller DE, Xia CH, Tang W, Zhu AX, Jakubowski M (February 1994). "Human rsk isoforms: cloning and characterization of tissue-specific expression". The American Journal of Physiology. 266 (2 Pt 1): C351–9. doi:10.1152/ajpcell.1994.266.2.C351. PMID 8141249.
  • Xing J, Ginty DD, Greenberg ME (August 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.
  • Trivier E, De Cesare D, Jacquot S, Pannetier S, Zackai E, Young I, Mandel JL, Sassone-Corsi P, Hanauer A (December 1996). "Mutations in the kinase Rsk-2 associated with Coffin-Lowry syndrome". Nature. 384 (6609): 567–70. Bibcode:1996Natur.384..567T. doi:10.1038/384567a0. PMID 8955270. S2CID 4242547.
  • Paudel HK (November 1997). "Phosphorylation by neuronal cdc2-like protein kinase promotes dimerization of Tau protein in vitro". The Journal of Biological Chemistry. 272 (45): 28328–34. doi:10.1074/jbc.272.45.28328. PMID 9353289.
  • Joel PB, Smith J, Sturgill TW, Fisher TL, Blenis J, Lannigan DA (April 1998). "pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167". Molecular and Cellular Biology. 18 (4): 1978–84. doi:10.1128/mcb.18.4.1978. PMC 121427. PMID 9528769.
  • Zheng-Fischhöfer Q, Biernat J, Mandelkow EM, Illenberger S, Godemann R, Mandelkow E (March 1998). "Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation". European Journal of Biochemistry. 252 (3): 542–52. doi:10.1046/j.1432-1327.1998.2520542.x. PMID 9546672.
  • Deak M, Clifton AD, Lucocq LM, Alessi DR (August 1998). "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB". The EMBO Journal. 17 (15): 4426–41. doi:10.1093/emboj/17.15.4426. PMC 1170775. PMID 9687510.
  • Du K, Montminy M (December 1998). "CREB is a regulatory target for the protein kinase Akt/PKB". The Journal of Biological Chemistry. 273 (49): 32377–9. doi:10.1074/jbc.273.49.32377. PMID 9829964.
  • Hanger DP, Betts JC, Loviny TL, Blackstock WP, Anderton BH (December 1998). "New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry". Journal of Neurochemistry. 71 (6): 2465–76. doi:10.1046/j.1471-4159.1998.71062465.x. PMID 9832145.
  • Jacquot S, Merienne K, De Cesare D, Pannetier S, Mandel JL, Sassone-Corsi P, Hanauer A (December 1998). "Mutation analysis of the RSK2 gene in Coffin-Lowry patients: extensive allelic heterogeneity and a high rate of de novo mutations". American Journal of Human Genetics. 63 (6): 1631–40. doi:10.1086/302153. PMC 1377634. PMID 9837815.
  • Jacquot S, Merienne K, Pannetier S, Blumenfeld S, Schinzel A, Hanauer A (1999). "Germline mosaicism in Coffin-Lowry syndrome". European Journal of Human Genetics. 6 (6): 578–82. doi:10.1038/sj.ejhg.5200230. PMID 9887375.
  • Smith JA, Poteet-Smith CE, Malarkey K, Sturgill TW (January 1999). "Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo". The Journal of Biological Chemistry. 274 (5): 2893–8. doi:10.1074/jbc.274.5.2893. PMID 9915826.
  • Abidi F, Jacquot S, Lassiter C, Trivier E, Hanauer A, Schwartz CE (January 1999). "Novel mutations in Rsk-2, the gene for Coffin-Lowry syndrome (CLS)". European Journal of Human Genetics. 7 (1): 20–6. doi:10.1038/sj.ejhg.5200231. PMID 10094187.
  • Merienne K, Jacquot S, Pannetier S, Zeniou M, Bankier A, Gecz J, Mandel JL, Mulley J, Sassone-Corsi P, Hanauer A (May 1999). "A missense mutation in RPS6KA3 (RSK2) responsible for non-specific mental retardation". Nature Genetics. 22 (1): 13–4. doi:10.1038/8719. PMID 10319851. S2CID 30949315.
  • External links[edit]

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

  • LATS2
  • MAST1
  • MAST2
  • STK38
  • STK38L
  • CIT
  • ROCK1
  • SGK
  • SGK2
  • SGK3
  • Protein kinase B
  • Ataxia telangiectasia mutated
  • mTOR
  • EIF-2 kinases
  • Wee1
  • Pyruvate dehydrogenase kinase (EC 2.7.11.2)

  • PDK2
  • PDK3
  • PDK4
  • Dephospho-(reductase kinase) kinase (EC 2.7.11.3)

  • PRKAA2
  • β
  • γ
  • 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)

  • BCKDHA
  • BCKDHB
  • (isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)

  • IDH3A
  • IDH3B
  • IDH3G
  • (tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)

    Myosin-heavy-chain kinase (EC 2.7.11.7)

  • Aurora B kinase
  • Aurora C kinase
  • Fas-activated serine/threonine kinase (EC 2.7.11.8)

  • STK10
  • Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)

    • -

    IκB kinase (EC 2.7.11.10)

  • IKK2
  • TBK1
  • IKBKE
  • IKBKG
  • IKBKAP
  • cAMP-dependent protein kinase (EC 2.7.11.11)

  • PRKACG
  • PRKACB
  • PRKACA
  • PRKY
  • cGMP-dependent protein kinase (EC 2.7.11.12)

  • PRKG1
  • Protein kinase C (EC 2.7.11.13)

  • Protein kinase Cζ
  • PKC alpha
  • PRKCB1
  • PRKCD
  • PRKCE
  • PRKCH
  • PRKCG
  • PRKCI
  • PRKCQ
  • Protein kinase N1
  • PKN2
  • PKN3
  • Rhodopsin kinase (EC 2.7.11.14)

    Beta adrenergic receptor kinase (EC 2.7.11.15)

  • Beta adrenergic receptor kinase-2
  • G-protein coupled receptor kinases (EC 2.7.11.16)

  • GRK5
  • GRK6
  • Ca2+/calmodulin-dependent (EC 2.7.11.17)

  • 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)

  • MYLK2
  • MYLK3
  • MYLK4
  • Phosphorylase kinase (EC 2.7.11.19)

  • PHKA2
  • PHKB
  • PHKG1
  • PHKG2
  • Elongation factor 2 kinase (EC 2.7.11.20)

  • STK19
  • Polo kinase (EC 2.7.11.21)

  • 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)

  • PLK2
  • PLK3
  • PLK4
  • Cyclin-dependent kinase (EC 2.7.11.22)

  • 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)

  • RPS6KA4
  • P70S6 kinase
  • P70-S6 Kinase 1
  • RPS6KB2
  • RPS6KA2
  • RPS6KA3
  • RPS6KA1
  • RPS6KC1
  • Mitogen-activated protein kinase (EC 2.7.11.24)

  • MAPK3
  • MAPK4
  • MAPK6
  • MAPK7
  • MAPK12
  • MAPK15
  • C-Jun N-terminal
  • P38 mitogen-activated protein
  • MAP3K (EC 2.7.11.25)

  • MAP3K2
  • MAP3K3
  • MAP3K4
  • MAP3K5
  • MAP3K6
  • MAP3K7
  • MAP3K8
  • RAFs
  • MLKs
  • CDC7
  • MAP3K14
  • Tau-protein kinase (EC 2.7.11.26)

  • 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)

  • BMPR1A
  • BMPR1B
  • BMPR2
  • ACVR1
  • ACVR1B
  • ACVR1C
  • ACVR2A
  • ACVR2B
  • ACVRL1
  • Anti-Müllerian hormone receptor
  • MAP2K2
  • MAP2K3
  • MAP2K4
  • MAP2K5
  • MAP2K6
  • MAP2K7
  • Activity

  • Binding site
  • Catalytic triad
  • Oxyanion hole
  • Enzyme promiscuity
  • Diffusion-limited enzyme
  • Cofactor
  • Enzyme catalysis
  • Regulation

  • Cooperativity
  • Enzyme inhibitor
  • Enzyme activator
  • Classification

  • Enzyme superfamily
  • Enzyme family
  • List of enzymes
  • Kinetics

  • Eadie–Hofstee diagram
  • Hanes–Woolf plot
  • Lineweaver–Burk plot
  • Michaelis–Menten kinetics
  • Types

  • EC2 Transferases (list)
  • EC3 Hydrolases (list)
  • EC4 Lyases (list)
  • EC5 Isomerases (list)
  • EC6 Ligases (list)
  • EC7 Translocases (list)

  • Retrieved from "https://en.wikipedia.org/w/index.php?title=RPS6KA3&oldid=1188159423"

    Categories: 
    Genes on human chromosome X
    EC 2.7.11
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